|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
439-1200 |
0e+00 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 1148.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGTSGNkVFSVEKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQTM 598
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGG-VLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 599 LLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQTAMKVLGISPDE 678
Cdd:cd01386 160 LLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 679 QKACWLILAAIYHLGAAGATKEAPEeqaeaaeaGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGCTLQRSTSFRQ 758
Cdd:cd01386 240 QRAIWSILAAIYHLGAAGATKAASA--------GRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 759 GPEESSlgDGTGPKLTALECLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGGSARGASFEELC 838
Cdd:cd01386 312 ESPARS--SSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLC 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 839 HNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLEPATDDSVAAVDQASHQSLVRSLARTDEARGLLWLLEEEALVPG 918
Cdd:cd01386 390 HNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQQALVRSDLRDEDRRGLLWLLDEEALYPG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 919 ATEDALLERLFSYYGPQEGDkKGQRPLLRSSKPHHFLLGHSHGTNWVEYNVSGWLSYTKQNPATQNAPRLLQDSQKKiis 998
Cdd:cd01386 470 SSDDTFLERLFSHYGDKEGG-KGHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE--- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 999 nlflgraggttvlsgsiagleggsqlalrratsmrktfttgMAAVKKKSLCIQIKLQVDALIDTIKKSKLHFVHCFLPVA 1078
Cdd:cd01386 546 -----------------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQH 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1079 EGWAGEprsassrrvsssseldlPSGDHCEAGLLQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1158
Cdd:cd01386 585 NAGKDE-----------------RSTSSPAAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPP 647
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1239919865 1159 LTKKHGRNYIVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd01386 648 LTKKLGLNSEVADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
440-1200 |
1.67e-148 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 477.08 E-value: 1.67e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGTSGNKVFS-----VEKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASA 593
Cdd:cd00124 82 ESGAGKTETTKLVLKYLAALSGSGSSKSSSsassiEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 594 SIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAEN---NVFGIVPLAKPEEKQKAAQQFSKLQTAMK 670
Cdd:cd00124 162 SIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYyylNDYLNSSGCDRIDGVDDAEEFQELLDALD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 671 VLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEagrkqfARHEWAQKAAYLLGCSLEELSSAIFKHQHKGctl 750
Cdd:cd00124 242 VLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEV------ADDESLKAAAKLLGVDAEDLEEALTTRTIKV--- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 751 qRSTSFR--QGPEEsslgdgtgpkltALECLEGMASGLYSELFTLLVSLVNRALKSS--QHSLCSMMIVDTPGFQNPEQg 826
Cdd:cd00124 313 -GGETITkpLTVEQ------------AEDARDALAKALYSRLFDWLVNRINAALSPTdaAESTSFIGILDIFGFENFEV- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 827 gsargASFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLEpatdDSVAAVD--QASHQSLVRSLarTDEAR 904
Cdd:cd00124 379 -----NSFEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDFP----DNQDCLDliEGKPLGILSLL--DEECL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 905 gllwlleeealVPGATEDALLERLFSYYGPQEGDKKGQRpllrsSKPHHFllGHSHGTNWVEYNVSGWLSYTKQNpatqn 984
Cdd:cd00124 448 -----------FPKGTDATFLEKLYSAHGSHPRFFSKKR-----KAKLEF--GIKHYAGDVTYDADGFLEKNKDT----- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 985 aprllqdsqkkiisnlflgraggttvLSGSIAGLeggsqlaLRRATSMRKtfttgmaavkkkslciqiklQVDALIDTIK 1064
Cdd:cd00124 505 --------------------------LPPDLVDL-------LRSGSQFRS--------------------QLDALMDTLN 531
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1065 KSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMV 1144
Cdd:cd00124 532 STQPHFVRCIKPNDEKKPG-----------------------------LFDPELVLEQLRCAGVLEAVRIRRAGYPVRLP 582
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239919865 1145 FSEFRRRFDVLAPHLTKKHgrnyiVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd00124 583 FDEFLKRYRILAPGATEKA-----SDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
420-1212 |
3.48e-118 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 391.52 E-value: 3.48e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 420 NAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQ 499
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 500 TAYRAMLMSRQDQSVILLGSSGSGKTTSCQHLVQYLATIAGtSGNKVFSVEKwQALYS--LLEAFGNSPTIMNGNATRFS 577
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG-SNTEVGSVED-QILESnpILEAFGNAKTLRNNNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 578 QILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHlAENNVFgivpLAKPEEKQK 657
Cdd:smart00242 159 KFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRY----LNQGGCLTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 658 A----AQQFSKLQTAMKVLGISPDEQKACWLILAAIYHLG----AAGATKEAPEEQAEaaeagrkqfarHEWAQKAAYLL 729
Cdd:smart00242 234 DgiddAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGniefEEGRNDNAASTVKD-----------KEELSNAAELL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 730 GCSLEELSSAIfkhqhkgctLQRSTSFRQGPEESslgdgtgpKLTALECLEG---MASGLYSELFTLLVSLVNRALKSSQ 806
Cdd:smart00242 303 GVDPEELEKAL---------TKRKIKTGGEVITK--------PLNVEQALDArdaLAKALYSRLFDWLVKRINQSLSFKD 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 807 HSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLEpatdDSVAAVD 886
Cdd:smart00242 366 GSTYFIGVLDIYGFEIFEVN------SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF----DNQDCID 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 887 --QASHQSLVRSLarTDEARgllwlleeealVPGATEDALLERLFSYYgpqegdKKGQRPLLRSSKPH-HFLLGHSHGTn 963
Cdd:smart00242 436 liEKKPPGILSLL--DEECR-----------FPKGTDQTFLEKLNQHH------KKHPHFSKPKKKGRtEFIIKHYAGD- 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 964 wVEYNVSGWLsytKQN--PATQNAPRLLQDSQKKIISNLFlgraggttvlsGSIAGleggsqlalrRATSMRKTFTTGMa 1041
Cdd:smart00242 496 -VTYDVTGFL---EKNkdTLSDDLIELLQSSKNPLIASLF-----------PSGVS----------NAGSKKRFQTVGS- 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1042 avkkkslciQIKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPsgdhceaglLQLDVPLLRA 1121
Cdd:smart00242 550 ---------QFKEQLNELMDTLNSTNPHFIRCIKP--------------------NEEKKP---------GDFDSSLVLH 591
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1122 QLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGrnyivMDERRAVEELLESLDLEKSSCCMGLSRVFFRA 1201
Cdd:smart00242 592 QLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWG-----GDAKKACEALLQSLGLDEDEYQLGKTKVFLRP 666
|
810
....*....|.
gi 1239919865 1202 GTLARLEEQRD 1212
Cdd:smart00242 667 GQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
401-1932 |
2.44e-111 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 391.36 E-value: 2.44e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 401 KLDHDGAILDVDEDDVEKANAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPaVYSEKVM 479
Cdd:COG5022 42 KEDGESVSVKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPyRDLG-IYTDDII 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 480 HMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLGSSGSGKTTSCQHLVQYLATIAGTSGNKVFSVEKwQALYS-- 557
Cdd:COG5022 121 QSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSIEK-QILATnp 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 558 LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHL-- 635
Cdd:COG5022 200 ILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLqn 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 636 ----NHLAENNVFGIVPLAKPEEkqkaaqqFSKLQTAMKVLGISPDEQKACWLILAAIYHLGaagatkeapEEQAEAAEA 711
Cdd:COG5022 280 pkdyIYLSQGGCDKIDGIDDAKE-------FKITLDALKTIGIDEEEQDQIFKILAAILHIG---------NIEFKEDRN 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 712 GRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHK--GCTLQRSTSFRQgpeesslgdgtgpkltALECLEGMASGLYSE 789
Cdd:COG5022 344 GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKtgGEWIVVPLNLEQ----------------ALAIRDSLAKALYSN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 790 LFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIE- 868
Cdd:COG5022 408 LFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKN------SFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEw 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 869 --LAFDDLEPATDdsvaavdqashqsLVRSLART-------DEARgllwlleeealVPGATEDALLERLFSYYgPQEGDK 939
Cdd:COG5022 482 sfIDYFDNQPCID-------------LIEKKNPLgilslldEECV-----------MPHATDESFTSKLAQRL-NKNSNP 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 940 KGQRPLLRSSKphhFLLGHSHGTnwVEYNVSGWLSYTKqNPATQNAPRLLQDSQKKIISNLFLGRAggttvlsgsiaglE 1019
Cdd:COG5022 537 KFKKSRFRDNK---FVVKHYAGD--VEYDVEGFLDKNK-DPLNDDLLELLKASTNEFVSTLFDDEE-------------N 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1020 GGSQLALRRATSMrktfttgmaavkkkslciqIKLQVDALIDTIKKSKLHFVHCFLP--VAEGWageprsassrrvssss 1097
Cdd:COG5022 598 IESKGRFPTLGSR-------------------FKESLNSLMSTLNSTQPHYIRCIKPneEKSPW---------------- 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1098 eldlpsgdhceagllQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNYIVMDERRAVE 1177
Cdd:COG5022 643 ---------------TFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPS-KSWTGEYTWKEDTKNAVK 706
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1178 ELLESLDLEKSSCCMGLSRVFFRAGTLARLEEQRDEQTSRNLTLFQAACRGYLARQHF-KKKKIQDlAIRCVQKNIKKNK 1256
Cdd:COG5022 707 SILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYlQALKRIK-KIQVIQHGFRLRR 785
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1257 GVKDWAWWKLFTTVRPLIEVQLSEEQIRSKDEEIQQLRSKLEKV----EKERNELRLSNDRLETRISEltSELTDERNTG 1332
Cdd:COG5022 786 LVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREkklrETEEVEFSLKAEVLIQKFGR--SLKAKKRFSL 863
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1333 ESASQLLDAEAAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDTGGEWRLKYERAMREVDF- 1411
Cdd:COG5022 864 LKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLe 943
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1412 ---TKKRLQQEFEDKLEVEQQNKRQLERRLGDL----QADIDESQRALQQLKKKCQRLTA------ELQDTKLHLEGQQV 1478
Cdd:COG5022 944 egpSIEYVKLPELNKLHEVESKLKETSEEYEDLlkksTILVREGNKANSELKNFKKELAElskqygALQESTKQLKELPV 1023
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1479 RNHELEKKQRRfdseLSQAHEEAQREKlqreKLQREKDTLLAEAFSLKQQLeekdmdiagftqKVVSLEAELQDIssqES 1558
Cdd:COG5022 1024 EVAELQSASKI----ISSESTELSILK----PLQKLKGLLLLENNQLQARY------------KALKLRRENSLL---DD 1080
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1559 KDEASLAKVKKQLRDLEAK---VKDQEEELDEQAGTIQMLEQAKLRLEMEMERM--RQTHSKEVESRDEEVEEARQSCQK 1633
Cdd:COG5022 1081 KQLYQLESTENLLKTINVKdleVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFlsQLVNTLEPVFQKLSVLQLELDGLF 1160
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1634 KLKQMEvqlEEEYEDKQKVLREKRELESKLTTL---SEQVSQRDLESE-----KRLRKDLKRTKALLADAQ-------IM 1698
Cdd:COG5022 1161 WEANLE---ALPSPPPFAALSEKRLYQSALYDEkskLSSSEVNDLKNElialfSKIFSGWPRGDKLKKLISegwvpteYS 1237
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1699 LDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEED 1778
Cdd:COG5022 1238 TSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFNALRTKASSLRWKSATEVN 1317
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1779 QEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRElETRL 1858
Cdd:COG5022 1318 YNSEELDDWCREFEISDVDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQNLKSRYDPADKENNLPK-EILK 1396
|
1530 1540 1550 1560 1570 1580 1590
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 1859 EFERTQVKRLESLASRLKENMEKLTEErdqrtaaENREKEQNKRLQRQLRDTKEEMGELarkEAEASRKKHELE 1932
Cdd:COG5022 1397 KIEALLIKQELQLSLEGKDETEVHLSE-------IFSEEKSLISLDRNSIYKEEVLSSL---SALLTKEKIALL 1460
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
428-1200 |
2.39e-110 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 368.53 E-value: 2.39e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 428 EDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLM 507
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 508 SRQDQSVILLGSSGSGKTTSCQHLVQYLATIAGT-SGNKVFSVEKwQALYS--LLEAFGNSPTIMNGNATRFSQILSLDF 584
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSgSAGNVGRLEE-QILQSnpILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 585 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHL---------NHLAENNVFGIvplakpeek 655
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLtnpkdyhylSQSGCYTIDGI--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 656 qKAAQQFSKLQTAMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEaaeagrkqFARHEWAQKAAYLLGCSLEE 735
Cdd:pfam00063 232 -DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAV--------PDDTENLQKAASLLGIDSTE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 736 LSSAIFKHQhkgctLQRSTSFRQGPEEsslgdgtgpKLTALECLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMM-I 814
Cdd:pfam00063 303 LEKALCKRR-----IKTGRETVSKPQN---------VEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIgV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 815 VDTPGFQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIE---LAFDDLEPATDdsvaavdqashq 891
Cdd:pfam00063 369 LDIYGFEIFEKN------SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEwtfIDFGDNQPCID------------ 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 892 sLVRS-----LARTDEArgllwlleeeALVPGATEDALLERLFSYYGpqeGDKKGQRPLLRSSKphHFLLGHSHGTnwVE 966
Cdd:pfam00063 431 -LIEKkplgiLSLLDEE----------CLFPKATDQTFLDKLYSTFS---KHPHFQKPRLQGET--HFIIKHYAGD--VE 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 967 YNVSGWLSYTKqNPATQNAPRLLQDSQKKIISNLFLGRAggttvLSGSIAGLEGGSQLALRRATSMRKtfTTGMaavkkk 1046
Cdd:pfam00063 493 YNVEGFLEKNK-DPLNDDLVSLLKSSSDPLLAELFPDYE-----TAESAAANESGKSTPKRTKKKRFI--TVGS------ 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1047 slciQIKLQVDALIDTIKKSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRAQLRGS 1126
Cdd:pfam00063 559 ----QFKESLGELMKTLNSTNPHYIRCIKPNEKKRAG-----------------------------VFDNSLVLHQLRCN 605
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 1127 RLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKhgrnyIVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:pfam00063 606 GVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPK-----WKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
440-1200 |
3.77e-102 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 344.45 E-value: 3.77e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPaVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPyKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGTSGNKVFSVEKW-----QALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVA 591
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKKgtledQILQAnpILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 592 SASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVFgIVPLAKPEEKQKAAQQFSKLQTAMKV 671
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFF-LSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 672 LGISPDEQKACWLILAAIYHLGAAGATKeapeeqaeaaeAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFK------ 742
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQ-----------RRREEQAEldgTEEADKAAHLLGVNSSDLLKALLKprikvg 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 743 --HQHKGCTLQRSTSfrqgpeesslgdgtgpkltaleCLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGF 820
Cdd:cd01377 309 reWVTKGQNKEQVVF----------------------SVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 821 Q----NpeqggsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAF----DDLEPATDdsvaavdqashqs 892
Cdd:cd01377 367 EifefN----------SFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfgLDLQPTID------------- 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 893 LVRS-----LARTDEargllwlleeEALVPGATEDALLERLFSyygpQEGDKKGQRPLLRSSKPH-HFLLGHSHGTnwVE 966
Cdd:cd01377 424 LIEKpnmgiLSILDE----------ECVFPKATDKTFVEKLYS----NHLGKSKNFKKPKPKKSEaHFILKHYAGD--VE 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 967 YNVSGWLSYTKqNPATQNAPRLLQDSQKKIISNLFlgraggttvlsgSIAGLEGGSQLALRRATSMRKTfttgMAAVKKK 1046
Cdd:cd01377 488 YNIDGWLEKNK-DPLNENVVALLKKSSDPLVASLF------------KDYEESGGGGGKKKKKGGSFRT----VSQLHKE 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1047 SLciqiklqvDALIDTIKKSKLHFVHCFLPVAEGWAGEprsassrrvsssseldlpsgdhceagllqLDVPLLRAQLRGS 1126
Cdd:cd01377 551 QL--------NKLMTTLRSTHPHFVRCIIPNEEKKPGK-----------------------------IDAPLVLHQLRCN 593
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 1127 RLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKhgrnyIVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd01377 594 GVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPK-----GFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
439-1200 |
1.22e-91 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 313.87 E-value: 1.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIA-----GTSGNKVFSVEKwQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVA 591
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVAsshkgRKDHNIPGELER-QLLQAnpILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 592 SASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVF--GIVPLAkpeeKQKAAQQFSKLQTAM 669
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsnGYIPIP----GQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 670 KVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEqaeaaeagRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQhkgct 749
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD--------QASMPENTVAQKLCHLLGMNVMEFTRAILTPR----- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 750 LQRSTSFRQGPEESSLGDGTgpkltalecLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgs 828
Cdd:cd14920 303 IKVGRDYVQKAQTKEQADFA---------VEALAKATYERLFRWLVHRINKALDRTKRQGASFIgILDIAGFEIFELN-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 829 argaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFD----DLEPATDdsvaAVDQASHQSLVrsLARTDEar 904
Cdd:cd14920 372 ----SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIdfglDLQPCID----LIERPANPPGV--LALLDE-- 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 905 gllwlleeEALVPGATEDALLERLFSYYGPQEGDKKGQRPLLRSSkphhFLLGHSHGTnwVEYNVSGWLsYTKQNPATQN 984
Cdd:cd14920 440 --------ECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD----FCIIHYAGK--VDYKADEWL-MKNMDPLNDN 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 985 APRLLQDSQKKIISNLF--LGRAGGTTVLSGsIAGLEGGSQLALRRAtsMRKTfttgMAAVKKKSLciqiklqvDALIDT 1062
Cdd:cd14920 505 VATLLHQSSDRFVAELWkdVDRIVGLDQVTG-MTETAFGSAYKTKKG--MFRT----VGQLYKESL--------TKLMAT 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1063 IKKSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRAQLRGSRLLDAMRMYRQGYPDH 1142
Cdd:cd14920 570 LRNTNPNFVRCIIPNHEKRAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNR 620
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1143 MVFSEFRRRFDVLAPHLTKKhgrnyIVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14920 621 IVFQEFRQRYEILTPNAIPK-----GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
439-1200 |
4.23e-85 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 294.97 E-value: 4.23e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIA-----GTSGNKVFSV-------EKWQALYS---LLEAFGNSPTIMNGNATRFSQILSLD 583
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAaskpkGSGAVPHPAVnpavligELEQQLLQanpILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 584 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHlAENNVF---GIVPLAKPEEkqkaAQ 660
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDD-VKSYAFlsnGSLPVPGVDD----YA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 661 QFSKLQTAMKVLGISPDEQKACWLILAAIYHLGAagatkeapEEQAEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAI 740
Cdd:cd14911 236 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGS--------MKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 741 FKHQHKgcTLQRSTSFRQGPEESSLGdgtgpkltalecLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPG 819
Cdd:cd14911 308 LTPRIK--VGRDFVTKAQTKEQVEFA------------VEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIgILDMAG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 820 FQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFD----DLEPATDdsvaavdqashqsLVr 895
Cdd:cd14911 374 FEIFELN------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIdfglDLQPTID-------------LI- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 896 slartDEARGLLWLLEEEALVPGATEDALLERLFSYYGPQEGDKKGQrplLRSSKphHFLLGHSHGTnwVEYNVSGWLsY 975
Cdd:cd14911 434 -----DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTD---FRGVA--DFAIVHYAGR--VDYSAAKWL-M 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 976 TKQNPATQNAPRLLQDSQKKIISNLFlgragGTTVLSGSIAGLEGGSQLALRRATSMRKTFTTgmaavkkkslciQIKLQ 1055
Cdd:cd14911 501 KNMDPLNENIVSLLQGSQDPFVVNIW-----KDAEIVGMAQQALTDTQFGARTRKGMFRTVSH------------LYKEQ 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1056 VDALIDTIKKSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRAQLRGSRLLDAMRMY 1135
Cdd:cd14911 564 LAKLMDTLRNTNPNFVRCIIPNHEKRAG-----------------------------KIDAPLVLDQLRCNGVLEGIRIC 614
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239919865 1136 RQGYPDHMVFSEFRRRFDVLAPHLTKKHgrnyiVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14911 615 RQGFPNRIPFQEFRQRYELLTPNVIPKG-----FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
439-1200 |
6.11e-85 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 294.23 E-value: 6.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGT-SGNKVFSV----EKwQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVA 591
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASShKGKKDTSItgelEK-QLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 592 SASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNV--FGIVPLAkpeeKQKAAQQFSKLQTAM 669
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFlsNGFVPIP----AAQDDEMFQETLEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 670 KVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEqaeaaeagRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQhkgct 749
Cdd:cd14921 236 SIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTD--------QASMPDNTAAQKVCHLMGINVTDFTRSILTPR----- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 750 LQRSTSFRQGPEESSLGDGTgpkltalecLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgs 828
Cdd:cd14921 303 IKVGRDVVQKAQTKEQADFA---------IEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFEIFEVN-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 829 argaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLepatddsvaAVDQashQSLVRSLARTDEARGLLW 908
Cdd:cd14921 372 ----SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDF---------GLDL---QPCIELIERPNNPPGVLA 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 909 LLEEEALVPGATEDALLERLFSyygPQEGDKKGQRPLLRSSKPHHFLLghsHGTNWVEYNVSGWLSyTKQNPATQNAPRL 988
Cdd:cd14921 436 LLDEECWFPKATDKSFVEKLCT---EQGNHPKFQKPKQLKDKTEFSII---HYAGKVDYNASAWLT-KNMDPLNDNVTSL 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 989 LQDSQKKIISNLFLGraggttvlSGSIAGLEGGSQLALRRATSMRKTfTTGMAavkkKSLCIQIKLQVDALIDTIKKSKL 1068
Cdd:cd14921 509 LNASSDKFVADLWKD--------VDRIVGLDQMAKMTESSLPSASKT-KKGMF----RTVGQLYKEQLGKLMTTLRNTTP 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1069 HFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 1148
Cdd:cd14921 576 NFVRCIIPNHEKRSG-----------------------------KLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 626
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1239919865 1149 RRRFDVLAPHLTKKHgrnyiVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14921 627 RQRYEILAANAIPKG-----FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
439-1200 |
2.19e-83 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 290.01 E-value: 2.19e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGTS------GNKVFS---VEKwQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQA 587
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFktkkdqSSIALShgeLEK-QLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 588 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVFGIVPLAKPEEKQKaaQQFSKLQT 667
Cdd:cd14932 160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDK--ELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 668 AMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEqaeaaeagRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKg 747
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSD--------QASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIK- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 748 ctLQRSTSFRQGPEESslgdgtgpkltALECLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQG 826
Cdd:cd14932 309 --VGRDYVQKAQTQEQ-----------AEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFELN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 827 gsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLEPATDDSVAAVDQASHQSLVrsLARTDEargl 906
Cdd:cd14932 376 ------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGI--LALLDE---- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 907 lwlleeEALVPGATEDALLERLFSYYGpqeGDKKGQRPlLRSSKPHHFLLGHSHGTnwVEYNVSGWLsYTKQNPATQNAP 986
Cdd:cd14932 444 ------ECWFPKATDKSFVEKVVQEQG---NNPKFQKP-KKLKDDADFCIIHYAGK--VDYKANEWL-MKNMDPLNENVA 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 987 RLLQDSQKKIISNLFlgRAGGTTVLSGSIAGLEGGSQLALRRATSMRKTFTTgmaavkkkslciQIKLQVDALIDTIKKS 1066
Cdd:cd14932 511 TLLNQSTDKFVSELW--KDVDRIVGLDKVAGMGESLHGAFKTRKGMFRTVGQ------------LYKEQLMNLMTTLRNT 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1067 KLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFS 1146
Cdd:cd14932 577 NPNFVRCIIPNHEKKAG-----------------------------KLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 1147 EFRRRFDVLAPHLTKKHgrnyiVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14932 628 EFRQRYEILTPNAIPKG-----FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
439-1200 |
9.97e-81 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 281.98 E-value: 9.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGTSGNKVFSVEKWQALYS---LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASI 595
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQanpILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 596 QTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVFGIVPLAKPEEKQKaaQQFSKLQTAMKVLGIS 675
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK--DMFQETMEAMRIMGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 676 PDEQKACWLILAAIYHLGAAGATKEAPEEqaeaaeagRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQhkgctLQRSTS 755
Cdd:cd14919 239 EEEQMGLLRVISGVLQLGNIVFKKERNTD--------QASMPDNTAAQKVSHLLGINVTDFTRGILTPR-----IKVGRD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 756 FRQGPEESSLGDGTgpkltalecLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsargaSF 834
Cdd:cd14919 306 YVQKAQTKEQADFA---------IEALAKATYERMFRWLVLRINKALDKTKRQGASFIgILDIAGFEIFDLN------SF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 835 EELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLEPATDDSVAAVDQASHQSLVrsLARTDEargllwlleeEA 914
Cdd:cd14919 371 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGI--LALLDE----------EC 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 915 LVPGATEDALLERLFSYYGPQegdKKGQRPLLRSSKPhHFLLGHSHGTnwVEYNVSGWLsYTKQNPATQNAPRLLQDSQK 994
Cdd:cd14919 439 WFPKATDKSFVEKVVQEQGTH---PKFQKPKQLKDKA-DFCIIHYAGK--VDYKADEWL-MKNMDPLNDNIATLLHQSSD 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 995 KIISNLFLGraggttvlSGSIAGLE---GGSQLALRRATSMRKTFTTGMAAVKKKslciqiklQVDALIDTIKKSKLHFV 1071
Cdd:cd14919 512 KFVSELWKD--------VDRIIGLDqvaGMSETALPGAFKTRKGMFRTVGQLYKE--------QLAKLMATLRNTNPNFV 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1072 HCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRR 1151
Cdd:cd14919 576 RCIIPNHEKKAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQR 626
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1239919865 1152 FDVLAPHLTKKHgrnyiVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14919 627 YEILTPNSIPKG-----FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
439-1200 |
9.85e-77 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 270.40 E-value: 9.85e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGT------SGNKVFS---VEKwQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQA 587
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdQNSLALShgeLEK-QLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 588 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVFGIVPLAKPEEKQKaaQQFSKLQT 667
Cdd:cd15896 160 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDK--DLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 668 AMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEqaeaaeagRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKg 747
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTD--------QASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIK- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 748 ctLQRSTSFRQGPEESslgdgtgpkltALECLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQG 826
Cdd:cd15896 309 --VGRDYVQKAQTQEQ-----------AEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFELN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 827 gsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLEPATDDSVAAVDQASHQSLVrsLARTDEargl 906
Cdd:cd15896 376 ------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGI--LALLDE---- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 907 lwlleeEALVPGATEDALLERLFSYYGPQEGDKKGQRplLRSSKphHFLLGHSHGTnwVEYNVSGWLsYTKQNPATQNAP 986
Cdd:cd15896 444 ------ECWFPKATDKSFVEKVLQEQGTHPKFFKPKK--LKDEA--DFCIIHYAGK--VDYKADEWL-MKNMDPLNDNVA 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 987 RLLQDSQKKIISNLFLGraggttvlSGSIAGLEGGSQLA-LRRATSMRKTFTTGMAAVKKKslciqiklQVDALIDTIKK 1065
Cdd:cd15896 511 TLLNQSTDKFVSELWKD--------VDRIVGLDKVSGMSeMPGAFKTRKGMFRTVGQLYKE--------QLSKLMATLRN 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1066 SKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVF 1145
Cdd:cd15896 575 TNPNFVRCIIPNHEKKAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 625
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1239919865 1146 SEFRRRFDVLAPHLTKKHgrnyiVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd15896 626 QEFRQRYEILTPNAIPKG-----FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
439-1200 |
1.41e-75 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 266.46 E-value: 1.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGTSGNKvfsvEKWQALY-------SLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVA 591
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESK----KKLGALEdqimqanPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 592 SASIQTMLLEKLRVARRPASEATFNVFYYLLACadgtlRTELHLNHLAENN-------VFGIVPLakpeEKQKAAQQFSK 664
Cdd:cd14929 157 SADIDIYLLEKSRVIFQQPGERNYHIFYQILSG-----KKELRDLLLVSANpsdfhfcSCGAVAV----ESLDDAEELLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 665 LQTAMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAgrkqfarhEWAQKAAYLLGCSLEELSsaifkhq 744
Cdd:cd14929 228 TEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGT--------ENADKAAFLMGINSSELV------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 745 hKGCTLQRstsFRQGPEESSlgdgTGPKLTALECLEG-MASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNP 823
Cdd:cd14929 293 -KGLIHPR---IKVGNEYVT----RSQNIEQVTYAVGaLSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEIL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 824 EQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIE-LAFD---DLEPATDdsvaavdqashqsLVrslar 899
Cdd:cd14929 365 DYN------SLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDwVSIDfglDLQACID-------------LI----- 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 900 tDEARGLLWLLEEEALVPGATEDALLERLFSYYgpqegdkKGQRPLLRSSKPH------HFLLGHSHGTnwVEYNVSGWL 973
Cdd:cd14929 421 -EKPMGIFSILEEECMFPKATDLTFKTKLFDNH-------FGKSVHFQKPKPDkkkfeaHFELVHYAGV--VPYNISGWL 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 974 SYTKqNPATQNAPRLLQDSQKKIISNLFlgraggTTVLSgsiagleGGSQLALRRATSMRKTFTTGMAAVKKKSLciqik 1053
Cdd:cd14929 491 EKNK-DLLNETVVAVFQKSSNRLLASLF------ENYIS-------TDSAIQFGEKKRKKGASFQTVASLHKENL----- 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1054 lqvDALIDTIKKSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRAQLRGSRLLDAMR 1133
Cdd:cd14929 552 ---NKLMTNLKSTAPHFVRCINPNVNKIPG-----------------------------VLDPYLVLQQLRCNGVLEGIR 599
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239919865 1134 MYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGrnyiVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14929 600 ICREGFPNRLLYADFKQRYCILNPRTFPKSK----FVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
439-1200 |
3.63e-73 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 259.64 E-value: 3.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGT-SGNKVFSVE---KWQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVAS 592
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSpKGRKEPGVPgelERQLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 593 ASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVFGIVPLAKPEEKQkaaQQFSKLQTAMKVL 672
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER---ELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 673 GISPDEQKACWLILAAIYHLGAAGATKEAPEEqaeaaeagRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQhkgctLQR 752
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNIVLKRERNTD--------QATMPDNTAAQKLCRLLGLGVTDFSRALLTPR-----IKV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 753 STSFRQGPEESSLGDGTgpkltalecLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsarg 831
Cdd:cd14930 305 GRDYVQKAQTKEQADFA---------LEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFEIFQLN----- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 832 aSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAF----DDLEPATDdsvaavdqashqslvrSLARTDEARGLL 907
Cdd:cd14930 371 -SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFldfgLDLQPCID----------------LIERPANPPGLL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 908 WLLEEEALVPGATEDALLERLFSYYGPQegdKKGQRPL-LRSSKPHHFLlghsHGTNWVEYNVSGWLsYTKQNPATQNAP 986
Cdd:cd14930 434 ALLDEECWFPKATDKSFVEKVAQEQGGH---PKFQRPRhLRDQADFSVL----HYAGKVDYKANEWL-MKNMDPLNDNVA 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 987 RLLQDSQKKIISNLFLGRAGgttvlsgsIAGLEGGSQL--ALRRATSMRKTFTTgMAAVKKKSLciqiklqvDALIDTIK 1064
Cdd:cd14930 506 ALLHQSTDRLTAEIWKDVEG--------IVGLEQVSSLgdGPPGGRPRRGMFRT-VGQLYKESL--------SRLMATLS 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1065 KSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMV 1144
Cdd:cd14930 569 NTNPSFVRCIVPNHEKRAG-----------------------------KLEPRLVLDQLRCNGVLEGIRICRQGFPNRIL 619
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239919865 1145 FSEFRRRFDVLAPHLTKKHgrnyiVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14930 620 FQEFRQRYEILTPNAIPKG-----FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
439-1200 |
5.05e-73 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 259.50 E-value: 5.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIA--GTSGNKVFSVEKWQALYSL----------LEAFGNSPTIMNGNATRFSQILSLDFDQ 586
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalGDGPGKKAQFLATKTGGTLedqiieanpaMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 587 AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLN------HLAENNVFGIVPLAKPEEkqkaaq 660
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmnpydyHFCSQGVTTVDNMDDGEE------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 661 qFSKLQTAMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAgrkqfarhEWAQKAAYLLGCSLEELSsai 740
Cdd:cd14927 235 -LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGT--------ESADKAAYLMGVSSADLL--- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 741 fkhqhKGCTLQRstsFRQGPEESSLGDGTGPKLTALECLegmASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGF 820
Cdd:cd14927 303 -----KGLLHPR---VKVGNEYVTKGQSVEQVVYAVGAL---AKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 821 QNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLEPatdDSVAAVDqashqsLVrslart 900
Cdd:cd14927 372 EIFEFN------SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGL---DLQACID------LI------ 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 901 DEARGLLWLLEEEALVPGATEDALLERLFSYYGPQEGDKKGQRPLLRSSKPHHFLLGHSHGTnwVEYNVSGWLSYTKqNP 980
Cdd:cd14927 431 EKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKYEAHFEVVHYAGV--VPYNIVGWLDKNK-DP 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 981 ATQNAPRLLQDSQKKIISNLFLGRAGgttvlSGSIAGLEGGSQLALRRATSmrktFTTgMAAVKKKSLciqiklqvDALI 1060
Cdd:cd14927 508 LNETVVAIFQKSQNKLLATLYENYVG-----SDSTEDPKSGVKEKRKKAAS----FQT-VSQLHKENL--------NKLM 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1061 DTIKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRAQLRGSRLLDAMRMYRQGYP 1140
Cdd:cd14927 570 TNLRATQPHFVRCIIP--------------------NETKTPG---------VMDPFLVLHQLRCNGVLEGIRICRKGFP 620
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1141 DHMVFSEFRRRFDVLAPHLTKKHGrnyiVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14927 621 NRILYADFKQRYRILNPSAIPDDK----FVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
439-1200 |
1.89e-71 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 254.38 E-value: 1.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIaGTSGNKVFSVEKWQALYS-------LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVA 591
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATV-GASKKTDEAAKSKGSLEDqvvqtnpVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 592 SASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNhlaeNNVFGIVPLAKPE---EKQKAAQQFSKLQTA 668
Cdd:cd14909 160 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLS----DNIYDYYIVSQGKvtvPNVDDGEEFSLTDQA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 669 MKVLGISPDEQKACWLILAAIYHLGAagatkeapeeqAEAAEAGRKQFARH---EWAQKAAYLLGCSLEELSSAIFKHQh 745
Cdd:cd14909 236 FDILGFTKQEKEDVYRITAAVMHMGG-----------MKFKQRGREEQAEQdgeEEGGRVSKLFGCDTAELYKNLLKPR- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 746 kgctLQRSTSF-RQGPEESSLGDGTGpkltalecleGMASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPE 824
Cdd:cd14909 304 ----IKVGNEFvTQGRNVQQVTNSIG----------ALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 825 QGGsargasFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLEPatdDSVAAVDQashqslvrslarTDEAR 904
Cdd:cd14909 370 YNG------FEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGM---DLLACIDL------------IEKPM 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 905 GLLWLLEEEALVPGATEDALLERLFSYYGPQEGDKKGQRPLLRSSKPHHFLLGHSHGTnwVEYNVSGWLSYTKqNPATQN 984
Cdd:cd14909 429 GILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAGC--VSYNITGWLEKNK-DPLNDT 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 985 APRLLQDSQKKIISNLFLGRAGGttvlSGSIAGLEGGsqlalrratsmRKTFTTGMAAVKKkslciQIKLQVDALIDTIK 1064
Cdd:cd14909 506 VVDQFKKSQNKLLIEIFADHAGQ----SGGGEQAKGG-----------RGKKGGGFATVSS-----AYKEQLNSLMTTLR 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1065 KSKLHFVHCFLPvaegwageprsassrrvsssSELDLPsgdhceaGLlqLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMV 1144
Cdd:cd14909 566 STQPHFVRCIIP--------------------NEMKQP-------GV--VDAHLVMHQLTCNGVLEGIRICRKGFPNRMM 616
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239919865 1145 FSEFRRRFDVLAPHLTKKHgrnyivMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14909 617 YPDFKMRYKILNPAGIQGE------EDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
440-1200 |
1.20e-69 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 249.20 E-value: 1.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLGS 519
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 520 SGSGKTTSCQHLVQYLATIAGTSGNKVFSVEKWQALYS--------LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVA 591
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 592 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcadgTLRTELHLNHLAENNVFGIVPLAKPEEKQKA---AQQFSKLQTA 668
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILS----NKKPELIELLLITTNPYDYPFISQGEILVASiddAEELLATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 669 MKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIfkhqhkgC 748
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKTAYLMGLNSSDLLKAL-------C 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 749 TlqrsTSFRQGPEESSLGDGTGPKLTALECLegmASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgs 828
Cdd:cd14913 303 F----PRVKVGNEYVTKGQTVDQVHHAVNAL---SKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN-- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 829 argaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLepatddsvaAVDQASHQSLVrslartDEARGLLW 908
Cdd:cd14913 374 ----SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF---------GMDLAACIELI------EKPMGIFS 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 909 LLEEEALVPGATEDALLERLFSYYGPQEGDKkgQRPLLRSSKPH-HFLLGHSHGTnwVEYNVSGWLSYTKqNPATQNAPR 987
Cdd:cd14913 435 ILEEECMFPKATDTSFKNKLYDQHLGKSNNF--QKPKVVKGRAEaHFSLIHYAGT--VDYSVSGWLEKNK-DPLNETVVG 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 988 LLQDSQKKIISNLFlgraggttvlsGSIAGLEGGSQlaLRRATSMRKTFTTGMAAVKKKSLciqiklqvDALIDTIKKSK 1067
Cdd:cd14913 510 LYQKSSNRLLAHLY-----------ATFATADADSG--KKKVAKKKGSSFQTVSALFRENL--------NKLMSNLRTTH 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1068 LHFVHCFLPvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSE 1147
Cdd:cd14913 569 PHFVRCIIP--------------------NETKTPGA---------MEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGD 619
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1239919865 1148 FRRRFDVLAPHLTKKhGRnyiVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14913 620 FKQRYRVLNASAIPE-GQ---FIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
439-1200 |
4.41e-69 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 247.24 E-value: 4.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14883 1 EGINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIagtsGNKVFSVEKwQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQ 596
Cdd:cd14883 81 ESGAGKTETTKLILQYLCAV----TNNHSWVEQ-QILEAntILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 597 TMLLEKLRVARRPASEATFNVFYYLLACADGT--LRTELHL---NHLAENNVFGIVPLAKPEEKQKaaqqFSKLQTAMKV 671
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGAKHSkeLKEKLKLgepEDYHYLNQSGCIRIDNINDKKD----FDHLRLAMNV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 672 LGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAGrkqfarhEWAQKAAYLLGCSLEELssaifkhqhKGCTLQ 751
Cdd:cd14883 232 LGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDK-------EILKIVAKLLGVDPDKL---------KKALTI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 752 RSTSFRQGPEESSLgdgtgpKLT-ALECLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsar 830
Cdd:cd14883 296 RQINVRGNVTEIPL------KVQeARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVN---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 831 gaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAfddlepatddSVAAVDQASHQSLVRS-----LARTDEarg 905
Cdd:cd14883 366 --SFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWS----------HIVFTDNQECLDLIEKpplgiLKLLDE--- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 906 llwlleeEALVPGATEDALLERLFSYYGPQEGDKKGQRPLLRSSkphhFLLGHSHGTnwVEYNVSGWLSytkQNPATQ-- 983
Cdd:cd14883 431 -------ECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTE----FGVKHYAGE--VTYTVQGFLD---KNKDTQqd 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 984 NAPRLLQDSQKKIISNLFLGRAggttvlsgsiagleggsQLALRRATSMRKTFTTGMAAVKKK-SLCIQIKLQVDALIDT 1062
Cdd:cd14883 495 DLFDLMSRSKNKFVKELFTYPD-----------------LLALTGLSISLGGDTTSRGTSKGKpTVGDTFKHQLQSLVDV 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1063 IKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRAQLRGSRLLDAMRMYRQGYPDH 1142
Cdd:cd14883 558 LSATQPWYVRCIKP--------------------NSLKEPN---------VFDDELVLAQLRYAGMLEIIRIRKEGFPIH 608
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1143 MVFSEFRRRFDVLAPHLtkkhgRNYIVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14883 609 LTFKEFVDRYLCLDPRA-----RSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
440-1157 |
2.83e-68 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 244.53 E-value: 2.83e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLGS 519
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 520 SGSGKTTSCQHLVQYLATIAGTSGnkvfSVEKwQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQT 597
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSS----GIEN-EILQTnpILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 598 MLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHL------NHLAENNVFGIVPLakpeekqKAAQQFSKLQTAMKV 671
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLksaseyKYLNQSNCLTIDGV-------DDAKKFHELKEALDT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 672 LGISPDEQKACWLILAAIYHLGaagatkeaPEEQAEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQ-HKGctl 750
Cdd:cd01383 228 VGISKEDQEHIFQMLAAVLWLG--------NISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKiQAG--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 751 qrstsfrqgpeesslGDGTGPKLT---ALECLEGMASGLYSELFTLLVSLVNRALKSSQH-SLCSMMIVDTPGFQnpeqg 826
Cdd:cd01383 297 ---------------GDKIVKKLTlqqAIDARDALAKAIYASLFDWLVEQINKSLEVGKRrTGRSISILDIYGFE----- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 827 gSARGASFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLEpatdDSVAAVDQASHQSL-VRSLarTDEarg 905
Cdd:cd01383 357 -SFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDFE----DNQECLDLIEKKPLgLISL--LDE--- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 906 llwlleeEALVPGATEDALLERLFSYYGPQEGDKKGQRPLlrsskphhFLLGHSHGTnwVEYNVSGWLSytkqnpatQNA 985
Cdd:cd01383 427 -------ESNFPKATDLTFANKLKQHLKSNSCFKGERGGA--------FTIRHYAGE--VTYDTSGFLE--------KNR 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 986 PRLLQDsqkkiISNLFLGRAGGTTVLSGSIAGLEGGSQLALRRATSMRKTfttgmaavkKKSLCIQIKLQVDALIDTIKK 1065
Cdd:cd01383 482 DLLHSD-----LIQLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQ---------KQSVATKFKGQLFKLMQRLEN 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1066 SKLHFVHCFLPVAEGWAGEprsassrrvsssSELDLpsgdhceagLLQldvpllraQLRGSRLLDAMRMYRQGYPDHMVF 1145
Cdd:cd01383 548 TTPHFIRCIKPNNKQLPGV------------FDQDL---------VLQ--------QLRCCGVLEVVRISRSGYPTRMTH 598
|
730
....*....|..
gi 1239919865 1146 SEFRRRFDVLAP 1157
Cdd:cd01383 599 QEFARRYGFLLP 610
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
441-1162 |
3.39e-67 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 241.43 E-value: 3.39e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 441 VLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLGS 519
Cdd:cd01384 3 VLHNLKVRYELDEIYTYTGNILIAVNPfKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 520 SGSGKTTSCQHLVQYLATIAGTSGNKVFSVEKwQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQT 597
Cdd:cd01384 83 SGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQ-QVLESnpLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 598 MLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHL------NHLAENNVFGIVPLAKPEEkqkaaqqFSKLQTAMKV 671
Cdd:cd01384 162 YLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLkdpkqfHYLNQSKCFELDGVDDAEE-------YRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 672 LGISPDEQKACWLILAAIYHLG----AAGAtkeapeeqaEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIfkhqhkg 747
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGniefSKGE---------EDDSSVPKDEKSEFHLKAAAELLMCDEKALEDAL------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 748 CTLQRSTsfRQGPEESSLGdgtgpKLTALECLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQnpeqgg 827
Cdd:cd01384 299 CKRVIVT--PDGIITKPLD-----PDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFE------ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 828 SARGASFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFddlepatddsVAAVDQASHQSLVRS-----LARTDE 902
Cdd:cd01384 366 SFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSY----------IEFVDNQDVLDLIEKkpggiIALLDE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 903 ArgllwlleeeALVPGATEDALLERLFSYYgpqeGDKKgqrpllRSSKP----HHFLLGHSHGTnwVEYNVSGWLSYTKQ 978
Cdd:cd01384 436 A----------CMFPRSTHETFAQKLYQTL----KDHK------RFSKPklsrTDFTIDHYAGD--VTYQTDLFLDKNKD 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 979 N--PATQNaprLLQDSQKKIISNLFlgraggttvlsgsiagleggSQLALRRATSMRKtFTtgmaavkkkSLCIQIKLQV 1056
Cdd:cd01384 494 YvvAEHQA---LLNASKCPFVAGLF--------------------PPLPREGTSSSSK-FS---------SIGSRFKQQL 540
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1057 DALIDTIKKSKLHFVHCFLPVAEgwageprsassrrvsssseldLPSGDHCEAGLLQldvpllraQLRGSRLLDAMRMYR 1136
Cdd:cd01384 541 QELMETLNTTEPHYIRCIKPNNL---------------------LKPGIFENANVLQ--------QLRCGGVLEAVRISC 591
|
730 740
....*....|....*....|....*.
gi 1239919865 1137 QGYPDHMVFSEFRRRFDVLAPHLTKK 1162
Cdd:cd01384 592 AGYPTRKPFEEFLDRFGLLAPEVLKG 617
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
440-1200 |
1.89e-66 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 239.62 E-value: 1.89e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLGS 519
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 520 SGSGKTTSCQHLVQYLATIAG---------TSGNKVFSVEKWQAlYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQV 590
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAigdrskkdqTPGKGTLEDQIIQA-NPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 591 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcadgTLRTELHLNHLAENNVFGIVPLAKPEEKQKA---AQQFSKLQT 667
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILS----NKKPELLDMLLITNNPYDYAFISQGETTVASiddAEELMATDN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 668 AMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAgrkqfarhEWAQKAAYLLGCSLEELSsaifkhqhKG 747
Cdd:cd14917 237 AFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGT--------EEADKSAYLMGLNSADLL--------KG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 748 CTLQRstsFRQGPEESSLGDGTGPKLTALECLegmASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGg 827
Cdd:cd14917 301 LCHPR---VKVGNEYVTKGQNVQQVIYATGAL---AKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 828 sargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLEPatdDSVAAVDQashqslvrslarTDEARGLL 907
Cdd:cd14917 374 -----SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGM---DLQACIDL------------IEKPMGIM 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 908 WLLEEEALVPGATEDALLERLFSYYGPQEGDKkgQRPLLRSSKPH-HFLLGHSHGTnwVEYNVSGWLSYTKqNPATQNAP 986
Cdd:cd14917 434 SILEEECMFPKATDMTFKAKLFDNHLGKSNNF--QKPRNIKGKPEaHFSLIHYAGT--VDYNIIGWLQKNK-DPLNETVV 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 987 RLLQDSQKKIISNLFLGRAGGTTVLSGSIAGLEGGSqlalrratsmrkTFTTgMAAVKKKSLciqiklqvDALIDTIKKS 1066
Cdd:cd14917 509 GLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGS------------SFQT-VSALHRENL--------NKLMTNLRST 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1067 KLHFVHCFLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFS 1146
Cdd:cd14917 568 HPHFVRCIIP--------------------NETKSPG---------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 618
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 1147 EFRRRFDVLAPHLTKKhGRnyiVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14917 619 DFRQRYRILNPAAIPE-GQ---FIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
440-1155 |
2.49e-63 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 230.77 E-value: 2.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLGS 519
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 520 SGSGKTTSCQHLVQYLATIAGTSGNKVFSVEKWQ----------ALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQ 589
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmqgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 590 VASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVF---GIVPLAKPEEKqkaaQQFSKLQ 666
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFvsqGEITVPSIDDQ----EELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 667 TAMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIfkhqhk 746
Cdd:cd14910 238 SAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKAAYLQNLNSADLLKAL------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 747 gCTlqrsTSFRQGPEESSLGDGTGPKLTALECLegmASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQG 826
Cdd:cd14910 304 -CY----PRVKVGNEYVTKGQTVQQVYNAVGAL---AKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 827 gsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLepatddsvaAVDQASHQSLVrslartDEARGL 906
Cdd:cd14910 376 ------SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDF---------GMDLAACIELI------EKPMGI 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 907 LWLLEEEALVPGATEDALLERLFSYYGPQEGDKKGQRPlLRSSKPHHFLLGHSHGTnwVEYNVSGWLSYTKqNPATQNAP 986
Cdd:cd14910 435 FSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKVEAHFSLIHYAGT--VDYNIAGWLDKNK-DPLNETVV 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 987 RLLQDSQKKIISNLFlgrAGGTTVLSGSIAGLEGGSQLAlrratsmrKTFTTGMAAVKKkslciqiklQVDALIDTIKKS 1066
Cdd:cd14910 511 GLYQKSSMKTLALLF---SGAAAAEAEEGGGKKGGKKKG--------SSFQTVSALFRE---------NLNKLMTNLRST 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1067 KLHFVHCFLPvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFS 1146
Cdd:cd14910 571 HPHFVRCIIP--------------------NETKTPGA---------MEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 621
|
....*....
gi 1239919865 1147 EFRRRFDVL 1155
Cdd:cd14910 622 DFKQRYKVL 630
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
439-1200 |
2.89e-63 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 230.30 E-value: 2.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGTS-----GNKVFSVEKWQAlYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASA 593
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGkqssdGKGSLEDQIIQA-NPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 594 SIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLnhlaennvfgiVPlaKPEEKQKAAQQFSKLQT------ 667
Cdd:cd14934 160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLL-----------VP--NPKEYHWVSQGVTVVDNmddgee 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 668 ------AMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIF 741
Cdd:cd14934 227 lqitdvAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTT--------EVADKVAHLMGLNSGELQKGIT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 742 KHQHKGCT--LQRSTSFRQGpeESSLGdgtgpkltalecleGMASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPG 819
Cdd:cd14934 299 RPRVKVGNefVQKGQNMEQC--NNSIG--------------ALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 820 FQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLEPatdDSVAAVDqashqslvrslaR 899
Cdd:cd14934 363 FEIFEFN------SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFGL---DLQACID------------L 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 900 TDEARGLLWLLEEEALVPGATEDALLERLF--------SYYGPQEGDKKGQRPllrsskphHFLLGHSHGTnwVEYNVSG 971
Cdd:cd14934 422 LEKPMGIFSILEEQCVFPKATDATFKAALYdnhlgkssNFLKPKGGKGKGPEA--------HFELVHYAGT--VGYNITG 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 972 WLSYTKqNPATQNAPRLLQDSQKKIISNLFLGRAGGttvlsgsiagleGGSQLALRRATSMrktfttgmaavkkkSLCIQ 1051
Cdd:cd14934 492 WLEKNK-DPLNETVVGLFQKSSLGLLALLFKEEEAP------------AGSKKQKRGSSFM--------------TVSNF 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1052 IKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssseldlpsGDHCEAGLlqLDVPLLRAQLRGSRLLDA 1131
Cdd:cd14934 545 YREQLNKLMTTLHSTAPHFVRCIVP---------------------------NEFKQSGV--VDAHLIMHQLACNGVLEG 595
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1132 MRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHgrnyiVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14934 596 IRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-----FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
440-1155 |
3.56e-63 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 230.00 E-value: 3.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLGS 519
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 520 SGSGKTTSCQHLVQYLATIA---------GTSGNKVFSVE-KWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQ 589
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAvtgekkkeeAASGKMQGTLEdQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 590 VASASIQTMLLEKLRVARRPASEATFNVFYYLLAcadgTLRTELHLNHLAENNVFGIVPLAKPEEKQKA---AQQFSKLQ 666
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMS----NKKPELIEMLLITTNPYDFAFVSQGEITVPSiddQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 667 TAMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIF----- 741
Cdd:cd14915 238 SAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKAAYLTSLNSADLLKALCyprvk 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 742 ---KHQHKGCTLQRSTsfrqgpeeSSLGdgtgpkltalecleGMASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTP 818
Cdd:cd14915 310 vgnEYVTKGQTVQQVY--------NSVG--------------ALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 819 GFQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLepatddsvaAVDQASHQSLVrsla 898
Cdd:cd14915 368 GFEIFDFN------SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDF---------GMDLAACIELI---- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 899 rtDEARGLLWLLEEEALVPGATEDALLERLFSYYGPQEGDKKGQRPlLRSSKPHHFLLGHSHGTnwVEYNVSGWLSYTKq 978
Cdd:cd14915 429 --EKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKAEAHFSLVHYAGT--VDYNIAGWLDKNK- 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 979 NPATQNAPRLLQDSQKKIISNLFLGraggttvlsGSIAGLEGGSqlalrratsmrktfttGMAAVKKKSLCIQ-----IK 1053
Cdd:cd14915 503 DPLNETVVGLYQKSGMKTLAFLFSG---------GQTAEAEGGG----------------GKKGGKKKGSSFQtvsalFR 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1054 LQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRAQLRGSRLLDAMR 1133
Cdd:cd14915 558 ENLNKLMTNLRSTHPHFVRCLIP--------------------NETKTPGA---------MEHELVLHQLRCNGVLEGIR 608
|
730 740
....*....|....*....|..
gi 1239919865 1134 MYRQGYPDHMVFSEFRRRFDVL 1155
Cdd:cd14915 609 ICRKGFPSRILYADFKQRYKVL 630
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
439-1076 |
1.40e-62 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 227.81 E-value: 1.40e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd01378 1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGTSGNKVFSVeKWQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQ 596
Cdd:cd01378 81 ESGAGKTEASKRIMQYIAAVSGGSESEVERV-KDMLLASnpLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 597 TMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHL------NHLAENNVF---GIvplakpeekqKAAQQFSKLQT 667
Cdd:cd01378 160 NYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLqrpeqyYYYSKSGCFdvdGI----------DDAADFKEVLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 668 AMKVLGISPDEQKACWLILAAIYHLGAAGATKeapeeqaeaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIfkhqhkg 747
Cdd:cd01378 230 AMKVIGFTEEEQDSIFRILAAILHLGNIQFAE---------DEEGNAAISDTSVLDFVAYLLGVDPDQLEKAL------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 748 ctLQRSTSFRQGPEESSLGDgtgpkLTALECLEG---MASGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGF--- 820
Cdd:cd01378 294 --THRTIETGGGGRSVYEVP-----LNVEQAAYArdaLAKAIYSRLFDWIVERINKSLAAKSGGKKKVIgVLDIYGFeif 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 821 -QNpeqggsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELA----FD-----DL-EpatddsvaavdqAS 889
Cdd:cd01378 367 eKN----------SFEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTpikyFNnkiicDLiE------------EK 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 890 HQSLVRSLartDEArgllwlleeEALVPGATEDALLERLfsyygpqegdkkgqrpLLRSSKPHHFLLGHSHGTNW----- 964
Cdd:cd01378 425 PPGIFAIL---DDA---------CLTAGDATDQTFLQKL----------------NQLFSNHPHFECPSGHFELRrgefr 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 965 -------VEYNVSGwlsYTKQNPAT--QNAPRLLQDSQKKIISNLFlgraggttvlsgsiagLEGGSQLALRRATsmrkt 1035
Cdd:cd01378 477 ikhyagdVTYNVEG---FLDKNKDLlfKDLKELMQSSSNPFLRSLF----------------PEGVDLDSKKRPP----- 532
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1239919865 1036 fTTGMaavkkkslciQIKLQVDALIDTIKKSKLHFVHCFLP 1076
Cdd:cd01378 533 -TAGT----------KFKNSANALVETLMKKQPSYIRCIKP 562
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
440-1155 |
1.46e-62 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 228.42 E-value: 1.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLGS 519
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 520 SGSGKTTSCQHLVQYLATIAgTSGNKVFSVE--KWQALYS--------LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQ 589
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIA-VTGDKKKEQQpgKMQGTLEdqiiqanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 590 VASASIQTMLLEKLRVARRPASEATFNVFYYLLAcadgTLRTELHLNHLAENNVFGIvPLAKPEEKQKA----AQQFSKL 665
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMS----NKKPELIDLLLISTNPFDF-PFVSQGEVTVAsiddSEELLAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 666 QTAMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAgrkqfarhEWAQKAAYLLGCSLEELSsaifkhqh 745
Cdd:cd14923 236 DNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKAGYLMGLNSAEML-------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 746 KGCTLQRstsFRQGPEESSLGDGTGPKLTALECLegmASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQ 825
Cdd:cd14923 300 KGLCCPR---VKVGNEYVTKGQNVQQVTNSVGAL---AKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 826 GgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLepatddsvaAVDQASHQSLVrslartDEARG 905
Cdd:cd14923 374 N------SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDF---------GMDLAACIELI------EKPMG 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 906 LLWLLEEEALVPGATEDALLERLFSYYGPQEGDKKGQRPlLRSSKPHHFLLGHSHGTnwVEYNVSGWLSYTKqNPATQNA 985
Cdd:cd14923 433 IFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKP-AKGKAEAHFSLVHYAGT--VDYNIAGWLDKNK-DPLNETV 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 986 PRLLQDSQKKIISNLFLGRAGGTtvlsgsiAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTIKK 1065
Cdd:cd14923 509 VGLYQKSSLKLLSFLFSNYAGAE-------AGDSGGSKKGGKKKGSSFQT----VSAVFRENL--------NKLMTNLRS 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1066 SKLHFVHCFLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVF 1145
Cdd:cd14923 570 THPHFVRCLIP--------------------NETKTPG---------VMDHYLVMHQLRCNGVLEGIRICRKGFPSRILY 620
|
730
....*....|
gi 1239919865 1146 SEFRRRFDVL 1155
Cdd:cd14923 621 ADFKQRYRIL 630
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
439-879 |
5.06e-62 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 226.58 E-value: 5.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMS----RQDQS 513
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPyKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSgvldPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 514 VILLGSSGSGKTTSCQHLVQYLATIagTSGNKVFSVEKWQALYS------------------LLEAFGNSPTIMNGNATR 575
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARI--TSGFAQGASGEGEAASEaieqtlgsledrvlssnpLLESFGNAKTLRNDNSSR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 576 FSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLnhlaENNVFGIVPLAK--PE 653
Cdd:cd14890 159 FGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKL----QTPVEYFYLRGEcsSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 654 EKQKAAQQFSKLQTAMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAeagrkqfARHEWAQKAAYLLGCSL 733
Cdd:cd14890 235 PSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDA-------TTLQSLKLAAELLGVNE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 734 EELSSAIfkhqhkgCTLQ---RSTSFRQgPEESSLgdgtgpkltALECLEGMASGLYSELFTLLVSLVNRALKSSQHSLC 810
Cdd:cd14890 308 DALEKAL-------LTRQlfvGGKTIVQ-PQNVEQ---------ARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWG 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239919865 811 SMMIVDTPGFQNPEQGGsargasFEELCHNYAQDRLQRLFHERTFVQELERYKEENIE---LAFDDLEPATD 879
Cdd:cd14890 371 FIGVLDIYGFEKFEWNT------FEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDwqyITFNDNQACLE 436
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
441-1155 |
1.69e-61 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 225.00 E-value: 1.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 441 VLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLGSS 520
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 521 GSGKTTSCQHLVQYLATIAGTSGNKVFSVEKWQALYS--------LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVAS 592
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 593 ASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVF---GIVPLAKPEEKqkaaQQFSKLQTAM 669
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFvsqGEITVPSIDDQ----EELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 670 KVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIfkhqhkgCT 749
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKAAYLQSLNSADLLKAL-------CY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 750 lqrsTSFRQGPEESSLGDGTGPKLTALECLegmASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsa 829
Cdd:cd14918 304 ----PRVKVGNEYVTKGQTVQQVYNAVGAL---AKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN--- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 830 rgaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLepatddsvaAVDQASHQSLVrslartDEARGLLWL 909
Cdd:cd14918 374 ---SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF---------GMDLAACIELI------EKPLGIFSI 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 910 LEEEALVPGATEDALLERLFSYYGPQEGDKkgQRP-LLRSSKPHHFLLGHSHGTnwVEYNVSGWLSYTKqNPATQNAPRL 988
Cdd:cd14918 436 LEEECMFPKATDTSFKNKLYDQHLGKSANF--QKPkVVKGKAEAHFSLIHYAGT--VDYNITGWLDKNK-DPLNDTVVGL 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 989 LQDSQKKIISNLFlgraggttvlsGSIAGLEGGSQlALRRATSMRKTFTTGMAAVKKkslciqiklQVDALIDTIKKSKL 1068
Cdd:cd14918 511 YQKSAMKTLASLF-----------STYASAEADSG-AKKGAKKKGSSFQTVSALFRE---------NLNKLMTNLRSTHP 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1069 HFVHCFLPvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 1148
Cdd:cd14918 570 HFVRCIIP--------------------NETKTPGA---------MEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDF 620
|
....*..
gi 1239919865 1149 RRRFDVL 1155
Cdd:cd14918 621 KQRYKVL 627
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
440-1200 |
1.78e-61 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 224.94 E-value: 1.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLGS 519
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 520 SGSGKTTSCQHLVQYLATIAG---------TSGNKVFSVEKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQV 590
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAigdrskkenPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 591 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcadgTLRTELHLNHLAENNVFGIVPLAKPEEKQKA---AQQFSKLQT 667
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILS----NKKPELLDMLLVTNNPYDYAFVSQGEVSVASiddSEELLATDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 668 AMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAgrkqfarhEWAQKAAYLLGCSLEELSsaifkhqhKG 747
Cdd:cd14916 238 AFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGT--------EDADKSAYLMGLNSADLL--------KG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 748 CTLQRstsFRQGPEESSLGDGTGPKLTALECLegmASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGg 827
Cdd:cd14916 302 LCHPR---VKVGNEYVTKGQSVQQVYYSIGAL---AKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 828 sargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLEPatdDSVAAVDQashqslvrslarTDEARGLL 907
Cdd:cd14916 375 -----SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGM---DLQACIDL------------IEKPMGIM 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 908 WLLEEEALVPGATEDALLERLFSYYGPQEGDKKGQRPlLRSSKPHHFLLGHSHGTnwVEYNVSGWLSYTKqNPATQNAPR 987
Cdd:cd14916 435 SILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRN-VKGKQEAHFSLVHYAGT--VDYNILGWLEKNK-DPLNETVVG 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 988 LLQDSQKKIISNLFLGRAGGTTvlsgsiaGLEGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKKSK 1067
Cdd:cd14916 511 LYQKSSLKLMATLFSTYASADT-------GDSGKGKGGKKKGSSFQT-----VSALHRENL--------NKLMTNLKTTH 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1068 LHFVHCFLPvaegwageprsassrrvsssseldlpsGDHCEAGLlqLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSE 1147
Cdd:cd14916 571 PHFVRCIIP---------------------------NERKAPGV--MDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGD 621
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1239919865 1148 FRRRFDVLAPhLTKKHGRnyiVMDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14916 622 FRQRYRILNP-AAIPEGQ---FIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
440-1155 |
1.32e-60 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 222.69 E-value: 1.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLGS 519
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 520 SGSGKTTSCQHLVQYLATIAGTSGNKVFSVEKWQ----------ALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQ 589
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKmqgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 590 VASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVF---GIVPLAKPEEKqkaaQQFSKLQ 666
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFvsqGEISVASIDDQ----EELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 667 TAMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQHK 746
Cdd:cd14912 238 SAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGT--------EVADKAAYLQSLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 747 gctlQRSTSFRQGPEESSLGDGTGpkltalecleGMASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQG 826
Cdd:cd14912 310 ----VGNEYVTKGQTVEQVTNAVG----------ALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 827 gsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLepatddsvaAVDQASHQSLVrslartDEARGL 906
Cdd:cd14912 376 ------SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF---------GMDLAACIELI------EKPMGI 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 907 LWLLEEEALVPGATEDALLERLFSYYGPQEGDKkgQRP-LLRSSKPHHFLLGHSHGTnwVEYNVSGWLSYTKqNPATQNA 985
Cdd:cd14912 435 FSILEEECMFPKATDTSFKNKLYEQHLGKSANF--QKPkVVKGKAEAHFSLIHYAGV--VDYNITGWLDKNK-DPLNETV 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 986 PRLLQDSQKKIISNLFlgraGGTTVLSGSIAGleGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTIKK 1065
Cdd:cd14912 510 VGLYQKSAMKTLAYLF----SGAQTAEGASAG--GGAKKGGKKKGSSFQT----VSALFRENL--------NKLMTNLRS 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1066 SKLHFVHCFLPvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVF 1145
Cdd:cd14912 572 THPHFVRCIIP--------------------NETKTPGA---------MEHELVLHQLRCNGVLEGIRICRKGFPSRILY 622
|
730
....*....|
gi 1239919865 1146 SEFRRRFDVL 1155
Cdd:cd14912 623 ADFKQRYKVL 632
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
440-873 |
8.20e-60 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 218.95 E-value: 8.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYG-ASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGTSGNKVfSVEKwQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQ 596
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET-QVEE-KVLASnpIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 597 TMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHlAENNVFGIVPLAKPEEKQKAAQQFSKLQTAMKVLGISP 676
Cdd:cd01380 160 TYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGS-AEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 677 DEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEagrkqfarHEWAQKAAYLLGCSLEELSSAIFKHQ--------HKGC 748
Cdd:cd01380 239 EEQMEIFRILAAILHLGNVEIKATRNDSASISPD--------DEHLQIACELLGIDESQLAKWLCKRKivtrseviVKPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 749 TLQRSTSFRqgpeesslgdgtgpkltaleclEGMASGLYSELFTLLVSLVNRALKSSQ-HSLCSMM-IVDTPGFQNPEQG 826
Cdd:cd01380 311 TLQQAIVAR----------------------DALAKHIYAQLFDWIVDRINKALASPVkEKQHSFIgVLDIYGFETFEVN 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1239919865 827 gsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDD 873
Cdd:cd01380 369 ------SFEQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFID 409
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
439-1157 |
1.19e-59 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 219.05 E-value: 1.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGtsgnKVFSVEKwQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQ 596
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISG----QHSWIEQ-QILEAnpILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 597 TMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNH------LAENNVFGIvplakpeEKQKAAQQFSKLQTAMK 670
Cdd:cd01381 156 QYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDasdyyyLTQGNCLTC-------EGRDDAAEFADIRSAMK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 671 VLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAGRKQFARhewaqkAAYLLGCSLEELSSAifkhqhkgctL 750
Cdd:cd01381 229 VLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDNLDASEVRDPPNLER------AAKLLEVPKQDLVDA----------L 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 751 QRSTSFRQGPEESSlgdgTGPKLTALECLEGMASGLYSELFTLLVSLVNRAL---KSSQHSLCSMMIVDTPGFQNPEQGg 827
Cdd:cd01381 293 TTRTIFTRGETVVS----PLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFGFENFEVN- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 828 sargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIE---LAFDDLEPATDdsVAAVDQASHQSLVrslartDEar 904
Cdd:cd01381 368 -----SFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINwqhIEFVDNQDVLD--LIALKPMNIMSLI------DE-- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 905 gllwlleeEALVPGATEDALLERLFSYYGpqegdKKGQRPLLRSSKPHHFLLGHSHGTnwVEYNVSGWLSytKQNPA-TQ 983
Cdd:cd01381 433 --------ESKFPKGTDQTMLEKLHSTHG-----NNKNYLKPKSDLNTSFGINHFAGV--VFYDTRGFLE--KNRDTfSA 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 984 NAPRLLQDSQKKIISNLFlgraggttvlsgsiagleggsQLALRRATSMRKtfttgmaavKKKSLCIQIKLQVDALIDTI 1063
Cdd:cd01381 496 DLLQLVQSSKNKFLKQLF---------------------NEDISMGSETRK---------KSPTLSSQFRKSLDQLMKTL 545
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1064 KKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPsgdhceaglLQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHM 1143
Cdd:cd01381 546 SACQPFFVRCIKP--------------------NEYKKP---------MLFDRELCVRQLRYSGMMETIRIRKAGYPIRH 596
|
730
....*....|....
gi 1239919865 1144 VFSEFRRRFDVLAP 1157
Cdd:cd01381 597 TFEEFVERYRVLVP 610
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
439-1200 |
2.50e-59 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 218.49 E-value: 2.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILL 517
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPyQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 518 GSSGSGKTTSCQHLVQYLATIAGtsGNKVFSVEKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQT 597
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--GLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 598 MLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAennVFGIVPLAKPEEKQKAAQQFSKLQTAMKVLGISPD 677
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANEC---AYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 678 EQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAGRkqfarhEWAQKAAYLLGCSLEELSSAIFKHQHKGCTLQRSTSFR 757
Cdd:cd14903 236 KQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGD------QGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 758 qgpeesslgdgtgpKLTALECLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEEL 837
Cdd:cd14903 310 --------------KDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHN------SFEQF 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 838 CHNYAQDRLQRLFHERTFVQELERYKEENIELAFddlepatddsvaaVDQASHQSLvrsLARTDEARGLLWLLEEEALVP 917
Cdd:cd14903 370 CINYANEKLQQKFTQDVFKTVQIEYEEEGIRWAH-------------IDFADNQDV---LAVIEDRLGIISLLNDEVMRP 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 918 GATEDALLERLFSYYgpqegdkKGQRPLL---RSSKPhHFLLGHSHGTnwVEYNVSGWLSYTKQNpatqnaprLLQD--- 991
Cdd:cd14903 434 KGNEESFVSKLSSIH-------KDEQDVIefpRTSRT-QFTIKHYAGP--VTYESLGFLEKHKDA--------LLPDlsd 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 992 ----SQKKIISNLFlgraggttvlsGSIAGLEGGSQLALRRATSMRKTFTTGMAAVKkkslcIQIKLQVDALIDTIKKSK 1067
Cdd:cd14903 496 lmrgSSKPFLRMLF-----------KEKVESPAAASTSLARGARRRRGGALTTTTVG-----TQFKDSLNELMTTIRSTN 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1068 LHFVHCFLPVAEGWAGEprsassrrvsssseldlpsgdhceagllqLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSE 1147
Cdd:cd14903 560 VHYVRCIKPNSIKSPTE-----------------------------LDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEE 610
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 1148 FRRRFDVLAPhltkKHGRNYIVMDER-RAVEELLESLDLEKSSccMGLSRVFFR 1200
Cdd:cd14903 611 FLDKFWLFLP----EGRNTDVPVAERcEALMKKLKLESPEQYQ--MGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
440-879 |
1.12e-58 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 215.99 E-value: 1.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLGS 519
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 520 SGSGKTTSCQHLVQYLaTIAGTSGNKVFSvEKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQTML 599
Cdd:cd01379 82 SGAGKTESANLLVQQL-TVLGKANNRTLE-EKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 600 LEKLRVARRPASEATFNVFYYLLA-------CADGTLRTELHLNHLAENNvfgiVPLAKPEEKQKAAQQFSKLQTAMKVL 672
Cdd:cd01379 160 LEKSRVVHQAIGERNFHIFYYIYAglaedkkLAKYKLPENKPPRYLQNDG----LTVQDIVNNSGNREKFEEIEQCFKVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 673 GISPDEQKACWLILAAIYHLG----AAGATKEAPEEqaeaaeagRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQ--HK 746
Cdd:cd01379 236 GFTKEEVDSVYSILAAILHIGdiefTEVESNHQTDK--------SSRISNPEALNNVAKLLGIEADELQEALTSHSvvTR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 747 GCTLQRSTSFRQgpeesslgdgtgpkltALECLEGMASGLYSELFTLLVSLVNRALKSSQHS---LCSMMIVDTPGFQNP 823
Cdd:cd01379 308 GETIIRNNTVEE----------------ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAsdePLSIGILDIFGFENF 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 824 EQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIEL---AFDDLEPATD 879
Cdd:cd01379 372 QKN------SFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVdliEYEDNRPLLD 424
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
440-1002 |
1.29e-58 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 215.71 E-value: 1.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGTSGNkvFSVEKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQTM 598
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLSPSDDS--DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 599 LLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNH----------LAENNVFGIVplakpEEKQKAAQQFSKLQTA 668
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDpdchrilrddNRNRPVFNDS-----EELEYYRQMFHDLTNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 669 MKVLGISPDEQKACWLILAAIYHLG---------AAGATkeapeeqaeaaeagrkqFARHEWAQKAAYLLGCSLEELSSA 739
Cdd:cd14897 235 MKLIGFSEEDISVIFTILAAILHLTnivfipdedTDGVT-----------------VADEYPLHAVAKLLGIDEVELTEA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 740 IF--KHQHKGCTLQRSTSFRQgpeesslgdgtgpkltALECLEGMASGLYSELFTLLVSLVNRALKSSQ-----HSLCSM 812
Cdd:cd14897 298 LIsnVNTIRGERIQSWKSLRQ----------------ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKdfqimTRGPSI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 813 MIVDTPGFQNPEQGGsargasFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAfdDLEPATDDSVAAVDQASHQS 892
Cdd:cd14897 362 GILDMSGFENFKINS------FDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR--DIEYHDNDDVLELFFKKPLG 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 893 LvrsLARTDEargllwlleeEALVPGATEDALLERLFSYYGPQegdkkgqrPLLRSSKPHHFLLGHSHGTNWVEYNVSGW 972
Cdd:cd14897 434 I---LPLLDE----------ESTFPQSTDSSLVQKLNKYCGES--------PRYVASPGNRVAFGIRHYAEQVTYDADGF 492
|
570 580 590
....*....|....*....|....*....|
gi 1239919865 973 LSYTKQNpATQNAPRLLQDSQKKIISNLFL 1002
Cdd:cd14897 493 LEKNRDN-LSSDIVGCLLNSNNEFISDLFT 521
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
439-1156 |
5.52e-56 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 208.10 E-value: 5.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGTS-GNKVFSVEKwqaLYSLLEAFGNSPTIMNGNATRFSQILSLDFdQAGQVASASIQT 597
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQtEDRLRQPED---VLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVSH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 598 MLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHlAEN----NVFGIVPLAKPEEkqkaAQQFSKLQTAMKVLG 673
Cdd:cd14896 157 YLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQG-PETyyylNQGGACRLQGKED----AQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 674 ISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAaeagrkqfARHEWA--QKAAYLLGCSLEELSSAIFKhqhkgctlq 751
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQEVA--------AVSSWAeiHTAARLLQVPPERLEGAVTH--------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 752 RSTSFRQGPEESSLgdgtgPKLTALECLEGMASGLYSELFTLLVSLVNRAL--KSSQHSLCSMMIVDTPGFQnpeqggSA 829
Cdd:cd14896 295 RVTETPYGRVSRPL-----PVEGAIDARDALAKTLYSRLFTWLLKRINAWLapPGEAESDATIGVVDAYGFE------AL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 830 RGASFEELCHNYAQDRLQRLFHERTFVQELERYKEENIelafddlepatddSVAAVDQASHQSLVRSLArtDEARGLLWL 909
Cdd:cd14896 364 RVNGLEQLCINLASERLQLFSSQTLLAQEEEECQRELL-------------PWVPIPQPPRESCLDLLV--DQPHSLLSI 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 910 LEEEALVPGATEDALLERLFSYYGPQEGDKKGQRPLlrsskPhHFLLGHSHGTnwVEYNVSGWLSYTKQ--NPATQNapr 987
Cdd:cd14896 429 LDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPL-----P-VFTVRHYAGT--VTYQVHKFLNRNRDqlDPAVVE--- 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 988 LLQDSQKKIISNLFlgraggttvlsgsiagLEGGSQLALRRatsmrktfttgmaavKKKSLCIQIKLQVDALIDTIKKSK 1067
Cdd:cd14896 498 MLAQSQLQLVGSLF----------------QEAEPQYGLGQ---------------GKPTLASRFQQSLGDLTARLGRSH 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1068 LHFVHCFLPvaegwagEPRSassrrvsssseldLPsgdhceaGLlqLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSE 1147
Cdd:cd14896 547 VYFIHCLNP-------NPGK-------------LP-------GL--FDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQA 597
|
....*....
gi 1239919865 1148 FRRRFDVLA 1156
Cdd:cd14896 598 FLARFGALG 606
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
436-885 |
1.96e-55 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 206.63 E-value: 1.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 436 LNESSVLHTLRQRYGASLLHTYAGPS-LLVLSPRGAPAVYSEKVMHMFK-------GCRREDMAPHIYAVAQTAYRAMLM 507
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 508 SRQDQSVILLGSSGSGKTTSCQHLVQYLATIAGTS--GNKVfsVEKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFD 585
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSkkGTKL--SSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 586 QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVF---GIVPL-AKPEEKQkaAQQ 661
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasyGCHPLpLGPGSDD--AEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 662 FSKLQTAMKVLGISPDEQKACWLILAAIYHLgaagatkeapeeqaeaaeaGRKQFA-----RHEWA--------QKAAYL 728
Cdd:cd14879 237 FQELKTALKTLGFKRKHVAQICQLLAAILHL-------------------GNLEFTydhegGEESAvvkntdvlDIVAAF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 729 LGCSLEELSSAI---FKHQHKgctlQRSTSFRQgPEESSLG-DgtgpkltaleCLegmASGLYSELFTLLVSLVNRALKS 804
Cdd:cd14879 298 LGVSPEDLETSLtykTKLVRK----ELCTVFLD-PEGAAAQrD----------EL---ARTLYSLLFAWVVETINQKLCA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 805 SQHSLCSMM-IVDTPGFQNpeQGGSArGASFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAfddlEPATDDSVA 883
Cdd:cd14879 360 PEDDFATFIsLLDFPGFQN--RSSTG-GNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVP----ATSYFDNSD 432
|
..
gi 1239919865 884 AV 885
Cdd:cd14879 433 CV 434
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
440-1162 |
2.11e-55 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 207.82 E-value: 2.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMFK--------GCRREDMAPHIYAVAQTAYRAMLMS-R 509
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPlKPLPDLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPeR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 510 QDQSVILLGSSGSGKTTSCQHLVQYLATI-----AGTSGNKVFSVEKWQALYS--LLEAFGNSPTIMNGNATRFSQILSL 582
Cdd:cd14902 82 RNQSILVSGESGSGKTESTKFLMQFLTSVgrdqsSTEQEGSDAVEIGKRILQTnpILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 583 DFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAE---NNVFGIVPLAKPEEKQKAA 659
Cdd:cd14902 162 QFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKyelLNSYGPSFARKRAVADKYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 660 QQFSKLQTAMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAgrkqfARHEWAQKAAYLLGCSLEELSsa 739
Cdd:cd14902 242 QLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTA-----ASRFHLAKCAELMGVDVDKLE-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 740 ifkhqhkgcTLQRSTSFRQGPEESSLgdgtgpKLT---ALECLEGMASGLYSELFTLLVSLVN---------RALKSSQH 807
Cdd:cd14902 315 ---------TLLSSREIKAGVEVMVL------KLTpeqAKEICGSLAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 808 SLCSMMIVDTPGFQNPEQGGsargasFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFddlepatddsVAAVDQ 887
Cdd:cd14902 380 ELATIGILDIFGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKN----------ISYPSN 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 888 ASHQSLVrslarTDEARGLLWLLEEEALVPGATEDALLERLFSYYGPQEgdkkgqrpllrsskphHFLLGHSHGTnwVEY 967
Cdd:cd14902 444 AACLALF-----DDKSNGLFSLLDQECLMPKGSNQALSTKFYRYHGGLG----------------QFVVHHFAGR--VCY 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 968 NVSGWLSyTKQNPATQNAPRLLQDSQKKIISNLFL-GRAGGTTVLSGSiagleggsqlALRRATSMrktfttgmaaVKKK 1046
Cdd:cd14902 501 NVEQFVE-KNTDALPADASDILSSSSNEVVVAIGAdENRDSPGADNGA----------AGRRRYSM----------LRAP 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1047 SLCIQIKLQVDALIDTIKKSKLHFVHCFLPvaeGWAGEPRSassrrvsssseldlpsgdhceagllqLDVPLLRAQLRGS 1126
Cdd:cd14902 560 SVSAQFKSQLDRLIVQIGRTEAHYVRCLKP---NEVKKPGI--------------------------FDRERMVEQMRSV 610
|
730 740 750
....*....|....*....|....*....|....*.
gi 1239919865 1127 RLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKK 1162
Cdd:cd14902 611 GVLEAVRIARHGYSVRLAHASFIELFSGFKCFLSTR 646
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
440-1160 |
2.33e-55 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 206.18 E-value: 2.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPyQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGTS-----GNKVFSVEKWQALYS-LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVAS 592
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSlelslKEKTSCVEQAILESSpIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 593 ASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNhLAEN----NVFGIVPLAKPEEKqkaaQQFSKLQTA 668
Cdd:cd14873 162 GRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENyhylNQSGCVEDKTISDQ----ESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 669 MKVLGISPDEQKACWLILAAIYHLG------AAGAtkeapeeqaeaaeagrkQFARHEWAQKAAYLLGCSLEELSSAIfk 742
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGniefitAGGA-----------------QVSFKTALGRSAELLGLDPTQLTDAL-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 743 hqhkgctLQRSTSFRqGPEESSlgdgtgpKLT---ALECLEGMASGLYSELFTLLVSLVNRALKSSQHsLCSMMIVDTPG 819
Cdd:cd14873 298 -------TQRSMFLR-GEEILT-------PLNvqqAVDSRDSLAMALYARCFEWVIKKINSRIKGKED-FKSIGILDIFG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 820 FQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIElaFDDLEpatddsvaAVDQASHQSLVRS--- 896
Cdd:cd14873 362 FENFEVN------HFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLV--WEDID--------WIDNGECLDLIEKklg 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 897 -LARTDEargllwlleeEALVPGATEDALLERLFSYYGPQEGDKKgqrPLLRSskpHHFLLGHSHGTnwVEYNVSGWLsy 975
Cdd:cd14873 426 lLALINE----------ESHFPQATDSTLLEKLHSQHANNHFYVK---PRVAV---NNFGVKHYAGE--VQYDVRGIL-- 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 976 tKQNPAT--QNAPRLLQDSQKKIISNLF---LGRAGGTTvlsgsiagLEGGSQLalrratsmrktfttgmaavKKKSLCI 1050
Cdd:cd14873 486 -EKNRDTfrDDLLNLLRESRFDFIYDLFehvSSRNNQDT--------LKCGSKH-------------------RRPTVSS 537
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1051 QIKLQVDALIDTIKKSKLHFVHCFLPVAEgwageprsassrrvsssselDLPSgdhceagllQLDVPLLRAQLRGSRLLD 1130
Cdd:cd14873 538 QFKDSLHSLMATLSSSNPFFVRCIKPNMQ--------------------KMPD---------QFDQAVVLNQLRYSGMLE 588
|
730 740 750
....*....|....*....|....*....|
gi 1239919865 1131 AMRMYRQGYPDHMVFSEFRRRFDVLAPHLT 1160
Cdd:cd14873 589 TVRIRKAGYAVRRPFQDFYKRYKVLMRNLA 618
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
440-1164 |
1.51e-54 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 203.87 E-value: 1.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSE--KVMHMFKGCRRED----MAPHIYAVAQTAYRAMLMSR---- 509
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDetKEAYYEHGERRAAgerkLPPHVYAVADKAFRAMLFASrgqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 510 QDQSVILLGSSGSGKTTSCQHLVQYLATIAGTSGNKVFSVEKW----QALYS--LLEAFGNSPTIMNGNATRFSQILSLD 583
Cdd:cd14901 82 CDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATEREnvrdRVLESnpILEAFGNARTNRNNNSSRFGKFIRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 584 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFS 663
Cdd:cd14901 162 FASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 664 KLQTAMKVLGISPDEQKACWLILAAIYHLGAAGATKeapeeqaEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIfkh 743
Cdd:cd14901 242 KTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVK-------KDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTL--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 744 qhkgCTlqrsTSFRQGPE--ESSLgdgtgPKLTALECLEGMASGLYSELFTLLVSLVNRALK--SSQHSLCSMMIVDTPG 819
Cdd:cd14901 312 ----CT----REIRAGGEyiTMPL-----SVEQALLTRDVVAKTLYAQLFDWLVDRINESIAysESTGASRFIGIVDIFG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 820 FQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFddLEPATDDSVAAVDQASHQSLVRSLar 899
Cdd:cd14901 379 FEIFATN------SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTF--VEYPNNDACVAMFEARPTGLFSLL-- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 900 tDEargllwlleeEALVPGATEDALLErlfSYYgpqegDKKGQRPLLRSSKPHH----FLLGHSHGTnwVEYNVSGWLSY 975
Cdd:cd14901 449 -DE----------QCLLPRGNDEKLAN---KYY-----DLLAKHASFSVSKLQQgkrqFVIHHYAGA--VCYATDGFCDK 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 976 TKQNPATqNAPRLLQDSqkkiiSNLFLgragGTTVLSgsiagleggsqlalrratsmrktfttgmaavkkkslciQIKLQ 1055
Cdd:cd14901 508 NKDHVHS-EALALLRTS-----SNAFL----SSTVVA--------------------------------------KFKVQ 539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1056 VDALIDTIKKSKLHFVHCFLPVaegwageprsassrrvsssselDLPSGDhceagllQLDVPLLRAQLRGSRLLDAMRMY 1135
Cdd:cd14901 540 LSSLLEVLNATEPHFIRCIKPN----------------------DVLSPS-------EFDAKRVLEQLRCSGVLEAVKIS 590
|
730 740
....*....|....*....|....*....
gi 1239919865 1136 RQGYPDHMVFSEFRRRFDVLAPHLTKKHG 1164
Cdd:cd14901 591 RSGYPVRFPHDAFVHTYSCLAPDGASDTW 619
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
440-1200 |
5.21e-54 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 202.31 E-value: 5.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVM--HMFKGCRRedMAPHIYAVAQTAYRAMLMSRQDQSVILL 517
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMdqYMHKGPKE--MPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 518 GSSGSGKTTSCQHLVQYLATIAGTSGNkvfsVEKWQALYS-LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQ 596
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTNG----VEQRVLLANpILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 597 TMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNhlaenNVFGIVPLAKPEEKQKA--AQQFSKLQTAMKVLGI 674
Cdd:cd14872 156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSS-----AAYGYLSLSGCIEVEGVddVADFEEVVLAMEQLGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 675 SPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAGRKqfarhEWAQKAAYLLGCSLEELSSAIfkhqhkgctLQRST 754
Cdd:cd14872 231 DDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANR-----DVLKEVATLLGVDAATLEEAL---------TSRLM 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 755 SFRQGpeesslgDGTGPKLTALECLEG---MASGLYSELFTLLVSLVNRALKSSQHSL-CSMMIVDTPGFQNPEQGgsar 830
Cdd:cd14872 297 EIKGC-------DPTRIPLTPAQATDAcdaLAKAAYSRLFDWLVKKINESMRPQKGAKtTFIGVLDIFGFEIFEKN---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 831 gaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIE---LAFDDLEPATDdsvaavdqashqsLVRSlaRTDearGLL 907
Cdd:cd14872 366 --SFEQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKfehIDFIDNQPVLD-------------LIEK--KQP---GLM 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 908 WLLEEEALVPGATEDALLERLfsyyGPQEGDKKGQRPLLRSSKPHHFLLGHSHGTnwVEYNVSGWLSYTKqNPATQNAPR 987
Cdd:cd14872 426 LALDDQVKIPKGSDATFMIAA----NQTHAAKSTFVYAEVRTSRTEFIVKHYAGD--VTYDITGFLEKNK-DTLQKDLYV 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 988 LLQDSQKKIISNLFlgraggttvlsgsiagleggSQLALRRATSmrktfttgmaavkKKSLCIQIKLQVDALIDTIKKSK 1067
Cdd:cd14872 499 LLSSSKNKLIAVLF--------------------PPSEGDQKTS-------------KVTLGGQFRKQLSALMTALNATE 545
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1068 LHFVHCFLPVAEGWAgeprsassrrvsssselDLPSGDHCeaglLQldvpllraQLRGSRLLDAMRMYRQGYPDHMVFSE 1147
Cdd:cd14872 546 PHYIRCVKPNQEKRA-----------------RLFDGFMS----LE--------QLRYAGVFEAVKIRKTGYPFRYSHER 596
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1239919865 1148 FRRRFDVLAPHLTKKHGRnyivmDERRAVEELLESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd14872 597 FLKRYRFLVKTIAKRVGP-----DDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
440-1157 |
1.18e-53 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 201.32 E-value: 1.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPyKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGtsGNKVFSVEKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQTM 598
Cdd:cd14904 82 ESGAGKTETTKIVMNHLASVAG--GRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 599 LLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQTAMKVLGISPDE 678
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 679 QKACWLILAAIYHLGAAGATKEAPEEQAEAAEAGRKQFARhewaqkaayLLGCSLEELSSAIfkhqhkgCTlqRSTSFRQ 758
Cdd:cd14904 240 QRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQVAK---------MLGLPTTRIEEAL-------CN--RSVVTRN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 759 GPEESSLGdgtgpKLTALECLEGMASGLYSELFTLLVSLVNRALkSSQHSLCSMMI--VDTPGFQNPEQGGsargasFEE 836
Cdd:cd14904 302 ESVTVPLA-----PVEAEENRDALAKAIYSKLFDWMVVKINAAI-STDDDRIKGQIgvLDIFGFEDFAHNG------FEQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 837 LCHNYAQDRLQRLFHERTFVQELERYKEENieLAFDDLEpaTDDSVAAVDQASHQSLVRSLArTDEARGllwlleeealv 916
Cdd:cd14904 370 FCINYANEKLQQKFTTDVFKTVEEEYIREG--LQWDHIE--YQDNQGIVEVIDGKMGIIALM-NDHLRQ----------- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 917 PGATEDALLERLFSYYGPQEGDKKGQRPLLRSSKphhFLLGHSHGTnwVEYNVSGWLSytKQNPATQN-APRLLQDSQKK 995
Cdd:cd14904 434 PRGTEEALVNKIRTNHQTKKDNESIDFPKVKRTQ---FIINHYAGP--VTYETVGFME--KHRDTLQNdLLDLVLLSSLD 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 996 IISNLFlgraggttvlsgsiagleggSQLALRRATSMRKtftTGMAAVKKKSLCIQIKLQVDALIDTIKKSKLHFVHCFL 1075
Cdd:cd14904 507 LLTELF--------------------GSSEAPSETKEGK---SGKGTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVRCIK 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1076 PVAEGWAGEprsassrrvsssseldlpsgdhceagllqLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1155
Cdd:cd14904 564 PNANKSPTE-----------------------------FDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM 614
|
..
gi 1239919865 1156 AP 1157
Cdd:cd14904 615 FP 616
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
440-1157 |
1.55e-53 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 201.07 E-value: 1.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVM--HMFKGcrrEDMAPHIYAVAQTAYRAMLMSRQDQSVIL 516
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPfKTIPGLYSDEMLlkFIQPS---ISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 517 LGSSGSGKTTSCQHLVQYLATiAGTSGNKVFSVEKWQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQ-------- 586
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLAC-AGSEDIKKRSLVEAQVLESnpLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 587 -AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVFGIV--PLAKPEEKQKAAQQFS 663
Cdd:cd14888 158 dRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADakPISIDMSSFEPHLKFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 664 KLQ--------------------TAMKVLGISPDEQKACWLILAAIYHLGaagatkEAPEEQAEAAEAGRKQFA-RHEWA 722
Cdd:cd14888 238 YLTksschelpdvddleefestlYAMQTVGISPEEQNQIFSIVAAILYLG------NILFENNEACSEGAVVSAsCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 723 QKAAYLLGCSLEELssaifkhqhKGCTLQRSTSFRqgpEESSlgdgTGPKLT--ALECLEGMASGLYSELFTLLVSLVNR 800
Cdd:cd14888 312 EKVASLLGVDAEDL---------LNALCYRTIKTA---HEFY----TKPLRVdeAEDVRDALARALYSCLFDKVVERTNE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 801 AL-KSSQHSLCSMMIVDTPGFQnpeqggSARGASFEELCHNYAQDRLQRLFHERTFVQELERYKEENIElaFDDLE-PAT 878
Cdd:cd14888 376 SIgYSKDNSLLFCGVLDIFGFE------CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGIS--WNPLDfPDN 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 879 DDSVAAVdQASHQSLvrsLARTDEargllwlleeEALVPGATEDALLERLFSYYGpqeGDKkgqRPLLRSSKPHHFLLGH 958
Cdd:cd14888 448 QDCVDLL-QEKPLGI---FCMLDE----------ECFVPGGKDQGLCNKLCQKHK---GHK---RFDVVKTDPNSFVIVH 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 959 SHGTnwVEYNVSGWLSYTKqNPATQNAPRLLQDSQKKIISNLFlgraggttvlsgsiagleggsqlalrrATSMRKTFTT 1038
Cdd:cd14888 508 FAGP--VKYCSDGFLEKNK-DQLSVDAQEVIKNSKNPFISNLF---------------------------SAYLRRGTDG 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1039 GMAAVKKKSLCIQIKLQVDALIDTIKKSKLHFVHCFLPVAEGwageprsassrrvsSSSELDLPSgdhceagllqldvpl 1118
Cdd:cd14888 558 NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQN--------------VPDLFDRIS--------------- 608
|
730 740 750
....*....|....*....|....*....|....*....
gi 1239919865 1119 LRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1157
Cdd:cd14888 609 VNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
440-867 |
4.47e-53 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 200.29 E-value: 4.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLGS 519
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 520 SGSGKTTSCQHLVQYLATIAGTSGNKvfSVEkwQALYS---LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQ 596
Cdd:cd01385 82 SGSGKTESTNFLLHHLTALSQKGYGS--GVE--QTILGagpVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 597 TMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHL------NHLAENNVFGivplakpEEKQKAAQQFSKLQTAMK 670
Cdd:cd01385 158 KYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLkqpedyHYLNQSDCYT-------LEGEDEKYEFERLKQAME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 671 VLGISPDEQKACWLILAAIYHLGaagatkeapeeqaeAAEAGRKQFARHEWAQKA--------AYLLGCSLEELSSAIF- 741
Cdd:cd01385 231 MVGFLPETQRQIFSVLSAVLHLG--------------NIEYKKKAYHRDESVTVGnpevldiiSELLRVKEETLLEALTt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 742 -KHQHKGCTLQRSTSFrqgPEESSLGDgtgpkltalecleGMASGLYSELFTLLVSLVNRAL---KSSQHSLC-SMMIVD 816
Cdd:cd01385 297 kKTVTVGETLILPYKL---PEAIATRD-------------AMAKCLYSALFDWIVLRINHALlnkKDLEEAKGlSIGVLD 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 817 TPGFQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENI 867
Cdd:cd01385 361 IFGFEDFGNN------SFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGI 405
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
442-1156 |
4.85e-53 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 199.60 E-value: 4.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 442 LHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSekVMHMFKGCRREDMA----PHIYAVAQTAYRAMLMSR----QDQ 512
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPyKSIPLLYD--VPGFDSQRKEEATAssppPHVFSIAERAYRAMKGVGkgqgTPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 513 SVILLGSSGSGKTTSCQHLVQYLATIAgTSGNKVFSVEKWQALYS-----------LLEAFGNSPTIMNGNATRFSQILS 581
Cdd:cd14892 82 SIVVSGESGAGKTEASKYIMKYLATAS-KLAKGASTSKGAANAHEsieecvllsnlILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 582 LDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAEnnvFGIVPLAKPEEKQKA--A 659
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAES---FLFLNQGNCVEVDGVddA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 660 QQFSKLQTAMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAaeagrkQFARHEWAQKAAYLLGCSLEELssa 739
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFA------QSADGVNVAKAAGLLGVDAAEL--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 740 ifkhQHKGCTlqRSTSFRQGpeeSSLGDGTGPKlTALECLEGMASGLYSELFTLLVSLVNRAlkSSQHSLCSMMIVDTP- 818
Cdd:cd14892 309 ----MFKLVT--QTTSTARG---SVLEIKLTAR-EAKNALDALCKYLYGELFDWLISRINAC--HKQQTSGVTGGAASPt 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 819 -----------GFQnpeqggSARGASFEELCHNYAQDRLQRLFHERTFVQELERYKEENIE---LAFDDLEPATDdsvaa 884
Cdd:cd14892 377 fspfigildifGFE------IMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDvsaIEFQDNQDCLD----- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 885 VDQASHQSLVRSLartdEARGLLWLLEEEALVPGATEDALLERLFSYYGPQ-EGDkkgqrpllrsskphHFLLGHSHGTn 963
Cdd:cd14892 446 LIQKKPLGLLPLL----EEQMLLKRKTTDKQLLTIYHQTHLDKHPHYAKPRfECD--------------EFVLRHYAGD- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 964 wVEYNVSGWLSytKQNPATQNAPRLLQDSQKKiisnlflgraggttvlsgsiagleggsqlalrratsmrktFTTgmaav 1043
Cdd:cd14892 507 -VTYDVHGFLA--KNNDNLHDDLRDLLRSSSK----------------------------------------FRT----- 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1044 kkkslciqiklQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPSGDHCEagllqldvpLLRAQL 1123
Cdd:cd14892 539 -----------QLAELMEVLWSTTPSYIKCIKP--------------------NNLKFPGGFSCE---------LVRDQL 578
|
730 740 750
....*....|....*....|....*....|...
gi 1239919865 1124 RGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1156
Cdd:cd14892 579 IYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLA 611
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
439-1200 |
5.18e-53 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 199.59 E-value: 5.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGTSGNKVfsVEKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQaGQVASASIQTM 598
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLV--TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 599 LLEKLRVARRPASEATFNVFYYLLACADGTLRTE---------LHLNHLAENNVFGivplakpeekQKAAQQFSKLQTAM 669
Cdd:cd01387 158 LLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKyglqeaekyFYLNQGGNCEIAG----------KSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 670 KVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAGRKqfARHEWAqkaAYLLGCSLEELSSAIfkhqhkgct 749
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQEGVSVGSD--AEIQWV---AHLLQISPEGLQKAL--------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 750 LQRSTSFRQGPEESSLG-DgtgpklTALECLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgs 828
Cdd:cd01387 294 TFKVTETRRERIFTPLTiD------QALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSEN-- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 829 argaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIE---LAFDDLEPatddsvaavdqashqsLVRSLARtdEARG 905
Cdd:cd01387 366 ----SFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDwteIAFADNQP----------------VINLISK--KPVG 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 906 LLWLLEEEALVPGATEDALLERLFSYYGPQEgdkKGQRPLLRSSKphhFLLGHSHGTNWveYNVSGWLSYTKqNPATQNA 985
Cdd:cd01387 424 ILHILDDECNFPQATDHSFLEKCHYHHALNE---LYSKPRMPLPE---FTIKHYAGQVW--YQVHGFLDKNR-DQLRQDV 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 986 PRLLQDSQKKIISNLFlgraggttvlsgsiagleggSQLALRRATSMRKTFTTGMAAVKKKSLCIQIKLQ--VDALIDTI 1063
Cdd:cd01387 495 LELLVSSRTRVVAHLF--------------------SSHRAQTDKAPPRLGKGRFVTMKPRTPTVAARFQdsLLQLLEKM 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1064 KKSKLHFVHCFLPvaegwageprsassrrvsssseldlpsGDHCEAGLlqLDVPLLRAQLRGSRLLDAMRMYRQGYPDHM 1143
Cdd:cd01387 555 ERCNPWFVRCLKP---------------------------NHKKEPML--FDMDVVMAQLRYSGMLETIRIRKEGYPVRL 605
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1144 VFSEF--RRRFDVLAPHLTKKHGRNYIVMDERraveellESLDLEKSSCCMGLSRVFFR 1200
Cdd:cd01387 606 PFQVFidRYRCLVALKLPRPAPGDMCVSLLSR-------LCTVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
441-1155 |
6.44e-52 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 196.28 E-value: 6.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 441 VLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAML----MSRQDQSVIL 516
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 517 LGSSGSGKTTSCQHLVQYLATIAgtSGNKVFSVEKWQaLYSLLEAFGNSPTIMNGNATRFSQILSLDFdQAGQVASASIQ 596
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC--RGNSQLEQQILQ-VNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 597 TMLLEKLRVARRPASEATFNVFYYLLA---CAD----GTLRTELH--LNHLAENNvfgivplakpEEKQKAAQQFSKLQT 667
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAgisAEDrenyGLLDPGKYryLNNGAGCK----------REVQYWKKKYDEVCN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 668 AMKVLGISPDEQKACWLILAAIYHLG-AAGATKEAPEEQAEAAEAGrkqfarheWAQKAAYLLGCSLEELSSaifkhqhk 746
Cdd:cd14889 229 AMDMVGFTEQEEVDMFTILAGILSLGnITFEMDDDEALKVENDSNG--------WLKAAAGQFGVSEEDLLK-------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 747 gcTLQRSTSFRQGPEESSLGDgtgpKLTALECLEGMASGLYSELFTLLVSLVNRALKSSQHS---LCSMMIVDTPGFQNP 823
Cdd:cd14889 293 --TLTCTVTFTRGEQIQRHHT----KQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSsveLREIGILDIFGFENF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 824 EQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENI---ELAFDDLEPATDDSVAAVdqashqslVRSLART 900
Cdd:cd14889 367 AVN------RFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIdwkEITYKDNKPILDLFLNKP--------IGILSLL 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 901 DEargllwlleeEALVPGATEDALLERLFSYYGPQEGDKKGQRpllRSSKphhFLLGHSHGTnwVEYNVSGWLSYTKQN- 979
Cdd:cd14889 433 DE----------QSHFPQATDESFVDKLNIHFKGNSYYGKSRS---KSPK---FTVNHYAGK--VTYNASGFLEKNRDTi 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 980 PATQNAprLLQDSQKKIISNLFLGRAGGTTVLSGSIAGLEGGSQlalrratsmrktfttGMAAVKKKSLCIQIKLQVDAL 1059
Cdd:cd14889 495 PASIRT--LFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSD---------------NFNSTRKQSVGAQFKHSLGVL 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1060 IDTIKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRAQLRGSRLLDAMRMYRQGY 1139
Cdd:cd14889 558 MEKMFAASPHFVRCIKP--------------------NHVKVPG---------QLDSKYIQDQLRYNGLLETIRIRREGF 608
|
730
....*....|....*.
gi 1239919865 1140 PDHMVFSEFRRRFDVL 1155
Cdd:cd14889 609 SWRPSFAEFAERYKIL 624
|
|
| PDZ_MYO18-like |
cd06747 |
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein ... |
220-308 |
2.27e-51 |
|
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MYO18 protein and related domains. MYO18 (also known as myosin XVIIIA, KIAA0216, MysPDZ), a member of the myosin superfamily, is involved in regulating cell protrusion and migration, and Golgi trafficking and morphology, and is required for myoblast adhesion and muscle integrity. The MYO18A/MRCK/LRAP35a complex regulates actomyosin retrograde flow in cell protrusion and migration; the PtdIns(4)P/GOLPH3/MYO18A/F-actin complex is a hub for signals that regulate Golgi trafficking function. The MYO18A PDZ domain binds p190Rho-guanine nucleotide exchange factor (p190RhoGEF), Golgin45, and leucine repeat adaptor protein 1 (Lurap1, also known as Lrap35a). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MYO18-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.
Pssm-ID: 467229 [Multi-domain] Cd Length: 90 Bit Score: 175.96 E-value: 2.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 220 ELELQRRPTGDFGFSLRRTTMLDRGPE-GQVYRRVVHFAEPGAGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd06747 1 EITLKRQPTGDFGFSLRRGTIVERGPDdGQELKRTVHFAEPGAGTKNLATGLLPGDRLIEVNGVNVENASRDEIIEMIRK 80
|
90
....*....|
gi 1239919865 299 SGDSVRLKVQ 308
Cdd:cd06747 81 SGDTVTLKVQ 90
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
440-865 |
2.51e-49 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 188.23 E-value: 2.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPyFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAGTSGNkvfSVEKwQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQ 596
Cdd:cd01382 82 ESGAGKTESTKYILRYLTESWGSGAG---PIEQ-RILEAnpLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 597 TMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENnvfgivplakpeekqkaAQQFSKLQTAMKVLGISP 676
Cdd:cd01382 158 HYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLDD-----------------VGDFIRMDKAMKKIGLSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 677 DEQKACWLILAAIYHLGaagatKEAPEEQAEAAEAGRKQFARHEWA-QKAAYLLGCSLEELSSAIfkhqhkgctlqrSTS 755
Cdd:cd01382 221 EEKLDIFRVVAAVLHLG-----NIEFEENGSDSGGGCNVKPKSEQSlEYAAELLGLDQDELRVSL------------TTR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 756 FRQGPEESSLGDGTGPKLTALECLEG---MASGLYSELFTLLVSLVNRAL--KSSQHSLCsmmIVDTPGFQ----Npeqg 826
Cdd:cd01382 284 VMQTTRGGAKGTVIKVPLKVEEANNArdaLAKAIYSKLFDHIVNRINQCIpfETSSYFIG---VLDIAGFEyfevN---- 356
|
410 420 430
....*....|....*....|....*....|....*....
gi 1239919865 827 gsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEE 865
Cdd:cd01382 357 ------SFEQFCINYCNEKLQQFFNERILKEEQELYEKE 389
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
439-1155 |
9.63e-49 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 186.78 E-value: 9.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMFKGCRRE--------DMAPHIYAVAQTAYRAMLMSR 509
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPyKQIDNLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 510 QDQSVILLGSSGSGKTTSCQHLVQYLATIagtSGNKVFSVEKWQALYS--------------------LLEAFGNSPTIM 569
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQL---SQQEQNSEEVLTLTSSiratskstksieqkilscnpILEAFGNAKTVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 570 NGNATRFSQILSLDFD-QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHL-NHLAENNVFgiv 647
Cdd:cd14907 158 NDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLkNQLSGDRYD--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 648 PLAKPE----EKQKAAQQFSKLQTAMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAGRKQFarhewaQ 723
Cdd:cd14907 235 YLKKSNcyevDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSPCCVKNKETL------Q 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 724 KAAYLLGCSLEELSSAIFKHQhkgctlqrstsfRQGPeesslGDGTGPKLTALEC---LEGMASGLYSELFTLLVSLVNR 800
Cdd:cd14907 309 IIAKLLGIDEEELKEALTTKI------------RKVG-----NQVITSPLSKKECinnRDSLSKELYDRLFNWLVERLND 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 801 AL--------KSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFD 872
Cdd:cd14907 372 TImpkdekdqQLFQNKYLSIGLLDIFGFEVFQNN------SFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLN 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 873 DLePATDDsvaavdqashQSLVRSLARTDEarGLLWLLEEEALVPGATEDALLERLFSYYGpqeGDKKGQRPllRSSKPH 952
Cdd:cd14907 446 QL-SYTDN----------QDVIDLLDKPPI--GIFNLLDDSCKLATGTDEKLLNKIKKQHK---NNSKLIFP--NKINKD 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 953 HFLLGHSHGTnwVEYNVSGWLSYTKQ--NPATQNaprLLQDSQKKIISNLFLGraggttvlsgsiaglEGGSQlaLRRAT 1030
Cdd:cd14907 508 TFTIRHTAKE--VEYNIEGFREKNKDeiSQSIIN---CIQNSKNRIISSIFSG---------------EDGSQ--QQNQS 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1031 SMRKTFttgmaaVKKKSLCIQIKLQVDALIDTIKKSKLHFVHCFLPVAEGwageprsassrrvsssseldlpsgdhcEAG 1110
Cdd:cd14907 566 KQKKSQ------KKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEK---------------------------KAD 612
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1239919865 1111 LLQLDVPLLraQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1155
Cdd:cd14907 613 LFIQGYVLN--QIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
440-1156 |
4.21e-46 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 179.38 E-value: 4.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSekvMHMFkgcrREDM------APHIYAVAQTAYRAMLM----- 507
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPfKHIPGLYD---LHKY----REEMpgwtalPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 508 --SRQDQSVILLGSSGSGKTTSCQHLVQYLA-----TIAGTSGNKVFSVEKWQALYS--LLEAFGNSPTIMNGNATRFSQ 578
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskhTTATSSSKRRRAISGSELLSAnpILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 579 ILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNvFGIVPLAKPE 653
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQE-FQYISGGQCY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 654 EKQKAAQ---QFSKLQTAMKVLGISPDEQKACWLILAAIYHLG----------AAGATKEAPEEQAEAAEAGRKQFARHE 720
Cdd:cd14895 234 QRNDGVRddkQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGnvlfvassedEGEEDNGAASAPCRLASASPSSLTVQQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 721 WAQKAAYLLGCSLEELSSAIFKHQ--HKGCTLQRSTSFRQgpeesslgdgtgpkltALECLEGMASGLYSELFTLLVSLV 798
Cdd:cd14895 314 HLDIVSKLFAVDQDELVSALTTRKisVGGETFHANLSLAQ----------------CGDARDAMARSLYAFLFQFLVSKV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 799 NRALKSSQHSLCS-----------MMIVDTPGFQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENI 867
Cdd:cd14895 378 NSASPQRQFALNPnkaankdttpcIAVLDIFGFEEFEVN------QFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGI 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 868 ELAFDDLEpatDDSVAAVDQASHQSLVRSLarTDEargllwlleeEALVPGATEDALLERLFSYYgPQEGDKKGQRpllR 947
Cdd:cd14895 452 KWNAVDYE---DNSVCLEMLEQRPSGIFSL--LDE----------ECVVPKGSDAGFARKLYQRL-QEHSNFSASR---T 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 948 SSKPHHFLLGHSHGTnwVEYNVSGWLSYTKQNPaTQNAPRLLQDSQKKIISNLFlgraggtTVLSGSIAGLEGGSQLALR 1027
Cdd:cd14895 513 DQADVAFQIHHYAGA--VRYQAEGFCEKNKDQP-NAELFSVLGKTSDAHLRELF-------EFFKASESAELSLGQPKLR 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1028 RATSMRKTFTTGMaavkkkslciQIKLQVDALIDTIKKSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhc 1107
Cdd:cd14895 583 RRSSVLSSVGIGS----------QFKQQLASLLDVVQQTQTHYIRCIKPNDESASD------------------------ 628
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1239919865 1108 eagllQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1156
Cdd:cd14895 629 -----QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
440-1173 |
4.39e-44 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 172.03 E-value: 4.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMF-------------KGcrREDMAPHIYAVAQTAYRAM 505
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPfQKLPGLYSSDTMAKYllsfearssstrnKG--SDPMPPHIYQVAGEAYKAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 506 LMSR----QDQSVILLGSSGSGKTTSCQHLVQYLATIAGTSGNKVFSVEKWQALYS--------LLEAFGNSPTIMNGNA 573
Cdd:cd14900 80 MLGLngvmSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIAakvlqtniLLESFGNARTLRNDNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 574 TRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACAdgtlrtelhlnhlaennvfgivplakpE 653
Cdd:cd14900 160 SRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGA---------------------------S 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 654 EKQKAAQQFSKLQTAMKVLGISPDEQKACWLILAAIYHLGA---AGATKEAPEEQAEAAEAGRKQFARhewaQKAAYLLG 730
Cdd:cd14900 213 EAARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNltfEHDENSDRLGQLKSDLAPSSIWSR----DAAATLLS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 731 CSLEELSSAIfkhqhkgctlqRSTSFRQGPEESSLgdgtgpKLTALEC---LEGMASGLYSELFTLLVSLVNRALK---- 803
Cdd:cd14900 289 VDATKLEKAL-----------SVRRIRAGTDFVSM------KLSAAQAnnaRDALAKALYGRLFDWLVGKMNAFLKmdds 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 804 -SSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFddlePATDDSV 882
Cdd:cd14900 352 sKSHGGLHFIGILDIFGFEVFPKN------SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKY----VEFCDNQ 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 883 AAVDQAShQSLVRSLARTDEargllwlleeEALVPGATEDALLERLFSyygpqegdKKGQRPLLRSSKPHH----FLLGH 958
Cdd:cd14900 422 DCVNLIS-QRPTGILSLIDE----------ECVMPKGSDTTLASKLYR--------ACGSHPRFSASRIQRarglFTIVH 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 959 SHGTnwVEYNVSGWLSytkqnpatQNAPRLLQDsqkkiISNLFLGraggttvlsgsiagleggsqlalrratsmrktftt 1038
Cdd:cd14900 483 YAGH--VEYSTDGFLE--------KNKDVLHQE-----AVDLFVY----------------------------------- 512
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1039 gmaavkkkslCIQIKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssseldlpsGDHCEAGLLQLDVPL 1118
Cdd:cd14900 513 ----------GLQFKEQLTTLLETLQQTNPHYVRCLKP---------------------------NDLCKAGIYERERVL 555
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1119 lrAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL----APHLTKKHGrnYIVMDER 1173
Cdd:cd14900 556 --NQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLarakNRLLAKKQG--TSLPDTD 610
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
441-868 |
2.21e-43 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 170.22 E-value: 2.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 441 VLHTLRQRYGASLLH--TYAGPSLLVLSP-RGAPavysEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSR---QDQSV 514
Cdd:cd14891 3 ILHNLEERSKLDNQRpyTFMANVLIAVNPlRRLP----EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQSI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 515 ILLGSSGSGKTTSCQHLVQYLATIA-GTSGNKVFSVEKWQALYSL---------------LEAFGNSPTIMNGNATRFSQ 578
Cdd:cd14891 79 VISGESGAGKTETSKIILRFLTTRAvGGKKASGQDIEQSSKKRKLsvtslderlmdtnpiLESFGNAKTLRNHNSSRFGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 579 ILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHlnhlaennvfgivpLAKPEEKQK 657
Cdd:cd14891 159 FMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELL--------------LLSPEDFIY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 658 AAQ-------------QFSKLQTAMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAgrkqfarhEWAQK 724
Cdd:cd14891 225 LNQsgcvsddniddaaNFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIAS--------ESDKE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 725 A----AYLLGCSLEELSSAIfkhqhkgctLQRSTSFRqgpeesslGDGTGPKLTALECL---EGMASGLYSELFTLLVSL 797
Cdd:cd14891 297 AlataAELLGVDEEALEKVI---------TQREIVTR--------GETFTIKRNAREAVysrDAIAKSIYERLFLWIVQQ 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 798 VNRALKSSQHSLCSMMIVDTPGFQNPEqggsaRGASFEELCHNYAQDRLQRLFHERTFVQELERYKEENIE 868
Cdd:cd14891 360 INTSLGHDPDPLPYIGVLDIFGFESFE-----TKNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGID 425
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1251-1945 |
5.59e-42 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 169.59 E-value: 5.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1251 NIKKNKGVKDWAWWKLFTTVRPLIEVQLSEEQIRSKDE-EIQQLRSKLEKVEKERNELrlsndrlETRISELTSELtder 1329
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEgQLQELQARLSESERQRAEL-------AEKLSKLQSEL---- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1330 ntgESASQLLDAEAAERLRAEKEMKELQTQ-YDALKKQMEVMEMEVMEARLIRA--AEINGEVDDDDTGGEWRLKYERAM 1406
Cdd:pfam01576 443 ---ESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKLNLSTRLRQleDERNSLQEQLEEEEEAKRNVERQL 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1407 REVDF----TKKRLQQEFEdKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE 1482
Cdd:pfam01576 520 STLQAqlsdMKKKLEEDAG-TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1483 LEKKQRRFDSELSQ---AHEEAQREKLQREKLQREKDTllaEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSqeSK 1559
Cdd:pfam01576 599 LEKKQKKFDQMLAEekaISARYAEERDRAEAEAREKET---RALSLARALEEALEAKEELERTNKQLRAEMEDLVS--SK 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1560 DEA--SLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQSCQKKLKQ 1637
Cdd:pfam01576 674 DDVgkNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRE 753
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1638 MEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKRLrKDLKRTKALLADAQIMLDHLKNN-----APSKREI 1712
Cdd:pfam01576 754 LEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV-KQLKKLQAQMKDLQRELEEARASrdeilAQSKESE 832
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1713 AQLKN------QLEESeftCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELM 1786
Cdd:pfam01576 833 KKLKNleaellQLQED---LAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLN 909
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1787 KKHKAAVAQ---------ASRDLAQMND-LQAQLEEANKekqELQEKLQALQSQVEFLEqsmvdKSLVSRQEAKIRELET 1856
Cdd:pfam01576 910 DRLRKSTLQveqlttelaAERSTSQKSEsARQQLERQNK---ELKAKLQEMEGTVKSKF-----KSSIAALEAKIAQLEE 981
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1857 RLEFERTQ----VKRLESLASRLKENMEKLTEERDQRTAAENREKEQN---KRLQRQLRDTKEEMgelarKEAEASRKKh 1929
Cdd:pfam01576 982 QLEQESRErqaaNKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNsrmKQLKRQLEEAEEEA-----SRANAARRK- 1055
|
730
....*....|....*.
gi 1239919865 1930 eLEMDLESLEAANQSL 1945
Cdd:pfam01576 1056 -LQRELDDATESNESM 1070
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
440-1168 |
2.05e-41 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 165.15 E-value: 2.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSVILL 517
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPyKDISSIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 518 GSSGSGKTTSCQHLVQYLATIAGTS-------GNKVFSVEKwQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQA- 587
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNqqqnnnnNNNNNSIEK-DILTSnpILEAFGNSRTTKNHNSSRFGKFLKIEFRSSd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 588 GQVASASIQTMLLEKLRVARRP-ASEATFNVFYYLLACADGTLRTELHLNH--------LAENNVFGIV------PLAKP 652
Cdd:cd14906 161 GKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNdpskyrylDARDDVISSFksqssnKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 653 EEKQKAAQQFSKLQTAMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAGRKqfarhEWAQKAAYLLGCS 732
Cdd:cd14906 241 NNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVT-----ASLESVSKLLGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 733 LEELSSAIFKHQHKGCTlqRSTSFRQgPEESSlgdgtgpklTALECLEGMASGLYSELFTLLVSLVNR-----------A 801
Cdd:cd14906 316 ESVFKQALLNRNLKAGG--RGSVYCR-PMEVA---------QSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 802 LKSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELA---FDDlepaT 878
Cdd:cd14906 384 GGSNKKNNLFIGVLDIFGFENLSSN------SLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSnsnFID----N 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 879 DDSVAAVDQASHQSLvrSLArTDEArgllwlleeeaLVPGATEDALLERLFSYYgpQEGDKKGQRPLLRSSkphhflLGH 958
Cdd:cd14906 454 KECIELIEKKSDGIL--SLL-DDEC-----------IMPKGSEQSLLEKYNKQY--HNTNQYYQRTLAKGT------LGI 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 959 SHGTNWVEYNVSGWLSYTKQNPATqNAPRLLQDSQKKIISNLFLGRAGGTTvlsgsiagleggsqlalrrATSMRKTFTT 1038
Cdd:cd14906 512 KHFAGDVTYQTDGWLEKNRDSLYS-DVEDLLLASSNFLKKSLFQQQITSTT-------------------NTTKKQTQSN 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1039 GMAAvkkkslciQIKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvssSSELDLPSGDHCEagllqldvpl 1118
Cdd:cd14906 572 TVSG--------QFLEQLNQLIQTINSTSVHYIRCIKP-------------------NQTMDCNNFNNVH---------- 614
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1119 LRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYI 1168
Cdd:cd14906 615 VLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPK 664
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
439-871 |
1.09e-40 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 162.33 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQ--DQSV 514
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPfKPVPQLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 515 ILLGSSGSGKTTSCQHLVQYLATIAGTS----GNKVFSVEKWQALYS--LLEAFGNSPTIMNGNATRFSQILSLDFDQAG 588
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPtsweSHKIAERIEQRILNSnpVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 589 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELhlnHLAENNVFGIVPlakPEEKQKAAQQFSKLQTA 668
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQW---HLPEGAAFSWLP---NPERNLEEDCFEVTREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 669 MKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAGRKQFARhewaqKAAYLLGCSLEELSSAIfkhQHKGC 748
Cdd:cd14880 235 MLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVR-----TSALLLKLPEDHLLETL---QIRTI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 749 TLQRSTSFRQGPEESSLGDgtgpklTALECLegmASGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQN-PEQg 826
Cdd:cd14880 307 RAGKQQQVFKKPCSRAECD------TRRDCL---AKLIYARLFDWLVSVINSSICADTDSWTTFIgLLDVYGFESfPEN- 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1239919865 827 gsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAF 871
Cdd:cd14880 377 ------SLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSF 415
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
442-1200 |
3.51e-40 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 161.35 E-value: 3.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 442 LHTLRQRYGA--------SLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQS 513
Cdd:cd14887 4 LENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 514 VILLGSSGSGKTTSCQHLVQYLATI------AGTSGNKvfsvEKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQA 587
Cdd:cd14887 84 ILISGESGAGKTETSKHVLTYLAAVsdrrhgADSQGLE----ARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 588 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLlaCADGTLRTELHLNhlaennvfgivplakPEEKQKAAQQFSKLQT 667
Cdd:cd14887 160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYAL--CNAAVAAATQKSS---------------AGEGDPESTDLRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 668 AMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAGRKQFARHEWAQKAAYLLgcSLEELSSAIFKHQHKG 747
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADRSHSS--EVKCLSSGLKVTEASR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 748 CTLQRSTSFRQGPEESSLGDGTGPKLTALECLEGMAS---------------GLYSELFTLLVSLVNRALKSSQHSLCSM 812
Cdd:cd14887 301 KHLKTVARLLGLPPGVEGEEMLRLALVSRSVRETRSFfdldgaaaardaackNLYSRAFDAVVARINAGLQRSAKPSESD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 813 MIVDTP--------------GFQNPEQGGSARgasFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAFDDLEPAT 878
Cdd:cd14887 381 SDEDTPsttgtqtigildlfGFEDLRNHSKNR---LEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 879 DDSVAAVDQASHQSlVRSLARTDEARGLLWLLEEEALVPGATedaLLERLFSYYGPQEGDKKGQRplLRSSKPHHFLLGH 958
Cdd:cd14887 458 SFPLASTLTSSPSS-TSPFSPTPSFRSSSAFATSPSLPSSLS---SLSSSLSSSPPVWEGRDNSD--LFYEKLNKNIINS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 959 SHGTNWVEYNVSGWLSYTkqnpATQNAPRLLQDSQKKIISNLflgraggtTVLSGSIAGLEGGSQLALRRATSMRKTFTT 1038
Cdd:cd14887 532 AKYKNITPALSRENLEFT----VSHFACDVTYDARDFCRANR--------EATSDELERLFLACSTYTRLVGSKKNSGVR 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1039 GMAAvKKKSLCIQIKLQVDALIDTIKKSKLHFVHCFLPVAEGwageprsassrrvsssseldlpsgdhcEAGLLQLDvpL 1118
Cdd:cd14887 600 AISS-RRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQ---------------------------EAGIFEDA--Y 649
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1119 LRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPhltkkhgrnyivMDERRAVEELLESLDLEKSSCC------M 1192
Cdd:cd14887 650 VHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLP------------MALREALTPKMFCKIVLMFLEInsnsytF 717
|
....*...
gi 1239919865 1193 GLSRVFFR 1200
Cdd:cd14887 718 GKTKIFFR 725
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
439-858 |
4.08e-39 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 157.28 E-value: 4.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMF---KGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVI 515
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 516 LLGSSGSGKTTSCQHLVQYLATIAGTSGNKVFSveKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDF-DQAGQVASAS 594
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDS--RFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 595 IQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVfgiVPLAKPEEKQKAA-----QQFSKLQTAM 669
Cdd:cd14878 159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRY---LNQTMREDVSTAErslnrEKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 670 KVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAI------FK- 742
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDL--------QLLEQVAGMLQVSTDELASALttdiqyFKg 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 743 ----HQHkgcTLQRSTSFRqgpeesslgdgtgpkltaleclEGMASGLYSELFTLLVSLVNRALKsSQHSLCSMM----- 813
Cdd:cd14878 308 dmiiRRH---TIQIAEFYR----------------------DLLAKSLYSRLFSFLVNTVNCCLQ-SQDEQKSMQtldig 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1239919865 814 IVDTPGFQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQE 858
Cdd:cd14878 362 ILDIFGFEEFQKN------EFEQLCVNMTNEKMHHYINEVLFLQE 400
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
374-1076 |
3.60e-38 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 155.96 E-value: 3.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 374 LVHKDgfSLGSQLKSEELSLPEGKVrvkldhdgaiLDVDEDDVEKANAP-SCDRLEDLASLVYLNESSVLHTLRQRYGAS 452
Cdd:PTZ00014 56 LVLPG--STGEKLTLKQIDPPTNST----------FEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 453 LLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSVILLGSSGSGKTTSCQHL 531
Cdd:PTZ00014 124 QIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDsDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 532 VQYLAtiAGTSGNKVFSVEK--WQAlYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRP 609
Cdd:PTZ00014 204 MRYFA--SSKSGNMDLKIQNaiMAA-NPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 610 ASEATFNVFYYLLACADGTLRTELHLNHLAE----NN----VFGIVPlakpeekqkaAQQFSKLQTAMKVLGISPDEQKA 681
Cdd:PTZ00014 281 DDERSYHIFYQLLKGANDEMKEKYKLKSLEEykyiNPkcldVPGIDD----------VKDFEEVMESFDSMGLSESQIED 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 682 CWLILAAIYHLGAA---GATKEAPEEQAEAAEAGRKQFarhewaQKAAYLLGCSLEELS-SAIFKHQHKGCtlQRSTSFR 757
Cdd:PTZ00014 351 IFSILSGVLLLGNVeieGKEEGGLTDAAAISDESLEVF------NEACELLFLDYESLKkELTVKVTYAGN--QKIEGPW 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 758 QGPEESSLGDgtgpkltalecleGMASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEEL 837
Cdd:PTZ00014 423 SKDESEMLKD-------------SLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNN------SLEQL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 838 CHNYAQDRLQRLFHERTFVQELERYKEENI---ELAFDDLEPATD------DSVAAV--DQashqslvrSLArtdeargl 906
Cdd:PTZ00014 484 FINITNEMLQKNFVDIVFERESKLYKDEGIsteELEYTSNESVIDllcgkgKSVLSIleDQ--------CLA-------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 907 lwlleeealvPGATEDALLERLFSYYGPQEGDKKGQRpllrsSKPHHFLLGHSHGTnwVEYNVSGWLSYTKqNPATQNAP 986
Cdd:PTZ00014 548 ----------PGGTDEKFVSSCNTNLKNNPKYKPAKV-----DSNKNFVIKHTIGD--IQYCASGFLFKNK-DVLRPELV 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 987 RLLQDSQKKIISNLFlgraGGTTVLSGSIAgleggsqlalrratsmrktfttgmaavKKKSLCIQIKLQVDALIDTIKKS 1066
Cdd:PTZ00014 610 EVVKASPNPLVRDLF----EGVEVEKGKLA---------------------------KGQLIGSQFLNQLDSLMSLINST 658
|
730
....*....|
gi 1239919865 1067 KLHFVHCFLP 1076
Cdd:PTZ00014 659 EPHFIRCIKP 668
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
439-1152 |
7.98e-38 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 154.10 E-value: 7.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMF----------KGCRREDMAPHIYAVAQTAYRAMLM 507
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPfQDLPQLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 508 SRQDQSVILLGSSGSGKTTSCQHLVQYLATIAGTSGNKVFSVEKW-------------QALYS--LLEAFGNSPTIMNGN 572
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESIsppaspsrttieeQVLQSnpILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 573 ATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLA----CADGTLRTELHLNHLAEN-NVFGI 646
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSadnnCVSKEQKQVLALSGGPQSfRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 647 VPLAKPEEKQKAAQQFSKLQTAMKVLGISPDEQKACWLILAAIYHLGAAG----ATKEAPEEQAEAAEAGRKQFARHEWA 722
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDfeqiPHKGDDTVFADEARVMSSTTGAFDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 723 QKAAYLLGCSLEELSSAIFKHQhkgctLQRSTSFRQGPEESSLGDGTGPKLTaLEClegmasglYSELFTLLVSLVNRAL 802
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRW-----LHASNETLVVGVDVAHARNTRNALT-MEC--------YRLLFEWLVARVNNKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 803 K---------------SSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENI 867
Cdd:cd14899 387 QrqasapwgadesdvdDEEDATDFIGLLDIFGFEDMAEN------SFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGI 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 868 ELAFDDLEpatdDSVAAVDQASHQSLvrslartdearGLLWLLEEEALVPGATEDALLERlfsYYgpQEGDKKGQRPLLR 947
Cdd:cd14899 461 RWSFVDFP----NNRACLELFEHRPI-----------GIFSLTDQECVFPQGTDRALVAK---YY--LEFEKKNSHPHFR 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 948 SS----KPHHFLLGHSHGTnwVEYNVSGWLSYTKqNPATQNAPRLLQDSQKKIISNLflgRAGGTTVLSGSIAGLEGGSQ 1023
Cdd:cd14899 521 SApliqRTTQFVVAHYAGC--VTYTIDGFLAKNK-DSFCESAAQLLAGSSNPLIQAL---AAGSNDEDANGDSELDGFGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1024 LALRRATSmrktfttgmaAVKKKSLCIQIKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssseldlps 1103
Cdd:cd14899 595 RTRRRAKS----------AIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKP--------------------------- 637
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1239919865 1104 GDHCEAGLLQldVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRF 1152
Cdd:cd14899 638 NDSHVGSLFQ--STRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
440-871 |
1.25e-36 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 150.06 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFK--GCRRE-------DMAPHIYAVAQTAYRAMLM-SR 509
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiespqALGPHVFAIADRSYRQMMSeIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 510 QDQSVILLGSSGSGKTTSCQHLVQYLATIA---------GTSGNKVFSVEKWQALYSLLEAFGNSPTIMNGNATRFSQIL 580
Cdd:cd14908 82 ASQSILISGESGAGKTESTKIVMLYLTTLGngeegapneGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKFI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 581 SLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVFGivplakPEEKQKAAQ 660
Cdd:cd14908 162 ELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGGLQL------PNEFHYTGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 661 -------------QFSKLQTAMKVLGISPDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAeagrkQFARHEWAQKAAY 727
Cdd:cd14908 236 ggapdlreftdedGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIA-----EEGNEKCLARVAK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 728 LLGCSLEELSSAifkhqhkgctLQRSTSFRQGPEESSlgdgtgpKLT---ALECLEGMASGLYSELFTLLVSLVNRALK- 803
Cdd:cd14908 311 LLGVDVDKLLRA----------LTSKIIVVRGKEITT-------KLTphkAYDARDALAKTIYGALFLWVVATVNSSINw 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 804 -SSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELAF 871
Cdd:cd14908 374 eNDKDIRSSVGVLDIFGFECFAHN------SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAF 436
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
440-882 |
3.12e-36 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 147.35 E-value: 3.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPrgAPAVYSEKVMHMFKGCRREdMAPHIYAVAQTAYRAMLMSrQDQSVILLGS 519
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNP--YETIYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 520 SGSGKTTSCQHLVQYLatIAGTSGNKvfSVEK-WQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDqaGQVASASIQTM 598
Cdd:cd14898 78 SGSGKTENAKLVIKYL--VERTASTT--SIEKlITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 599 LLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVFGIVPLakpeekqkaAQQFSKLQTAMKVLGISpdE 678
Cdd:cd14898 152 LLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFIDTSSTAGNKESIVQL---------SEKYKMTCSAMKSLGIA--N 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 679 QKACWLILAAIYHLGAagatkeapeeqAEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH--QHKGCTLQRSTSF 756
Cdd:cd14898 221 FKSIEDCLLGILYLGS-----------IQFVNDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFsiQVKGETIEVFNTL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 757 RQgpeesslgdgtgpkltALECLEGMASGLYSELFTLLVSLVNRALK-SSQHSLCsmmIVDTPGFQNPEQGGsargasFE 835
Cdd:cd14898 290 KQ----------------ARTIRNSMARLLYSNVFNYITASINNCLEgSGERSIS---VLDIFGFEIFESNG------LD 344
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1239919865 836 ELCHNYAQDRLQRLFHERTFVQELERYKEENIElaFDDLEPATDDSV 882
Cdd:cd14898 345 QLCINWTNEKIQNDFIKKMFRAKQGMYKEEGIE--WPDVEFFDNNQC 389
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1288-1965 |
1.26e-33 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 142.62 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1288 EEI-QQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDErntgESASQLLDAEaaeRLRAEKEMKELQTQYDALKKQ 1366
Cdd:pfam01576 74 EEIlHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEE----EAARQKLQLE---KVTTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1367 MEVMEMEVMEARLiRAAEINGEVDDDDTG----GEWRLKYERAMREVDftkKRLQQEFEDKLEVEQqNKRQLERRLGDLQ 1442
Cdd:pfam01576 147 NSKLSKERKLLEE-RISEFTSNLAEEEEKakslSKLKNKHEAMISDLE---ERLKKEEKGRQELEK-AKRKLEGESTDLQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1443 ADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEA 1522
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1523 FSLKQQLEEkdmdiagfTQKVVSLEAELQdissqeSKDEASLAKVKK-----------QLRDLEAKVKDQEEELDEQagt 1591
Cdd:pfam01576 302 EALKTELED--------TLDTTAAQQELR------SKREQEVTELKKaleeetrsheaQLQEMRQKHTQALEELTEQ--- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1592 iqmLEQAKlRLEMEMERMRQTHSKEVESRDEEV---EEARQSCQKKLKQMEVQLEE---EYEDKQKVLREKRELESKLTT 1665
Cdd:pfam01576 365 ---LEQAK-RNKANLEKAKQALESENAELQAELrtlQQAKQDSEHKRKKLEGQLQElqaRLSESERQRAELAEKLSKLQS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1666 LSEQVSQRDLESEK---RLRKDLKRTKALLADAQIML-------------------------DHLKNNAPSKREI----- 1712
Cdd:pfam01576 441 ELESVSSLLNEAEGkniKLSKDVSSLESQLQDTQELLqeetrqklnlstrlrqledernslqEQLEEEEEAKRNVerqls 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1713 ------AQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQRE----------KNEIQSRLE 1776
Cdd:pfam01576 521 tlqaqlSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElddllvdldhQRQLVSNLE 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1777 EDQEDMNELMKKHKAAVAQAS--RDLAQMN---------DLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM--VDKSL 1843
Cdd:pfam01576 601 KKQKKFDQMLAEEKAISARYAeeRDRAEAEareketralSLARALEEALEAKEELERTNKQLRAEMEDLVSSKddVGKNV 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1844 VSRQEAKiRELETRLEFERTQVKRLESLAS-------RLKENME--KLTEERDQRTAAENREkEQNKRLQRQLRDTKEEM 1914
Cdd:pfam01576 681 HELERSK-RALEQQVEEMKTQLEELEDELQatedaklRLEVNMQalKAQFERDLQARDEQGE-EKRRQLVKQVRELEAEL 758
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 1915 GELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED 1965
Cdd:pfam01576 759 EDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD 809
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1274-1996 |
1.29e-33 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 142.50 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1274 IEVQLSEEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRAEKEM 1353
Cdd:TIGR02168 225 LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1354 KELQTQYDALKKQMEV--MEMEVMEARLIRAAEINGEVDDddtggewrlKYERAMREVDftkkrlqqEFEDKLEVEQQNK 1431
Cdd:TIGR02168 305 QILRERLANLERQLEEleAQLEELESKLDELAEELAELEE---------KLEELKEELE--------SLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1432 RQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfdSELSQAHEEAQREKLQR--E 1509
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI----EELLKKLEEAELKELQAelE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1510 KLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQEskdeASLAKVKKQLRDLEAKVKDQEEELDEQA 1589
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL----DSLERLQENLEGFSEGVKALLKNQSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1590 GTIQMLEQ-----AKLRLEMEM---ERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELES 1661
Cdd:TIGR02168 520 GILGVLSElisvdEGYEAAIEAalgGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEG 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1662 KLTTLSEQVsqrdlESEKRLRKDLKrtkALLA------DAQIMLDHLKNNAPSKReIAQLKNQL--------EESEFTCA 1727
Cdd:TIGR02168 600 FLGVAKDLV-----KFDPKLRKALS---YLLGgvlvvdDLDNALELAKKLRPGYR-IVTLDGDLvrpggvitGGSAKTNS 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1728 AAVKARKAM---EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMN 1804
Cdd:TIGR02168 671 SILERRREIeelEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1805 DLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDkslvsrQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTE 1884
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE------LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1885 ERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1964
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
730 740 750
....*....|....*....|....*....|...
gi 1239919865 1965 D-EMESDENEDLITSLQDMVTKYQKRKNKPEGD 1996
Cdd:TIGR02168 905 ElESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1290-1982 |
2.06e-33 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 142.13 E-value: 2.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1290 IQQLRSKLEKVEKERNELRLSNDRLETRISELTSE---LTDERNTGESASQLL----DAEAAERLR----AEKEMKELQT 1358
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerLRREREKAERYQALLkekrEYEGYELLKekeaLERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1359 QYDALKKQMEVMEMEVM------EARLIRAAEINGEVDDDDTGGEWRLKYERAMREVDFTK-KRLQQEFEDKLEVEQQNK 1431
Cdd:TIGR02169 245 QLASLEEELEKLTEEISelekrlEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1432 RQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKL 1511
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1512 QREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDE-------ASLAKVKKQLRDLEAKVKDQEEE 1584
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1585 LDE----------QAGTIQMLEQAKLRLEMEME--------------RMRQTHSKEVES-----------RDEEVEearQ 1629
Cdd:TIGR02169 485 LSKlqrelaeaeaQARASEERVRGGRAVEEVLKasiqgvhgtvaqlgSVGERYATAIEVaagnrlnnvvvEDDAVA---K 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1630 SCQKKLKQME----------------------------------VQLEEEYEDKQK-VLREK---RELES--------KL 1663
Cdd:TIGR02169 562 EAIELLKRRKagratflplnkmrderrdlsilsedgvigfavdlVEFDPKYEPAFKyVFGDTlvvEDIEAarrlmgkyRM 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1664 TTL--------------------SEQVSQRDLESEKRLRKDLKRTKALLADAQIMLDHLKNNA--------PSKREIAQL 1715
Cdd:TIGR02169 642 VTLegelfeksgamtggsraprgGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLdelsqelsDASRKIGEI 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1716 KNQLEESEFTcAAAVKAR--------KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEI-----QSRLEEDQEDM 1782
Cdd:TIGR02169 722 EKEIEQLEQE-EEKLKERleeleedlSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAEL 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1783 NELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVD--------KSLVSRQEAKIREL 1854
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngkkeelEEELEELEAALRDL 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1855 ETRLEFERTQVKRLESLASRLKENMEKLTEERD-------QRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRK 1927
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEkkrkrlsELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAEL 960
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239919865 1928 KhELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED-EMESDENEDLITSLQDM 1982
Cdd:TIGR02169 961 Q-RVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKlEEERKAILERIEEYEKK 1015
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
441-868 |
5.28e-32 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 135.40 E-value: 5.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 441 VLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMFKGCRRE-----DMAPHIYAVAQTAYRAMLMSRQDQSV 514
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPfKQIRNLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 515 ILLGSSGSGKTTSCQHLVQYLATIAGTSGNKVFSVEKWQALysLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASAS 594
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSLILGSNP--LLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 595 IQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVF--GIVPLAKPEEKQKaaqQFSKLQTAMKVL 672
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLnaSKCYDAPGIDDQK---EFAPVRSQLEKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 673 gISPDEQKACWLILAAIYHLGaagatKEAPEEQAEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIfkhqhkgctLQR 752
Cdd:cd14886 238 -FSKNEIDSFYKCISGILLAG-----NIEFSEEGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAI---------ITK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 753 STSFRQGPEESSLgdgtgPKLTALECLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsarga 832
Cdd:cd14886 303 VVVINNETIISPV-----TQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERN------ 371
|
410 420 430
....*....|....*....|....*....|....*.
gi 1239919865 833 SFEELCHNYAQDRLQRLFHERTFVQELERYKEENIE 868
Cdd:cd14886 372 TYEQLLINYANERLQQYFINQVFKSEIQEYEIEGID 407
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
440-891 |
8.34e-32 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 134.48 E-value: 8.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKvMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQE-FHAKYRCKsRSDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAgtSGNKVfSVEKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQTM 598
Cdd:cd14882 81 ESYSGKTTNARLLIKHLCYLG--DGNRG-ATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 599 LLEKLRVARRPASEATFNVFYYLLACADGTLRteLHLNHLAENNVFGIVPLAKPEEKQKA----------AQQFSKLQTA 668
Cdd:cd14882 158 QLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNR--LKEYNLKAGRNYRYLRIPPEVPPSKLkyrrddpegnVERYKEFEEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 669 MKVLGISPDEQKACWLILAAIYHLGaagatkeapeEQAEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHqhkgC 748
Cdd:cd14882 236 LKDLDFNEEQLETVRKVLAAILNLG----------EIRFRQNGGYAELENTEIASRVAELLRLDEKKFMWALTNY----C 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 749 TLQRSTSFRQgpeesslgdgtgpKLTALECLEG---MASGLYSELFTLLVSLVN------RALKSSQHSLcsmMIVDTPG 819
Cdd:cd14882 302 LIKGGSAERR-------------KHTTEEARDArdvLASTLYSRLVDWIINRINmkmsfpRAVFGDKYSI---SIHDMFG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 820 FQNPEQGGsargasFEELCHNYAQDRLQRLFHERTFVQELERYKEENI----------ELAFDDLEPATDDSVAAVDQAS 889
Cdd:cd14882 366 FECFHRNR------LEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIptinlrfydnKTAVDQLMTKPDGLFYIIDDAS 439
|
..
gi 1239919865 890 HQ 891
Cdd:cd14882 440 RS 441
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
439-1158 |
1.34e-31 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 134.71 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKGCRRE----------DMAPHIYAVAQTAYRAMLMS 508
Cdd:cd14893 1 NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 509 RQDQSVILLGSSGSGKTTSCQHLVQYLATIA--------GTSGNKVFSVEKWQAL--YSLLEAFGNSPTIMNGNATRFSQ 578
Cdd:cd14893 81 GEDQAVILLGGMGAGKSEAAKLIVQYLCEIGdeteprpdSEGASGVLHPIGQQILhaFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 579 ILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACA--DGTLRTELHLNHLAENnvFGIVPLAKPEEKQ 656
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVqhDPTLRDSLEMNKCVNE--FVMLKQADPLATN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 657 KA--AQQFSKLQTAMKVLGISPDEQKACWLILAAIYHLGAAGATKeaPEEQAEAAEAGRKQFARHEWA----QKAAYLLG 730
Cdd:cd14893 239 FAldARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVP--DPEGGKSVGGANSTTVSDAQScalkDPAQILLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 731 CSLEELSSAIFKHQHKgctLQRSTSFRQGPEESSLGDGTGPKltALECLEGMASGLYSELFTLLVSLVN--------RAL 802
Cdd:cd14893 317 AKLLEVEPVVLDNYFR---TRQFFSKDGNKTVSSLKVVTVHQ--ARKARDTFVRSLYESLFNFLVETLNgilggifdRYE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 803 KS-----SQhslcSMMIVDTPGFQN--PEQGGsargasFEELCHNYAQDRLQRLFHERTFVQELERYKEE---------- 865
Cdd:cd14893 392 KSnivinSQ----GVHVLDMVGFENltPSQNS------FDQLCFNYWSEKVHHFYVQNTLAINFSFLEDEsqqvenrltv 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 866 --NIELAFDD---LEPATDDSVAAVDQASHQSLVRS----------LARTDEARGLLWlleeealvPGATEDALLERLfs 930
Cdd:cd14893 462 nsNVDITSEQekcLQLFEDKPFGIFDLLTENCKVRLpndedfvnklFSGNEAVGGLSR--------PNMGADTTNEYL-- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 931 yygpqeGDKKGQRPLlrsskphhFLLGHSHGTnwVEYNVSGwLSYTKQNPATQNAPRLLQDSQkkiisNLFLGRAGGTTV 1010
Cdd:cd14893 532 ------APSKDWRLL--------FIVQHHCGK--VTYNGKG-LSSKNMLSISSTCAAIMQSSK-----NAVLHAVGAAQM 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1011 LSGSIAglEGGSQLALRRATS--MRKTFTTGMAAVK-KKSLCIQIKLQVDALIDTIKKSKLHFVHCFLPvaegwageprs 1087
Cdd:cd14893 590 AAASSE--KAAKQTEERGSTSskFRKSASSARESKNiTDSAATDVYNQADALLHALNHTGKNFLVCIKP----------- 656
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 1088 assrrvssssELDLPSGdhceagllQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1158
Cdd:cd14893 657 ----------NETLEEG--------VFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH 709
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1413-1964 |
1.62e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 135.45 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1413 KKRLQQEFEDKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1492
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1493 ELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR 1572
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1573 DLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQThSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKV 1652
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1653 LREKRELESKLTTLSEQVSQRDLE-----SEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLkNQLEESEFTCA 1727
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEElaeaaARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL-IGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1728 AAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQ 1807
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1808 AQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERD 1887
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239919865 1888 QRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1964
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
492-1162 |
4.74e-31 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 132.24 E-value: 4.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 492 PHIYAVAQTAYRAMLM-SRQDQSVILLGSSGSGKTTSCQHLVQYLATIAGT-SGN--------KVFSVEKWQAlySLLEA 561
Cdd:cd14875 56 PHIWQVAHKAFNAIFVqGLGNQSVVISGESGSGKTENAKMLIAYLGQLSYMhSSNtsqrsiadKIDENLKWSN--PVMES 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 562 FGNSPTIMNGNATRFSQILSLDFDQA-GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACAD-------GTLRTEL 633
Cdd:cd14875 134 FGNARTVRNDNSSRFGKYIKLYFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSpeekkelGGLKTAQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 634 HLNHLAENNVFgiVPLAKPEEKQKAAQQFSKLQTAMKVLGISPDEQKACWLILAAIYHLGAAGATKeapeeqaeaaeagr 713
Cdd:cd14875 214 DYKCLNGGNTF--VRRGVDGKTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFES-------------- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 714 KQFARHEWAQKAAYLLGCSLEELSSAIFKHqhkgCTLQRStsfrqgpeESSLGDGTGPKLTALECLEGMASGLYSELFTL 793
Cdd:cd14875 278 DQNDKAQIADETPFLTACRLLQLDPAKLRE----CFLVKS--------KTSLVTILANKTEAEGFRNAFCKAIYVGLFDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 794 LVSLVNRALKSSQH-SLCSMM-IVDTPGFQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENIE--- 868
Cdd:cd14875 346 LVEFVNASITPQGDcSGCKYIgLLDIFGFENFTRN------SFEQLCINYANESLQNHYNKYTFINDEEECRREGIQipk 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 869 LAFddlePATDDSVAAVDQAShqslVRSLARTDEargllwlleeEALVPGATEDALLERLFSyygpQEGDKKGQRPLLRS 948
Cdd:cd14875 420 IEF----PDNSECVNMFDQKR----TGIFSMLDE----------ECNFKGGTTERFTTNLWD----QWANKSPYFVLPKS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 949 SKPHHFllGHSHGTNWVEYNVSGWLSytkqnpatQNAPRLLQDSQKkiisnlflgraggtTVLSGSiagleggsqlalrr 1028
Cdd:cd14875 478 TIPNQF--GVNHYAAFVNYNTDEWLE--------KNTDALKEDMYE--------------CVSNST-------------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1029 ATSMRKTFTTGMA-AVKKKSLCIQIKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssseldlpsgdHC 1107
Cdd:cd14875 520 DEFIRTLLSTEKGlARRKQTVAIRFQRQLTDLRTELESTETQFIRCIKP-----------------------------NM 570
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1239919865 1108 EAGLLQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKK 1162
Cdd:cd14875 571 EASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTAS 625
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
439-1157 |
9.00e-31 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 131.15 E-value: 9.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVmhmFKGCrredmapHIYAVAQTAYRAML-MSRQDQSVILL 517
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLV---IKKC-------HISGVAENALDRIKsMSSNAESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 518 GSSGSGKTTSCQHLVQYLATiagTSGNKVFSVEKwQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQT 597
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTS---QPKSKVTTKHS-SAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 598 MLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLaeNNVFGIVPLAKPEEKQKAAQQFSKLQTAMKVLGISPD 677
Cdd:cd14874 147 VPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL--QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 678 EQKACWLILAAIYHLGAAG-ATKEAPEEQAEAAEAGrkQFARHEWaqkAAYLLGCSLEELSSAIFKHQHKGCTLQRStsf 756
Cdd:cd14874 225 HCISIYKIISTILHIGNIYfRTKRNPNVEQDVVEIG--NMSEVKW---VAFLLEVDFDQLVNFLLPKSEDGTTIDLN--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 757 rqgpeesslgdgtgpklTALECLEGMASGLYSELFTLLVSLVNRALKSSQHSlCSMMIVDTPGFQNPEQGGsargasFEE 836
Cdd:cd14874 297 -----------------AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHT-GVISILDHYGFEKYNNNG------VEE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 837 LCHNYAQDRLQRLFHERTFVQELERYKEENIELafDDLEPATDDSVAAVDQ--ASHQSLVRSLarTDEARgllwlleeea 914
Cdd:cd14874 353 FLINSVNERIENLFVKHSFHDQLVDYAKDGISV--DYKVPNSIENGKTVELlfKKPYGLLPLL--TDECK---------- 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 915 lVPGATEDALLERL------FSYYGPQegdkkgqrpllRSSKPHHFLLGHSHGTNWveYNVSGWLSYTKQNpATQNAPRL 988
Cdd:cd14874 419 -FPKGSHESYLEHCnlnhtdRSSYGKA-----------RNKERLEFGVRHCIGTTW--YNVTDFFSRNKRI-ISLSAVQL 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 989 LQDSQKKIISNLFLGRAGGTTVLSGSIAgleggsQLALRRATSmrktfttgmaavkkkslciqiklqvdaLIDTIKKSKL 1068
Cdd:cd14874 484 LRSSKNPIIGLLFESYSSNTSDMIVSQA------QFILRGAQE---------------------------IADKINGSHA 530
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1069 HFVHCflpvaegwageprsassrrvsssseldLPSGDHCEAGllQLDVPLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 1148
Cdd:cd14874 531 HFVRC---------------------------IKSNNERQPK--KFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTF 581
|
....*....
gi 1239919865 1149 RRRFDVLAP 1157
Cdd:cd14874 582 ARQYRCLLP 590
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1265-1949 |
1.62e-29 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 129.14 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1265 KLFTTVRPLIEVQLSEEQIRSKDEEiqQLRSKLEK----VEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLD 1340
Cdd:pfam01576 176 KSLSKLKNKHEAMISDLEERLKKEE--KGRQELEKakrkLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1341 AEAAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRA------AEINGEVDD--DDTGGEWRLKYERAmREVDFT 1412
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRdlgeelEALKTELEDtlDTTAAQQELRSKRE-QEVTEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1413 KKRLQQE---FEDKL-EVEQQNKRQLErrlgDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQR 1488
Cdd:pfam01576 333 KKALEEEtrsHEAQLqEMRQKHTQALE----ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1489 RFDSELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVK 1568
Cdd:pfam01576 409 KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLS 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1569 KQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRdEEVEEARQSCQKKLKQMEVQLEEEYED 1648
Cdd:pfam01576 489 TRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL-EALEEGKKRLQRELEALTQQLEEKAAA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1649 KQKVLREKRELESKLTTLS-EQVSQRDLES--EKRLRK---DLKRTKALLADAQIMLDHLKNNAPSKREIA-QLKNQLEE 1721
Cdd:pfam01576 568 YDKLEKTKNRLQQELDDLLvDLDHQRQLVSnlEKKQKKfdqMLAEEKAISARYAEERDRAEAEAREKETRAlSLARALEE 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1722 SEFTCAAAVKARKAMEVEMEDLHLQIDDIAKaktaleeqlsrlqrekneiqsrleedqeDMNELMKKHKAAVAQASRDLA 1801
Cdd:pfam01576 648 ALEAKEELERTNKQLRAEMEDLVSSKDDVGK----------------------------NVHELERSKRALEQQVEEMKT 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1802 QMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQE--AKIRELETRLEFERTQvkRLESLASRLKENM 1879
Cdd:pfam01576 700 QLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQlvKQVRELEAELEDERKQ--RAQAVAAKKKLEL 777
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 1880 EKLTEERDQRTAAENREK--EQNKRLQRQLRDTKEEMGE--LARKEAEASRKkhELEMDLESLEAANQSLQADL 1949
Cdd:pfam01576 778 DLKELEAQIDAANKGREEavKQLKKLQAQMKDLQRELEEarASRDEILAQSK--ESEKKLKNLEAELLQLQEDL 849
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
440-887 |
2.87e-28 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 123.86 E-value: 2.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMF-------KGCRREDMAPHIYAVAQTAYRAMLMSRQD 511
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPyKPLKELYDQDVMNVYlhkksnsAASAAPFPKAHIYDIANMAYKNMRGKLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 512 QSVILLGSSGSGKTTSCQHLVQYLATIAGTSgNKVFSVEKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQ----- 586
Cdd:cd14884 82 QTIVVSGHSGSGKTENCKFLFKYFHYIQTDS-QMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 587 ----AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLL-ACADgtlrTELHLNHLAEN-NVFGIVPLAK--------- 651
Cdd:cd14884 161 knmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLrGLSD----EDLARRNLVRNcGVYGLLNPDEshqkrsvkg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 652 ------------PEEKQKAAQQFSKLQTAMKVLGISPDEQKACWLILAAIYHLGaagatkeapeeqaeaaeagrkqfarh 719
Cdd:cd14884 237 tlrlgsdsldpsEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLG-------------------------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 720 EWAQKAAY-LLGCSLEELSSAIfkhqhKGCTLQRSTSFRQGPEEsslgdgtgpKLTALECLEGMASGLYSELFTLLVSLV 798
Cdd:cd14884 291 NRAYKAAAeCLQIEEEDLENVI-----KYKNIRVSHEVIRTERR---------KENATSTRDTLIKFIYKKLFNKIIEDI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 799 NRALKSSQHSLCSM------------MIVDTPGFQnpeqggSARGASFEELCHNYAQDRLQRLFHERTFVQELERYKEEN 866
Cdd:cd14884 357 NRNVLKCKEKDESDnediysineaiiSILDIYGFE------ELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYAREN 430
|
490 500
....*....|....*....|.
gi 1239919865 867 IeLAFDDLEPATDDSVAAVDQ 887
Cdd:cd14884 431 I-ICCSDVAPSYSDTLIFIAK 450
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1282-1966 |
8.86e-28 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 123.36 E-value: 8.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1282 QIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERntgesasqlldaeaAERLRAEKEMKELQTQYD 1361
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESER--------------AARNKAEKQRRDLGEELE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1362 ALK------------KQMEVMEMEVMEARLIRAAEINGEVDDDDTGgEWRLKYERAMRE--------------VDFTKKR 1415
Cdd:pfam01576 303 ALKteledtldttaaQQELRSKREQEVTELKKALEEETRSHEAQLQ-EMRQKHTQALEElteqleqakrnkanLEKAKQA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1416 LQQEFED-----------KLEVEQQNKRqLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELE 1484
Cdd:pfam01576 382 LESENAElqaelrtlqqaKQDSEHKRKK-LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1485 KKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASL 1564
Cdd:pfam01576 461 KDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1565 AKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMER--MRQTHSKEVESRDEEVeearqscQKKLKQMevqL 1642
Cdd:pfam01576 541 EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDllVDLDHQRQLVSNLEKK-------QKKFDQM---L 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1643 EEE-------YEDKQKVLREKRELESKLTTLSeqvsqRDLESEKRLRKDLKRT-KALLADAQIML---DHLKNNA----P 1707
Cdd:pfam01576 611 AEEkaisaryAEERDRAEAEAREKETRALSLA-----RALEEALEAKEELERTnKQLRAEMEDLVsskDDVGKNVheleR 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1708 SKR----EIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQID-DIAKAKTALEEQLSRLQREKNEIQSRLEEDQedm 1782
Cdd:pfam01576 686 SKRaleqQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFErDLQARDEQGEEKRRQLVKQVRELEAELEDER--- 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1783 nelmKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLeQSMVDKSLVSRQEAKIRELETRlefer 1862
Cdd:pfam01576 763 ----KQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL-QRELEEARASRDEILAQSKESE----- 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1863 tqvKRLESLASRLKENMEKL-TEERDQRTAAENREkeqnkrlqrqlrdtkeemgELARKEAEASRKKHELEMDLESLEAa 1941
Cdd:pfam01576 833 ---KKLKNLEAELLQLQEDLaASERARRQAQQERD-------------------ELADEIASGASGKSALQDEKRRLEA- 889
|
730 740
....*....|....*....|....*
gi 1239919865 1942 nqslqadlklafkRIGDLQAAIEDE 1966
Cdd:pfam01576 890 -------------RIAQLEEELEEE 901
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1274-1889 |
3.76e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 121.70 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1274 IEVQLSEEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRAEKEM 1353
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1354 KELQTQYDALKKQMEVMEMEVMEARL-IRAAEINGEVDDDDTGGEWRLKYERAMREVDFTKKRLQQEFEDK---LEVEQQ 1429
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNeIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELeeeLEELQE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1430 NKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAE---LQDTKLHLEGQQ--VRNHELEKKQR-----------RFDSE 1493
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARldsLERLQENLEGFSegVKALLKNQSGLsgilgvlseliSVDEG 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1494 LSQAHEEAQREKLQR----------------EKLQREKDTLLAEAFSLKQQLEEKDMDI-------AGFTQKVVSLEAEL 1550
Cdd:TIGR02168 535 YEAAIEAALGGRLQAvvvenlnaakkaiaflKQNELGRVTFLPLDSIKGTEIQGNDREIlkniegfLGVAKDLVKFDPKL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1551 QD--------------------------------------------ISSQESKDEASLAKVKKQLRDLEAKVKDQEEELD 1586
Cdd:TIGR02168 615 RKalsyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKIA 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1587 EQAGTIQMLEQAKLRLEMEME-------RMRQTHS------KEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVL 1653
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEqlrkeleELSRQISalrkdlARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1654 REKRELESKLTTLSEQV--SQRDLESEKR----LRKDLKRTKALLADAQIMLDHLKNNAPSK-REIAQLKNQLEESEftc 1726
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIeqLKEELKALREaldeLRAELTLLNEEAANLRERLESLERRIAATeRRLEDLEEQIEELS--- 851
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1727 aaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDL 1806
Cdd:TIGR02168 852 ----EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1807 QAQLEEANKEKQELQEKL-----------QALQSQVEFLEQSMVDKslVSRQEAKI--------------RELETRLEFE 1861
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLseeysltleeaEALENKIEDDEEEARRR--LKRLENKIkelgpvnlaaieeyEELKERYDFL 1005
|
730 740
....*....|....*....|....*...
gi 1239919865 1862 RTQVKRLESLASRLKENMEKLTEERDQR 1889
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1275-1904 |
7.61e-27 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 119.74 E-value: 7.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLS--EEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRAE-- 1350
Cdd:TIGR04523 123 EVELNklEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEll 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1351 --------KEMKELQTQYDALKKQMEVMEMEVMEarliRAAEINGEVDdddtggewrlkyeramrEVDFTKKRLQQefed 1422
Cdd:TIGR04523 203 lsnlkkkiQKNKSLESQISELKKQNNQLKDNIEK----KQQEINEKTT-----------------EISNTQTQLNQ---- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1423 kLEVEQQN-KRQLERRlgdlQADIDESQRALQQLKKKCQRLTAELQDtkLHLEGQQVRNHEL-------EKKQRRFDSEL 1494
Cdd:TIGR04523 258 -LKDEQNKiKKQLSEK----QKELEQNNKKIKELEKQLNQLKSEISD--LNNQKEQDWNKELkselknqEKKLEEIQNQI 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1495 SQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKdmdiagftqkvvslEAELQDISSQESKDEASLAKVKKQLRDL 1574
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK--------------QNEIEKLKKENQSYKQEIKNLESQINDL 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1575 EAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHS------KEVESRD-------EEVEEARQSCQKKLKQMEVQ 1641
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseiKDLTNQDsvkeliiKNLDNTRESLETQLKVLSRS 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1642 ---LEEEYEDKQKVLREKrelESKLTTLSEQVSQrdleSEKRLrKDLKRTKALLADAQIMLDHLKNNApsKREIAQLKNQ 1718
Cdd:TIGR04523 477 inkIKQNLEQKQKELKSK---EKELKKLNEEKKE----LEEKV-KDLTKKISSLKEKIEKLESEKKEK--ESKISDLEDE 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1719 LEESEFTcaaavkarkamevemedlhLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASR 1798
Cdd:TIGR04523 547 LNKDDFE-------------------LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1799 DLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEA--KIRELETRL-EFERTQVKRLE 1869
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVkqiketIKEIRNKWPEIikKIKESKTKIdDIIELMKDWLK 687
|
650 660 670
....*....|....*....|....*....|....*..
gi 1239919865 1870 SLASRLKENMEKLTEERDQRTAAENRE--KEQNKRLQ 1904
Cdd:TIGR04523 688 ELSLHYKKYITRMIRIKDLPKLEEKYKeiEKELKKLD 724
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
441-1076 |
1.62e-26 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 117.78 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 441 VLHTLRQRYGASLLHTYAGPSLLVLSP---------------RGAPAVysekvmhmfkgcrrEDMAPHIYAVAQTAYRAM 505
Cdd:cd14876 3 VLDFLKHRYLKNQIYTTADPLLVAINPfkdlgnatdewirkyRDAPDL--------------TKLPPHVFYTARRALENL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 506 LMSRQDQSVILLGSSGSGKTTSCQHLVQYLAtiAGTSGNKVFSVEKW-QALYSLLEAFGNSPTIMNGNATRFSQILSLDF 584
Cdd:cd14876 69 HGVNKSQTIIVSGESGAGKTEATKQIMRYFA--SAKSGNMDLRIQTAiMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 585 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENN--------VFGIVPLAkpeekq 656
Cdd:cd14876 147 ASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKflnpkcldVPGIDDVA------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 657 kaaqQFSKLQTAMKVLGISPDEQKACWLILAAIYHLG---AAGATKEAPEEQAEAAEAGRKQFarhewaQKAAYLLGCSL 733
Cdd:cd14876 221 ----DFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGnvkITGKTEQGVDDAAAISNESLEVF------KEACSLLFLDP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 734 EELSSAIF-KHQHKGCtlQRSTSFRQGPEESSLgdgtgpKLTaleclegMASGLYSELFTLLVSLVNRALKSSQHSLCSM 812
Cdd:cd14876 291 EALKRELTvKVTKAGG--QEIEGRWTKDDAEML------KLS-------LAKAMYDKLFLWIIRNLNSTIEPPGGFKNFM 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 813 MIVDTPGFQNPEQGgsargaSFEELCHNYAQDRLQRLFHERTFVQELERYKEENI---ELAFDDLEPATD------DSVA 883
Cdd:cd14876 356 GMLDIFGFEVFKNN------SLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIptaELEYTSNAEVIDvlcgkgKSVL 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 884 AV--DQAshqslvrsLArtdeargllwlleeealvPGATEDALLERLFSyygpQEGDKKGQRPLLRSSKpHHFLLGHSHG 961
Cdd:cd14876 430 SIleDQC--------LA------------------PGGSDEKFVSACVS----KLKSNGKFKPAKVDSN-INFIVVHTIG 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 962 TnwVEYNVSGWLSYTKqNPATQNAPRLLQDSQKKIISNLFlgraGGTTVLSGSIA-GLEGGSQLalrratsMRktfttgm 1040
Cdd:cd14876 479 D--IQYNAEGFLFKNK-DVLRAELVEVVQASTNPVVKALF----EGVVVEKGKIAkGSLIGSQF-------LK------- 537
|
650 660 670
....*....|....*....|....*....|....*.
gi 1239919865 1041 aavkkkslciqiklQVDALIDTIKKSKLHFVHCFLP 1076
Cdd:cd14876 538 --------------QLESLMGLINSTEPHFIRCIKP 559
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
439-1001 |
1.87e-26 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 117.81 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 439 SSVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYsekvMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLatIAGTSGNKVFSVEKWQALYsLLEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASASIQTM 598
Cdd:cd14937 77 ESGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNF-ILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 599 LLEKLRVARRPASEATFNVFYYLLACADGTL------RTELHLNHLAENNVfgIVPlakpeeKQKAAQQFSKLQTAMKVL 672
Cdd:cd14937 154 LLENIRVVSQEEEERGYHIFYQIFNGMSQELknkykiRSENEYKYIVNKNV--VIP------EIDDAKDFGNLMISFDKM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 673 GISpDEQKACWLILAAIYHLGAAGATKEAPEEQAEAAEAGRKQFarhEWAQKAAYLLGCSLEELssaifkhqhKGCTLQR 752
Cdd:cd14937 226 NMH-DMKDDLFLTLSGLLLLGNVEYQEIEKGGKTNCSELDKNNL---ELVNEISNLLGINYENL---------KDCLVFT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 753 STSFRQGPEESSLGDGtgpklTALECLEGMASGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsarga 832
Cdd:cd14937 293 EKTIANQKIEIPLSVE-----ESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKN------ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 833 SFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELafDDLEPATDDSVaaVDQASHQSLVRSLARtDEARGllwllee 912
Cdd:cd14937 362 SLEQLLINIANEEIHSIYLYIVYEKETELYKAEDILI--ESVKYTTNESI--IDLLRGKTSIISILE-DSCLG------- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 913 ealvPGATEDALLERLFSYYGPQEGDKKGQRPLLRSskphhFLLGHShgTNWVEYNVSGWLSYTKQNPATqNAPRLLQDS 992
Cdd:cd14937 430 ----PVKNDESIVSVYTNKFSKHEKYASTKKDINKN-----FVIKHT--VSDVTYTITNFISKNKDILPS-NIVRLLKVS 497
|
....*....
gi 1239919865 993 QKKIISNLF 1001
Cdd:cd14937 498 NNKLVRSLY 506
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1424-2004 |
4.40e-25 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 113.96 E-value: 4.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1424 LEVEQQNK-RQLERRLGDLQADIDESQRALQQL-------KKKCQRLTAELQDtkLHLEGQQVRNHELEKKQR--RFDSE 1493
Cdd:TIGR04523 27 IANKQDTEeKQLEKKLKTIKNELKNKEKELKNLdknlnkdEEKINNSNNKIKI--LEQQIKDLNDKLKKNKDKinKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1494 LSQAHEEAQREKLQREKLQREKDtllaeafSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKdeaslakVKKQLRD 1573
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELN-------KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1574 LEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEM---ERMRQTHsKEVESRDEEVEEARQSCQKKLKQmevqLEEEYEDKQ 1650
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKN-KSLESQISELKKQNNQLKDNIEK----KQQEINEKT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1651 KVLREKrelESKLTTLSEQvSQRDLESEKRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESeftCAAAV 1730
Cdd:TIGR04523 246 TEISNT---QTQLNQLKDE-QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS------EISDLNNQKEQD---WNKEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1731 KAR-KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNE------LMKKHKAAVAQASRDL-AQ 1802
Cdd:TIGR04523 313 KSElKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEkqneieKLKKENQSYKQEIKNLeSQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1803 MNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQ--------------EAKIRELETRLEFERTQVKR 1867
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlKETIIKNnseikdltnqdsvkELIIKNLDNTRESLETQLKV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1868 LESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQA 1947
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1948 DLKLAF--KRIGDLQAAIEdemESDENEDLITSLQDmvTKYQKRKNKPEGDSDVDSELE 2004
Cdd:TIGR04523 553 ELKKENleKEIDEKNKEIE---ELKQTQKSLKKKQE--EKQELIDQKEKEKKDLIKEIE 606
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1200-1989 |
5.81e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 114.85 E-value: 5.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1200 RAGTLARLEEQRDEQTSRNLTLF---QAACRGYLARQHFKKKKIQDlAIRCVQ----KNIKKNKGVKDWAWWKLFTTVRP 1272
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIArkaEDARKAEEARKAEDAKKAEA-ARKAEEvrkaEELRKAEDARKAEAARKAEEERK 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1273 LIEVQLSEEQIRS----KDEEIQQLRSKLEKVEKERNE---LRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAE 1345
Cdd:PTZ00121 1214 AEEARKAEDAKKAeavkKAEEAKKDAEEAKKAEEERNNeeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1346 RLRAEKEMKELqtqyDALKKQMEVMEMEVMEARliRAAEINGEVDDDDTGGEWRLKYERAMREVDFTKKRLQQEFEDKLE 1425
Cdd:PTZ00121 1294 EAKKAEEKKKA----DEAKKKAEEAKKADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1426 VEQQNKRQLERRLGDLQADIDESQRAlQQLKKKCQRLTAELQDTKlHLEGQQVRNHELEKK--QRRFDSELSQAHEEAQR 1503
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKaeEKKKADEAKKKAEEAKK 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1504 EKLQREKLQREKdtllaEAFSLKQQLEEKDmdiagftqkvvsleaelqdiSSQESKDEASLAKVKKQLRDLEAKVKDQEE 1583
Cdd:PTZ00121 1446 ADEAKKKAEEAK-----KAEEAKKKAEEAK--------------------KADEAKKKAEEAKKADEAKKKAEEAKKKAD 1500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1584 ELDEQAGTIQMLEQAKlrlEMEMERMRQTHSKEVESRdeEVEEARQSCQKKlKQMEVQLEEEY---EDKQKVLREKRELE 1660
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAK---KAEEAKKADEAKKAEEAK--KADEAKKAEEKK-KADELKKAEELkkaEEKKKAEEAKKAEE 1574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1661 SKLTTL-----SEQVSQRDLESEKRLRKDLKRTKALLA----DAQIMLDHLKNNAPSKREIAQLKNQLEES--------- 1722
Cdd:PTZ00121 1575 DKNMALrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkaeelkk 1654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1723 ---EFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTalEEQLSRLQREK---NEIQSRLEEDQEDMNELMKKHKAAVAQA 1796
Cdd:PTZ00121 1655 aeeENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA--AEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENKIKA 1732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1797 SRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTqVKRLESLASRLK 1876
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK-IKDIFDNFANII 1811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1877 E---------NMEKLTEERDQRTAA--ENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSL 1945
Cdd:PTZ00121 1812 EggkegnlviNDSKEMEDSAIKEVAdsKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1239919865 1946 QADLKlafkrigDLQAAIEDEMESDENEDLITSLQDmVTKYQKR 1989
Cdd:PTZ00121 1892 KIDKD-------DIEREIPNNNMAGKNNDIIDDKLD-KDEYIKR 1927
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1275-1973 |
2.76e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 112.54 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLSEEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRL--ETRISELTSELTDERNTgESASQLLDAEAAERLRAEKE 1352
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaeDARKAEEARKAEDAKRV-EIARKAEDARKAEEARKAED 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1353 MKELQTQYDALKKQMEVMEMEVMEARLIRAAEingevddddtggewrlKYERAMREVDFTKKRLQQEFEDKLEVEQQNKR 1432
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEELRKAEDARKAEAAR----------------KAEEERKAEEARKAEDAKKAEAVKKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1433 QLERRLGdlqadidESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKK--QRRFDSELSQAHEEAQREKLQREK 1510
Cdd:PTZ00121 1239 AEEAKKA-------EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1511 LQREKdtllAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-AKVKDQEEELDEQA 1589
Cdd:PTZ00121 1312 EEAKK----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkEEAKKKADAAKKKA 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1590 GTIQMLEQAKLRLEMEMERMRQTHSKEVESRdeEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQ 1669
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKADELKKAAAAKK--KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1670 VSQRDLESEKRLRKDLKR----TKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCA-AAVKARKAMEVEMEDLH 1744
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKkadeAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkKAEEAKKADEAKKAEEK 1545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1745 LQIDDIAKAktalEEQLSRLQREKNEIQSRLEEDQ-------EDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEK 1817
Cdd:PTZ00121 1546 KKADELKKA----EELKKAEEKKKAEEAKKAEEDKnmalrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1818 QELQEKLQALQSQVEFLEQSMVDKSlvsRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTAAENREK 1897
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEK---KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1898 EQNKRLQR-------------QLRDTKEE----MGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQ 1960
Cdd:PTZ00121 1699 EEAKKAEElkkkeaeekkkaeELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
730
....*....|...
gi 1239919865 1961 AAIEDEMESDENE 1973
Cdd:PTZ00121 1779 AVIEEELDEEDEK 1791
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1275-1888 |
2.91e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.95 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLSEEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRAEKEMK 1354
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1355 ELQTQYDALKKQmevmeMEVMEARLIRAAEingevddddtggewrlkyERAMREVDftkkrlQQEFEDKLEVEQQNKRQL 1434
Cdd:COG1196 320 ELEEELAELEEE-----LEELEEELEELEE------------------ELEEAEEE------LEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1435 ERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQRE 1514
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1515 KDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEAslAKVKKQLRDLEAKVKDQEEELDEQAGTIQM 1594
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE--AEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1595 LEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEyedkqKVLREKRELESKLTTLSEQVSQRD 1674
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL-----DKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1675 LESEKRLRKDLKRTKALLADAQIMLDHLKNNApsKREIAQLKNQLEESEFTcAAAVKARKAMEVEmedlhlQIDDIAKAK 1754
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLEAA--LRRAVTLAGRLREVTLE-GEGGSAGGSLTGG------SRRELLAAL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1755 TALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSqvEFL 1834
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE--EEA 752
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239919865 1835 EQSMVDKSLVSRQEAKIRELETRL------------EFERTQvKRLESLASRLKEnmekLTEERDQ 1888
Cdd:COG1196 753 LEELPEPPDLEELERELERLEREIealgpvnllaieEYEELE-ERYDFLSEQRED----LEEARET 813
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1270-1997 |
3.74e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 108.69 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1270 VRPLIEVQLSEEQIRSKDEEIQQLRSKLEKVEKerneLRLSNDRLETRISELTSELTDERNTGE--SASQLLDAEAAERL 1347
Cdd:PTZ00121 1133 ARKAEDARKAEEARKAEDAKRVEIARKAEDARK----AEEARKAEDAKKAEAARKAEEVRKAEElrKAEDARKAEAARKA 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1348 RAEKEMKELQTQYDALK----KQMEVMEMEVMEARliRAAEINGEVDDDDTGGEWRLKYERAMREVDFTKKRLQQEF--- 1420
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKaeavKKAEEAKKDAEEAK--KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELkka 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1421 EDKLEVEQQNKRQLERRLGDLQADIDESQRAlQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEE 1500
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1501 AQREKLQREKLQREKDTLLAEAFSLKQQLEEKDmdiagftqkvvslEAELQDISSQESKDEASLAKVKKQLRDlEAKVKD 1580
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK-------------KAEEDKKKADELKKAAAAKKKADEAKK-KAEEKK 1431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1581 QEEELDEQAGTIQMLEQAKLRLEmEMERMRQTHSKEVESRdeEVEEARQSCQKKLKQMEVQLE-EEYEDKQKVLREKREL 1659
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAE-EAKKAEEAKKKAEEAK--KADEAKKKAEEAKKADEAKKKaEEAKKKADEAKKAAEA 1508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1660 ESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQIMLDHLKN-----NAPSKREIAQLKNQLEESEFTCAAAVKARK 1734
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKaeelkKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1735 AMEVEMEDLHLQIDDIAK-----AKTALEEQLSRLQREKNE--------IQSRLEEDQEDMNELMKKHKAAVAQASRDLA 1801
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKmkaeeAKKAEEAKIKAEELKKAEeekkkveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1802 QMNDLQAQLEEANKEKQELQEKLQALQSQVEflEQSMVDKsLVSRQEAKIRELEtrlefertQVKRLESLaSRLKENMEK 1881
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAE--EAKKAEE-LKKKEAEEKKKAE--------ELKKAEEE-NKIKAEEAK 1736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1882 LTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQaDLKLAFKRI----- 1956
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK-DIFDNFANIieggk 1815
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1239919865 1957 -GDLQAAIEDEMESDENEDLITSLQ------DMVTKYQKRKNKPEGDS 1997
Cdd:PTZ00121 1816 eGNLVINDSKEMEDSAIKEVADSKNmqleeaDAFEKHKFNKNNENGED 1863
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1275-1857 |
4.05e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.10 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLSEEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRAEKEMK 1354
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1355 ELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDTGGEWRLKYERAmREVDFTKKRLQQEFEDKLEVEQQNKRQL 1434
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL-AEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1435 ERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKK--QRRFDSELSQAHEEAQREKLQREKLQ 1512
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELlaELLEEAALLEAALAELLEELAEAAAR 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1513 REKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASL-AKVKKQLRDLEAKVKDQEEELDEQAG- 1590
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaAALQNIVVEDDEVAAAAIEYLKAAKAg 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1591 --TIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSE 1668
Cdd:COG1196 573 raTFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1669 QVSQRDLESEKRLRKDLKRTKALLADAQIMLDhlknnapsKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQID 1748
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEEL--------AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1749 DIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMN--DLQAqLEEAnkekQELQEKLQA 1826
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvNLLA-IEEY----EELEERYDF 799
|
570 580 590
....*....|....*....|....*....|.
gi 1239919865 1827 LQSQVEFLEQSMvdKSLVSRqeakIRELETR 1857
Cdd:COG1196 800 LSEQREDLEEAR--ETLEEA----IEEIDRE 824
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1499-2018 |
2.22e-22 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 105.53 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1499 EEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKdmdiagftQKVVSLEAELQD-ISSQESKDEASLAKVKK---QLRDL 1574
Cdd:PRK03918 148 EKVVRQILGLDDYENAYKNLGEVIKEIKRRIERL--------EKFIKRTENIEElIKEKEKELEEVLREINEissELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1575 EAKVKDQE---EELDEQAGTIQMLEQAKLRLEMEM----ERMRQTHS--KEVESRDEEVEEARqscqKKLKQMEvQLEEE 1645
Cdd:PRK03918 220 REELEKLEkevKELEELKEEIEELEKELESLEGSKrkleEKIRELEEriEELKKEIEELEEKV----KELKELK-EKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1646 Y----EDKQKVLREKRELESKLTTLSEQVS--QRDLESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQL 1719
Cdd:PRK03918 295 YiklsEFYEEYLDELREIEKRLSRLEEEINgiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1720 EEseftcaaaVKARKAMEvEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELmKKHKAAVAQASRD 1799
Cdd:PRK03918 375 ER--------LKKRLTGL-TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL-KKAKGKCPVCGRE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1800 LAQ------MNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEA---KIRELETRL------------ 1858
Cdd:PRK03918 445 LTEehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeQLKELEEKLkkynleelekka 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1859 -EFERT---------QVKRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQ----LRDTKEEMGELA---RKE 1921
Cdd:PRK03918 525 eEYEKLkekliklkgEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEpfyNEY 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1922 AEASRKKHELEMDLESLEaanqSLQADLKLAFKRIGDLQAAIE------DEMESDENEDLITSLQDmvtKYQKRKNKPEG 1995
Cdd:PRK03918 605 LELKDAEKELEREEKELK----KLEEELDKAFEELAETEKRLEelrkelEELEKKYSEEEYEELRE---EYLELSRELAG 677
|
570 580
....*....|....*....|...
gi 1239919865 1996 DSDVDSELEDRVDGVKSWLSKNK 2018
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLK 700
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
440-879 |
2.24e-22 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 104.79 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSP-RGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLG 518
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPlRYLPFLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 519 SSGSGKTTSCQHLVQYLATIAgtsgnkvFSVEKWQALYSL-----LEAFGNSPTIMNGNATRFSQILSLDFDQAGQVASA 593
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTD-------LSRSKYLRDYILesgiiLESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 594 SIQTMLLEKLRVARRPASEATFNVFYYLLAcadgtlrtelhlnhlaennvfGIVplakpeEKQKAAQQFSKLQTamkvlg 673
Cdd:cd14905 153 KLYSYFLDENRVTYQNKGERNFHIFYQFLK---------------------GIT------DEEKAAYQLGDINS------ 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 674 ispdeqkacwlilaaiYH-LGAAGATKEAPEEQAEAAEAGRKQFARHEWAQKAAYLLGCSLE---ELSSAIF-----KHQ 744
Cdd:cd14905 200 ----------------YHyLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSfiiILGNVTFfqkngKTE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 745 HKGCTLQRSTSFRQGPEESSL-----GDGTGPKLTALECLEGMASGLYSELFTLLVSLVNRALKSSQHSLcSMMIVDTPG 819
Cdd:cd14905 264 VKDRTLIESLSHNITFDSTKLeniliSDRSMPVNEAVENRDSLARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFG 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 820 FQNPEQGGsargasFEELCHNYAQDRLQRLFHERTFVQELERYKEENI----ELAFDDLEPATD 879
Cdd:cd14905 343 QESSQLNG------YEQFSINFLEERLQQIYLQTVLKQEQREYQTERIpwmtPISFKDNEESVE 400
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1396-1964 |
3.81e-22 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 104.87 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1396 GEWRLKYERAMREVDFTKKRLQQEFEDKLEVEQ------QNKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDT 1469
Cdd:pfam01576 29 KELEKKHQQLCEEKNALQEQLQAETELCAEAEEmrarlaARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1470 KLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREkdtllaeafslKQQLEEKdmdiagftqkvvslEAE 1549
Cdd:pfam01576 109 EEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKE-----------RKLLEER--------------ISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1550 LQDISSQESKDEASLAKVKKQlrdLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSkEVESRDEEVEEARQ 1629
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNK---HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA-ELQAQIAELRAQLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1630 SCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLseqvsQRDLESEKRLRKDLKRTK-----ALLADAQIMLDHLKN 1704
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISEL-----QEDLESERAARNKAEKQRrdlgeELEALKTELEDTLDT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1705 NAP-----SKR--EIAQLKNQLEESEFTCAAAVKA-RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLE 1776
Cdd:pfam01576 315 TAAqqelrSKReqEVTELKKALEEETRSHEAQLQEmRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1777 EDQEDMNELMKKHKAAVaqasrdlAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLeqsmvdKSLVSRQEAKIRELEt 1856
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLE-------GQLQELQARLSESERQRAELAEKLSKLQSELESV------SSLLNEAEGKNIKLS- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1857 rlefertqvKRLESLASRLKENMEKLTEERDQRTAAENR----EKEQNKrLQRQLRDTKEEMGELAR-------KEAEAS 1925
Cdd:pfam01576 461 ---------KDVSSLESQLQDTQELLQEETRQKLNLSTRlrqlEDERNS-LQEQLEEEEEAKRNVERqlstlqaQLSDMK 530
|
570 580 590
....*....|....*....|....*....|....*....
gi 1239919865 1926 RKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1964
Cdd:pfam01576 531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1280-1977 |
7.06e-22 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 103.65 E-value: 7.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1280 EEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSE---LTDERNTGESASQLLDAEAAERlrAEKEMKel 1356
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdLIKENNATRHLCNLLKETCARS--AEKTKK-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1357 qTQYDALKKQMEVMEMEVMEARLIRAAEingevddddtggEWRLKYERAMREVDFtkkRLQQEFEDKLEVEQQNKRQler 1436
Cdd:pfam05483 174 -YEYEREETRQVYMDLNNNIEKMILAFE------------ELRVQAENARLEMHF---KLKEDHEKIQHLEEEYKKE--- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1437 rlgdlqadIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREkd 1516
Cdd:pfam05483 235 --------INDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMS-- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1517 tlLAEAFSLKQQLEEkDMDIAGFTQKVVSLEAELQDISSQESKDEASL--AKVKKQLRDLEAKVKDQEEELDEQAGTIQM 1594
Cdd:pfam05483 305 --LQRSMSTQKALEE-DLQIATKTICQLTEEKEAQMEELNKAKAAHSFvvTEFEATTCSLEELLRTEQQRLEKNEDQLKI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1595 LEQAKLRLEMEMERMRQ-THSKEVESRD-EEVEEARQSCQKKLKQMEvQLEEEYEDKQKVL------REKR----ELESK 1662
Cdd:pfam05483 382 ITMELQKKSSELEEMTKfKNNKEVELEElKKILAEDEKLLDEKKQFE-KIAEELKGKEQELifllqaREKEihdlEIQLT 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1663 LTTLSEQVSQRDLESEK-RLRKD-LKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaaaVKARKAMEvem 1740
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKtELEKEkLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED--------IINCKKQE--- 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1741 EDLHLQIDDIAKAKTALEEQLSRLQRE----KNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKE 1816
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDELESVREEfiqkGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1817 KQELQEKLQALQsqveflEQSMVDKSLVSRQEAKIRELEtrLEFERTQVKRLESLASRLKE------NMEKLTEERDQRT 1890
Cdd:pfam05483 610 IEELHQENKALK------KKGSAENKQLNAYEIKVNKLE--LELASAKQKFEEIIDNYQKEiedkkiSEEKLLEEVEKAK 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1891 A----AENREKEQNKRLQRQL------------------RDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQAD 1948
Cdd:pfam05483 682 AiadeAVKLQKEIDKRCQHKIaemvalmekhkhqydkiiEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQ 761
|
730 740
....*....|....*....|....*....
gi 1239919865 1949 LKLAFKRIGDLQaaiedeMESDENEDLIT 1977
Cdd:pfam05483 762 LEIEKEEKEKLK------MEAKENTAILK 784
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1275-1939 |
1.03e-21 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 103.18 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLSEEQIRSKDEEIQQLRSKLEKVEKERNE----LRLSNDR---LETRISELTSELTDERNTGESasqlLDAEA---A 1344
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKdeekINNSNNKikiLEQQIKDLNDKLKKNKDKINK----LNSDLskiN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1345 ERLRAEKEMK-ELQTQYDALKKQMEVMEMEVmearliraAEINGEVDDDDTggewrlkyeramrEVDFTKKRLQQEFEDK 1423
Cdd:TIGR04523 110 SEIKNDKEQKnKLEVELNKLEKQKKENKKNI--------DKFLTEIKKKEK-------------ELEKLNNKYNDLKKQK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1424 LEVEQQnKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLhLEGQQVrnhELEKKQRRFDSELSQAHEEAQR 1503
Cdd:TIGR04523 169 EELENE-LNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKS-LESQIS---ELKKQNNQLKDNIEKKQQEINE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1504 EKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQES-----KDEASLAKVKKQLRDLEAKV 1578
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1579 KDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSkeveSRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKVLREKRE 1658
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEQISQLKKELTNSESENS----EKQRELEEK----QNEIEKLKKENQSYKQEIKNLESQIND 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1659 LESKLTTLSEQVSQRD-----LESEKRLRkdLKRTKALLADaqimldhlknNAPSKREIAQLKNQLEESEftcaaavkar 1733
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDeqikkLQQEKELL--EKEIERLKET----------IIKNNSEIKDLTNQDSVKE---------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1734 kamevemedlhLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEdmnELMKKHKaavaqasrdlaqmndlqaQLEEA 1813
Cdd:TIGR04523 454 -----------LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK---ELKSKEK------------------ELKKL 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1814 NKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFERTQVKR--LESLASRLKENMEKLTEERDQRT 1890
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKlESEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLK 581
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1891 AAENR------EKEQNKR---------------LQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLE 1939
Cdd:TIGR04523 582 KKQEEkqelidQKEKEKKdlikeieekekkissLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
470-588 |
8.57e-21 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 91.64 E-value: 8.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 470 APAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSVILLGSSGSGKTTSCQHLVQYLATIAGTSGNK---- 545
Cdd:cd01363 11 LPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKgete 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1239919865 546 ---------VFSVEKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQAG 588
Cdd:cd01363 91 gwvylteitVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAG 142
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1419-2005 |
8.77e-21 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 100.53 E-value: 8.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1419 EFEDKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKK------KCQRLTAELQDTKLHLEGQQVRNHELEKKQrrFDS 1492
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRerekaeRYQALLKEKREYEGYELLKEKEALERQKEA--IER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1493 ELSQAheEAQREKLQREKLQREKDtlLAEAFSLKQQLEEKDMDIAGFTQkvVSLEAELQDISSQESKDEASLAKVKKQLR 1572
Cdd:TIGR02169 245 QLASL--EEELEKLTEEISELEKR--LEEIEQLLEELNKKIKDLGEEEQ--LRVKEKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1573 DLEAKVKDQEEELDEQAGTIQML----EQAKLRLEMEMERM--RQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEY 1646
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELereiEEERKRRDKLTEEYaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1647 EDKQKVLREKRELESKLTTLSEQVSQ------------RDLESE--------KRLRKDLKRTKALLADAQIMLDHLKNN- 1705
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADlnaaiagieakiNELEEEkedkaleiKKQEWKLEQLAADLSKYEQELYDLKEEy 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1706 -------APSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAK----TALE---------------- 1758
Cdd:TIGR02169 479 drvekelSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGeryaTAIEvaagnrlnnvvvedda 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1759 ---EQLSRLQREK---------NEIQ------SRLEEDQE-----DMNELMKKHKAAVAQASRDLAQMNDLQA------- 1808
Cdd:TIGR02169 559 vakEAIELLKRRKagratflplNKMRderrdlSILSEDGVigfavDLVEFDPKYEPAFKYVFGDTLVVEDIEAarrlmgk 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1809 ------------------------------------QLEEANKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKI 1851
Cdd:TIGR02169 639 yrmvtlegelfeksgamtggsraprggilfsrsepaELQRLRERLEGLKRELSSLQSELRRIENRLDElSQELSDASRKI 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1852 RELETRLEF----ERTQVKRLESLASRLKENMEKLTEERDQRTAAENREKEqnkrLQRQLRDTKEEMGELARK------- 1920
Cdd:TIGR02169 719 GEIEKEIEQleqeEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE----LEEDLHKLEEALNDLEARlshsrip 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1921 ----EAEASRKKH-ELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED-----EMESDENEDLITSLQDMVTKYQKRK 1990
Cdd:TIGR02169 795 eiqaELSKLEEEVsRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDlkeqiKSIEKEIENLNGKKEELEEELEELE 874
|
730
....*....|....*
gi 1239919865 1991 NKPEgdsDVDSELED 2005
Cdd:TIGR02169 875 AALR---DLESRLGD 886
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1289-1913 |
1.09e-20 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 100.43 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1289 EIQQLRSKLEK--VEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAeAAERLRAEKEM-------KELQTQ 1359
Cdd:TIGR00618 197 ELLTLRSQLLTlcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREA-QEEQLKKQQLLkqlrariEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1360 YDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDTGGEWRLKYERAMREVDFTKKR---------------LQQEFEDKL 1424
Cdd:TIGR00618 276 EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAahvkqqssieeqrrlLQTLHSQEI 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1425 EVEQQNKRQ------------LERRLGDLQADIDESQRALQQLKKKCQRLTAE-------------LQDTKLHLEGQQVR 1479
Cdd:TIGR00618 356 HIRDAHEVAtsireiscqqhtLTQHIHTLQQQKTTLTQKLQSLCKELDILQREqatidtrtsafrdLQGQLAHAKKQQEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1480 NHELEKKQRRFDSElsQAHEEAQREKLQREKLQ--REKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISS-- 1555
Cdd:TIGR00618 436 QQRYAELCAAAITC--TAQCEKLEKIHLQESAQslKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhp 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1556 -QESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRD---EEVEEARQSC 1631
Cdd:TIGR00618 514 nPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNrskEDIPNLQNIT 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1632 QKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKRLRK-DLKRTKALLADAQIMLDHLKNNAPSKR 1710
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtALHALQLTLTQERVREHALSIRVLPKE 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1711 EIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHK 1790
Cdd:TIGR00618 674 LLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1791 AAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFErTQVKRLES 1870
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCE-TLVQEEEQ 832
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1239919865 1871 LASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQLRDTKEE 1913
Cdd:TIGR00618 833 FLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1271-2004 |
1.88e-20 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 99.66 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1271 RPLIEVQLSEEQIRSKDEEIQqlRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRAE 1350
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELK--LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1351 KEMKELQTQYDALKKQMEVMEmevmeaRLIRAAEINGEVDDDDTGGEwrlkyERAMREVDFTKKRLQQEFEDKLEVEQQN 1430
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKEN------KEEEKEKKLQEEELKLLAKE-----EEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1431 KRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREK 1510
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1511 LQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAG 1590
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1591 TIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVE--EARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSE 1668
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKdgVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1669 QVSQRDLESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLH---- 1744
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKesak 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1745 -----------LQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEA 1813
Cdd:pfam02463 643 akesglrkgvsLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1814 NKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTAAE 1893
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1894 NRE--KEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDE 1971
Cdd:pfam02463 803 LRAleEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ 882
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1239919865 1972 NEDLITS---------LQDMVTKYQkRKNKPEGDSDVDSELE 2004
Cdd:pfam02463 883 KLKDELEskeekekeeKKELEEESQ-KLNLLEEKENEIEERI 923
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1380-1959 |
4.97e-20 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 97.83 E-value: 4.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1380 IRAAEINGEVDDDD---------TGGEwrlKYERA-------MREVDFTKKRLQQEFEDKLEVEQQNKRQlERRLGDLQA 1443
Cdd:PRK03918 132 IRQGEIDAILESDEsrekvvrqiLGLD---DYENAyknlgevIKEIKRRIERLEKFIKRTENIEELIKEK-EKELEEVLR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1444 DIDESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRRFDSELSQAhEEAQREKLQREKLQREKDTLLA 1520
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIREL-EERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1521 EAfslkQQLEEKDMDIAGFTQKVVSleaELQDISSQESKDEASLAKVKKQLRDLE---AKVKDQEEELDEQAGTIQMLEQ 1597
Cdd:PRK03918 287 EL----KEKAEEYIKLSEFYEEYLD---ELREIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1598 AKLRLEMEMERMRQTHSKEVESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQrdLES 1677
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGLTPEKL----EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE--LKK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1678 EKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcAAAVKARKAMEVEMEDLHLQidDIAKAKTAL 1757
Cdd:PRK03918 434 AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR---KELRELEKVLKKESELIKLK--ELAEQLKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1758 EEQLSRLQREKNEiqsRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQS 1837
Cdd:PRK03918 509 EEKLKKYNLEELE---KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1838 MVD------KSL---------VSRQEAKIRELETRLEFERTQV-----------KRLESLASRLKENMEKLTEERDQRTA 1891
Cdd:PRK03918 586 SVEeleerlKELepfyneyleLKDAEKELEREEKELKKLEEELdkafeelaeteKRLEELRKELEELEKKYSEEEYEELR 665
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1892 AENREKEqnKRLQRqLRDTKEEMGELaRKEAEASRKKheLEMDLESLEAANQSLQaDLKLAFKRIGDL 1959
Cdd:PRK03918 666 EEYLELS--RELAG-LRAELEELEKR-REEIKKTLEK--LKEELEEREKAKKELE-KLEKALERVEEL 726
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1279-1926 |
5.37e-20 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 97.83 E-value: 5.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1279 SEEQIrskDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELtderntgesasqlldaeaaerlraeKEMKELQT 1358
Cdd:PRK03918 187 RTENI---EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-------------------------KELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1359 QYDALKKQmevmemevmearliraaeingevddddtggewrlkyeramrevdftkkrlqqefedkLEVEQQNKRQLERRL 1438
Cdd:PRK03918 239 EIEELEKE---------------------------------------------------------LESLEGSKRKLEEKI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1439 GDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNhELEKKQRRFDSELSQAHEEAQ--REKLQ-REKLQREK 1515
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINgiEERIKeLEEKEERL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1516 DTLLAEAFSLKQQLEEKDMDIAGFtQKVVSLEAELQDISSQESkdEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQML 1595
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRLT--GLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1596 EQAKLRLEMEMERMRQTHSK----EVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVS 1671
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1672 QRDLESE-KRLRKDLKrtkalladaQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDI 1750
Cdd:PRK03918 498 LKELAEQlKELEEKLK---------KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEL 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1751 AKAKTALEEQLSRLQREK-NEIQSRLEEDQEDMNELMKKhKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQS 1829
Cdd:PRK03918 569 EEELAELLKELEELGFESvEELEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1830 QVEFLEQSMVDKSLvSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTAAenreKEQNKRLQRQLRD 1909
Cdd:PRK03918 648 ELEELEKKYSEEEY-EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA----KKELEKLEKALER 722
|
650
....*....|....*..
gi 1239919865 1910 TKEEMGELARKEAEASR 1926
Cdd:PRK03918 723 VEELREKVKKYKALLKE 739
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1549-1925 |
1.51e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 96.68 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1549 ELQDISSQESKDEASLAK---VKKQLRDLEAKVkdqeEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVE 1625
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEEleeVEENIERLDLII----DEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1626 EARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQimldhlknn 1705
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLE--------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1706 apskREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNEL 1785
Cdd:TIGR02169 308 ----RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1786 MKKHKAAVaqasrdlAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFERTQV 1865
Cdd:TIGR02169 384 RDELKDYR-------EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI------EAKINELEEEKEDKALEI 450
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1866 KRLESLASRLKENMEKLTEERDQRtaaenreKEQNKRLQRQLRDTKEemgELARKEAEAS 1925
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKELSKLQR---ELAEAEAQAR 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1632-1988 |
3.15e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 95.51 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1632 QKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQrdLESEKRLRKDLKRTKALLadaqimldhlknnapSKRE 1711
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEK--AERYKELKAELRELELAL---------------LVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1712 IAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKA 1791
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1792 AVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEferTQVKRLESL 1871
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA------ELEELEAELEELESRLE---ELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1872 ASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKE-AEASRKKHELEMDLESLEAANQSLQADLK 1950
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1239919865 1951 LAFKRIGDLQAAIeDEMESDENE--DLITSLQDMVTKYQK 1988
Cdd:TIGR02168 465 ELREELEEAEQAL-DAAERELAQlqARLDSLERLQENLEG 503
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1274-2007 |
5.53e-19 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 94.80 E-value: 5.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1274 IEVQLSEEQIRSKDEEiQQLRSKLEKVEKERNELRLSNDRLETRISELTSE---LTDERNTgESASQ----------LLD 1340
Cdd:pfam15921 76 IERVLEEYSHQVKDLQ-RRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMErdaMADIRRR-ESQSQedlrnqlqntVHE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1341 AEAAERLRaEKEMKELQTQYDALKKQMEVMEMEVMEAR--LIRAAEINGE-VDDDDTGGEWRLK-----YERAMREVD-- 1410
Cdd:pfam15921 154 LEAAKCLK-EDMLEDSNTQIEQLRKMMLSHEGVLQEIRsiLVDFEEASGKkIYEHDSMSTMHFRslgsaISKILRELDte 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1411 --FTKKRLQqEFEDKLEV---EQQNKRQLerrlgdlqadidesqrALQQLKKKCQRLTAElqdTKLHLEGQQVRNHELEK 1485
Cdd:pfam15921 233 isYLKGRIF-PVEDQLEAlksESQNKIEL----------------LLQQHQDRIEQLISE---HEVEITGLTEKASSARS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1486 KQRRFDSELSQAHEEAQREK----LQREKLQREKDTLLAEAFSLKQQLEEKdmdIAGFTQKVVSLEAELQDISSQESKDE 1561
Cdd:pfam15921 293 QANSIQSQLEIIQEQARNQNsmymRQLSDLESTVSQLRSELREAKRMYEDK---IEELEKQLVLANSELTEARTERDQFS 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1562 ASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRqthsKEVESRDEEVeearQSCQKKLKQMEVQ 1641
Cdd:pfam15921 370 QESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLR----RELDDRNMEV----QRLEALLKAMKSE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1642 LEEEYEDKQKVLREKRELESKLTTLSEQvsqrdLESEKRLrkdLKRTKALLADAQIMLDHlknnapSKREIAQLKNQLEE 1721
Cdd:pfam15921 442 CQGQMERQMAAIQGKNESLEKVSSLTAQ-----LESTKEM---LRKVVEELTAKKMTLES------SERTVSDLTASLQE 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1722 SE----FTCAAAVKARKAMEVEMEDL-HLQIDDIAKAKTALEEQLSRLQ-REKNEIQSRLEEDQEDMNELmkkhkaaVAQ 1795
Cdd:pfam15921 508 KEraieATNAEITKLRSRVDLKLQELqHLKNEGDHLRNVQTECEALKLQmAEKDKVIEILRQQIENMTQL-------VGQ 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1796 ASRDLAQMNDLQAQLE-EANKEKQELQEKlqalqsqvefleqsmvdKSLVSRQEAKIRELETRL-EFERTQVKRLESLAS 1873
Cdd:pfam15921 581 HGRTAGAMQVEKAQLEkEINDRRLELQEF-----------------KILKDKKDAKIRELEARVsDLELEKVKLVNAGSE 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1874 RLKEnMEKLTEERDQ-----RTAAE--NREKEQNKRLQRQLRDTKEEMGELARK-EAEASRKKHELEM---DLESLEAAN 1942
Cdd:pfam15921 644 RLRA-VKDIKQERDQllnevKTSRNelNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQtrnTLKSMEGSD 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1943 -------QSLQADLKLAFKRIGDLQAAI---EDEMESDENEDLI-----TSLQDMVTKYQKRKNKPEGDSDVDSELEDRV 2007
Cdd:pfam15921 723 ghamkvaMGMQKQITAKRGQIDALQSKIqflEEAMTNANKEKHFlkeekNKLSQELSTVATEKNKMAGELEVLRSQERRL 802
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1269-1777 |
9.72e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 93.98 E-value: 9.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1269 TVRPLIEVQLSEEQIRSKD--EEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDA----- 1341
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAEtrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEleeek 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1342 -EAAERLRA-----------------------------EKEMKELQTQYDALKKQMEVMEMEVMEAR------------- 1378
Cdd:TIGR02169 444 eDKALEIKKqewkleqlaadlskyeqelydlkeeydrvEKELSKLQRELAEAEAQARASEERVRGGRaveevlkasiqgv 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1379 ------LIR-------AAEINGE-------VDDDDTGGEW--RLKYERA----------MRE------------------ 1408
Cdd:TIGR02169 524 hgtvaqLGSvgeryatAIEVAAGnrlnnvvVEDDAVAKEAieLLKRRKAgratflplnkMRDerrdlsilsedgvigfav 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1409 --VDFTKK---RLQQEFEDKLEVE--QQNKRQLER-RLGDLQADIDESQRAL--------------QQLKKKCQRLTAEL 1466
Cdd:TIGR02169 604 dlVEFDPKyepAFKYVFGDTLVVEdiEAARRLMGKyRMVTLEGELFEKSGAMtggsraprggilfsRSEPAELQRLRERL 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1467 QDTKLHLEGqqvrnheLEKKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSL 1546
Cdd:TIGR02169 684 EGLKRELSS-------LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1547 EAELQDISSQESKDEASLAKVKKQLRDLEAK------------VKDQEEELDEQAGTIQMLEQAKLRLEMEMERMR---- 1610
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARlshsripeiqaeLSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEkeiq 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1611 --QTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEE------EYEDKQKVLREKR-ELESKLTTLSEQVSQRDLESEKrL 1681
Cdd:TIGR02169 837 elQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEleaalrDLESRLGDLKKERdELEAQLRELERKIEELEAQIEK-K 915
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1682 RKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaaAVKARKAMEVEMEDLH----LQIDD---IAKAK 1754
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED-------VQAELQRVEEEIRALEpvnmLAIQEyeeVLKRL 988
|
650 660
....*....|....*....|...
gi 1239919865 1755 TALEEQLSRLQREKNEIQSRLEE 1777
Cdd:TIGR02169 989 DELKEKRAKLEEERKAILERIEE 1011
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
440-693 |
2.09e-18 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 92.21 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSPRGAPAVYSEKVMHMFKgCRR--EDMAPHIYAVAQTAYRAMLMSRQDQSVILL 517
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYK-CIDciEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 518 GSSGSGKTTSCQHLVQYLA-------------TIAGTSGNKVFSVEKWQALYS--------LLEAFGNSPTIMNGNATRF 576
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAyqvkgsrrlptnlNDQEEDNIHNEENTDYQFNMSemlkhvnvVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 577 SQILSLDFDQAgQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLNHLAENNVFGivpLAKPEEKQ 656
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLN---NEKGFEKF 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 1239919865 657 KA-AQQFSKLQTAMKVLGISPDEQKACWLILAAIYHLG 693
Cdd:cd14938 237 SDySGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLG 274
|
|
| PDZ_NHERF-like |
cd06768 |
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ... |
219-307 |
3.08e-18 |
|
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the Na+/H+ exchange regulatory cofactor (NHERF) family of multi-PDZ-domain-containing scaffolding proteins (NHERF1-4), and related domains. The NHERF family includes NHERF1 (also known as EBP50), NHERF2 (also known as E3KARP; TKA-1; SIP-1), NHERF3 (also known as CAP70; CLAMP; Napi-Cap-1; PDZD1) and NHERF4 (also known as IKEPP; PDZK2; Napi-Cap-2). NHERF1 and NHERF2 have tandem PDZ domains (PDZ1-2); NHERF3 and NHERF4 have four PDZ domains (PDZ1-4). NHERFs are involved in the regulation of multiple receptors or transporters, such as type II sodium-phosphate cotransporter (Npt2a), purinergic P2Y1 receptor P2Y1R, the beta2-adrenergic receptor (beta2-AR), parathyroid hormone receptor type 1 (PTHR), the lysophosphatidic acid receptors (LPARs), sodium-hydrogen exchanger 3 (NHE3), and cystic fibrosis transmembrane conductance regulator (CFTR). NHERF-PDZ1 domain interaction partners include Npt2a, purinergic P2Y1 receptor, beta2-AR, CFTR, PTHR, NH3, G-protein-coupled receptor kinase 6 (GRK6A), platelet-derived growth factor receptor (PDGFR), B1 subunit of the H+ATPase, cholesterol, receptor for activated C-kinase RACK1, aquaporin 9, among others. The NHERF PDZ2 domain interacts with fewer proteins: NHERF1 PDZ2 binds Npt2a, PTHR, beta-catenin, aquaporin 9, and RACK1; NHERF2 PDZ2 binds LPA2, P2Y1R, and NHE3, cGMP-dependent protein kinase type II (cGKII). NHERF4 PDZ1 and PDZ4 bind the epithelial Ca(2+) channels TRPV5 and TRPV6. NHERF2/NHERF3 heterodimerization is mediated by PDZ domains of NHERF2 and the C-terminal PDZ domain recognition motif of NHERF3. NHERF4 regulates several transporters mediating influx of xenobiotics and nutrients in the small intestine. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This NHERF-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467249 [Multi-domain] Cd Length: 80 Bit Score: 81.33 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 219 RELELQRRPTGdFGFSLRRttmlDRGPEGQVYRRVvhfaEPGaGTKDLAlGLVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd06768 1 RLCHLVKGPEG-YGFNLHA----EKGRPGHFIREV----DPG-SPAERA-GLKDGDRLVEVNGENVEGESHEQVVEKIKA 69
|
....*....
gi 1239919865 299 SGDSVRLKV 307
Cdd:cd06768 70 SGNQVTLLV 78
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1285-1682 |
3.78e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 92.04 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1285 SKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRAEKEMKELQTQYDALK 1364
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1365 KQMEvmemevmearliraaeingevddddtggewRLKYERAmrevdftkkrlqqEFEDKLEVEQQNKRQLERRLGDLQAD 1444
Cdd:TIGR02168 754 KELT------------------------------ELEAEIE-------------ELEERLEEAEEELAEAEAEIEELEAQ 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1445 IDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQrekdtllAEAFS 1524
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-------AEIEE 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1525 LKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEakvkDQEEELDEQAGTIQM-LEQAKLRLE 1603
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR----RELEELREKLAQLELrLEGLEVRID 939
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1604 MEMERMRQTHS---KEVESRDEEVEEARQSCQKKLKQMEVQLE----------EEYEDKQK----VLREKRELESKLTTL 1666
Cdd:TIGR02168 940 NLQERLSEEYSltlEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaiEEYEELKErydfLTAQKEDLTEAKETL 1019
|
410
....*....|....*.
gi 1239919865 1667 SEQVSQRDLESEKRLR 1682
Cdd:TIGR02168 1020 EEAIEEIDREARERFK 1035
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1272-2017 |
5.05e-18 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 91.65 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1272 PLIEVQLSEEQIRSKDEEIQQLRSKLEKVEKERNELRLS----------------NDRLETRISELTS---ELTD----- 1327
Cdd:TIGR00606 249 PLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSElelkmekvfqgtdeqlNDLYHNHQRTVREkerELVDcqrel 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1328 ERNTGEsaSQLLDAEAAERL----RAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDTggewrLKYE 1403
Cdd:TIGR00606 329 EKLNKE--RRLLNQEKTELLveqgRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHT-----LVIE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1404 RAMREVDfTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQdtklHLEGQQVRNHEL 1483
Cdd:TIGR00606 402 RQEDEAK-TAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ----QLEGSSDRILEL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1484 EKKQRRFDSELSQAHEEAQREKLQREK--LQREKDTLLAEAFSLKQQLEEKDMDIAGFTQ------KVVSLEAELQDISS 1555
Cdd:TIGR00606 477 DQELRKAERELSKAEKNSLTETLKKEVksLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQmemltkDKMDKDEQIRKIKS 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1556 QESKDEASLAKV---KKQLRD----LEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVeear 1628
Cdd:TIGR00606 557 RHSDELTSLLGYfpnKKQLEDwlhsKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVC---- 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1629 qSCQkklkQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEK--RLRKDLKRTKALLADAQIMLDHLKNNA 1706
Cdd:TIGR00606 633 -GSQ----DEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccPVCQRVFQTEAELQEFISDLQSKLRLA 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1707 PSKreiaqlknqLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELM 1786
Cdd:TIGR00606 708 PDK---------LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIM 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1787 KKHKAAvAQASRDLAQMNDLQAQLEEANKEKQELQEKLQA--LQSQVEFLEQSMVDKSLVSRQ-EAKIRELETRLEFERT 1863
Cdd:TIGR00606 779 PEEESA-KVCLTDVTIMERFQMELKDVERKIAQQAAKLQGsdLDRTVQQVNQEKQEKQHELDTvVSKIELNRKLIQDQQE 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1864 QVKRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQ---RQLRDTKEEMGELA--------RKEAEASRKKHE-- 1930
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQsliREIKDAKEQDSPLEtflekdqqEKEELISSKETSnk 937
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1931 -LEMDLESLEAANQSLQADLKLAFKRIgdlQAAIEDEMESDENEdlITSLQDMVTKYQKRKNKPEGDSDVDSELEDRVDG 2009
Cdd:TIGR00606 938 kAQDKVNDIKEKVKNIHGYMKDIENKI---QDGKDDYLKQKETE--LNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
....*...
gi 1239919865 2010 VKSWLSKN 2017
Cdd:TIGR00606 1013 QERWLQDN 1020
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1462-1962 |
7.57e-18 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 90.21 E-value: 7.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1462 LTAELQDTKLHLEGQQVRNHELEKKQRRfdsELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQ 1541
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELK---ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1542 KVvsleaELQDISSQESKDEASLAKVKKQLRDLEAkvkdQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRD 1621
Cdd:COG4717 124 LL-----QLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1622 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQvsqrdlesekrlrKDLKRTKALLADAQIMLdh 1701
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-------------ERLKEARLLLLIAAALL-- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1702 lknnapskrEIAQLKNQLEESEFTCAAAVKARKAMevemedLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQED 1781
Cdd:COG4717 260 ---------ALLGLGGSLLSLILTIAGVLFLVLGL------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1782 MNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKlQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFE 1861
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVED------EEELRAALEQAEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1862 RTQVKRLESLASRLKENMEKLTEERDQRTAAENREKEQnkRLQRQLRDTKEEMGELARKEAEASRKKHELEMD--LESLE 1939
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEELEEELE--ELEEELEELEEELEELREELAELEAELEQLEEDgeLAELL 475
|
490 500
....*....|....*....|...
gi 1239919865 1940 AANQSLQADLKLAFKRIGDLQAA 1962
Cdd:COG4717 476 QELEELKAELRELAEEWAALKLA 498
|
|
| PDZ_canonical |
cd00136 |
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ... |
220-308 |
9.50e-18 |
|
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467153 [Multi-domain] Cd Length: 81 Bit Score: 79.89 E-value: 9.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 220 ELELQRRPTGDFGFSLRRTTMLDRGPegqvyrrVVHFAEPGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQS 299
Cdd:cd00136 1 TVTLEKDPGGGLGFSIRGGKDGGGGI-------FVSRVEPG-GPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLKSA 72
|
....*....
gi 1239919865 300 GDSVRLKVQ 308
Cdd:cd00136 73 GGEVTLTVR 81
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1412-1994 |
1.09e-17 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 90.41 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1412 TKKRLQQEFEDKLEVEQQNKRQLE---RRLGDLQADIDESQRALQQLKKKCQRLTA-----ELQDTKLHLEGQQVRNHEL 1483
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHaylTQKREAQEEQLKKQQLLKQLRARIEELRAqeavlEETQERINRARKAAPLAAH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1484 EKKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQ--LEEKDMDIAGFTQKVVSLEAELQDISSQESKDE 1561
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1562 ASLAKVKKQLRDLEAKVK---DQEEELDEQAGTIQMLEQAKLRLEMEMERMRqthsKEVESRDEEVEEARQSCQKKLkQM 1638
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQslcKELDILQREQATIDTRTSAFRDLQGQLAHAK----KQQELQQRYAELCAAAITCTA-QC 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1639 EVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKRL-------RKDLKRTKALLADAQIMLDHLKNNAPSKR- 1710
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqeepCPLCGSCIHPNPARQDIDNPGPLTRRMQRg 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1711 --EIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEdmnELMKK 1788
Cdd:TIGR00618 534 eqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE---AEDML 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1789 HKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ---------EAKIRELETRLE 1859
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlpkellasrQLALQKMQSEKE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1860 FERTQVKRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEA--------SRKKHEL 1931
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkarteahFNNNEEV 770
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1932 EMDL------ESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLITSLQdMVTKYQKRKNKPE 1994
Cdd:TIGR00618 771 TAALqtgaelSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCET-LVQEEEQFLSRLE 838
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1281-1768 |
1.87e-17 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 89.06 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1281 EQIRSKDEEIQQLRSKLEKVEKERNELrlsnDRLETRISELTSELTDERNTGESASQLLDAEA--AERLRAEKEMKELQT 1358
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1359 QYDALKKQMEVMEmevmearliraaeingevddddtggEWRLKYERAMREVDFTKKRLQQEFEDKLEVEQQNKRQLERRL 1438
Cdd:COG4717 147 RLEELEERLEELR-------------------------ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1439 GDLQADIDESQRALQQLKKKCQRLTAELQDTKlhlegqqvrnhelekkqrrfdselSQAHEEAQREKLQREKLQREKDTL 1518
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLE------------------------NELEAAALEERLKEARLLLLIAAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1519 LAEAFSLKQQLEEKDMDIAGFTQKVVSLeaeLQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQA 1598
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1599 KL-RLEMEMERMRQTHSKEVESRDEE----VEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQR 1673
Cdd:COG4717 335 SPeELLELLDRIEELQELLREAEELEeelqLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEEL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1674 --------DLESEKRLRKDLKRTKALLADAQIMLDHLknnapsKREIAQLKNQLE--ESEFTCAAAVKARKAMEVEMEDL 1743
Cdd:COG4717 415 lgeleellEALDEEELEEELEELEEELEELEEELEEL------REELAELEAELEqlEEDGELAELLQELEELKAELREL 488
|
490 500
....*....|....*....|....*
gi 1239919865 1744 HLQIDDIAKAKTALEEQLSRLQREK 1768
Cdd:COG4717 489 AEEWAALKLALELLEEAREEYREER 513
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1712-1974 |
1.99e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1712 IAQLKNQLEESEftcAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKA 1791
Cdd:COG1196 195 LGELERQLEPLE---RQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1792 AVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSL-VSRQEAKIRELETRLEFERTQVKRLES 1870
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEeLAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1871 LASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLK 1950
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260
....*....|....*....|....
gi 1239919865 1951 LAFKRIGDLQAAIEDEMESDENED 1974
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELE 455
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1493-1899 |
2.83e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.97 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1493 ELSQAHEEAQREKLQR--EKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQ 1570
Cdd:TIGR02169 666 ILFSRSEPAELQRLRErlEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1571 LRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEME----RMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEY 1646
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1647 EDKQKVLREKRELESKLTTLSEQVSQRdlesekrlrkdlkrtkalladaqimldhlknnapsKREIAQLKNQLEEseftc 1726
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSI-----------------------------------EKEIENLNGKKEE----- 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1727 aaavkarkaMEVEMEDLHLQIDDiakaktaLEEQLSRLQREKNEIQSRLEEDQEDMNELMkkhkaavAQASRDLAQMNDL 1806
Cdd:TIGR02169 866 ---------LEEELEELEAALRD-------LESRLGDLKKERDELEAQLRELERKIEELE-------AQIEKKRKRLSEL 922
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1807 QAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELE-----TRLEFERTQVKRLEslasrLKENMEK 1881
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlAIQEYEEVLKRLDE-----LKEKRAK 997
|
410 420
....*....|....*....|.
gi 1239919865 1882 LTEERDQ---RTAAENREKEQ 1899
Cdd:TIGR02169 998 LEEERKAileRIEEYEKKKRE 1018
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1581-1964 |
3.04e-17 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 89.08 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1581 QEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSK-----------------------------------------EVES 1619
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQlceeknalqeqlqaetelcaeaeemrarlaarkqeleeilhELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1620 RDEEVEEARQSCQ---KKLKQ----MEVQLEEEYEDKQKVLREKRELESKLTTLSEQV-----SQRDLESEKRLRK---- 1683
Cdd:pfam01576 83 RLEEEEERSQQLQnekKKMQQhiqdLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDIllledQNSKLSKERKLLEeris 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1684 DLKRTKALLADAQIMLDHLKNNAPSKreIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSR 1763
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHEAM--ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1764 LQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVE-FLEQSMVDKS 1842
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1843 LVSRQEAKIRELETRLEFE-RTQVKRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKE 1921
Cdd:pfam01576 321 LRSKREQEVTELKKALEEEtRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1239919865 1922 AEASRKKHELEMDLESLEA-ANQSLQADLKLAfKRIGDLQAAIE 1964
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQArLSESERQRAELA-EKLSKLQSELE 443
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1327-1917 |
7.77e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 87.66 E-value: 7.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1327 DERNTGESASQLLD------------AEAAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDT 1394
Cdd:COG4913 219 EEPDTFEAADALVEhfddlerahealEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1395 ggEWRLKYERAMREVDFTKKRLQQEFEDKLEVEQQ-------NKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQ 1467
Cdd:COG4913 299 --ELRAELARLEAELERLEARLDALREELDELEAQirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1468 DTKLHLEGQQvrnHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQ------------------- 1528
Cdd:COG4913 377 ASAEEFAALR---AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRksniparllalrdalaeal 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1529 -LEEKDMDIAGftqkvvsleaELQDISSQESK------------------DEASLAKVKKQLR--DLEAKVKDQEEELDE 1587
Cdd:COG4913 454 gLDEAELPFVG----------ELIEVRPEEERwrgaiervlggfaltllvPPEHYAAALRWVNrlHLRGRLVYERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1588 QAGTIQMLEQ----AKLR---------LEMEMERmRQTHSKeVESRDEEVEEAR---QSCQKKL------KQMEVQLEEE 1645
Cdd:COG4913 524 PDPERPRLDPdslaGKLDfkphpfrawLEAELGR-RFDYVC-VDSPEELRRHPRaitRAGQVKGngtrheKDDRRRIRSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1646 Y------EDKQKVLREKR-ELESKLTTLSEQVSQRdleseKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQ 1718
Cdd:COG4913 602 YvlgfdnRAKLAALEAELaELEEELAEAEERLEAL-----EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1719 ---LEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDmnelmkkhkaAVAQ 1795
Cdd:COG4913 677 lerLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL----------ARLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1796 ASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDK--SLVSRQEAKIRELETRLEFERTQVKRLESL-A 1872
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAmrAFNREWPAETADLDADLESLPEYLALLDRLeE 826
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1239919865 1873 SRLKENMEKLteeRDQRTAAENREKEQ-NKRLQRQLRDTKEEMGEL 1917
Cdd:COG4913 827 DGLPEYEERF---KELLNENSIEFVADlLSKLRRAIREIKERIDPL 869
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1423-1986 |
9.24e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.40 E-value: 9.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1423 KLEVEQQNKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEkkqrrfdsELSQAHEEAQ 1502
Cdd:PRK02224 193 KAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE--------TLEAEIEDLR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1503 REKLQREklqREKDTLLAEAFSLKQQLEEkdmdiagftqkvvsLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQE 1582
Cdd:PRK02224 265 ETIAETE---REREELAEEVRDLRERLEE--------------LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1583 EELDEQAGTIQMLEQaklrlemEMERMRQThSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEdkqkvlrEKRELESK 1662
Cdd:PRK02224 328 DRLEECRVAAQAHNE-------EAESLRED-ADDLEERAEELREEAAELESELEEAREAVEDRRE-------EIEELEEE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1663 LTTLSEQVSQRDLESEK------RLRKDLKRTKALLADAQIMLDHLKNNApskREIAQLKNQ---------LEESEFTCA 1727
Cdd:PRK02224 393 IEELRERFGDAPVDLGNaedfleELREERDELREREAELEATLRTARERV---EEAEALLEAgkcpecgqpVEGSPHVET 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1728 AAVK--ARKAMEVEMEDLHLQIDDIAKAKTALEEqLSRLQREKneiqSRLEEDQEDMNELMKKHKAAVAQASRDLAQMN- 1804
Cdd:PRK02224 470 IEEDreRVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRI----ERLEERREDLEELIAERRETIEEKRERAEELRe 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1805 ---DLQAQLEEANKEKQELQEKLQALQSQVEFLEQsmvdkslvsrqeaKIRELETRLEFERTQVKRLESLASrLKENMEK 1881
Cdd:PRK02224 545 raaELEAEAEEKREAAAEAEEEAEEAREEVAELNS-------------KLAELKERIESLERIRTLLAAIAD-AEDEIER 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1882 LTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHE-----LEMDLESLEAANQSLQadlklafKRI 1956
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEeyleqVEEKLDELREERDDLQ-------AEI 683
|
570 580 590
....*....|....*....|....*....|..
gi 1239919865 1957 GDLQAAIEdEMES--DENEDLITSLQDMVTKY 1986
Cdd:PRK02224 684 GAVENELE-ELEElrERREALENRVEALEALY 714
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1273-1914 |
2.68e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 85.79 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1273 LIEVQLSEEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAErlraEKE 1352
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE----EKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1353 MKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDTGGEWRLKYERAMREVDFTKKRLQQEFE--DKLEVEQQN 1430
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggRIISAHGRL 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1431 KRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEEAQREKLQREK 1510
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLK---LPLKSIAVLEIDPILNLAQL 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1511 LQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQE------SKDEASLAKVKKQLRDLEAKVKDQEEE 1584
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaekSEVKASLSELTKELLEIQELQEKAESE 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1585 LDEQAGTIQMLEQAKLRLEMEmERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLT 1664
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREK-EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1665 TLSEQVSQRDLESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLH 1744
Cdd:pfam02463 768 ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK 847
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1745 LQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVA------QASRDLAQMNDLQAQLEEANKEKQ 1818
Cdd:pfam02463 848 LEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEekkeleEESQKLNLLEEKENEIEERIKEEA 927
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1819 ELQEKLQALQsqvefLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTAAENREKE 1898
Cdd:pfam02463 928 EILLKYEEEP-----EELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEE 1002
|
650
....*....|....*.
gi 1239919865 1899 QNKRLQRQLRDTKEEM 1914
Cdd:pfam02463 1003 EKKKLIRAIIEETCQR 1018
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1271-2000 |
5.31e-16 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 85.10 E-value: 5.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1271 RPLIEVQLSEEQIRSKDEEIQ--QLRSKLEKVEKE-------RNELRLSNDRLETR---ISELTSELTDERNTGESASQL 1338
Cdd:TIGR00606 351 RLQLQADRHQEHIRARDSLIQslATRLELDGFERGpfserqiKNFHTLVIERQEDEaktAAQLCADLQSKERLKQEQADE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1339 LDAEAA--------ERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDTGGEWRLKYERAMR--- 1407
Cdd:TIGR00606 431 IRDEKKglgrtielKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQnek 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1408 -EVDFTKKRLQQEFE-----------------DKLEVEQQ--------------------NKRQLERRLGDLQADIDESQ 1449
Cdd:TIGR00606 511 aDLDRKLRKLDQEMEqlnhhtttrtqmemltkDKMDKDEQirkiksrhsdeltsllgyfpNKKQLEDWLHSKSKEINQTR 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1450 RALQQLKKKCQRLtaELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAhEEAQREKLQREKLQREKD-TLLAEAFSLK-- 1526
Cdd:TIGR00606 591 DRLAKLNKELASL--EQNKNHINNELESKEEQLSSYEDKLFDVCGSQD-EESDLERLKEEIEKSSKQrAMLAGATAVYsq 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1527 --QQLEEKDMDIAGFTQKVVSLEAELQDISSqesKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEM 1604
Cdd:TIGR00606 668 fiTQLTDENQSCCPVCQRVFQTEAELQEFIS---DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEK 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1605 EMERMRQTHSK------EVESRDEEVEEARQSCQKKLKQMEV---------QLEEEYED-KQKVLREKRELESKLTTLS- 1667
Cdd:TIGR00606 745 EIPELRNKLQKvnrdiqRLKNDIEEQETLLGTIMPEEESAKVcltdvtimeRFQMELKDvERKIAQQAAKLQGSDLDRTv 824
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1668 EQVSQRDLESEKRLRK---DLKRTKALLADAQIMLDHLKNNApskreiaqlkNQLEESEFTCAAAVKARKAMEVEMEDLH 1744
Cdd:TIGR00606 825 QQVNQEKQEKQHELDTvvsKIELNRKLIQDQQEQIQHLKSKT----------NELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1745 LQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQ---------------------- 1802
Cdd:TIGR00606 895 TEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgymkdienkiqdgkddylkq 974
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1803 ----MNDLQAQLEEANKEKQELQEKLQALQSQVE---FLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLasRL 1875
Cdd:TIGR00606 975 keteLNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVL--QM 1052
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1876 KENMEKLTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEAsrKKHELEMDLESLEAANQSL--------QA 1947
Cdd:TIGR00606 1053 KQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE--KYREMMIVMRTTELVNKDLdiyyktldQA 1130
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239919865 1948 DLKLAFKRIGDLQAAIED--------------EMESDENEDliTSLQDMVTKYQKRKNKPEGDSDVD 2000
Cdd:TIGR00606 1131 IMKFHSMKMEEINKIIRDlwrstyrgqdieyiEIRSDADEN--VSASDKRRNYNYRVVMLKGDTALD 1195
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1280-1761 |
6.33e-16 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 84.84 E-value: 6.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1280 EEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISEL---TSELTDERNTGESAsqlldaeaaeRLRAEKEMKEL 1356
Cdd:pfam01576 656 ERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMktqLEELEDELQATEDA----------KLRLEVNMQAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1357 QTQYDAlkkqmevmemevmearliraaEINGEvddDDTGGEWRLKYERAMREvdftkkrLQQEFEDKLEVEQQ---NKRQ 1433
Cdd:pfam01576 726 KAQFER---------------------DLQAR---DEQGEEKRRQLVKQVRE-------LEAELEDERKQRAQavaAKKK 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1434 LERRLGDLQADIDESQR----ALQQLKK---KCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKL 1506
Cdd:pfam01576 775 LELDLKELEAQIDAANKgreeAVKQLKKlqaQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASER 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1507 QREKLQREKDtllaeafslkqqleekdmdiagftqkvvsleaELQDISSQESKDEASLAKVKkqlRDLEAKVKDQEEELD 1586
Cdd:pfam01576 855 ARRQAQQERD--------------------------------ELADEIASGASGKSALQDEK---RRLEARIAQLEEELE 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1587 EQAGTIQMLEQAKLRLEMEMERMRQTHSKEvESRDEEVEEARQSCQKKLKQMEVQL-EEEYEDKQKVLREKRELESKLTT 1665
Cdd:pfam01576 900 EEQSNTELLNDRLRKSTLQVEQLTTELAAE-RSTSQKSESARQQLERQNKELKAKLqEMEGTVKSKFKSSIAALEAKIAQ 978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1666 LSEQvsqrdLESEKRLR----KDLKRTKALLADAQIMLDHLKNNAPSKREIA--------QLKNQLEESEFTCAAAVKAR 1733
Cdd:pfam01576 979 LEEQ-----LEQESRERqaanKLVRRTEKKLKEVLLQVEDERRHADQYKDQAekgnsrmkQLKRQLEEAEEEASRANAAR 1053
|
490 500
....*....|....*....|....*...
gi 1239919865 1734 KAMEVEMEDLHLQIDDIAKAKTALEEQL 1761
Cdd:pfam01576 1054 RKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1284-1895 |
8.84e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.94 E-value: 8.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1284 RSKDEEIQQLRSKLEkvEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDaEAAERLRAEKEMKElqtqydal 1363
Cdd:PRK02224 183 SDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRD-EADEVLEEHEERRE-------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1364 kkqmevmemevmearliRAAEINGEVDDddtggeWRLKYERAMREVDFTKKRLqqefedkleveqqnkRQLERRLGDLQA 1443
Cdd:PRK02224 252 -----------------ELETLEAEIED------LRETIAETEREREELAEEV---------------RDLRERLEELEE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1444 DIDEsqralqqLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEAF 1523
Cdd:PRK02224 294 ERDD-------LLAEAGLDDADAEAVEARRE-------ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1524 SLKQQLEEkdmdiagftqkvvsLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLE 1603
Cdd:PRK02224 360 ELREEAAE--------------LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELR 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1604 MEMERMRQThskeVESRDEEVEEARQ--------SCQKKLKQME-VQLEEEYEDKQKVLREKRE-LESKLTTLSEQVSQ- 1672
Cdd:PRK02224 426 EREAELEAT----LRTARERVEEAEAlleagkcpECGQPVEGSPhVETIEEDRERVEELEAELEdLEEEVEEVEERLERa 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1673 RDL-ESEKRLRKDLKRTKA---LLADAQIMLDHLKNNAPSKREIAQ-LKNQLEESEftcAAAVKARKAMEVEMEdlhlQI 1747
Cdd:PRK02224 502 EDLvEAEDRIERLEERREDleeLIAERRETIEEKRERAEELRERAAeLEAEAEEKR---EAAAEAEEEAEEARE----EV 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1748 DDIAKAKTALEEQLSRLQREKnEIQSRLEEDQEDMNELMKKHKaavaqasrDLAQMNDL-QAQLEEANKEKQELQEKLQA 1826
Cdd:PRK02224 575 AELNSKLAELKERIESLERIR-TLLAAIADAEDEIERLREKRE--------ALAELNDErRERLAEKRERKRELEAEFDE 645
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1827 lqsqvEFLEQSMVDKslvSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTAAENR 1895
Cdd:PRK02224 646 -----ARIEEAREDK---ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENR 706
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
440-886 |
1.01e-15 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 83.24 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 440 SVLHTLRQRYGASLLHTYAGPSLLVLSP---RGAPAVYSEKvmhmfkgcRREDMAPHIYAVAQTAYRAMLMSRQDQSVIL 516
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPyrdVGNPLTLTST--------RSSPLAPQLLKVVQEAVRQQSETGYPQAIIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 517 LGSSGSGKTTSCQHLVQYLATIAGtSGNKVFSVEKWQALYSLLEAFGNSPTIMNGNATRFSQILSLDFDQaGQVASASIQ 596
Cdd:cd14881 74 SGTSGSGKTYASMLLLRQLFDVAG-GGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GALYRTKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 597 TMLLEKLRVARRPASEATFNVFYYLLACADGTLRTELHLN--------HLAENNVFgivplakpEEKQKAAQQFSKLQTA 668
Cdd:cd14881 152 CYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgyspanlrYLSHGDTR--------QNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 669 MKVLGIsP--DEQKacwlILAAIYHLGAAGATKeapeeqaeaaEAGRKQFARHEWAQKA-AYLLGCSleelSSAIFKhqh 745
Cdd:cd14881 224 LGILGI-PflDVVR----VLAAVLLLGNVQFID----------GGGLEVDVKGETELKSvAALLGVS----GAALFR--- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 746 kgCTLQRSTSFRqGPEESSLGDGTGPKLTAlECLegmASGLYSELFTLLVSLVNrALKSSQHSLC------SMMIVDTPG 819
Cdd:cd14881 282 --GLTTRTHNAR-GQLVKSVCDANMSNMTR-DAL---AKALYCRTVATIVRRAN-SLKRLGSTLGthatdgFIGILDMFG 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239919865 820 FQNPeqggsaRGASFEELCHNYAQDRLQRLFHERTFVQELERYKEENIELafdDLEPATDDSVAAVD 886
Cdd:cd14881 354 FEDP------KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQC---EVEVDYVDNVPCID 411
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1414-1886 |
1.43e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 82.89 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1414 KRLQQEFEDKLEVEQQNkRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNhELEKKQRRFdse 1493
Cdd:COG4717 74 KELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA-ELAELPERL--- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1494 lsqahEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKdmdiagFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1573
Cdd:COG4717 149 -----EELEERLEELRELEEELEELEAELAELQEELEEL------LEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1574 LEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQSCQKKLKQME--VQLEEEYEDKQK 1651
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLglLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1652 VLREKRELESKLTTLSEQVSQRDLESE-KRLRKDLKRTKALLADAQIMLDHLKNnapSKREIAQLKNQLEESEFtcaaav 1730
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELlAALGLPPDLSPEELLELLDRIEELQE---LLREAEELEEELQLEEL------ 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1731 kaRKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQAsrdlaQMNDLQAQL 1810
Cdd:COG4717 369 --EQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE-----ELEELEEEL 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239919865 1811 EEANKEKQELQEKLQALQSQVEFLEQSmvdkSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEER 1886
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEED----GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1605-2010 |
2.47e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.81 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1605 EMERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEvQLEEEYEDK---QKVLREKRELESKLTtlseqvsqrdLESEKRL 1681
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLE-RLRREREKAeryQALLKEKREYEGYEL----------LKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1682 RKDLKRTKALLADAQimldhlknnapskREIAQLKNQLEESEFTCAAAvkarkamEVEMEDLHLQIDDIAKAKT-ALEEQ 1760
Cdd:TIGR02169 236 ERQKEAIERQLASLE-------------EELEKLTEEISELEKRLEEI-------EQLLEELNKKIKDLGEEEQlRVKEK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1761 LSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALqsqvefleqsmvd 1840
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL------------- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1841 kslvsrqEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARK 1920
Cdd:TIGR02169 363 -------KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1921 EAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAaiedemESDENEDLITSLQDMVTKYQKRKNKPE----GD 1996
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE------EYDRVEKELSKLQRELAEAEAQARASEervrGG 509
|
410
....*....|....
gi 1239919865 1997 SDVDSELEDRVDGV 2010
Cdd:TIGR02169 510 RAVEEVLKASIQGV 523
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1413-1889 |
8.97e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 80.20 E-value: 8.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1413 KKRLQQEFEDKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKKKCQ--RLTAELQDTKLHLEGQQVRNHELEKKQRrf 1490
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLE-- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1491 dsELSQAHEEAQREKLQREKLQREKDTLLAE-AFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKK 1569
Cdd:COG4717 157 --ELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1570 QLRDLEAKVKDQEEEL----------------------DEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVE-----SRDE 1622
Cdd:COG4717 235 ELEAAALEERLKEARLllliaaallallglggsllsliLTIAGVLFLVLGLLALLFLLLAREKASLGKEAEelqalPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1623 EVEEARQSCQKKLKQMEVQLE-EEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKrlrkdlkrtKALLADAQI-MLD 1700
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSpEELLELLDRIEELQELLREAEELEEELQLEELEQEI---------AALLAEAGVeDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1701 HLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEdlhlqiddiakaKTALEEQLSRLQREKNEIQSRLEEDQE 1780
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD------------EEELEEELEELEEELEELEEELEELRE 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1781 DMNELmkKHKAAVAQASRDLAQmndLQAQLEEANKEKQELQEKLQALQSQVEFLEQsmvdkslvsrqeakireleTRLEF 1860
Cdd:COG4717 454 ELAEL--EAELEQLEEDGELAE---LLQELEELKAELRELAEEWAALKLALELLEE-------------------AREEY 509
|
490 500
....*....|....*....|....*....
gi 1239919865 1861 ERTQVKRLESLASRLkenMEKLTEERDQR 1889
Cdd:COG4717 510 REERLPPVLERASEY---FSRLTDGRYRL 535
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1302-1971 |
1.13e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 80.40 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1302 KERNELRLSNDRLEtRISELTSELTDERNTGESASQLLDaeaaERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIR 1381
Cdd:TIGR00618 163 KEKKELLMNLFPLD-QYTQLALMEFAKKKSLHGKAELLT----LRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1382 AAEINGEVDDDDTGGEWRLKYERAMREVDFTKKRLQQEfEDKLEvEQQNKRQLERRlgdlQADIDESQRALQQLKKKCQR 1461
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ-EAVLE-ETQERINRARK----AAPLAAHIKAVTQIEQQAQR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1462 LTAELQDTK------LHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMD 1535
Cdd:TIGR00618 312 IHTELQSKMrsraklLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1536 iagfTQKVVSLEAELQDISSQESKDEASLAK---VKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQT 1612
Cdd:TIGR00618 392 ----TQKLQSLCKELDILQREQATIDTRTSAfrdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1613 HsKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSE-QVSQRDLEsekRLRKDLKRTKAL 1691
Cdd:TIGR00618 468 L-KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpGPLTRRMQ---RGEQTYAQLETS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1692 LADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKAR-KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNE 1770
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDiPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1771 IQSRLEEDQEDMN--ELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQE 1848
Cdd:TIGR00618 624 EQDLQDVRLHLQQcsQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQ 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1849 AKIRELETRLEFERTQVKRLE----SLASRLKENMEKLTE-----ERDQRTAAENREKEQNKRLQR-------------- 1905
Cdd:TIGR00618 704 TLLRELETHIEEYDREFNEIEnassSLGSDLAAREDALNQslkelMHQARTVLKARTEAHFNNNEEvtaalqtgaelshl 783
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 1906 ------QLRDTKEEMGELARKEAE--ASRKKHELEMDLESLEAANQSLQADLKLAFKriGDLQAAIEDEMESDE 1971
Cdd:TIGR00618 784 aaeiqfFNRLREEDTHLLKTLEAEigQEIPSDEDILNLQCETLVQEEEQFLSRLEEK--SATLGEITHQLLKYE 855
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1281-1826 |
1.54e-14 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 79.78 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1281 EQIRSKDEEIQqLRSKLEKVEKERNELRLSndrLETRISELTSELTDERNTGE------SASQLLDAEAAERLRAEKEMK 1354
Cdd:pfam05557 3 ELIESKARLSQ-LQNEKKQMELEHKRARIE---LEKKASALKRQLDRESDRNQelqkriRLLEKREAEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1355 ELQTQY-DALKKQMEVMEMEVMEARLIRAAeINGEVddddtgGEWRLKYERAMREVDFTKKRLQqEFEDKLEVEQQNKRQ 1433
Cdd:pfam05557 79 RLKKKYlEALNKKLNEKESQLADAREVISC-LKNEL------SELRRQIQRAELELQSTNSELE-ELQERLDLLKAKASE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1434 LERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKL--HLEGQQVRNHELEKKQRRFDSELSQAHE--------EAQR 1503
Cdd:pfam05557 151 AEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvkNSKSELARIPELEKELERLREHNKHLNEnienklllKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1504 EKLQR-----EKLQREKDTLLAEAFSLKQQLEE-------------KDMDIAGFT----QKVVSLEAELQDISSQESKDE 1561
Cdd:pfam05557 231 EDLKRklereEKYREEAATLELEKEKLEQELQSwvklaqdtglnlrSPEDLSRRIeqlqQREIVLKEENSSLTSSARQLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1562 ASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQThskeVESRDEEVEEARQSCQKKLKQMEVq 1641
Cdd:pfam05557 311 KARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAI----LESYDKELTMSNYSPQLLERIEEA- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1642 leEEYEDKQKVLREkrELESKLTTLSEQV-SQRDLESEKRLRKDLKRTKALLADAqimldhlknnAPSKREIAQLKNQLE 1720
Cdd:pfam05557 386 --EDMTQKMQAHNE--EMEAQLSVAEEELgGYKQQAQTLERELQALRQQESLADP----------SYSKEEVDSLRRKLE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1721 ESEFTCAAAVKARKAMEVEMED--------------LHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELM 1786
Cdd:pfam05557 452 TLELERQRLREQKNELEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVL 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1239919865 1787 KKHKAAVAQASRDLaqmNDLQAQLEEANKEKQELQEKLQA 1826
Cdd:pfam05557 532 RLPETTSTMNFKEV---LDLRKELESAELKNQRLKEVFQA 568
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1415-1989 |
2.67e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.19 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1415 RLQQEFEDKLEVEQQNKRQLERRlgDLQADIDESQRALQQLKKKCQRLtaELQDTKLHLEGQQVRNHELEKKQRRFDSEL 1494
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQI--ELLEPIRELAERYAAARERLAEL--EYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1495 SQAHEEAQREKLQREKLQREKDTLLAEAFS--------LKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAK 1566
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1567 VKKQLR----DLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSkeveSRDEEVEEARQSCQKKLKQME--- 1639
Cdd:COG4913 385 LRAEAAalleALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS----NIPARLLALRDALAEALGLDEael 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1640 ------VQLEEEYEDKQ----KVLREKR-------ELESKLTTLseqVSQRDLesekRLRKDLKRTKALLADAQIMLDHl 1702
Cdd:COG4913 461 pfvgelIEVRPEEERWRgaieRVLGGFAltllvppEHYAAALRW---VNRLHL----RGRLVYERVRTGLPDPERPRLD- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1703 KNNAPSKREIAQ------LKNQLEES-EFTCAAAVKA----RKAMEVE----MEDLHLQIDDIAKAKTAL------EEQL 1761
Cdd:COG4913 533 PDSLAGKLDFKPhpfrawLEAELGRRfDYVCVDSPEElrrhPRAITRAgqvkGNGTRHEKDDRRRIRSRYvlgfdnRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1762 SRLQREKNEIQSRLEEdqedmnelmkkhkaavaqasrdlaqmndLQAQLEEANKEKQELQEKLQALQSQVEFLEqSMVDk 1841
Cdd:COG4913 613 AALEAELAELEEELAE----------------------------AEERLEALEAELDALQERREALQRLAEYSW-DEID- 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1842 slVSRQEAKIRELETRLE-FERT--QVKRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELA 1918
Cdd:COG4913 663 --VASAEREIAELEAELErLDASsdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1919 RKEAEASR----KKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMES------DENEDLITSLQDmVTKYQK 1988
Cdd:COG4913 741 DLARLELRalleERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewpAETADLDADLES-LPEYLA 819
|
.
gi 1239919865 1989 R 1989
Cdd:COG4913 820 L 820
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1492-1838 |
1.18e-13 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 76.41 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1492 SELSQAHEEAQREKLQREKLQRE-KDTLLAEAFS-------LKQQLEEKDMDIAGFTQKVVS---LEAE--LQDISSQES 1558
Cdd:PRK04778 129 QELLESEEKNREEVEQLKDLYRElRKSLLANRFSfgpaldeLEKQLENLEEEFSQFVELTESgdyVEAReiLDQLEEELA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1559 KDEASLAKVKKQLRDLEAKVKDQEEELdeQAGTIQMLEQ----AKLRLEMEMERMRQTHSK---EVESRD-EEVEEARQS 1630
Cdd:PRK04778 209 ALEQIMEEIPELLKELQTELPDQLQEL--KAGYRELVEEgyhlDHLDIEKEIQDLKEQIDEnlaLLEELDlDEAEEKNEE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1631 CQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEkRLR-------KDLKRTKALLADAQIM----L 1699
Cdd:PRK04778 287 IQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEID-RVKqsytlneSELESVRQLEKQLESLekqyD 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1700 DHLKNNAPSKREIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLE--- 1776
Cdd:PRK04778 366 EITERIAEQEIAYSELQEELEEIL-------KQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEksn 438
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 1777 -----EDQEDMNELMKKHkaaVAQASRDLAQ----MNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM 1838
Cdd:PRK04778 439 lpglpEDYLEMFFEVSDE---IEALAEELEEkpinMEAVNRLLEEATEDVETLEEETEELVENATLTEQLI 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1709-1925 |
1.48e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 74.80 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1709 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKK 1788
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1789 -------HKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQsmvdkslvsRQEAKIRELETRLEFE 1861
Cdd:COG4942 113 lyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA---------ELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 1862 RTQVKRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEAS 1925
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1499-2009 |
1.53e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.62 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1499 EEAQREKLQREKLQREKDTLLAEafsLKQQLEEKDMdiAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKV 1578
Cdd:PRK02224 169 ERASDARLGVERVLSDQRGSLDQ---LKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1579 KDQEEELDEqagtIQMLEQAKLRLEM---EMERMRQTHSKEVESRDEEVEEARQscqkKLKQMEVQLEEEYEDKQKVLRE 1655
Cdd:PRK02224 244 EEHEERREE----LETLEAEIEDLREtiaETEREREELAEEVRDLRERLEELEE----ERDDLLAEAGLDDADAEAVEAR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1656 KRELESKLTTLSEQVSQRDLeSEKRLRKDLKRtkaLLADAqimlDHLKNNAPSKREIA-QLKNQLEESEFTCAAAVKARK 1734
Cdd:PRK02224 316 REELEDRDEELRDRLEECRV-AAQAHNEEAES---LREDA----DDLEERAEELREEAaELESELEEAREAVEDRREEIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1735 AMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAA---------------------V 1793
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAealleagkcpecgqpvegsphV 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1794 AQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQvkrleslAS 1873
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER-------AE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1874 RLKENMEKLTEErdqrtAAENREKEQNKRlqrqlrdtkEEMGELARKEAEASRKKHELEMDLESLEaanqslqadlklaf 1953
Cdd:PRK02224 541 ELRERAAELEAE-----AEEKREAAAEAE---------EEAEEAREEVAELNSKLAELKERIESLE-------------- 592
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239919865 1954 kRIGDLQAAIEDemESDENEDLITSLQDMVTKYQKRKNKPEGDSDVDSELEDRVDG 2009
Cdd:PRK02224 593 -RIRTLLAAIAD--AEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDE 645
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1281-1941 |
2.00e-13 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 76.42 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1281 EQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAErLRAEKEMkELQTQY 1360
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKE-KRDELNG-ELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1361 DALKKQMEVMEMEVMEARLIRAAEINGEVDDDDTGGEWRLKYERAMREVD-FTKK--RLQQEFED-KLEVEQQNKRQLER 1436
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKaLTGKhqDVTAKYNRrRSKIKEQNNRDIAG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1437 RLGDLQADIDESQRALQQLKKKCQRLTAELqdtklhlegqqvrNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKD 1516
Cdd:pfam12128 395 IKDKLAKIREARDRQLAVAEDDLQALESEL-------------REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1517 TLLaeafslkqQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDE-------QA 1589
Cdd:pfam12128 462 LLL--------QLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDElelqlfpQA 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1590 GTIQMLeqaklrLEMEMERMRQTHSKEVESR-------DEEVEEARQSCQKKLKQMEVQLEE----EYEDKQKVLREKRE 1658
Cdd:pfam12128 534 GTLLHF------LRKEAPDWEQSIGKVISPEllhrtdlDPEVWDGSVGGELNLYGVKLDLKRidvpEWAASEEELRERLD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1659 LESKlTTLSEQVSQRDLESE-KRLRKDLKRTKALLADAqimLDHLKNNapsKREIAQLKNQLEESEFTCAAAVKARKAME 1737
Cdd:pfam12128 608 KAEE-ALQSAREKQAAAEEQlVQANGELEKASREETFA---RTALKNA---RLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1738 VEmedlhlQIDDIAKAKTALEeqlsrlqrekNEIQSRLEEDQEDMNElmkkHKAAVAQASRDLaqMNDLQAQLEEANKEK 1817
Cdd:pfam12128 681 NE------RLNSLEAQLKQLD----------KKHQAWLEEQKEQKRE----ARTEKQAYWQVV--EGALDAQLALLKAAI 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1818 QELQEKLQALQSQVEF-----LEQSMVDKSLVSRQEAKIRELETRLEfertQVKRLESLASRLKENMEKLTEERDQRTAA 1892
Cdd:pfam12128 739 AARRSGAKAELKALETwykrdLASLGVDPDVIAKLKREIRTLERKIE----RIAVRRQEVLRYFDWYQETWLQRRPRLAT 814
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1239919865 1893 ENREKEQNkrlQRQLRDtkeemgELARKEAEASRKKHELEMDLESLEAA 1941
Cdd:pfam12128 815 QLSNIERA---ISELQQ------QLARLIADTKLRRAKLEMERKASEKQ 854
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1751-1966 |
2.37e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 74.42 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1751 AKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQ 1830
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1831 VEFLEQ---SMVDKSLVSRQEAKIREL---ETRLEFERTqVKRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQ 1904
Cdd:COG4942 99 LEAQKEelaELLRALYRLGRQPPLALLlspEDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239919865 1905 RQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDE 1966
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1494-1696 |
2.43e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 74.42 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1494 LSQAHEEAQREKlQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1573
Cdd:COG4942 16 AAQADAAAEAEA-ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1574 LEAKVKDQEEELDEQAGTIQML-EQAKLRLEM------EMERMRQTHSKEVESRDEEVEEARQScQKKLKQMEVQLEEEY 1646
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLgRQPPLALLLspedflDAVRRLQYLKYLAPARREQAEELRAD-LAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1647 EDKQKVLREKRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQ 1696
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1724-1955 |
2.66e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 74.03 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1724 FTCAAAVKARKAMEVEMEDLHLQIDdiakaktALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQM 1803
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIA-------ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1804 NDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAK-----IRELETRLEFERTQVKRLESLASRLKEN 1878
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239919865 1879 MEKLTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKR 1955
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1397-1839 |
6.66e-13 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 74.12 E-value: 6.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1397 EWRLKYEramrevDFTKKRLQqEFEDKL-EVEQQNKRqleRRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKlhleg 1475
Cdd:pfam06160 49 EWRKKWD------DIVTKSLP-DIEELLfEAEELNDK---YRFKKAKKALDEIEELLDDIEEDIKQILEELDELL----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1476 qqvrnhELEKKQRRFDSELsqaheeaqreklqREKLQREKDTLLAEAFS-------LKQQLEEKDMDIAGFTQKVVS--- 1545
Cdd:pfam06160 114 ------ESEEKNREEVEEL-------------KDKYRELRKTLLANRFSygpaideLEKQLAEIEEEFSQFEELTESgdy 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1546 LEAE--LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGTIQMLEQ----AKLRLEMEMERMRQTHSKEVES 1619
Cdd:pfam06160 175 LEARevLEKLEEETDALEELMEDIPPLYEELKTELPDQLEEL--KEGYREMEEEgyalEHLNVDKEIQQLEEQLEENLAL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1620 ----RDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQ----------------------VSQR 1673
Cdd:pfam06160 253 lenlELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQnkelkeelervqqsytlnenelERVR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1674 DLESE-KRLRKDLKRTKALLADAQI----MLDHLKnnapskreiaQLKNQLEEseftcaaavkarkaMEVEMEDLHLQID 1748
Cdd:pfam06160 333 GLEKQlEELEKRYDEIVERLEEKEVayseLQEELE----------EILEQLEE--------------IEEEQEEFKESLQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1749 DIAKAKTALEEQLSRLQREKNEIQSRLEEDQ-----EDMNELMKKHKAAVAQASRDLAQ----MNDLQAQLEEANKEKQE 1819
Cdd:pfam06160 389 SLRKDELEAREKLDEFKLELREIKRLVEKSNlpglpESYLDYFFDVSDEIEDLADELNEvplnMDEVNRLLDEAQDDVDT 468
|
490 500
....*....|....*....|
gi 1239919865 1820 LQEKLQALQSQVEFLEQSMV 1839
Cdd:pfam06160 469 LYEKTEELIDNATLAEQLIQ 488
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1606-2008 |
6.90e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 74.77 E-value: 6.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1606 MERMRQTHSKEVESRDEEVEEA-----------RQSC---QKKLKQMEVQLEEEYEDKQKVLREKRELESKLttlseQVS 1671
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESnelhekqkfylRQSVidlQTKLQEMQMERDAMADIRRRESQSQEDLRNQL-----QNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1672 QRDLESEKRLRKDLkrtkalLADAQIMLDHLKNNAPSK----REIAQLKNQLEES------EFTCAAAVKARK---AMEV 1738
Cdd:pfam15921 151 VHELEAAKCLKEDM------LEDSNTQIEQLRKMMLSHegvlQEIRSILVDFEEAsgkkiyEHDSMSTMHFRSlgsAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1739 EMEDLHLQIDDIAKAKTALEEQLSRLQRE-KNEIQSRLEEDQEDMNELMKKHKAAVA----QASRDLAQMNDLQAQLE-- 1811
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEITglteKASSARSQANSIQSQLEii 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1812 --EANKEKQELQEKLQALQSQVEFLEQSMVDKSLVsrQEAKIRELETRLEFE-------RTQVKRLESLASRLKENMEKL 1882
Cdd:pfam15921 305 qeQARNQNSMYMRQLSDLESTVSQLRSELREAKRM--YEDKIEELEKQLVLAnselteaRTERDQFSQESGNLDDQLQKL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1883 TEERDQRTAAENREKEQNKR--------------LQRQLRDTKEEMGEL-ARKEAEASRKKHELEMDLESLEAANQSLQ- 1946
Cdd:pfam15921 383 LADLHKREKELSLEKEQNKRlwdrdtgnsitidhLRRELDDRNMEVQRLeALLKAMKSECQGQMERQMAAIQGKNESLEk 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239919865 1947 -ADLKLAFKRIGDLQAAIEDEMESDEN--EDLITSLQDMVTKYQKRKNKPEGDSDVDSELEDRVD 2008
Cdd:pfam15921 463 vSSLTAQLESTKEMLRKVVEELTAKKMtlESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD 527
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1430-2008 |
7.98e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 7.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1430 NKRQLERRLGDLQADIDESQRALQqlkkkcQRLTAelqdtKLHLEGQQ--------------------VRNHELEKKQ-- 1487
Cdd:COG4913 156 DIRALKARLKKQGVEFFDSFSAYL------ARLRR-----RLGIGSEKalrllhktqsfkpigdlddfVREYMLEEPDtf 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1488 RRFDS------ELSQAHEEAQREKLQREKLQREKDtlLAEAF-SLKQQLEEKDMDIAGFTQKVVSLEAELQdissqeskd 1560
Cdd:COG4913 225 EAADAlvehfdDLERAHEALEDAREQIELLEPIRE--LAERYaAARERLAELEYLRAALRLWFAQRRLELL--------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1561 EASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKL--------RLEMEMERMRQTHskevesrdEEVEEARQSCQ 1632
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLEREL--------EERERRRARLE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1633 KKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQImLDHLKNNAPskREI 1712
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS-LERRKSNIP--ARL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1713 AQLKNQLEEseftcAAAVKARKA------MEVEMED--------------------------------------LHLQID 1748
Cdd:COG4913 443 LALRDALAE-----ALGLDEAELpfvgelIEVRPEEerwrgaiervlggfaltllvppehyaaalrwvnrlhlrGRLVYE 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1749 DI------AKAKTALEEQLSR-LQREKNEIQSRLE------------EDQEDmnelMKKHKAAVAQA-----SRDLAQMN 1804
Cdd:COG4913 518 RVrtglpdPERPRLDPDSLAGkLDFKPHPFRAWLEaelgrrfdyvcvDSPEE----LRRHPRAITRAgqvkgNGTRHEKD 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1805 DL-------------QAQLEEANKEKQELQEKLQALQSQVEFLEQSMvdKSLVSRQEAKIRELETRleFERTQVKRLESL 1871
Cdd:COG4913 594 DRrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAEL--DALQERREALQRLAEYS--WDEIDVASAERE 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1872 ASRLKENMEKLTEERDQRTAAENREKEQNKR---LQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEA-ANQSLQA 1947
Cdd:COG4913 670 IAELEAELERLDASSDDLAALEEQLEELEAEleeLEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlARLELRA 749
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1948 DLKLAFKRIG------DLQAAIEDEMES--DENEDLITSLQDMVTKYQKRknKPEGDSDVDSELEDRVD 2008
Cdd:COG4913 750 LLEERFAAALgdaverELRENLEERIDAlrARLNRAEEELERAMRAFNRE--WPAETADLDADLESLPE 816
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1494-1821 |
1.42e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 73.23 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1494 LSQAHEEAQREKLQREKLQREKDTLLAEaFSLKQQLEEKDMDIAGFTQKVVSLEAElQDISSQESKDEASLAKVKKQLRD 1573
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKARE-VERRRKLEEAEKARQAEMDRQAAIYAE-QERMAMERERELERIRQEERKRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1574 LEakvKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQ--THSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQK 1651
Cdd:pfam17380 362 LE---RIRQEEIAMEISRMRELERLQMERQQKNERVRQelEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1652 VLREKRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQimlDHLKNNAPSKREIaqLKNQLEESEFTCAAAVK 1731
Cdd:pfam17380 439 RLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK---RDRKRAEEQRRKI--LEKELEERKQAMIEEER 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1732 ARKAMEVEMEDlhlqiddiaKAKTALEEQlsrlQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASR--DLAQMNDLQAQ 1809
Cdd:pfam17380 514 KRKLLEKEMEE---------RQKAIYEEE----RRREAEEERRKQQEMEERRRIQEQMRKATEERSRleAMEREREMMRQ 580
|
330
....*....|..
gi 1239919865 1810 LEEANKEKQELQ 1821
Cdd:pfam17380 581 IVESEKARAEYE 592
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1281-1819 |
1.97e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1281 EQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERntGESASQLLDAEAAERLRAEKEMKELQTQy 1360
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL--AEAGLDDADAEAVEARREELEDRDEELR- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1361 DALKKQMevmemevmearlIRAAEINGEVddddtggewrlkyERAMREVDftkkrlqqEFEDKLEVEQQNKRQLERRLGD 1440
Cdd:PRK02224 328 DRLEECR------------VAAQAHNEEA-------------ESLREDAD--------DLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1441 LQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEkkqrrfdSELSQAHEeaqREKLQREKLQREKDTlLA 1520
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR-------EERDELRE---REAELEATLRTARER-VE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1521 EAFSLK---------QQLEEKDM--DIAGFTQKVVSLEAELQDISSQESKDEASLAKVkKQLRDLEAKVkdqeEELDEQA 1589
Cdd:PRK02224 444 EAEALLeagkcpecgQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRI----ERLEERR 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1590 GTI-QMLEQAKLRLEMEMERMRQTHsKEVESRDEEVEEARQSCQKKLKQMEVQLEE--EYEDKQKVLREKRElesKLTTL 1666
Cdd:PRK02224 519 EDLeELIAERRETIEEKRERAEELR-ERAAELEAEAEEKREAAAEAEEEAEEAREEvaELNSKLAELKERIE---SLERI 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1667 SEQVSQRDlesekRLRKDLKRTKALLADAQIMLDHLKNNAPSKRE-IAQLKNQLEESEFTCAAAVKARkaMEVEMEDLHL 1745
Cdd:PRK02224 595 RTLLAAIA-----DAEDEIERLREKREALAELNDERRERLAEKRErKRELEAEFDEARIEEAREDKER--AEEYLEQVEE 667
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239919865 1746 QIDDIAKAKTALEEQLSRLqreKNEIQsRLEEDQEDMNELMKKHKA--AVAQASRDLAQM-NDLQAQLEEANKEKQE 1819
Cdd:PRK02224 668 KLDELREERDDLQAEIGAV---ENELE-ELEELRERREALENRVEAleALYDEAEELESMyGDLRAELRQRNVETLE 740
|
|
| PDZ |
smart00228 |
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
218-309 |
2.56e-12 |
|
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.
Pssm-ID: 214570 [Multi-domain] Cd Length: 85 Bit Score: 64.71 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 218 LRELELQRRPTGdFGFSLRrttMLDRGPEGQVYRRVVhfaEPGAGTKDlalGLVPGDRLVEINGHNVESKSRDEIVEMIR 297
Cdd:smart00228 2 PRLVELEKGGGG-LGFSLV---GGKDEGGGVVVSSVV---PGSPAAKA---GLRVGDVILEVNGTSVEGLTHLEAVDLLK 71
|
90
....*....|..
gi 1239919865 298 QSGDSVRLKVQP 309
Cdd:smart00228 72 KAGGKVTLTVLR 83
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1275-1790 |
2.86e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLSEEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTseltderntgesasqlldaeaaERLRAEKEMK 1354
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE----------------------ERHELYEEAK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1355 ELQTQYDALKKQMEVmemevmearliraaeingevddddtggewrLKYERAMREVDFTKKRlQQEFEDKLEVEQQNKRQL 1434
Cdd:PRK03918 369 AKKEELERLKKRLTG------------------------------LTPEKLEKELEELEKA-KEEIEEEISKITARIGEL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1435 ERRLGDLQADIDEsqraLQQLKKKCQRLTAELQDtklhlegqqvrnHELEKKQRRFDSELSQAHEEAQREKLQREKLQRE 1514
Cdd:PRK03918 418 KKEIKELKKAIEE----LKKAKGKCPVCGRELTE------------EHRKELLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1515 KDTLLAEAFSLKQQLEEKDMdiagfTQKVVSLEAELQDISSQE-SKDEASLAKVKKQLRDLEAKVKDQEEELDEQagtiq 1593
Cdd:PRK03918 482 LRELEKVLKKESELIKLKEL-----AEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL----- 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1594 mleqaklrlememermrqthsKEVESRDEEVEEARQSCQKKLKQMEVQLEEE-YEDKQKVLREKRELES---KLTTLSEq 1669
Cdd:PRK03918 552 ---------------------EELKKKLAELEKKLDELEEELAELLKELEELgFESVEELEERLKELEPfynEYLELKD- 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1670 vSQRDLESEKRLRKDLKRTkalLADAQIMLDHLKNNAPSKR-EIAQLKNQLEESEFTCAAAVKARKAMEV-----EMEDL 1743
Cdd:PRK03918 610 -AEKELEREEKELKKLEEE---LDKAFEELAETEKRLEELRkELEELEKKYSEEEYEELREEYLELSRELaglraELEEL 685
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1239919865 1744 HLQIDDIAKAKTALEEQLSRLQREKNEIQSrLEEDQEDMNELMKKHK 1790
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEELREKVK 731
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1603-1943 |
3.17e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 72.08 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1603 EMEMERMRQTH---SKEVESRD--EEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTlsEQVSQRDLES 1677
Cdd:pfam17380 295 KMEQERLRQEKeekAREVERRRklEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKREL--ERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1678 EKRLRKDLKRtkalladaqIMLDHLKNNAPSKREI-AQLKNQLEESEFTcaaavKARKAMEVEMEDLHLQIDDiakaktA 1756
Cdd:pfam17380 373 EISRMRELER---------LQMERQQKNERVRQELeAARKVKILEEERQ-----RKIQQQKVEMEQIRAEQEE------A 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1757 LEEQLSRLQREKNEIQSRLEEDqedmnELMKKHkaavaqasrdlaQMNDLQAQLEEANKEKQELqEKLQALQSQVEFLEQ 1836
Cdd:pfam17380 433 RQREVRRLEEERAREMERVRLE-----EQERQQ------------QVERLRQQEEERKRKKLEL-EKEKRDRKRAEEQRR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1837 SMVDKSLVSRQEAKIRELETRLEFERtqvkrleslasRLKENMEKLTEERDQRTAAENREKEQN----KRLQRQLRDTKE 1912
Cdd:pfam17380 495 KILEKELEERKQAMIEEERKRKLLEK-----------EMEERQKAIYEEERRREAEEERRKQQEmeerRRIQEQMRKATE 563
|
330 340 350
....*....|....*....|....*....|...
gi 1239919865 1913 EMGEL--ARKEAEASRKKHELEMDLESLEAANQ 1943
Cdd:pfam17380 564 ERSRLeaMEREREMMRQIVESEKARAEYEATTP 596
|
|
| PDZ_SHANK1_3-like |
cd06746 |
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ... |
219-307 |
3.17e-12 |
|
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SHANK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.
Pssm-ID: 467228 [Multi-domain] Cd Length: 101 Bit Score: 64.92 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 219 RELELQRRPTGdFGFSLRRT---------TMLDRGPEGQVYRRVvhfaEPGaGTKDLAlGLVPGDRLVEINGHNVESKSR 289
Cdd:cd06746 7 RTVVLQKGDKG-FGFVLRGAkavgpilefTPTPAFPALQYLESV----DPG-GVADKA-GLKKGDFLLEINGEDVVKASH 79
|
90
....*....|....*...
gi 1239919865 290 DEIVEMIRQSGDSVRLKV 307
Cdd:cd06746 80 EQVVNLIRQSGNTLVLKV 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1746-2005 |
3.32e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1746 QIDDIAKAK-----TALEEQ--LSRLQREKNEIQSRLEEDQEDM-------NELMK-----KHKAAVAQASRDL------ 1800
Cdd:TIGR02168 145 KISEIIEAKpeerrAIFEEAagISKYKERRKETERKLERTRENLdrledilNELERqlkslERQAEKAERYKELkaelre 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1801 --------------AQMNDLQAQLEEANKEKQELQEKLQALQSQVEFL--EQSMVDKSLVSRQE------AKIRELETRL 1858
Cdd:TIGR02168 225 lelallvlrleelrEELEELQEELKEAEEELEELTAELQELEEKLEELrlEVSELEEEIEELQKelyalaNEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1859 EFERTQVKRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESL 1938
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239919865 1939 EAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLITSLQDMVTKYQKRKNKPEGDSDVDSELED 2005
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1428-1651 |
6.64e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.79 E-value: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1428 QQNKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQ 1507
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1508 REKLQREKDTLLAEAFSLKQQLEEKD-MDIAGFTQKVVSLEAeLQDISSQeskDEASLAKVKKQLRDLEAKVKDQEEELD 1586
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALlLSPEDFLDAVRRLQY-LKYLAPA---RREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1587 EQAGTIQMLEQAKLRLEMEMERMRQT---HSKEVESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQK 1651
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLlarLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1493-1859 |
7.71e-12 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 70.31 E-value: 7.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1493 ELSQAHEEAQREK-LQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISsqeskdeASLAKVKKQL 1571
Cdd:pfam07888 45 ELLQAQEAANRQReKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELS-------ASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1572 RDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQScQKKLKQMEVQLeeeyedkqk 1651
Cdd:pfam07888 118 DALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-QAKLQQTEEEL--------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1652 vlrekRELESKLTTLSEQVSQRDlESEKRLRKDLKRTKALLADAQimlDHLKNNAPSKREIAQLKNQLEESEFTCAA--- 1728
Cdd:pfam07888 188 -----RSLSKEFQELRNSLAQRD-TQVLQLQDTITTLTQKLTTAH---RKEAENEALLEELRSLQERLNASERKVEGlge 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1729 ----AVKARKAMEVEMEDLHLQIDD----IAKAKTALEEQLSRLQREKNEIQSRLEEDQEDM----NELMKKHKAAVAQA 1796
Cdd:pfam07888 259 elssMAAQRDRTQAELHQARLQAAQltlqLADASLALREGRARWAQERETLQQSAEADKDRIeklsAELQRLEERLQEER 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239919865 1797 SR------DLAQMNDL-QAQLEEANKEKQELQEKLQALQSQVEFLeqsmvdksLVSRQE--AKIRELETRLE 1859
Cdd:pfam07888 339 MEreklevELGREKDCnRVQLSESRRELQELKASLRVAQKEKEQL--------QAEKQEllEYIRQLEQRLE 402
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1651-1920 |
1.14e-11 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 70.04 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1651 KVLREK-RELESKLTTLSEQVS--QRDLESEKRLRKDL-KRTKALLADAQIMLDHLKNNAPS-KREIAQLKNQLEEseft 1725
Cdd:PHA02562 170 KLNKDKiRELNQQIQTLDMKIDhiQQQIKTYNKNIEEQrKKNGENIARKQNKYDELVEEAKTiKAEIEELTDELLN---- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1726 caaavkarkaMEVEMEDLHLQIDDIAKAKTALEEQLSRLQR-----EKNEIQSRLEEDQEDMNELMKKHKAavaqasrdl 1800
Cdd:PHA02562 246 ----------LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyEKGGVCPTCTQQISEGPDRITKIKD--------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1801 aQMNDLQAQLEEANKEKQELQEKLqalqsqVEFLEQSMvdkslvsrqeaKIRELETRLEFERTQVKRLESLASRLKENME 1880
Cdd:PHA02562 307 -KLKELQHSLEKLDTAIDELEEIM------DEFNEQSK-----------KLLELKNKISTNKQSLITLVDKAKKVKAAIE 368
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1239919865 1881 KLTEERDQRtaaenreKEQNKRLQRQLRDTKEEMGELARK 1920
Cdd:PHA02562 369 ELQAEFVDN-------AEELAKLQDELDKIVKTKSELVKE 401
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1641-2028 |
1.14e-11 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 69.16 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1641 QLEEEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQimldhlknnapskREIAQLKNQLE 1720
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR-------------EELEQLEEELE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1721 ESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDL 1800
Cdd:COG4372 70 QAR-------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1801 AQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENME 1880
Cdd:COG4372 143 SEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1881 KLTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQ 1960
Cdd:COG4372 223 AKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1961 AAIEDEMESDENEDLITSLQDMVTKYQKRKNKPEGDSDVDSELEDRVDGVKSWLSKNKGPSKAASDDG 2028
Cdd:COG4372 303 NLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1275-1605 |
1.40e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.48 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLSEEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRA----- 1349
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAelskl 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1350 EKEMKELQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDtggEWRLKYERAMREVDFTKKRLQqEFEDKLEVEQQ 1429
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLE----KEIQELQEQRI---DLKEQIKSIEKEIENLNGKKE-ELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1430 NKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVrnhelekkqrrfdselsqaheeaqreklQRE 1509
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA----------------------------KLE 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1510 KLQREKDTLLAEAFSLKQQLEEkDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQA 1589
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
330
....*....|....*.
gi 1239919865 1590 GTIQMLEQAKLRLEME 1605
Cdd:TIGR02169 1007 ERIEEYEKKKREVFME 1022
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1559-2043 |
1.57e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 70.39 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1559 KDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQmlEQAKLRLEMEMERMR-----------QTHSKEVESRDEEVEEA 1627
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQ--AKKALEYYQLKEKLEleeeyllyldyLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1628 RQSCQKKLKQmEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQIMLD-----HL 1702
Cdd:pfam02463 249 EQEEIESSKQ-EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEkekkkAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1703 KNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQedm 1782
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE--- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1783 NELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFER 1862
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1863 TQVKRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAeASRKKHELEMDLESLEAAN 1942
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA-ISTAVIVEVSATADEVEER 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1943 QSLQADLKLAFKRIGDLQAAIEDEmESDENEDLITSLQDMVTKYQKRKNKPEGDSDVDSELEDRVDGVKSWLSKNKGPSK 2022
Cdd:pfam02463 564 QKLVRALTELPLGARKLRLLIPKL-KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642
|
490 500
....*....|....*....|.
gi 1239919865 2023 AASDDGSLKSSRTALNTSGKE 2043
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSE 663
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1619-1986 |
2.97e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 69.43 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1619 SRDEEVEEARqscqkklkqmEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQrdlesekrLRKDLKRTKALLADAQIM 1698
Cdd:pfam01576 1 TRQEEEMQAK----------EEELQKVKERQQKAESELKELEKKHQQLCEEKNA--------LQEQLQAETELCAEAEEM 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1699 LDHLKNNAPSKREIAQ-LKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTAL-------------------- 1757
Cdd:pfam01576 63 RARLAARKQELEEILHeLESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLqlekvtteakikkleedill 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1758 -EEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQE--------------LQE 1822
Cdd:pfam01576 143 lEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQElekakrklegestdLQE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1823 KLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFERTQ----VKRLESLASRLKENMEKLTEERDQRTAAEnreke 1898
Cdd:pfam01576 223 QIAELQAQIAELRAQL------AKKEEELQAALARLEEETAQknnaLKKIRELEAQISELQEDLESERAARNKAE----- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1899 qnkrlqRQLRDTKEEMGELarkeaeasrkKHELEMDLESlEAANQSLQADLKlafKRIGDLQAAIEDEMESDEnedliTS 1978
Cdd:pfam01576 292 ------KQRRDLGEELEAL----------KTELEDTLDT-TAAQQELRSKRE---QEVTELKKALEEETRSHE-----AQ 346
|
....*...
gi 1239919865 1979 LQDMVTKY 1986
Cdd:pfam01576 347 LQEMRQKH 354
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1415-1952 |
2.98e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 69.60 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1415 RLQQEFED-KLEVEQQNKRQ--LERRLGDLQADIDE----------SQRALQQLKKKC-------QRLTAELQDTKLHLE 1474
Cdd:PRK04863 562 ELEARLESlSESVSEARERRmaLRQQLEQLQARIQRlaarapawlaAQDALARLREQSgeefedsQDVTEYMQQLLERER 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1475 GQQVRNHELEKKQRRFDSelsQAHEEAQREKLQREKLQREKDT----LLAEAFS-------------------------- 1524
Cdd:PRK04863 642 ELTVERDELAARKQALDE---EIERLSQPGGSEDPRLNALAERfggvLLSEIYDdvsledapyfsalygparhaivvpdl 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1525 --LKQQLEEKD----------MDIAGFTQKVVSLEAELQDISSQESKDEASLAKV-----------KKQLRDLEAKVKDQ 1581
Cdd:PRK04863 719 sdAAEQLAGLEdcpedlylieGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFpevplfgraarEKRIEQLRAEREEL 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1582 EEELDEQAGTIQMLEqaklRLEMEMERMRQTHSKEveSRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQkvlrekrELES 1661
Cdd:PRK04863 799 AERYATLSFDVQKLQ----RLHQAFSRFIGSHLAV--AFEADPEAELRQLNRRRVELERALADHESQEQ-------QQRS 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1662 KLTTLSEQVSQrdlesekrLRKDLKRTKaLLADaqimlDHLKNnapskrEIAQLKNQLEESEFtcAAAVKARKAMEVEme 1741
Cdd:PRK04863 866 QLEQAKEGLSA--------LNRLLPRLN-LLAD-----ETLAD------RVEEIREQLDEAEE--AKRFVQQHGNALA-- 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1742 dlhlQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQE---DMNELM-KKHKAAVAQASRDLAQMNDLQAQLEEANKEK 1817
Cdd:PRK04863 922 ----QLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafALTEVVqRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQA 997
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1818 QELQEKL--QALQSQVEFLEQSMVDKSLVSRQEAKireLETRLEFERtqvkRLESLASRLKENME-KLTEERDQRTAAEN 1894
Cdd:PRK04863 998 EQERTRAreQLRQAQAQLAQYNQVLASLKSSYDAK---RQMLQELKQ----ELQDLGVPADSGAEeRARARRDELHARLS 1070
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1895 REKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEmdlESLEAANQSLQADLKLA 1952
Cdd:PRK04863 1071 ANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR---EQVVNAKAGWCAVLRLV 1125
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1279-1505 |
3.02e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.87 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1279 SEEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELtderntgesasQLLDAEAAErlrAEKEMKELQT 1358
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----------RALEQELAA---LEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1359 QYDALKKQmeVMEMEVMEARLIRAAEINGEVD--------DDDTGGEWRLKYERAMREVDftKKRLQQEFEDKLEVEQQN 1430
Cdd:COG4942 91 EIAELRAE--LEAQKEELAELLRALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPAR--REQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239919865 1431 KRQLERR--LGDLQADIDESQRALQQLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFDSELSQAHEEAQREK 1505
Cdd:COG4942 167 AELEAERaeLEALLAELEEERAALEALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1486-2067 |
3.14e-11 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 69.16 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1486 KQRRFDSELSQahEEAQREKLQREKLqrEKDTLLAEAFSLKQQLEekdmdiagftqkvvSLEAELQDISSQESKDEAS-- 1563
Cdd:PRK01156 136 GQGEMDSLISG--DPAQRKKILDEIL--EINSLERNYDKLKDVID--------------MLRAEISNIDYLEEKLKSSnl 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1564 -LAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMrQTHSKEVESRDEEVEEArqscqkklkQMEVQL 1642
Cdd:PRK01156 198 eLENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNEL-SSLEDMKNRYESEIKTA---------ESDLSM 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1643 EEEYEDKQKVLREKReleSKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEs 1722
Cdd:PRK01156 268 ELEKNNYYKELEERH---MKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIK- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1723 eftcaaavkarkaMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQ 1802
Cdd:PRK01156 344 -------------KKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKE 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1803 MNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM-----------------VDKSL---------VSRQEAKIRELEt 1856
Cdd:PRK01156 411 LNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgEEKSNhiinhynekKSRLEEKIREIE- 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1857 rleferTQVKRLESLASRLKENMEKLTEERDQRTAAENRekeQNKRLQRQLRDTKEEMGELARKEAEASRKKHELE-MDL 1935
Cdd:PRK01156 490 ------IEVKDIDEKIVDLKKRKEYLESEEINKSINEYN---KIESARADLEDIKIKINELKDKHDKYEEIKNRYKsLKL 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1936 ESLEA------------------ANQSLQADLKLAFKRIGDLQAAIEDEMESDE--NEDLITSLQDMVTKYQKRKNKPEG 1995
Cdd:PRK01156 561 EDLDSkrtswlnalavislidieTNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyIDKSIREIENEANNLNNKYNEIQE 640
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239919865 1996 DSDVDSELEDRVDGVKSWLSKNKGPSKaasddgSLKSSRTALNTSGKEGKGVEERPASALSSLsYRKRLTLK 2067
Cdd:PRK01156 641 NKILIEKLRGKIDNYKKQIAEIDSIIP------DLKEITSRINDIEDNLKKSRKALDDAKANR-ARLESTIE 705
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1754-1978 |
4.23e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 67.55 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1754 KTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKL----QALQ- 1828
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraRALYr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1829 --SQVEFLEQSMVDKS---LVSRQEAkireLETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRL 1903
Cdd:COG3883 98 sgGSVSYLDVLLGSESfsdFLDRLSA----LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239919865 1904 QRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLITS 1978
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1298-1968 |
4.91e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 68.83 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1298 EKVEKERNELRLSNDRLETRiSELTSELTDERntgesasqlldAEAAERL-RAEKEMKELQTQY-------DALkkQMEV 1369
Cdd:COG3096 347 EKIERYQEDLEELTERLEEQ-EEVVEEAAEQL-----------AEAEARLeAAEEEVDSLKSQLadyqqalDVQ--QTRA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1370 MEMEVMEARLIRAAEINGEVD-DDDTGGEWrlkyeramrevdftkkrlQQEFEDKLEVEQQNKRQLERRLGDLQADIDES 1448
Cdd:COG3096 413 IQYQQAVQALEKARALCGLPDlTPENAEDY------------------LAAFRAKEQQATEEVLELEQKLSVADAARRQF 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1449 QRALQQLKKkcqrLTAELQDTKLHLEGQQV-RNHELEKKQRRFDSELSQAHEEAQREKLQREKLQRekdtlLAEAF--SL 1525
Cdd:COG3096 475 EKAYELVCK----IAGEVERSQAWQTARELlRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAER-----LLEEFcqRI 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1526 KQQLEEKDMdiagFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKdqeeELDEQAgtiqmleQAKLRLEME 1605
Cdd:COG3096 546 GQQLDAAEE----LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK----ELAARA-------PAWLAAQDA 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1606 MERMRQTHSKEVESRdEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKREL-------ESKLTTLSEQVSQrDLESE 1678
Cdd:COG3096 611 LERLREQSGEALADS-QEVTAAMQQLLEREREATVERDELAARKQALESQIERLsqpggaeDPRLLALAERLGG-VLLSE 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1679 -----------------KRLRK-----DLKRTKALLADAQIMLDHL----------KNNAPSKRE-----IAQLKN-QLE 1720
Cdd:COG3096 689 iyddvtledapyfsalyGPARHaivvpDLSAVKEQLAGLEDCPEDLyliegdpdsfDDSVFDAEEledavVVKLSDrQWR 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1721 ESEFTcAAAVKARKAMEVEMEDLHLQIDDIAK--AKTALEEQ-LSRLQ-----------------------REKNEIQSR 1774
Cdd:COG3096 769 YSRFP-EVPLFGRAAREKRLEELRAERDELAEqyAKASFDVQkLQRLHqafsqfvgghlavafapdpeaelAALRQRRSE 847
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1775 LEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEkqELQEKLQALQSQVEFLEQsmvDKSLVSRQEAKIREL 1854
Cdd:COG3096 848 LERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE--TLADRLEELREELDAAQE---AQAFIQQHGKALAQL 922
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1855 ETRL----------EFERTQVKRLESLASRLKENMEKLTEERDQRTA----------AENRekEQNKRLQRQLRDTKEEM 1914
Cdd:COG3096 923 EPLVavlqsdpeqfEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfsyedavgllGENS--DLNEKLRARLEQAEEAR 1000
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1915 GElARKEAEASRKKHE----LEMDLES-LEAANQSLQAdlklAFKRIGDLQAAIEDEME 1968
Cdd:COG3096 1001 RE-AREQLRQAQAQYSqynqVLASLKSsRDAKQQTLQE----LEQELEELGVQADAEAE 1054
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1614-1947 |
5.37e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 68.46 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1614 SKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELES---KLTTLSEQVSQRDLESEKRLRKDLKRTKA 1690
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYyqlKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1691 LLADAQIMLDHLKNNAP-SKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKN 1769
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEkEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1770 EIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKL----QALQSQVEFLEQSMVDKSLVS 1845
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKklesERLSSAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1846 RQEAKIRELETRLEFERTqvKRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEAS 1925
Cdd:pfam02463 405 KEAQLLLELARQLEDLLK--EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330 340
....*....|....*....|..
gi 1239919865 1926 RKKHELEMDLESLEAANQSLQA 1947
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESK 504
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1622-1847 |
5.87e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.10 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1622 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVsqRDLESE-KRLRKDLKRTKALLADAQIMLD 1700
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI--RALEQElAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1701 HLKNN-APSKREIAQLKNQ------LEESEFtcAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQS 1773
Cdd:COG4942 101 AQKEElAELLRALYRLGRQpplallLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239919865 1774 ---RLEEDQEDMNELMKKHKAAVAQASRDLAQmndLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ 1847
Cdd:COG4942 179 llaELEEERAALEALKAERQKLLARLEKELAE---LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1542-1948 |
6.05e-11 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 67.84 E-value: 6.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1542 KVVSLEAELQDISSQESKDEASLakvKKQLRDLEAKVKDQEEELDEQAgtiqmleQAKLRLEMEMERMRQTHSKEVESRD 1621
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH---KRARIELEKKASALKRQLDRES-------DRNQELQKRIRLLEKREAEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1622 EEVEEARQsCQKKLKQMEvQLEEEYEDKQKVLRE-KRELESKLTTLSEQVSQRDLEsekrlrkdLKRTKALLADAQIMLD 1700
Cdd:pfam05557 73 EQAELNRL-KKKYLEALN-KKLNEKESQLADAREvISCLKNELSELRRQIQRAELE--------LQSTNSELEELQERLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1701 HLKNNApskREIAQLKNQLEESEFTCAAAVKARKAMEVEMEdlhLQIDDIAKAKTALEEQLS--RLQREkneiQSRLEED 1778
Cdd:pfam05557 143 LLKAKA---SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQ---SQEQDSEIVKNSKSELARipELEKE----LERLREH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1779 QEDMNELMKKH---KAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQ-----------------ALQSQVEFLEQSm 1838
Cdd:pfam05557 213 NKHLNENIENKlllKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQswvklaqdtglnlrspeDLSRRIEQLQQR- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1839 vDKSLVSRQ-----------------EAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERD-QRTAAENREKEQN 1900
Cdd:pfam05557 292 -EIVLKEENssltssarqlekarrelEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgYRAILESYDKELT 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1901 -KRLQRQLRDTKEEMGELARK-EAEASRKKHELEMDLESLEAANQSLQAD 1948
Cdd:pfam05557 371 mSNYSPQLLERIEEAEDMTQKmQAHNEEMEAQLSVAEEELGGYKQQAQTL 420
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1281-1897 |
6.53e-11 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 68.54 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1281 EQIRSKDE----EIQQLRSKLEKVekerNELRLSNDR---LETRISELTSELTDERNTGESASQLLDaEAAErlrAEKEm 1353
Cdd:TIGR01612 1135 EEIKKKSEnyidEIKAQINDLEDV----ADKAISNDDpeeIEKKIENIVTKIDKKKNIYDEIKKLLN-EIAE---IEKD- 1205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1354 kelQTQYDALKKQMEVMEMEVMEARLiraaeinGEVDDDDTGGEWRLK-YERAMREVDFTKKRlQQEFEDKLEVEQQNKR 1432
Cdd:TIGR01612 1206 ---KTSLEEVKGINLSYGKNLGKLFL-------EKIDEEKKKSEHMIKaMEAYIEDLDEIKEK-SPEIENEMGIEMDIKA 1274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1433 QLErrlgdlQADIDESqralqqlKKKCQRLTAELQDTKLhlegQQVRNHELEKKQRRF-DSELSQAHEEAQREKLQREKL 1511
Cdd:TIGR01612 1275 EME------TFNISHD-------DDKDHHIISKKHDENI----SDIREKSLKIIEDFSeESDINDIKKELQKNLLDAQKH 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1512 QREKDTLLAEAFSLKQQLEEKDM-----DIAGFTQKVvslEAELQDISSQESKDEASLAKVKKQLRDLEAKVKdQEEELD 1586
Cdd:TIGR01612 1338 NSDINLYLNEIANIYNILKLNKIkkiidEVKEYTKEI---EENNKNIKDELDKSEKLIKKIKDDINLEECKSK-IESTLD 1413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1587 EQ--AGTIQMLEQAKLRLEMEmERMRQTHSKEVESRDEEV-------EEARQSCQKKLKQMEVQLEEEYEDKQKVLREKR 1657
Cdd:TIGR01612 1414 DKdiDECIKKIKELKNHILSE-ESNIDTYFKNADENNENVlllfkniEMADNKSQHILKIKKDNATNDHDFNINELKEHI 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1658 ELESKLTTLSEQvSQRDLESEKRLRKDLKRTKALLADAQIMLDhLKNN-APSKREIAQLKNQLEE--SEFTCAAAVKARK 1734
Cdd:TIGR01612 1493 DKSKGCKDEADK-NAKAIEKNKELFEQYKKDVTELLNKYSALA-IKNKfAKTKKDSEIIIKEIKDahKKFILEAEKSEQK 1570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1735 AMEVEMEDLHLQiDDIAKAKTAleeqlsrlQREKNEIQSRLEEDQedmNELMKKhkAAVAQASRD-LAQMNDLQAQLE-- 1811
Cdd:TIGR01612 1571 IKEIKKEKFRIE-DDAAKNDKS--------NKAAIDIQLSLENFE---NKFLKI--SDIKKKINDcLKETESIEKKISsf 1636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1812 EANKEKQELQEKLQALQSQVEFLEqSMVDkslvsrQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTA 1891
Cdd:TIGR01612 1637 SIDSQDTELKENGDNLNSLQEFLE-SLKD------QKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIA 1709
|
....*.
gi 1239919865 1892 AENREK 1897
Cdd:TIGR01612 1710 IANKEE 1715
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1448-1998 |
7.12e-11 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 67.92 E-value: 7.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1448 SQRALQQLKKKCQRLTAELqdtKLHLEGQQVRNHELEKKQRrfDSELSQAHEEAQREKLQRekLQREKDTLLAEAFSLKQ 1527
Cdd:pfam10174 65 TQEENQHLQLTIQALQDEL---RAQRDLNQLLQQDFTTSPV--DGEDKFSTPELTEENFRR--LQSEHERQAKELFLLRK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1528 QLEEKDMDIAgfTQKvvsleaelqdiSSQESKDEAslakVKKQLRDLEAKVKDQEEELDEQAGTIQMLEqAKLRLEmEME 1607
Cdd:pfam10174 138 TLEEMELRIE--TQK-----------QTLGARDES----IKKLLEMLQSKGLPKKSGEEDWERTRRIAE-AEMQLG-HLE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1608 RMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQ--KVLREKRELESKLTTLSeqvSQRDLESEKRlRKDL 1685
Cdd:pfam10174 199 VLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKisSLERNIRDLEDEVQMLK---TNGLLHTEDR-EEEI 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1686 KRTKALLADAQIMldhlknnapsKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQ 1765
Cdd:pfam10174 275 KQMEVYKSHSKFM----------KNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQ 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1766 REKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEfleqsMVDKSLVS 1845
Cdd:pfam10174 345 TEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLR-----DKDKQLAG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1846 RQEAkIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQrtaaENREK-EQNKRLQRQLRDTKEEMGELARKEAEA 1924
Cdd:pfam10174 420 LKER-VKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQRER----EDRERlEELESLKKENKDLKEKVSALQPELTEK 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1925 SRKKHELEMDLESLeaANQSLQADLKLAFKRI-------------GDLQAAIEDEMESDENEDL---ITSLQDMVTKYQK 1988
Cdd:pfam10174 495 ESSLIDLKEHASSL--ASSGLKKDSKLKSLEIaveqkkeecskleNQLKKAHNAEEAVRTNPEIndrIRLLEQEVARYKE 572
|
570
....*....|
gi 1239919865 1989 RKNKPEGDSD 1998
Cdd:pfam10174 573 ESGKAQAEVE 582
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1275-1855 |
1.11e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.45 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLSEEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGEsasqlLDAEAAERLRAEKE-M 1353
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD-----LKLQELQHLKNEGDhL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1354 KELQTQYDALKKQMEVMEMEVMEAR--LIRAAEINGEvdDDDTGGEwrLKYERAMREVDFTKKRLQ-QEFEDKLEVEQQN 1430
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRqqIENMTQLVGQ--HGRTAGA--MQVEKAQLEKEINDRRLElQEFKILKDKKDAK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1431 KRQLERRLGDLQADI-------DESQRALQQLKKKCQRLTAELQDTKLHLEG---------QQVRN--HELEKKQRRFDS 1492
Cdd:pfam15921 620 IRELEARVSDLELEKvklvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSlsedyevlkRNFRNksEEMETTTNKLKM 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1493 ELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLE---------------------AELQ 1551
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEeamtnankekhflkeeknklsQELS 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1552 DISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQSC 1631
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSM 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1632 QKKL---------------KQMEVQLEEEYEDKQKVLRE--KRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLAD 1694
Cdd:pfam15921 860 KPRLlqpasftrthsnvpsSQSTASFLSHHSRKTNALKEdpTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALD 939
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1695 AQIMLDHLKNNAPSK---REIAQLKNQLEESEFTCAAAVKARKAMevEMEDLHLQIDDIAKAKTALEEQLSR---LQREK 1768
Cdd:pfam15921 940 DRVRDCIIESSLRSDichSSSNSLQTEGSKSSETCSREPVLLHAG--ELEDPSSCFTFPSTASPSVKNSASRsfhSSPKK 1017
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1769 NEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQmnDLQAQ-LEEANKEKQELQEKLQALQSQVEFLE---QSMvdKSLV 1844
Cdd:pfam15921 1018 SPVHSLLTSSAEGSIGSSSQYRSAKTIHSPDSVK--DSQSLpIETTGKTCRKLQNRLESLQTLVEDLQlknQAM--SSMI 1093
|
650
....*....|.
gi 1239919865 1845 SRQEAKIRELE 1855
Cdd:pfam15921 1094 RNQEKRIQKVK 1104
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1555-1989 |
1.72e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 66.92 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1555 SQESKDEASLAKVKKQLRDLEAKVKDQ--EEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEveSRDEEVEEARQSCQ 1632
Cdd:TIGR00618 182 ALMEFAKKKSLHGKAELLTLRSQLLTLctPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL--TQKREAQEEQLKKQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1633 KKLKQMEVQlEEEYEDKQKVL---REKRELESK---LTTLSEQVSQRDLESEkRLRKDLKRTKALLADAQIMLDHLKNNA 1706
Cdd:TIGR00618 260 QLLKQLRAR-IEELRAQEAVLeetQERINRARKaapLAAHIKAVTQIEQQAQ-RIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1707 PSKREIAQLKNQL--EESEFTCAAAVKA--RKAMEVEMEDLHlQIDDIAKAKTALEEQ-------LSRLQREKNEIQSRL 1775
Cdd:TIGR00618 338 SSIEEQRRLLQTLhsQEIHIRDAHEVATsiREISCQQHTLTQ-HIHTLQQQKTTLTQKlqslckeLDILQREQATIDTRT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1776 EEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSqvefLEQSMVDKSLVSRQEAKIRELE 1855
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE----REQQLQTKEQIHLQETRKKAVV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1856 trlefertqVKRLESLASRLKENMEKLTEERDQRTAAENREKEQ---------NKRLQRQLRDTKEEMGELARKEAEASR 1926
Cdd:TIGR00618 493 ---------LARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTrrmqrgeqtYAQLETSEEDVYHQLTSERKQRASLKE 563
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1927 KKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESD-----ENEDLITSLQDMVTKYQKR 1989
Cdd:TIGR00618 564 QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEdmlacEQHALLRKLQPEQDLQDVR 631
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1265-1664 |
2.12e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 66.28 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1265 KLFTTVRPLIEVQLSEEQIRSKDE--------EIQQLRSKLEKVEKERNELRLSNDRLETRISElTSELTDERNTGESAS 1336
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEdqlkiitmELQKKSSELEEMTKFKNNKEVELEELKKILAE-DEKLLDEKKQFEKIA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1337 QLLDAEAAERL----RAEKEMKELQTQYDALKKQMEVMEMevmearliraaeingEVDDDDTggewRLKYERaMREVDFT 1412
Cdd:pfam05483 432 EELKGKEQELIfllqAREKEIHDLEIQLTAIKTSEEHYLK---------------EVEDLKT----ELEKEK-LKNIELT 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1413 KKRLQQEFEDKLEVEQQNKRQLErrLGDLQADIDESQRALQQLKKKCQRLtaELQDTKLHLEGQQVRNhELEKKQRRFDS 1492
Cdd:pfam05483 492 AHCDKLLLENKELTQEASDMTLE--LKKHQEDIINCKKQEERMLKQIENL--EEKEMNLRDELESVRE-EFIQKGDEVKC 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1493 ELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLE----AELQDISSQE---SKDEASLA 1565
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsAENKQLNAYEikvNKLELELA 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1566 KVKKQL--------RDLEAKVKDQEEELDE-QAGTIQMLEQAKLRLEME-------------MERMRQTHSKEVESRDEE 1623
Cdd:pfam05483 647 SAKQKFeeiidnyqKEIEDKKISEEKLLEEvEKAKAIADEAVKLQKEIDkrcqhkiaemvalMEKHKHQYDKIIEERDSE 726
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1624 V-----EEARQSCQKKLKQMEV------------QLEEEYEDKQKVLREKRELESKLT 1664
Cdd:pfam05483 727 LglyknKEQEQSSAKAALEIELsnikaellslkkQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1275-1895 |
2.64e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 66.40 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLSEEQIRS-KDEEIQQLRSKLEKVEKERNELRLSNDRL--------------ETRISELTSELTD--ERNTGESASQ 1337
Cdd:pfam12128 323 ELEALEDQHGAfLDADIETAAADQEQLPSWQSELENLEERLkaltgkhqdvtakyNRRRSKIKEQNNRdiAGIKDKLAKI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1338 lldAEAAERLRAEKEmKELQTQYDALKKQMEVMEMEVMEARL---IRAAEINGEVDDDDTGGEWRLKYERAMREVDFTKK 1414
Cdd:pfam12128 403 ---REARDRQLAVAE-DDLQALESELREQLEAGKLEFNEEEYrlkSRLGELKLRLNQATATPELLLQLENFDERIERARE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1415 RLQQEFedkleveqQNKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRfDSEL 1494
Cdd:pfam12128 479 EQEAAN--------AEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAP-DWEQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1495 SQAhEEAQREKLQREKLQREKDTLLAEA----FSLKQQLEEkdMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQ 1570
Cdd:pfam12128 550 SIG-KVISPELLHRTDLDPEVWDGSVGGelnlYGVKLDLKR--IDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1571 LRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQ 1650
Cdd:pfam12128 627 LVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQK 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1651 KVLREKRelESKLTTLSEQVSQRDLEsekrlrkdLKRTKALLADAQIMLdhlknnapsKREIAQLKNQLEESEFTCAAAV 1730
Cdd:pfam12128 707 EQKREAR--TEKQAYWQVVEGALDAQ--------LALLKAAIAARRSGA---------KAELKALETWYKRDLASLGVDP 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1731 KARKAMEVEMEDLHLQIDDIAKAKTALEE----QLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDL 1806
Cdd:pfam12128 768 DVIAKLKREIRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEME 847
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1807 QAQLEEANKEKQELQEKLQALQSQVEFLeqsmvdkslvsRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEER 1886
Cdd:pfam12128 848 RKASEKQQVRLSENLRGLRCEMSKLATL-----------KEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHF 916
|
....*....
gi 1239919865 1887 DQRTAAENR 1895
Cdd:pfam12128 917 KNVIADHSG 925
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1741-1946 |
2.71e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 65.81 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1741 EDLHLQIDDIAKAKTALEEQLsrlqrekNEIQSRLEEDQEDMNELMKKHKAAVAQAsrdlaQMNDLQAQLEEANKEKQEL 1820
Cdd:COG3206 164 QNLELRREEARKALEFLEEQL-------PELRKELEEAEAALEEFRQKNGLVDLSE-----EAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1821 QEKLQALQSQVEFLEQSM----------VDKSLVSRQEAKIRELETRLEFERT-------QVKRLESLASRLKENMEKLT 1883
Cdd:COG3206 232 RAELAEAEARLAALRAQLgsgpdalpelLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 1884 EERDQRTAAENRE-KEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQ 1946
Cdd:COG3206 312 QRILASLEAELEAlQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1274-1933 |
2.72e-10 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 66.39 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1274 IEVQLSEEQIRSKDeeIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESasqllDAEAAERLRAEKEM 1353
Cdd:PTZ00440 786 KDTILNKENKISND--INILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFPT-----EDENLNLKELEKEF 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1354 KELQTQYDALKKQMEvmemevmearliraaEINGEVDdddtggewrlkyerAMREVDFTKKRL---QQEFEDKLEVEQQN 1430
Cdd:PTZ00440 859 NENNQIVDNIIKDIE---------------NMNKNIN--------------IIKTLNIAINRSnsnKQLVEHLLNNKIDL 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1431 KRQLERRLGDLQAD----IDESQRALQQLKKKCQRLTAELQDTK---LHLEGQQVRNHeLEKKQRRFDSELSQAHEEAQR 1503
Cdd:PTZ00440 910 KNKLEQHMKIINTDniiqKNEKLNLLNNLNKEKEKIEKQLSDTKinnLKMQIEKTLEY-YDKSKENINGNDGTHLEKLDK 988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1504 EKLQREKLQREKDTLLAEAFSLKQQ-------------------LEEKDMDIAGFTQKVVSLEAELQD-ISSQESKDEAS 1563
Cdd:PTZ00440 989 EKDEWEHFKSEIDKLNVNYNILNKKiddlikkqhddiielidklIKEKGKEIEEKVDQYISLLEKMKTkLSSFHFNIDIK 1068
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1564 L---AKVKKQLRDLEAKVKDQEEELDEQagtiqmleqaklrlEMEMERMRQTHSKEVESRDEEVEEARQSCQKKLKQMev 1640
Cdd:PTZ00440 1069 KyknPKIKEEIKLLEEKVEALLKKIDEN--------------KNKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKSL-- 1132
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1641 qlEEEYEDKQKVLREKRELESKLTTLSEqVSQRDLESEKrlrkdlkrtkalladaqIMLDHLKNnapskreiaQLKNQLE 1720
Cdd:PTZ00440 1133 --EKIYKQMEKTLKELENMNLEDITLNE-VNEIEIEYER-----------------ILIDHIVE---------QINNEAK 1183
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1721 ESeftcaaavkarkamEVEMEDLHLQIDDI--AKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASR 1798
Cdd:PTZ00440 1184 KS--------------KTIMEEIESYKKDIdqVKKNMSKERNDHLTTFEYNAYYDKATASYENIEELTTEAKGLKGEANR 1249
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1799 DlAQMNDLQ-------AQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLV----SRQEAKIRELETRLEFERTqvkr 1867
Cdd:PTZ00440 1250 S-TNVDELKeiklqvfSYLQQVIKENNKMENALHEIKNMYEFLISIDSEKILKeilnSTKKAEEFSNDAKKELEKT---- 1324
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 1868 lESLASRLKENMEKLTEERDQRTAAENREK-EQN----KRLQRQLRDTKEEMGELArKEAEASRKKHELEM 1933
Cdd:PTZ00440 1325 -DNLIKQVEAKIEQAKEHKNKIYGSLEDKQiDDEikkiEQIKEEISNKRKEINKYL-SNIKSNKEKCDLHV 1393
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1738-1936 |
3.11e-10 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 62.63 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1738 VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQ---EDMNELMKKHKAAVAQASrdlAQMNDLQAQLEEAN 1814
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKtelEDLEKEIKRLELEIEEVE---ARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1815 KEKQelqekLQALQSQVEFLEqsmvdkslvsrqeakireletrlefertqvKRLESLASRLKENMEKLTEERDQRTAAEN 1894
Cdd:COG1579 87 NNKE-----YEALQKEIESLK------------------------------RRISDLEDEILELMERIEELEEELAELEA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1239919865 1895 REKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLE 1936
Cdd:COG1579 132 ELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1400-2050 |
4.77e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 65.45 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1400 LKYERAMREVDFTKKRLQQ---EFEDKLE-VEQQNKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQdtklhLEG 1475
Cdd:TIGR00606 265 MKLDNEIKALKSRKKQMEKdnsELELKMEkVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERR-----LLN 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1476 QQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISS 1555
Cdd:TIGR00606 340 QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1556 QESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQSCQKKL 1635
Cdd:TIGR00606 420 KERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1636 KQMEVQLEEeyedkqkvlrEKRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQIMldhlKNNAPSKREIAQL 1715
Cdd:TIGR00606 500 KKEVKSLQN----------EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR----KIKSRHSDELTSL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1716 ------KNQLEeseftcaaavkarKAMEVEMEDLHLQIDDIAKaktaLEEQLSRLQREKNEIQSRLEEDQEDMNELMKKH 1789
Cdd:TIGR00606 566 lgyfpnKKQLE-------------DWLHSKSKEINQTRDRLAK----LNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1790 KAAVAQASRDlAQMNDLQAQLEEANKEKQELQEKlQALQSQveFLEQSMVDKS-------LVSRQEAKIRE----LETRL 1858
Cdd:TIGR00606 629 FDVCGSQDEE-SDLERLKEEIEKSSKQRAMLAGA-TAVYSQ--FITQLTDENQsccpvcqRVFQTEAELQEfisdLQSKL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1859 EFERTQVKRLESLASRLKENMEKLTEERDQRtaaenrekeqnkrlQRQLRDTKEEMGELARKEAEASRKKHELEMDLESL 1938
Cdd:TIGR00606 705 RLAPDKLKSTESELKKKEKRRDEMLGLAPGR--------------QSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1939 EAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLITSL------QDMVTKYQK-RKNKPEGDSDVDSELEDRVDGVK 2011
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQaaklqgSDLDRTVQQvNQEKQEKQHELDTVVSKIELNRK 850
|
650 660 670
....*....|....*....|....*....|....*....
gi 1239919865 2012 SWLSKNKGPSKAASDDGSLKSSRTALNTSGKEGKGVEER 2050
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQ 889
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1451-1831 |
7.07e-10 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 64.54 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1451 ALQQLKKKCQRLT-AELQDTKLHLEGQQVRNhELEKKQRRFDSEL-SQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQ 1528
Cdd:pfam15964 333 AYEQVKQAVQMTEeANFEKTKALIQCEQLKS-ELERQKERLEKELaSQQEKRAQEKEALRKEMKKEREELGATMLALSQN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1529 LEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ-----AGTIQMLEQA----- 1598
Cdd:pfam15964 412 VAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEhreyrTKTGRQLEIKdqeie 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1599 KLRLEMEMERMRqthskeVESRDEEVEEARQSCQK---KLKQMEVQLEEEYEDKQKVLREKRElESKLTTLSEQVSQRDL 1675
Cdd:pfam15964 492 KLGLELSESKQR------LEQAQQDAARAREECLKlteLLGESEHQLHLTRLEKESIQQSFSN-EAKAQALQAQQREQEL 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1676 -----ESEKRLRKDLKRTKALLADAQIMLDHLKnnapskREIAQLKNQLEEseftcaAAVKARKAME---VEMEDLHLQI 1747
Cdd:pfam15964 565 tqkmqQMEAQHDKTVNEQYSLLTSQNTFIAKLK------EECCTLAKKLEE------ITQKSRSEVEqlsQEKEYLQDRL 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1748 DDIAKAKTALEEQLSRLQREKNEIQSRLEEdqedmnelMKKHKAAVAQasrDLAQMNDLQAQLEeanKEKQELQEKLQAL 1827
Cdd:pfam15964 633 EKLQKRNEELEEQCVQHGRMHERMKQRLRQ--------LDKHCQATAQ---QLVQLLSKQNQLF---KERQNLTEEVQSL 698
|
....
gi 1239919865 1828 QSQV 1831
Cdd:pfam15964 699 RSQV 702
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1650-1826 |
7.61e-10 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 61.48 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1650 QKVLREKRELESKLTTLSEQVsqRDLESE-KRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESEFTCAA 1728
Cdd:COG1579 13 QELDSELDRLEHRLKELPAEL--AELEDElAALEARLEAAKTELEDLEKEIKRLEL------EIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1729 AVKAR--KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAqasrdlaqmnDL 1806
Cdd:COG1579 85 VRNNKeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA----------EL 154
|
170 180
....*....|....*....|
gi 1239919865 1807 QAQLEEANKEKQELQEKLQA 1826
Cdd:COG1579 155 EAELEELEAEREELAAKIPP 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1493-1683 |
1.01e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 61.09 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1493 ELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQlR 1572
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1573 DLEAKVKdqeeELDEQAGTIQMLEQAKLRLEMEMErmrqthskEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKv 1652
Cdd:COG1579 90 EYEALQK----EIESLKRRISDLEDEILELMERIE--------ELEEELAELEAELAELEAELEEKKAELDEELAELEA- 156
|
170 180 190
....*....|....*....|....*....|.
gi 1239919865 1653 lrEKRELESKLTTLSEQVSQRDLESEKRLRK 1683
Cdd:COG1579 157 --ELEELEAEREELAAKIPPELLALYERIRK 185
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1502-1914 |
1.04e-09 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 63.70 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1502 QREKLQR-EKLQREKDTLlaEAFSLKQQLEE-KDMDIAGFTQKVV-SLEAELQDISSqeskdeASLAKVKKQLRDLEA-- 1576
Cdd:PRK04778 24 RKRNYKRiDELEERKQEL--ENLPVNDELEKvKKLNLTGQSEEKFeEWRQKWDEIVT------NSLPDIEEQLFEAEEln 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1577 ------KVKDQEEELDEQagtIQMLEQaklrlemEMERMRqthskevesrdEEVEEARQSCQKKLKQMEvQLEEEYEDKQ 1650
Cdd:PRK04778 96 dkfrfrKAKHEINEIESL---LDLIEE-------DIEQIL-----------EELQELLESEEKNREEVE-QLKDLYRELR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1651 KVLREKR--------ELESKLTTLSEQVSQRDLESEK-----------RLRKDLKRTKALLADAQIMLDHLKNNAPSkrE 1711
Cdd:PRK04778 154 KSLLANRfsfgpaldELEKQLENLEEEFSQFVELTESgdyveareildQLEEELAALEQIMEEIPELLKELQTELPD--Q 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1712 IAQLKN---QLEESEFtcaaaVKARKAMEVEMEDLHLQIDDIAKAKTAL-----EEQLSRLQREKNEIQSRLEEDQEDMN 1783
Cdd:PRK04778 232 LQELKAgyrELVEEGY-----HLDHLDIEKEIQDLKEQIDENLALLEELdldeaEEKNEEIQERIDQLYDILEREVKARK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1784 ELMKKHKAAVAQASRDLAQMNDLQAQLEE-------ANKEK---QELQEKLQALQSQVEFLEQSMVDKSLV-SRQEAKIR 1852
Cdd:PRK04778 307 YVEKNSDTLPDFLEHAKEQNKELKEEIDRvkqsytlNESELesvRQLEKQLESLEKQYDEITERIAEQEIAySELQEELE 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239919865 1853 ELETRL-EFERTQVKrleslasrLKENMEKLTEErdqrtaaENREKEQNKRLQRQLRDTKEEM 1914
Cdd:PRK04778 387 EILKQLeEIEKEQEK--------LSEMLQGLRKD-------ELEAREKLERYRNKLHEIKRYL 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1288-1545 |
1.08e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1288 EEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRAEKEMKELQTQYDALKKQM 1367
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1368 EVMEMEVmeARLIRAAEINGEVDdddtggewrlkyeramrevdftkkrlqqefEDKLEVEQQNKRQLERRLGDLQADIDE 1447
Cdd:COG4942 100 EAQKEEL--AELLRALYRLGRQP------------------------------PLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1448 SQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQ 1527
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
250
....*....|....*...
gi 1239919865 1528 QLEEKDMDIAGFTQKVVS 1545
Cdd:COG4942 228 LIARLEAEAAAAAERTPA 245
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1408-1908 |
1.11e-09 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 63.99 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1408 EVDFTKKRLQQEFEDKLEVEQQNKR---QLERRLGDLQADIDESQRALQQLKKKCQRLTA--ELQDTKLHLEGQQVR--- 1479
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRariELEKKASALKRQLDRESDRNQELQKRIRLLEKreAEAEEALREQAELNRlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1480 --NHELEKKQRRFDSELSQAHE-------EAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAEL 1550
Cdd:pfam05557 83 kyLEALNKKLNEKESQLADAREvisclknELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1551 QDISSQESK-------------DEASLAKVKKQLR---DLEAKVKDQEEE---LDEQAGTIQMLEQAKLRLEMEMERMRQ 1611
Cdd:pfam05557 163 SSLAEAEQRikelefeiqsqeqDSEIVKNSKSELAripELEKELERLREHnkhLNENIENKLLLKEEVEDLKRKLEREEK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1612 THSKEV--ESRDEEVEEARQSCQKKLKQMEVQLE---------EEYEDKQKVLREKR-ELESKLttLSEQVSQRDLESEK 1679
Cdd:pfam05557 243 YREEAAtlELEKEKLEQELQSWVKLAQDTGLNLRspedlsrriEQLQQREIVLKEENsSLTSSA--RQLEKARRELEQEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1680 R--------LRKDLKRTKALLADAQimldhlKNNAPSKREIAQLKNQLE--ESEFTCAAAVKARKAMEVEMEDLhlqIDD 1749
Cdd:pfam05557 321 AqylkkiedLNKKLKRHKALVRRLQ------RRVLLLTKERDGYRAILEsyDKELTMSNYSPQLLERIEEAEDM---TQK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1750 IAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNelMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQS 1829
Cdd:pfam05557 392 MQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQ--ALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEM 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1830 QVEFLEQSMvDKSLVSRQEAKIRELETRLEFERT--QVKRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQL 1907
Cdd:pfam05557 470 ELERRCLQG-DYDPKKTKVLHLSMNPAAEAYQQRknQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDL 548
|
.
gi 1239919865 1908 R 1908
Cdd:pfam05557 549 R 549
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1288-1840 |
1.37e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 63.77 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1288 EEIQQLRSKLEKVEKERNELRLSNDRLET---RISELTSELTDERNTGESASQLLDAEAAERLRAEKEMKELQTQYDALK 1364
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELENikkQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1365 KqmEVMEMEVMEARLIRAAEINGEVddddTGGEWRLKyERAMREVDFTKKRLQQEFEDKLEVEqqNKRQLerrLGDLQAD 1444
Cdd:PRK01156 253 R--YESEIKTAESDLSMELEKNNYY----KELEERHM-KIINDPVYKNRNYINDYFKYKNDIE--NKKQI---LSNIDAE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1445 I---DESQRALQQLKK------KCQRLTAELQDTKLHLEGQQ------VRNHELEKKQRRfdselsqahEEAQREKLQRE 1509
Cdd:PRK01156 321 InkyHAIIKKLSVLQKdyndyiKKKSRYDDLNNQILELEGYEmdynsyLKSIESLKKKIE---------EYSKNIERMSA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1510 KLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLA------------------KVKKQL 1571
Cdd:PRK01156 392 FISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeeKSNHII 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1572 RDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQSCqkklkqmevqleEEYEDKQK 1651
Cdd:PRK01156 472 NHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADL------------EDIKIKIN 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1652 VLREKrelESKLTTLSEQVSQRDLESekrlrKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLE------ESEFT 1725
Cdd:PRK01156 540 ELKDK---HDKYEEIKNRYKSLKLED-----LDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLEsrlqeiEIGFP 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1726 CAAAV--KARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIqSRLEEDQEDMNELmkkhkaaVAQASRDLAQM 1803
Cdd:PRK01156 612 DDKSYidKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQI-AEIDSIIPDLKEI-------TSRINDIEDNL 683
|
570 580 590
....*....|....*....|....*....|....*..
gi 1239919865 1804 NDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVD 1840
Cdd:PRK01156 684 KKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1275-1681 |
1.77e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLSEEQIRSKDEEIQQLRSKLEKVEK-------------ERNELRLSN-DRLETRISELTSELTDERNTGESASQLLD 1340
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRErfgdapvdlgnaeDFLEELREErDELREREAELEATLRTARERVEEAEALLE 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1341 A----------EAAERLRAEKEMKElqtqydalkkqmevmemevmearliRAAEINGEVDDddtggewrLKYERAMREVD 1410
Cdd:PRK02224 451 AgkcpecgqpvEGSPHVETIEEDRE-------------------------RVEELEAELED--------LEEEVEEVEER 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1411 FTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKlhlegqqvrnhelekkqrrf 1490
Cdd:PRK02224 498 LERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKR-------------------- 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1491 dSELSQAHEEAQREKLQREKLQREKDTLLAEAFSLkQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQ 1570
Cdd:PRK02224 558 -EAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRER 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1571 LRDLEAKVkdQEEELDEQAGTIQMLEQAKLRLEMEMERMR------QTHSKEVESRDEEVEEarqscqkkLKQMEVQLEE 1644
Cdd:PRK02224 636 KRELEAEF--DEARIEEAREDKERAEEYLEQVEEKLDELReerddlQAEIGAVENELEELEE--------LRERREALEN 705
|
410 420 430
....*....|....*....|....*....|....*..
gi 1239919865 1645 EYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKRL 1681
Cdd:PRK02224 706 RVEALEALYDEAEELESMYGDLRAELRQRNVETLERM 742
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1740-1994 |
2.64e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 61.08 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1740 MEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQE 1819
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1820 LQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEF-----------ERTQVKRLESLASRLKENMEKLTEERDQ 1888
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWrqqtevlspeeEKELVEKIKELEKELEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1889 RTAaenreKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIeDEME 1968
Cdd:COG1340 163 KEL-----RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEI-IELQ 236
|
250 260
....*....|....*....|....*...
gi 1239919865 1969 SDENE--DLITSLQDMVTKYQKRKNKPE 1994
Cdd:COG1340 237 KELRElrKELKKLRKKQRALKREKEKEE 264
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1237-1777 |
2.86e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 62.53 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1237 KKKIQDLAIRCVQKniKKNKGVKDWAWWKLFTTVRPLIEVQLS--EEQIRSKDEEIQQLRSKLEKVEKERNE-------L 1307
Cdd:pfam10174 203 QKEKENIHLREELH--RRNQLQPDPAKTKALQTVIEMKDTKISslERNIRDLEDEVQMLKTNGLLHTEDREEeikqmevY 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1308 RLSNDRLETRISELTSELTderntgesasqlldaeaaerlRAEKEMKELQTQYDALK------KQMEVMEMEVMEARLIR 1381
Cdd:pfam10174 281 KSHSKFMKNKIDQLKQELS---------------------KKESELLALQTKLETLTnqnsdcKQHIEVLKESLTAKEQR 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1382 AAEINGEVDdddtggEWRLKYERamrevdftKKRLQQEFEDKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKKKCQR 1461
Cdd:pfam10174 340 AAILQTEVD------ALRLRLEE--------KESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIEN 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1462 LTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAhEEAQREK---LQREKLQREKD--TLLAEAFSLKQQLEEKDMDI 1536
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTL-EEALSEKeriIERLKEQREREdrERLEELESLKKENKDLKEKV 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1537 AGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEE---LDEQAGTIQMLEQA---------KLR-LE 1603
Cdd:pfam10174 485 SALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEEcskLENQLKKAHNAEEAvrtnpeindRIRlLE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1604 MEMERMRQTHSK---EVESRDE---EVEEARQSCQKKLKQMEVQLEEEYEDKQK------------------VLREKREL 1659
Cdd:pfam10174 565 QEVARYKEESGKaqaEVERLLGilrEVENEKNDKDKKIAELESLTLRQMKEQNKkvanikhgqqemkkkgaqLLEEARRR 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1660 ESKLTTLSEQVSQRDLESE-KRLRKDLKRTKALLADAQIMLD----HLKNNAPSKREiaQLKNQLEESEFTCAAAVKARK 1734
Cdd:pfam10174 645 EDNLADNSQQLQLEELMGAlEKTRQELDATKARLSSTQQSLAekdgHLTNLRAERRK--QLEEILEMKQEALLAAISEKD 722
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1239919865 1735 AmevemeDLHLQIDDIAKAKTALEEQLSrLQREKNEIQSRLEE 1777
Cdd:pfam10174 723 A------NIALLELSSSKKKKTQEEVMA-LKREKDRLVHQLKQ 758
|
|
| PDZ7_MUPP1-PD6_PATJ-like |
cd06671 |
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ... |
219-310 |
2.90e-09 |
|
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of MUPP1 and PDZ domain 6 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467159 [Multi-domain] Cd Length: 96 Bit Score: 56.17 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 219 RELELQRRPTGDFGFSL---RrtTMLDRGPEGQVYRRVV--HFAE-PGAGTKDLalgLVPGDRLVEINGHNVESKSRDEI 292
Cdd:cd06671 3 RRVELWREPGKSLGISIvggR--VMGSRLSNGEEIRGIFikHVLEdSPAGRNGT---LKTGDRILEVNGVDLRNATHEEA 77
|
90
....*....|....*...
gi 1239919865 293 VEMIRQSGDSVRLKVQPI 310
Cdd:cd06671 78 VEAIRNAGNPVVFLVQSL 95
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1746-2012 |
3.84e-09 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 61.95 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1746 QIDDIAKAKT-ALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAqasrdlaqmnDLQAQLEEANKEKQELQEKL 1824
Cdd:PHA02562 167 EMDKLNKDKIrELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA----------RKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1825 QALQSQVEFLEQSMVDkslVSRQEAKIRELETRLefeRTQVKRLESLASRLKEN------MEKLTEERDQRTAAENREKE 1898
Cdd:PHA02562 237 EELTDELLNLVMDIED---PSAALNKLNTAAAKI---KSKIEQFQKVIKMYEKGgvcptcTQQISEGPDRITKIKDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1899 QNKRLqRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDemESDENEDLITS 1978
Cdd:PHA02562 311 LQHSL-EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD--NAEELAKLQDE 387
|
250 260 270
....*....|....*....|....*....|....
gi 1239919865 1979 LQDMVTKYQKRKNKPEGDSDVDSELEDrvDGVKS 2012
Cdd:PHA02562 388 LDKIVKTKSELVKEKYHRGIVTDLLKD--SGIKA 419
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1710-1888 |
4.30e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 59.55 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1710 REIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELmkkh 1789
Cdd:COG1579 17 SELDRLEHRLKELP-------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1790 kaavaqasRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFERtqvKRLE 1869
Cdd:COG1579 86 --------RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEE------LAELEAELAELEAELEEKK---AELD 148
|
170
....*....|....*....
gi 1239919865 1870 SLASRLKENMEKLTEERDQ 1888
Cdd:COG1579 149 EELAELEAELEELEAEREE 167
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1277-1718 |
5.63e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.06 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1277 QLSEEQiRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETR-------ISELTSELTDERNTGESASQLLDAEAAE-RLR 1348
Cdd:pfam15921 367 QFSQES-GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1349 AEKEMKELQTQYDALKKqmevmeMEVMEARLIRAAEINGEVDDDDTGGEWRLkyERAMREVDFTKKRLQqefEDKLEVEQ 1428
Cdd:pfam15921 446 MERQMAAIQGKNESLEK------VSSLTAQLESTKEMLRKVVEELTAKKMTL--ESSERTVSDLTASLQ---EKERAIEA 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1429 QNKRqlerrLGDLQADIDESQRALQQLKKK---CQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREK 1505
Cdd:pfam15921 515 TNAE-----ITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQ 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1506 LQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEEL 1585
Cdd:pfam15921 590 VEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNEL 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1586 DEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQS-------------------------------CQKK 1634
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghamkvamgmqkqitakrgqidaLQSK 749
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1635 LKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKrLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQ 1714
Cdd:pfam15921 750 IQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEKVANMEVALDKASLQFAECQDIIQ 828
|
....
gi 1239919865 1715 LKNQ 1718
Cdd:pfam15921 829 RQEQ 832
|
|
| PDZ_FRMPD1_3_4-like |
cd06769 |
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ... |
220-307 |
6.19e-09 |
|
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of FRMPD1, FRMPD3, FRMPD4, and related domains. FRMPD1 (also known as FERM domain-containing protein 2, FRMD2), inhibits the malignant phenotype of lung cancer by activating the Hippo pathway via interaction with WWC3; the FRMPD1 PDZ domain binds WWC3. FRMPD3 is a target gene of the neuron-specific transcription factor NPAS4 that is involved in synaptic plasticity. FRMPD4 (also known as PDZ domain-containing protein 10, PDZD10, PDZK10, PSD-95-interacting regulator of spine morphogenesis, and Preso) regulates dendritic spine morphogenesis, and mGluR1/5 signaling; the FRMPD4 PDZ domain binds PAK-interacting exchange factor-beta (betaPix). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This FRMPD1,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467250 [Multi-domain] Cd Length: 75 Bit Score: 54.56 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 220 ELELQRRPTGDFGFSLrrttmldrGPEGQVyrrVVHFAEPGaGTKDlalG-LVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd06769 1 TVEIQRDAVLGFGFVA--------GSERPV---VVRSVTPG-GPSE---GkLLPGDQILKINNEPVEDLPRERVIDLIRE 65
|
....*....
gi 1239919865 299 SGDSVRLKV 307
Cdd:cd06769 66 CKDSIVLTV 74
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1275-1968 |
7.22e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.51 E-value: 7.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLSEEQIRSKDEEIQQLRSKLEKVekeRNELRLSN--DRLETRISELTSELTDERNTGESASQLLDAEAAERLRAEKE 1352
Cdd:PRK04863 315 ELAELNEAESDLEQDYQAASDHLNLV---QTALRQQEkiERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1353 MKELQTQ-------YDALkkQMEVMEMEVMEARLIRAAEINGEVD-DDDTGGEWrlkyeramrevdftkkrlQQEFEDKL 1424
Cdd:PRK04863 392 VDELKSQladyqqaLDVQ--QTRAIQYQQAVQALERAKQLCGLPDlTADNAEDW------------------LEEFQAKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1425 EVEQQNKRQLERRLGDLQADIDESQRALQQLKK---KCQRLTA--ELQDTKLHLEGQQVRNHELEKKQRRFdSELSQAHE 1499
Cdd:PRK04863 452 QEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagEVSRSEAwdVARELLRRLREQRHLAEQLQQLRMRL-SELEQRLR 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1500 EAQR-EKLQREKLQREKDTLLAEAFsLKQQLEEkdmdiagftqkvvsLEAELQDISSQeskdeaslakvKKQLRDLEAKV 1578
Cdd:PRK04863 531 QQQRaERLLAEFCKRLGKNLDDEDE-LEQLQEE--------------LEARLESLSES-----------VSEARERRMAL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1579 KDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRdEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRE 1658
Cdd:PRK04863 585 RQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS-QDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1659 L-------ESKLTTLSEQ---VSQRDLESEKRLrKDLKRTKALLADAQ--IMLDHLKNnapSKREIAQLKNQLEE----- 1721
Cdd:PRK04863 664 LsqpggseDPRLNALAERfggVLLSEIYDDVSL-EDAPYFSALYGPARhaIVVPDLSD---AAEQLAGLEDCPEDlylie 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1722 -------------SEFTCAAAVK-----------------ARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQR----- 1766
Cdd:PRK04863 740 gdpdsfddsvfsvEELEKAVVVKiadrqwrysrfpevplfGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRlhqaf 819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1767 ------------------EKNEIQSRLEEDQEDMNELMKK---HKAAVAQASRDLAQMNDLQAQL-----EEANKEKQEL 1820
Cdd:PRK04863 820 srfigshlavafeadpeaELRQLNRRRVELERALADHESQeqqQRSQLEQAKEGLSALNRLLPRLnlladETLADRVEEI 899
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1821 QEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRT--AAENREK- 1897
Cdd:PRK04863 900 REQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfSYEDAAEm 979
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239919865 1898 -EQNKRLQRQLRdtkeemGELARKEAEASRKKHELEMDLESLEAANQsLQADLKLAFKRIGDLQAAIEDEME 1968
Cdd:PRK04863 980 lAKNSDLNEKLR------QRLEQAEQERTRAREQLRQAQAQLAQYNQ-VLASLKSSYDAKRQMLQELKQELQ 1044
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1417-1830 |
7.30e-09 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 61.20 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1417 QQEFEDklEVEQQNkrqLERRLGDLQADIDESQRALQQLKkkcQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQ 1496
Cdd:pfam05667 219 AQEWEE--EWNSQG---LASRLTPEEYRKRKRTKLLKRIA---EQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTT 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1497 AHEEAQREKLQR-EKLQREKDTLLAEAFSLKQQLEEKDMDIAGfTQKVVSLEAELQDISSqeskdeaSLAKVKKQLRDLE 1575
Cdd:pfam05667 291 DTGLTKGSRFTHtEKLQFTNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLES-------SIQELEKEIKKLE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1576 AKVKDQEEELDEQAGTIQMLEQaklrlemEMERMRQTHsKEVESRDEEVEEARQSCQKKLKQMeVQLEEEYEDKQKVL-R 1654
Cdd:pfam05667 363 SSIKQVEEELEELKEQNEELEK-------QYKVKKKTL-DLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLiE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1655 EKRELESKLTTLSEQvSQRDLESEKRLRkdlKRTKALLADAQimldhlknnapSKRE-IAQLKNQLEE-------SEFTc 1726
Cdd:pfam05667 434 EYRALKEAKSNKEDE-SQRKLEEIKELR---EKIKEVAEEAK-----------QKEElYKQLVAEYERlpkdvsrSAYT- 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1727 aaavkaRKAMEVeMEDLHLQIDDIAKaktALEEQLSrLQREKNEIQSRLEEDQEDMNELM---KKHKAAVAQASRDLAQM 1803
Cdd:pfam05667 498 ------RRILEI-VKNIKKQKEEITK---ILSDTKS-LQKEINSLTGKLDRTFTVTDELVfkdAKKDESVRKAYKYLAAL 566
|
410 420 430
....*....|....*....|....*....|....
gi 1239919865 1804 NDLQAQL----EEANK---EKQELQEKLQALQSQ 1830
Cdd:pfam05667 567 HENCEQLiqtvEETGTimrEIRDLEEQIETESGK 600
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1706-1901 |
1.00e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1706 APSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNEL 1785
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1786 ---MKKHKAAV-----------------------AQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMV 1839
Cdd:COG3883 92 araLYRSGGSVsyldvllgsesfsdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239919865 1840 D-KSLVSRQEAKIRELETRlefERTQVKRLESLASRLKENMEKLTEERDQRTAAENREKEQNK 1901
Cdd:COG3883 172 ElEAQQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1455-1731 |
1.65e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 60.03 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1455 LKKKCQRLTAELQ--DTKLHLEGQQVrnheleKKQRRFDSELsqahEEAQREKLQRekLQREKDTLLAEAFSLKQQLEEk 1532
Cdd:PHA02562 172 NKDKIRELNQQIQtlDMKIDHIQQQI------KTYNKNIEEQ----RKKNGENIAR--KQNKYDELVEEAKTIKAEIEE- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1533 dmdiagftqkvvsLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK--DQEEELDEQAGTIQMLEQAklrLEMEMERMR 1610
Cdd:PHA02562 239 -------------LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfQKVIKMYEKGGVCPTCTQQ---ISEGPDRIT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1611 QTHSKEVEsrdeeveearqsCQKKLKqmevQLEEEYEDKQKVLREKRELESKLTTLSEQVSQRDlESEKRLRKDLKRTKA 1690
Cdd:PHA02562 303 KIKDKLKE------------LQHSLE----KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNK-QSLITLVDKAKKVKA 365
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1239919865 1691 LLADAQimldhlKNNAPSKREIAQLKNQLEESEFTCAAAVK 1731
Cdd:PHA02562 366 AIEELQ------AEFVDNAEELAKLQDELDKIVKTKSELVK 400
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1709-1925 |
1.75e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.03 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1709 KREIAQLKNQLEESEftcaAAVKARKAmEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEdqedMNELMKK 1788
Cdd:COG3206 181 EEQLPELRKELEEAE----AALEEFRQ-KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA----LRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1789 HKAAVAQASRDlAQMNDLQAQLEEANKEKQELQEKL-------QALQSQVEFLEQSmvdksLVSRQEAKIRELETRLEFE 1861
Cdd:COG3206 252 GPDALPELLQS-PVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQ-----LQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 1862 RTQVKRLESLASRLKENMEKLTEERDQRTaaenrekeqnkRLQRQLRDTKEEMGELARKEAEAS 1925
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELR-----------RLEREVEVARELYESLLQRLEEAR 378
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1278-1629 |
2.23e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 59.75 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1278 LSEEQIRSKDEEIQQLRSKLEKVEKERNELRlsndRLETRISELTSELTDERNTGESASQlldaeaaERLRAEKEMKELQ 1357
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVER----RRKLEEAEKARQAEMDRQAAIYAEQ-------ERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1358 TQYDALKKQMEVMEMEVMEARLIRAAEINgevddddtggewRLKYERAMRevdftKKRLQQEfedkLEVEQQNKRQLERR 1437
Cdd:pfam17380 353 IRQEERKRELERIRQEEIAMEISRMRELE------------RLQMERQQK-----NERVRQE----LEAARKVKILEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1438 LGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHlEGQQVRNHELEKKQRRfdSELSQAHEEAQREKLQREKLQREKDt 1517
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR-EMERVRLEEQERQQQV--ERLRQQEEERKRKKLELEKEKRDRK- 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1518 lLAEAFS---LKQQLEEKDMDIAGFTQKVVSLEAELQD----ISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAG 1590
Cdd:pfam17380 488 -RAEEQRrkiLEKELEERKQAMIEEERKRKLLEKEMEErqkaIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
330 340 350
....*....|....*....|....*....|....*....
gi 1239919865 1591 TIQMLEQaklrlemEMERMRQThsKEVESRDEEVEEARQ 1629
Cdd:pfam17380 567 RLEAMER-------EREMMRQI--VESEKARAEYEATTP 596
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1281-1921 |
2.24e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1281 EQIRSKDEEIQQLRSKLEKVEKERNELRLsnDRLETRISELTSELTDERntgesasQLLDAEAAERLRAEKEMKELQTQY 1360
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAELEELR-------AELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1361 DALKKQMEVMEMEVMeARLirAAEINGEVDDDDTGGEWRLKYERAMREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGD 1440
Cdd:COG4913 326 DELEAQIRGNGGDRL-EQL--EREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1441 LQADIDESQRALQQLKKKCQRLTAELQ----------------------------------------------------- 1467
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIAslerrksniparllalrdalaealgldeaelpfvgelievrpeeerwrgaier 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1468 --------------------------DTKLHLEGQQVRNHELEKKQRRFDS---------ELSQAHEEAQREKLQR---- 1508
Cdd:COG4913 483 vlggfaltllvppehyaaalrwvnrlHLRGRLVYERVRTGLPDPERPRLDPdslagkldfKPHPFRAWLEAELGRRfdyv 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1509 -----EKLQREKDTLLAEA-FSLKQQLEEKDMDIA-------GFT--QKVVSLEAELQDIssqeskdEASLAKVKKQLRD 1573
Cdd:COG4913 563 cvdspEELRRHPRAITRAGqVKGNGTRHEKDDRRRirsryvlGFDnrAKLAALEAELAEL-------EEELAEAEERLEA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1574 LEAkvkdQEEELDEQAGTIQMLEQaklrLEMEMERMRQTHsKEVESRDEEVEEARQSCQ--KKLKQMEVQLEEEYED--- 1648
Cdd:COG4913 636 LEA----ELDALQERREALQRLAE----YSWDEIDVASAE-REIAELEAELERLDASSDdlAALEEQLEELEAELEElee 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1649 -KQKVLREKRELESKLTTLSEQVSQrdleSEKRL-RKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftc 1726
Cdd:COG4913 707 eLDELKGEIGRLEKELEQAEEELDE----LQDRLeAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR--- 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1727 AAAVKARKAMEVEMEDL----HLQIDDIAKAKTALEEQLSRLQREKNEiqsRLEEDQEDMNELMKKhkaavaQASRDLAq 1802
Cdd:COG4913 780 ARLNRAEEELERAMRAFnrewPAETADLDADLESLPEYLALLDRLEED---GLPEYEERFKELLNE------NSIEFVA- 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1803 mnDLQAQLEEANKE-KQELQEKLQALQsQVEFLEqsmvDKSLvsrqeakireletRLEFERTQVKRLESLASRLKENMEK 1881
Cdd:COG4913 850 --DLLSKLRRAIREiKERIDPLNDSLK-RIPFGP----GRYL-------------RLEARPRPDPEVREFRQELRAVTSG 909
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1239919865 1882 LTEERDQrtAAENREkEQNKRLQRQLRDTKEEMGELARKE 1921
Cdd:COG4913 910 ASLFDEE--LSEARF-AALKRLIERLRSEEEESDRRWRAR 946
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1273-1680 |
2.36e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 59.14 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1273 LIEVQLsEEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRAEKE 1352
Cdd:pfam07888 31 LLQNRL-EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1353 MKELQTQYDALKKQMEvmemevmeARLIRAAEINGEVDdddtggewrlkyeramrevdfTKKRLQQEFEDKLEVEQQNKR 1432
Cdd:pfam07888 110 SEELSEEKDALLAQRA--------AHEARIRELEEDIK---------------------TLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1433 QLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHeeaQREKlqreklq 1512
Cdd:pfam07888 161 KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH---RKEA------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1513 rEKDTLLAEAFSLKQQLEEKDmdiagftQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTI 1592
Cdd:pfam07888 231 -ENEALLEELRSLQERLNASE-------RKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARW 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1593 QMlEQAKLRLEMEMERMR-QTHSKEVESRDEEVEEARQSCQKklkqMEVQLEEEYEDKQKVL----REKRELESKLTTLs 1667
Cdd:pfam07888 303 AQ-ERETLQQSAEADKDRiEKLSAELQRLEERLQEERMEREK----LEVELGREKDCNRVQLsesrRELQELKASLRVA- 376
|
410
....*....|...
gi 1239919865 1668 eQVSQRDLESEKR 1680
Cdd:pfam07888 377 -QKEKEQLQAEKQ 388
|
|
| PDZ_SNX27-like |
cd23070 |
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ... |
219-307 |
2.47e-08 |
|
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SNX27, and related domains. SNX27 is involved in retrograde transport from endosome to plasma membrane. The PDZ domain of SNX27 links cargo identification to retromer-mediated transport. SNX27 binds to the retromer complex (vacuolar protein sorting 26(VPS26)-VPS29-VPS35), via its PDZ domain binding to VPS26. The SNX27 PDZ domain also binds to cargo including the G-protein-coupled receptors (GPCRs): beta2-adrenergic receptor (beta2AR), beta1AR, parathyroid hormone receptor (PTHR), alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs), NMDA receptors, 5-hydroxytryptamine 4a receptors, frizzled receptors, and somatostatin receptor subtype 5 (SSTR5). Additional binding partners of the SNX27 PDZ domain include G protein-gated inwardly rectifying potassium (Kir3) channels, angiotensin-converting enzyme 2 (ACE2), and PTEN (phosphatase and tensin homolog deleted on chromosome 10); PTEN binding to SNX27 prevents SNX27's association with the retromer complex. SNX27 has been reported to be a host factor needed for efficient entry of an engineered SARS-CoV-2 variant, the spike protein of which contains a deletion at the S1/S2 subunit cleavage site; the PDZ domain of SNX27 binds angiotensin-converting enzyme 2 (ACE2), and may be involved in recycling ACE2 to the plasma membrane, thereby promoting viral entry. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SNX27-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467283 [Multi-domain] Cd Length: 93 Bit Score: 53.57 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 219 RELELQRRPTGdFGFSLRrTTMLDRGP----EGQVYRRVVHFA---EPGAGTKDlalGLVPGDRLVEINGHNVESKSRDE 291
Cdd:cd23070 1 RVVTIVKSETG-FGFNVR-GQVSEGGQlrsiNGELYAPLQHVSavlEGGAADKA---GVRKGDRILEVNGVNVEGATHKQ 75
|
90
....*....|....*.
gi 1239919865 292 IVEMIRQSGDSVRLKV 307
Cdd:cd23070 76 VVDLIKSGGDELTLTV 91
|
|
| PDZ |
pfam00595 |
PDZ domain; PDZ domains are found in diverse signaling proteins. |
220-308 |
2.66e-08 |
|
PDZ domain; PDZ domains are found in diverse signaling proteins.
Pssm-ID: 395476 [Multi-domain] Cd Length: 81 Bit Score: 53.05 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 220 ELELQRRPTGDFGFSLRRttMLDRGPEGQVYRRVVHFaepGAGTKDlalGLVPGDRLVEINGHNVESKSRDEIVEMIRQS 299
Cdd:pfam00595 1 QVTLEKDGRGGLGFSLKG--GSDQGDPGIFVSEVLPG---GAAEAG---GLKVGDRILSINGQDVENMTHEEAVLALKGS 72
|
....*....
gi 1239919865 300 GDSVRLKVQ 308
Cdd:pfam00595 73 GGKVTLTIL 81
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1281-1889 |
3.56e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 59.07 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1281 EQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRAEKE-------M 1353
Cdd:pfam10174 60 EQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKElfllrktL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1354 KELQTQYDALK-------------------KQMEVMEMEVMEARLIRAAEINGEVDDDDTGGEWRLKYERAMREVDFTKK 1414
Cdd:pfam10174 140 EEMELRIETQKqtlgardesikkllemlqsKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRN 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1415 RLQQEFEdKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKKkcqrlTAELQDTKLHLEGQQVrnhELEKKQRRF-DSE 1493
Cdd:pfam10174 220 QLQPDPA-KTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKT-----NGLLHTEDREEEIKQM---EVYKSHSKFmKNK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1494 LSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1573
Cdd:pfam10174 291 IDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1574 LEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMrQTHSKEVESRDEEVEEARQSCQKKLKQMEVQL---EEEYEDKQ 1650
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENL-QEQLRDKDKQLAGLKERVKSLQTDSSNTDTALttlEEALSEKE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1651 KV---LREKRELEsklttlsEQVSQRDLESEKRLRKDLKRT----KALLADAQIMLDHLKNNAPSKREIAQLKNQLEESe 1723
Cdd:pfam10174 450 RIierLKEQRERE-------DRERLEELESLKKENKDLKEKvsalQPELTEKESSLIDLKEHASSLASSGLKKDSKLKS- 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1724 ftCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEED---QEDMNELMK-----------KH 1789
Cdd:pfam10174 522 --LEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESgkaQAEVERLLGilrevenekndKD 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1790 KAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELE-TRLEFERTQvKRL 1868
Cdd:pfam10174 600 KKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEkTRQELDATK-ARL 678
|
650 660
....*....|....*....|.
gi 1239919865 1869 ESLASRLKENMEKLTEERDQR 1889
Cdd:pfam10174 679 SSTQQSLAEKDGHLTNLRAER 699
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1275-1682 |
4.20e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLSEEQIRskdEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSEltdernTGESASQLLDAEAAERLRAEkEMK 1354
Cdd:PRK02224 318 ELEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLEERAEELREE------AAELESELEEAREAVEDRRE-EIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1355 ELQTQYDALKKQMEVMEMEVMEA--RLIRAAEINGEVDDDDTGGEWRLKYERAMREvdfTKKRLQ---------QEFEDK 1423
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAedFLEELREERDELREREAELEATLRTARERVE---EAEALLeagkcpecgQPVEGS 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1424 LEVEQQNKRqlERRLGDLQADIDESQRALQQLKKKCQRLTaELQDTKLHLEgqqvrnhELEKKQRRFDSELSQAHEEAQR 1503
Cdd:PRK02224 465 PHVETIEED--RERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIE-------RLEERREDLEELIAERRETIEE 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1504 EKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESkdeaSLAKVKKQLRDLEAKVKDQEE 1583
Cdd:PRK02224 535 KRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE----SLERIRTLLAAIADAEDEIER 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1584 ELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKL 1663
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL 690
|
410
....*....|....*....
gi 1239919865 1664 TTLSEQVSQRDLESEKRLR 1682
Cdd:PRK02224 691 EELEELRERREALENRVEA 709
|
|
| PDZ4_Scribble-like |
cd06701 |
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ... |
215-307 |
4.32e-08 |
|
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467185 [Multi-domain] Cd Length: 98 Bit Score: 53.00 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 215 PPALRELELQRRPTGDFGFSLR------RTTMLDRGPEGQVYRRVVHfaePGAGTKDlalG-LVPGDRLVEINGHNVESK 287
Cdd:cd06701 1 PPGLQELTIVKEPGEKLGISIRggakghAGNPLDPTDEGIFISKINP---DGAAARD---GrLKVGQRILEVNGQSLLGA 74
|
90 100
....*....|....*....|
gi 1239919865 288 SRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06701 75 THQEAVRILRSVGDTLTLLV 94
|
|
| PDZ4_MAGI-1_3-like |
cd06734 |
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
270-309 |
4.52e-08 |
|
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467216 [Multi-domain] Cd Length: 84 Bit Score: 52.62 E-value: 4.52e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1239919865 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06734 45 LKVGDRILAVNGISILNLSHGDIVNLIKDSGLSVTLTIVP 84
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1432-1588 |
4.54e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.47 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1432 RQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDtklhlegqqvrnheLEKKQRRFDSELSQAHEEAQR--EKLQRE 1509
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELED--------------LEKEIKRLELEIEEVEARIKKyeEQLGNV 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1510 KLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1588
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1280-1881 |
5.04e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.76 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1280 EEQIRSKDEEIQQLRSKLEKVEKernELRLSNDRLEtRISELTSELTDERNTGESASQLLDAEAAERLRAEKEMKELQTq 1359
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEK---SHSITLKEIE-RLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAES- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1360 yDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDTGGEWRLKYeramrevDFTKKRlqqEFEDKLEVEQQNKRQLERRLG 1439
Cdd:PRK01156 264 -DLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKN-------DIENKK---QILSNIDAEINKYHAIIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1440 DLQADIDEsqraLQQLKKKCQRLTAELQDTKLHLEGQQ--VRNHELEKKQRRfdselsqahEEAQREKLQREKLQREKDT 1517
Cdd:PRK01156 333 VLQKDYND----YIKKKSRYDDLNNQILELEGYEMDYNsyLKSIESLKKKIE---------EYSKNIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1518 LLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLA------------------KVKKQLRDLEAKVK 1579
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeeKSNHIINHYNEKKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1580 DQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQSCqkklkqmevqleEEYEDKQKVLREKrel 1659
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADL------------EDIKIKINELKDK--- 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1660 ESKLTTLSEQVSQRDLESekrlrKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEeseftcaaavKARKAMEVE 1739
Cdd:PRK01156 545 HDKYEEIKNRYKSLKLED-----LDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLE----------SRLQEIEIG 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1740 MEDLHLQIDDIAKaktALEEQLSRLQREKNEIQSrLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQE 1819
Cdd:PRK01156 610 FPDDKSYIDKSIR---EIENEANNLNNKYNEIQE-NKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKK 685
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239919865 1820 LQEKLQ-ALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLaSRLKENMEK 1881
Cdd:PRK01156 686 SRKALDdAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDL-KRLREAFDK 747
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1421-1974 |
5.10e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 58.66 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1421 EDKLEVEQQNKRQ----LERRlGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNH-ELEKKQRRFDSELS 1495
Cdd:PRK10246 232 EKQLLTAQQQQQQslnwLTRL-DELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHwERIQEQSAALAHTR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1496 QAHEE---------AQREKLqREKLQREKDTLLAEAFSLKQQLEEKDMdIAGFTQKVVSLEAELqdisSQESKDEASLAK 1566
Cdd:PRK10246 311 QQIEEvntrlqstmALRARI-RHHAAKQSAELQAQQQSLNTWLAEHDR-FRQWNNELAGWRAQF----SQQTSDREQLRQ 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1567 VKKQLRDLEAKVKDQEE-----ELDEQAGTI-QMLEQAKLRlememERMRQTHSKEV--ESRDEEVEEARQSCQKKLKQM 1638
Cdd:PRK10246 385 WQQQLTHAEQKLNALPAitltlTADEVAAALaQHAEQRPLR-----QRLVALHGQIVpqQKRLAQLQVAIQNVTQEQTQR 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1639 EVQLEEeyedKQKVLREKRELESKLTTLSEQvsqrdlesEKRLrKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKnq 1718
Cdd:PRK10246 460 NAALNE----MRQRYKEKTQQLADVKTICEQ--------EARI-KDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALE-- 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1719 LEESEFTCAAAVKARKAMEVEMEDLHLQIDdiakaktALEEQlsrLQREKNEIQSRLEEDQedmnELMKKHKAAVAQASR 1798
Cdd:PRK10246 525 PGVNQSRLDALEKEVKKLGEEGAALRGQLD-------ALTKQ---LQRDESEAQSLRQEEQ----ALTQQWQAVCASLNI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1799 DLAQMNDLQAQLEEANKEKQELQE--KLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFERTQVK-RLESLASRL 1875
Cdd:PRK10246 591 TLQPQDDIQPWLDAQEEHERQLRLlsQRHELQGQIA-------------AHNQQIIQYQQQIEQRQQQLLtALAGYALTL 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1876 KENMEKLT--EERDQRTAAENREKEQNKRLQRQ------LRDTKEEMGELARKEAEAS----RKKHElemDLESLEAANQ 1943
Cdd:PRK10246 658 PQEDEEASwlATRQQEAQSWQQRQNELTALQNRiqqltpLLETLPQSDDLPHSEETVAldnwRQVHE---QCLSLHSQLQ 734
|
570 580 590
....*....|....*....|....*....|.
gi 1239919865 1944 SLQADLKLAFKRIGDLQAAIEDEMESDENED 1974
Cdd:PRK10246 735 TLQQQDVLEAQRLQKAQAQFDTALQASVFDD 765
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1561-2010 |
5.14e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.81 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1561 EASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQ----AKLRLEMEMERMRQThsKEVESRDEEVEEarqscqkklk 1636
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSARESDLEQdyqaASDHLNLVQTALRQQ--EKIERYQEDLEE---------- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1637 qmevqLEEEYEDKQKVLREkrelesklttLSEQVSQRDLESEkRLRKDLKRTKALLADAQIMLDHLKNNAPSKReiaQLK 1716
Cdd:COG3096 359 -----LTERLEEQEEVVEE----------AAEQLAEAEARLE-AAEEEVDSLKSQLADYQQALDVQQTRAIQYQ---QAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1717 NQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEedqedmneLMKKHKAAVA-- 1794
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE--------LVCKIAGEVErs 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1795 ----QASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQvefleqsmvdkslvSRQEAKIRELETRLEFERTQVKRLES 1870
Cdd:COG3096 492 qawqTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQ--------------QNAERLLEEFCQRIGQQLDAAEELEE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1871 LASRLKENMEKLTEErdQRTAAENRekeqnKRLQRQLRDTKEEMGELARKE----AEASRKKHELEMDLESLEAANQSLQ 1946
Cdd:COG3096 558 LLAELEAQLEELEEQ--AAEAVEQR-----SELRQQLEQLRARIKELAARApawlAAQDALERLREQSGEALADSQEVTA 630
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239919865 1947 AdlklafkrigdLQAAIEDEMESDENEDLITSLQDMVTKYQKRKNKPEGDSDVD-SELEDRVDGV 2010
Cdd:COG3096 631 A-----------MQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRlLALAERLGGV 684
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1431-1855 |
7.42e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 57.73 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1431 KRQLERRLGDLQADIDESQRALQ-------QLKKKCQRLTAELQDTKLHLEGQQVrnhelEKKQRRFDSELSQ------- 1496
Cdd:pfam05701 37 RKLVELELEKVQEEIPEYKKQSEaaeaakaQVLEELESTKRLIEELKLNLERAQT-----EEAQAKQDSELAKlrveeme 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1497 ---AHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEkdmdiagfTQKVVSLEAELQDISSQESKDEASLAK-VKKQLR 1572
Cdd:pfam05701 112 qgiADEASVAAKAQLEVAKARHAAAVAELKSVKEELES--------LRKEYASLVSERDIAIKRAEEAVSASKeIEKTVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1573 DLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQSCQKKlKQMEVQLEEEYEdkqKV 1652
Cdd:pfam05701 184 ELTIELIATKESLESAHAAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQQLLSA-KDLKSKLETASA---LL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1653 LREKREL----ESKLTTLSEQVSQRDlESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIA-QLKNQLEEsEFTCA 1727
Cdd:pfam05701 260 LDLKAELaaymESKLKEEADGEGNEK-KTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAaSLRSELEK-EKAEL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1728 AAVKARKAMEvemedlhlqiddiAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKhkaaVAQASRDLAQMNDL- 1806
Cdd:pfam05701 338 ASLRQREGMA-------------SIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQ----LQQAAQEAEEAKSLa 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1239919865 1807 QAQLEEANKEKQElQEKLQALQSQVEfleqsmvdkslvSRQEAKIRELE 1855
Cdd:pfam05701 401 QAAREELRKAKEE-AEQAKAAASTVE------------SRLEAVLKEIE 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1341-1589 |
8.57e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1341 AEAAERLRAEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDDDDtggewrlkyeramREVDFTKKRLqQEF 1420
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKK--------EEKALLKQLAALE-------------RRIAALARRI-RAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1421 EDKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKKKCQRLtAELQDTKLHLEGQQVRnhELEKKQRRFDSELSQAHEE 1500
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1501 AQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD 1580
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
....*....
gi 1239919865 1581 QEEELDEQA 1589
Cdd:COG4942 232 LEAEAAAAA 240
|
|
| PDZ5_MAGI-1_3-like |
cd06735 |
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
222-309 |
9.17e-08 |
|
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5, and belongs to this MAGI1,2,3-like family. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467217 [Multi-domain] Cd Length: 84 Bit Score: 51.43 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 222 ELQRRPTGdFGFSLRrttmldrgpEGQVYRR----VVHFAEPGAGTKDlalG-LVPGDRLVEINGHNVESKSRDEIVEMI 296
Cdd:cd06735 5 ELERGPKG-FGFSIR---------GGREYNNmplyVLRLAEDGPAQRD---GrLRVGDQILEINGESTQGMTHAQAIELI 71
|
90
....*....|...
gi 1239919865 297 RQSGDSVRLKVQP 309
Cdd:cd06735 72 RSGGSVVRLLLRR 84
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1280-1725 |
1.11e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1280 EEQIRSKD-EEIQQLRSKLEKVEKERNELRLSNDRLETRISELT--------------SELTDERNTGESASQLLDAEAA 1344
Cdd:COG4913 329 EAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGlplpasaeefaalrAEAAALLEALEEELEALEEALA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1345 ERLRAEKEMK----ELQTQYDALKKQMEVMEMEVMEAR--LIRAAEING----------EVDDDDtgGEWRL-------- 1400
Cdd:COG4913 409 EAEAALRDLRrelrELEAEIASLERRKSNIPARLLALRdaLAEALGLDEaelpfvgeliEVRPEE--ERWRGaiervlgg 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1401 ----------KYERAMREVDFTK--KRLQQEFEDKLEVEQQNKRQLERRL-GDLQADIDESQRALQQLKKK-----CQRL 1462
Cdd:COG4913 487 faltllvppeHYAAALRWVNRLHlrGRLVYERVRTGLPDPERPRLDPDSLaGKLDFKPHPFRAWLEAELGRrfdyvCVDS 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1463 TAELQDTK--LHLEGQQVRNHELEKKQRR----------FDSELSQAHEEAQREKLQRE---------KLQREKDTL--L 1519
Cdd:COG4913 567 PEELRRHPraITRAGQVKGNGTRHEKDDRrrirsryvlgFDNRAKLAALEAELAELEEElaeaeerleALEAELDALqeR 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1520 AEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDIssqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAK 1599
Cdd:COG4913 647 REALQRLAEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL 722
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1600 LRLEmemERMRQTHSKEVESRDEEVEEARQSCQKKLKQ-----MEVQLEEEYEDKQKVLREKRE-LESKLTTLSEQVSQR 1673
Cdd:COG4913 723 EQAE---EELDELQDRLEAAEDLARLELRALLEERFAAalgdaVERELRENLEERIDALRARLNrAEEELERAMRAFNRE 799
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 1674 DLESEKRLRKDLkrtkALLADAQIMLDHLKNNA-PSKRE-IAQLKNQLEESEFT 1725
Cdd:COG4913 800 WPAETADLDADL----ESLPEYLALLDRLEEDGlPEYEErFKELLNENSIEFVA 849
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1713-1967 |
1.13e-07 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 56.08 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1713 AQLKNQLEESEFTCAAAVKARKAM-EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEdqedmnELMKKHKA 1791
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED------ELNLRTSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1792 AvaqasrdlAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdkslvsrQEAKIRELETRLEFERTQVK----R 1867
Cdd:pfam00038 102 E--------NDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN---------HEEEVRELQAQVSDTQVNVEmdaaR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1868 LESLASRLKE-----------NMEKLTEERDQRTAAENREKEQNKrlqRQLRDTKEEMGELarkeaeaSRKKHELEMDLE 1936
Cdd:pfam00038 165 KLDLTSALAEiraqyeeiaakNREEAEEWYQSKLEELQQAAARNG---DALRSAKEEITEL-------RRTIQSLEIELQ 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 1239919865 1937 SLEAANQSLQADLK-------LAFKRIGDLQAAIEDEM 1967
Cdd:pfam00038 235 SLKKQKASLERQLAeteeryeLQLADYQELISELEAEL 272
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1274-1798 |
1.41e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.22 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1274 IEVQLSEEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRL-------------ETRISELTS-----------ELTDER 1329
Cdd:PRK01156 225 IEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLsmeleknnyykelEERHMKIINdpvyknrnyinDYFKYK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1330 NTGESASQLL---DAEAAERLRAEKEMKELQTQYDA-LKKQMevmemevmearliRAAEINGEVDDDDtggEWRLKYERA 1405
Cdd:PRK01156 305 NDIENKKQILsniDAEINKYHAIIKKLSVLQKDYNDyIKKKS-------------RYDDLNNQILELE---GYEMDYNSY 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1406 MREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGD---LQADIDESQRALQQLKKKCQRLTA----------ELQDTKLH 1472
Cdd:PRK01156 369 LKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDpdaIKKELNEINVKLQDISSKVSSLNQriralrenldELSRNMEM 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1473 LEGQQV----RNHELEKKQRR----FDSELSQAHEEAQREKLQREKLQREKDTLLaeafSLKQQLEEKDMD-IAGFTQKV 1543
Cdd:PRK01156 449 LNGQSVcpvcGTTLGEEKSNHiinhYNEKKSRLEEKIREIEIEVKDIDEKIVDLK----KRKEYLESEEINkSINEYNKI 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1544 VSLEAELQDissqeskDEASLAKVKKQlrdleakvKDQEEELDEQAGTIQmLEQAKLRLEMEMERMRQTHSKEVE---SR 1620
Cdd:PRK01156 525 ESARADLED-------IKIKINELKDK--------HDKYEEIKNRYKSLK-LEDLDSKRTSWLNALAVISLIDIEtnrSR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1621 DEEVEEARQSCQKKLKQMEVQLEeeyEDKQKVLREKRELESKLTTLSEQVSQrdLESEKRLRKDLKRTkalladaqimLD 1700
Cdd:PRK01156 589 SNEIKKQLNDLESRLQEIEIGFP---DDKSYIDKSIREIENEANNLNNKYNE--IQENKILIEKLRGK----------ID 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1701 HLKNNAPSKREIAQLKNQLeeseftcaaAVKARKaMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQE 1780
Cdd:PRK01156 654 NYKKQIAEIDSIIPDLKEI---------TSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
570
....*....|....*...
gi 1239919865 1781 DMnELMKKHKAAVAQASR 1798
Cdd:PRK01156 724 TL-ESMKKIKKAIGDLKR 740
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1204-1646 |
1.56e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1204 LARLEEQRDEQTSRNLTLFQAacrgyLARQHFKKKKIQDLAIRCVQKNIKKNKGVKDWAWWKLfttvrpLIEVQLSEEQI 1283
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAEL-----QEELEELEEELEELEAELEELREELEKLEKLLQLLPL------YQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1284 RSKDEEIQQLRSKLEkvekERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERL---------------R 1348
Cdd:COG4717 142 AELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELeelqqrlaeleeeleE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1349 AEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDTGGEWRLKYERAMREVDFTKKRLQQEFEDKLEVEQ 1428
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1429 QNKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQR 1508
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1509 EKLQREKDTL--LAEAFSLKQQLEEkdmdiagftqKVVSLEAELQDI--SSQESKDEASLAKVKKQLRDLEAKVKDQEEE 1584
Cdd:COG4717 378 EAGVEDEEELraALEQAEEYQELKE----------ELEELEEQLEELlgELEELLEALDEEELEEELEELEEELEELEEE 447
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239919865 1585 LDEqagtiqmLEQAKLRLEMEMERMrqthskeveSRDEEVEEARQSCQKKLKQMEvQLEEEY 1646
Cdd:COG4717 448 LEE-------LREELAELEAELEQL---------EEDGELAELLQELEELKAELR-ELAEEW 492
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1514-1908 |
1.62e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 57.27 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1514 EKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEAS-------LAKVKKQLRDLEAKVKDQEEeld 1586
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQTALRQQEKIERYQED--- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1587 eqagtiqmLEQAKLRLEMEMERMrqthsKEVESRDEEVEEARQSCQKKLKQMEVQLeeeyEDKQKVLREkreleskLTTL 1666
Cdd:COG3096 356 --------LEELTERLEEQEEVV-----EEAAEQLAEAEARLEAAEEEVDSLKSQL----ADYQQALDV-------QQTR 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1667 SEQVSQrdlesekrLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQ--------LKNQLEESEftcAAAVKARKAM-- 1736
Cdd:COG3096 412 AIQYQQ--------AVQALEKARALCGLPDLTPENAEDYLAAFRAKEQqateevleLEQKLSVAD---AARRQFEKAYel 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1737 ------EVEMEDLH---LQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQ---EDMNELMKKHKAAVAQASRDLAQMN 1804
Cdd:COG3096 481 vckiagEVERSQAWqtaRELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQnaeRLLEEFCQRIGQQLDAAEELEELLA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1805 DLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMvdKSLvSRQEAKIRELETRLEFERTQVKrlESLASR--LKENMEKL 1882
Cdd:COG3096 561 ELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI--KEL-AARAPAWLAAQDALERLREQSG--EALADSqeVTAAMQQL 635
|
410 420
....*....|....*....|....*.
gi 1239919865 1883 TEERDQRTAAENREKEQNKRLQRQLR 1908
Cdd:COG3096 636 LEREREATVERDELAARKQALESQIE 661
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1403-1759 |
1.84e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.06 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1403 ERAMREVDFTKKRLQQEFEDKLEVEQQNKRQLERrlgdLQADIDESQRALQQLKKKCQRLTAELQdtklhlegqqvrnhE 1482
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQLQ--------------A 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1483 LEKKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEA 1562
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1563 SLAKVKKQlrDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQL 1642
Cdd:COG4372 172 ELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1643 EEEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEES 1722
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
330 340 350
....*....|....*....|....*....|....*..
gi 1239919865 1723 EFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEE 1759
Cdd:COG4372 330 LALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAG 366
|
|
| PDZ_tamalin_CYTIP-like |
cd06713 |
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ... |
219-307 |
2.08e-07 |
|
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of tamalin, cytohesin-1-interacting protein, and related domains. Tamalin (trafficking regulator and scaffold protein tamalin, also known as general receptor for phosphoinositides 1-associated scaffold protein, GRASP) functions to link receptors, including group 1 metabotropic glutamate receptors (mGluRs), to neuronal proteins. The tamalin PDZ domain binds the C-terminal domains of group I mGluRs; it also binds potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (HCN2), neurotrophin-3 (NT3) TrkCT1-truncated receptor, SAP90/PSD-95-associated protein, and tamalin itself. CYTIP (cytohesin-1-interacting protein, also known as Pleckstrin homology Sec7 and coiled-coil domain-binding protein) sequesters cytohesin-1 in the cytoplasm, limiting its interaction with beta2 integrins; cytohesin-1 binds the CYTIP coiled coil domain. The CYTIP PDZ domain can bind the C-terminal peptide of protocadherin alpha-1 (PCDHA1), indicating a possible interaction between the two. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This tamalin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467197 [Multi-domain] Cd Length: 91 Bit Score: 50.70 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 219 RELELQRRPTGDFGF-------------SLRRTTMLDRgpegqvyrrvVHFAEPGagtkDLAlGLVPGDRLVEINGHNVE 285
Cdd:cd06713 4 RTIILEKQDNETFGFeiqtyglhhknsnEVEMCTYVCR----------VHEDSPA----YLA-GLTAGDVILSVNGVSVE 68
|
90 100
....*....|....*....|..
gi 1239919865 286 SKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06713 69 GASHQEIVELIRSSGNTLRLET 90
|
|
| PDZ2_L-delphilin-like |
cd06744 |
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ... |
224-308 |
2.70e-07 |
|
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which it is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467226 [Multi-domain] Cd Length: 75 Bit Score: 49.97 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 224 QRRPTGDFGFSLRrttmlDRGPegqVYRRVVhfaEPGaGTKDLAlGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSV 303
Cdd:cd06744 4 VYRGNGSFGFTLR-----GHAP---VYIESV---DPG-SAAERA-GLKPGDRILFLNGLDVRNCSHDKVVSLLQGSGSMP 70
|
....*
gi 1239919865 304 RLKVQ 308
Cdd:cd06744 71 TLVVE 75
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1423-1722 |
2.93e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.29 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1423 KLEVEQQNKRQLERRLGDLQADIDESQRA----LQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAH 1498
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKalfeLDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1499 EEAQREKLQREKLQREKDTLLAEAFSLKQQLEEkdmdiagFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKV 1578
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEE-------LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1579 KDQEEELDEQAGTIQMLEQAKLRLEMEM---ERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQ--KVL 1653
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDEllkEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAlsALL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1654 REKRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEES 1722
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1421-1630 |
3.73e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1421 EDKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEE 1500
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1501 AQREKLQREKLQ-----REKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE 1575
Cdd:COG3883 95 LYRSGGSVSYLDvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1239919865 1576 AKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQS 1630
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1571-1933 |
3.94e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.54 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1571 LRDLEAKVKDQE--EELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYED 1648
Cdd:pfam13868 8 LRELNSKLLAAKcnKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1649 KQKVLREKRELESKLttLSEQVSQRDLESEKRLRKDLKRTKALladaqimldhlknnapsKREIAQLKNQLEeseftcaa 1728
Cdd:pfam13868 88 KRQEEYEEKLQEREQ--MDEIVERIQEEDQAEAEEKLEKQRQL-----------------REEIDEFNEEQA-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1729 avKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQ----REKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMN 1804
Cdd:pfam13868 141 --EWKELEKEEEREEDERILEYLKEKAEREEEREAEReeieEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1805 DLQAQLEEANKEKQELQEKLQALQSQVEFleqsmvdkslvsRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTE 1884
Cdd:pfam13868 219 ERQKEREEAEKKARQRQELQQAREEQIEL------------KERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRM 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1239919865 1885 ERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEM 1933
Cdd:pfam13868 287 KRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEER 335
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1771-1980 |
4.43e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1771 IQSRLEED-QEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEA 1849
Cdd:COG4717 43 IRAMLLERlEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE------LEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1850 KIRELETRLEFeRTQVKRLESLASRLKENMEKLTEERDQRTAAENREKEQnKRLQRQLRDTKEEMGELARKEAEASRKK- 1928
Cdd:COG4717 117 ELEKLEKLLQL-LPLYQELEALEAELAELPERLEELEERLEELRELEEEL-EELEAELAELQEELEELLEQLSLATEEEl 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1239919865 1929 HELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLITSLQ 1980
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| cpPDZ_CPP-like |
cd06782 |
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ... |
269-309 |
4.81e-07 |
|
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CPP (also known as tail-specific protease, PRC protein, Protease Re, and Photosystem II D1 protein processing peptidase), and related domains. CPP belongs to the peptidase S41A family. It cleaves a C-terminal 11 residue peptide from the precursor form of penicillin-binding protein 3, and may have a role in protecting bacterium from thermal and osmotic stresses. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This CPP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.
Pssm-ID: 467623 [Multi-domain] Cd Length: 88 Bit Score: 49.79 E-value: 4.81e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1239919865 269 GLVPGDRLVEINGHNVESKSRDEIVEMIR-QSGDSVRLKVQP 309
Cdd:cd06782 31 GIKPGDVIVAVDGESVRGMSLDEVVKLLRgPKGTKVKLTIRR 72
|
|
| PDZ3_Dlg1-2-4-like |
cd06795 |
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ... |
219-312 |
4.85e-07 |
|
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila Dlg1, human Dlg1, 2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197; SAP-97), Dlg2 (also known as channel-associated protein of synapse-110; postsynaptic density protein 93, PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95; synapse-associated protein 90, SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling, regulating surface expression of NMDA receptors in dorsal horn neurons of the spinal cord; it interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. The Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development; postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467257 [Multi-domain] Cd Length: 91 Bit Score: 49.66 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 219 RELELQRRPTGdFGFSLRRttmldrGPEGQ-VYrrvVHFAEPGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIR 297
Cdd:cd06795 3 RKIVLHKGSTG-LGFNIVG------GEDGEgIF---ISFILAG-GPADLSGELRRGDQILSVNGVDLRNATHEQAAAALK 71
|
90
....*....|....*
gi 1239919865 298 QSGDSVRLKVQPIPE 312
Cdd:cd06795 72 NAGQTVTIIAQYKPE 86
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1414-1976 |
5.19e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.44 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1414 KRLQQEFEDKLEVEQQNKRQLERRLGDL---QADIDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRF 1490
Cdd:TIGR01612 557 KKLIHEIKKELEEENEDSIHLEKEIKDLfdkYLEIDDEIIYINKLKLELKEKIKNISDKNEYIKKAIDLKKIIENNNAYI 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1491 DselsqahEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDiagftqkvvSLEAELQDISSQESKDEaslAKVKKQ 1570
Cdd:TIGR01612 637 D-------ELAKISPYQVPEHLKNKDKIYSTIKSELSKIYEDDID---------ALYNELSSIVKENAIDN---TEDKAK 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1571 LRDLEAKVkdqeeelDEQAGTIQMLEQAKLRLememermrqtHSKEVESRDEE----VEEARQSCQKKLKQMEVQLEEEY 1646
Cdd:TIGR01612 698 LDDLKSKI-------DKEYDKIQNMETATVEL----------HLSNIENKKNElldiIVEIKKHIHGEINKDLNKILEDF 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1647 EDKQKvlrekrELESKLTTLSEQVSQRDLESEKrlrkdLKRTKALLADaQIMLDHLKNnapskrEIAQlKNQLEESEFTc 1726
Cdd:TIGR01612 761 KNKEK------ELSNKINDYAKEKDELNKYKSK-----ISEIKNHYND-QINIDNIKD------EDAK-QNYDKSKEYI- 820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1727 aaavkarKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVA--QASRDLAQMN 1804
Cdd:TIGR01612 821 -------KTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISddKLNDYEKKFN 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1805 DLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENME---- 1880
Cdd:TIGR01612 894 DSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDntli 973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1881 -KLTE-ERDQRTAAENREKEQNKRLQRQLRDTKEEMGelarkeaeaSRKKHELEMDLESLEAANQSLQADLKLAFKRIGD 1958
Cdd:TIGR01612 974 dKINElDKAFKDASLNDYEAKNNELIKYFNDLKANLG---------KNKENMLYHQFDEKEKATNDIEQKIEDANKNIPN 1044
|
570 580
....*....|....*....|
gi 1239919865 1959 LQAAIEDEME--SDENEDLI 1976
Cdd:TIGR01612 1045 IEIAIHTSIYniIDEIEKEI 1064
|
|
| PDZ_Par6-like |
cd06718 |
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ... |
219-297 |
5.26e-07 |
|
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F (RhoGAP100F), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Par6 (also known as PAR6 or Par-6), RhoGAP100F, and related domains. Par6 is part of a conserved machinery that directs metazoan cell polarity, a process necessary for the function of diverse cell types. Par6 forms a cell polarity-regulatory complex with atypical protein kinase C (aPKC) and Par3. Par6 can also directly associate with PALS1 (proteins associated with Lin7, also known as Stardust) providing a link between the Par3/aPKC/Par6 complex and the PALS1-PATJ (protein-associated TJ) complex. Binding partners of the Par6-PDZ domain include Par3, PALS1/Stardust; leucine-rich repeat-containing protein netrin-G ligand-2 (NGL-2), human crumbs (CRB3) involve in the morphogenesis of the tight junctions in mammalian epithelial cells, and PAR-6 co-operates with the Par6 semi-CRIB domain to bind CDC42. CDC42 regulates the Par6 PDZ domain through an allosteric CRIB-PDZ transition. Drosophila RhoGAP100F, also known as synapse defective protein 1 homolog (syd-1 homolog), is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound form. The RhoGAP100F-PDZ domain binds the neurexin C terminus to control synapse formation at the Drosophila neuromuscular junction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par6-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467202 [Multi-domain] Cd Length: 84 Bit Score: 49.49 E-value: 5.26e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 219 RELELQRRPTGDFGFSLRRTTMLDRGPeGQVYRRVVhfaePGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIR 297
Cdd:cd06718 1 RRVELIKPPGKPLGFYIRDGNGVERVP-GIFISRLV----LG-SLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMV 73
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1610-1944 |
5.28e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 55.15 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1610 RQTHSKEVESRDEEVEEARQ--------SCQKKLKQMEVQLEE---EYEDKQKVLREKRELESKLTTLSEQVSQRDLESE 1678
Cdd:pfam09731 94 QSGVSSEVAEEEKEATKDAAeakaqlpkSEQEKEKALEEVLKEaisKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1679 KRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAME--VEMEDLHLQIDDIAKAKTA 1756
Cdd:pfam09731 174 EISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEekVEKAQSLAKLVDQYKELVA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1757 LEEQLSRLQREK--NEIQSRLEEDQEDMNElmkKHKAAVAQASRDLAQmndLQAQLEEanKEKQELQEKLQALQSQVEFL 1834
Cdd:pfam09731 254 SERIVFQQELVSifPDIIPVLKEDNLLSND---DLNSLIAHAHREIDQ---LSKKLAE--LKKREEKHIERALEKQKEEL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1835 EQSmvDKSLVSRQEAKIRELET--RLEFERTQVKRLESLASRLKENMEKLTEERDQRTaaENREKEQNKRLQR-QLRDTK 1911
Cdd:pfam09731 326 DKL--AEELSARLEEVRAADEAqlRLEFEREREEIRESYEEKLRTELERQAEAHEEHL--KDVLVEQEIELQReFLQDIK 401
|
330 340 350
....*....|....*....|....*....|...
gi 1239919865 1912 EEMgelARKEAEASRKKHELEMDLESLEAANQS 1944
Cdd:pfam09731 402 EKV---EEERAGRLLKLNELLANLKGLEKATSS 431
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1238-1653 |
6.16e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.36 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1238 KKIQDLAIRCVQKNIKKNKGVKDWAWWKLFTTVRPLIEVQLSEEQIRSKDEEIQQLRSKLEK-VEKERNELRLSNDRLET 1316
Cdd:pfam02463 596 VLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGlAEKSEVKASLSELTKEL 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1317 RISELTSELTDERNTGESASQLLDAEAAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDTGG 1396
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1397 EWRLKYE-------------RAMREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKKKcqrLT 1463
Cdd:pfam02463 756 RLKKEEKeeekselslkekeLAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI---KE 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1464 AELQDTKLHLEGQQVRNHELEKKQRRfDSELSQAHEEAQREKLQREKLQREKD--------TLLAEAFSLKQQLEEKDMD 1535
Cdd:pfam02463 833 EELEELALELKEEQKLEKLAEEELER-LEEEITKEELLQELLLKEEELEEQKLkdeleskeEKEKEEKKELEEESQKLNL 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1536 IAGFTQKVVSLEAELQDISSQESKDEASLAKV-KKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERmrqths 1614
Cdd:pfam02463 912 LEEKENEIEERIKEEAEILLKYEEEPEELLLEeADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEE------ 985
|
410 420 430
....*....|....*....|....*....|....*....
gi 1239919865 1615 KEVESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQKVL 1653
Cdd:pfam02463 986 KEERYNKDELEKERLE-EEKKKLIRAIIEETCQRLKEFL 1023
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1514-1923 |
6.42e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1514 EKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESkdeaslakvkkqlrDLEakvkdqeeeldeqagtiQ 1593
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAES--------------DLE-----------------Q 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1594 MLEQAKLRLEMEMERMRQthskevesrdeeveearqscQKKLKQMEVQLEEeyedkqkvLREKreLESKLTTLSEQVSQR 1673
Cdd:PRK04863 329 DYQAASDHLNLVQTALRQ--------------------QEKIERYQADLEE--------LEER--LEEQNEVVEEADEQQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1674 DlESEKRLR---KDLKRTKALLADAQIMLDHLKnnapsKREIA--QLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQID 1748
Cdd:PRK04863 379 E-ENEARAEaaeEEVDELKSQLADYQQALDVQQ-----TRAIQyqQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1749 DIAKAKTALEEQLSRLQreknEIQSRLEedqedmnELMKKHKAAVAQASRDLAQmNDLQAQLEEANKEKQELQeKLQALQ 1828
Cdd:PRK04863 453 EATEELLSLEQKLSVAQ----AAHSQFE-------QAYQLVRKIAGEVSRSEAW-DVARELLRRLREQRHLAE-QLQQLR 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1829 SQVEFLEQsmvDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEErdQRTAAENREkeqnkRLQRQLR 1908
Cdd:PRK04863 520 MRLSELEQ---RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES--VSEARERRM-----ALRQQLE 589
|
410
....*....|....*
gi 1239919865 1909 DTKEEMGELARKEAE 1923
Cdd:PRK04863 590 QLQARIQRLAARAPA 604
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1617-1830 |
6.49e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1617 VESRDEEVEEARQSCQKKLKQMEVQLEEeyedKQKVLREKRElESKLTTLSEQVSQRdLESEKRLRKDLKRTKALLADAQ 1696
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQ-KNGLVDLSEEAKLL-LQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1697 IMLDHLKNNAPSKRE----------IAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDI-AKAKTALEEQLSRLQ 1765
Cdd:COG3206 240 ARLAALRAQLGSGPDalpellqspvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALrAQLQQEAQRILASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239919865 1766 REKNEIQSRLEEDQEDMNELmkkhKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQ 1830
Cdd:COG3206 320 AELEALQAREASLQAQLAQL----EARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| PDZ_SYNJ2BP-like |
cd06709 |
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ... |
220-308 |
6.70e-07 |
|
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNJ2BP, and related domains. SYNJ2BP (also known as mitochondrial outer membrane protein 25, OMP25) regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Binding partners of the SYNJ2BP PDZ domain include activin type II receptors (ActR-II), and SYNJ2. SYNJ2BP interacts with the PDZ binding motif of the Notch Delta-like ligand 1 (DLL1) and DLL4, promoting Delta-Notch signaling, and inhibiting sprouting angiogenesis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNJ2BP-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467193 [Multi-domain] Cd Length: 86 Bit Score: 49.21 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 220 ELELQRRPTGdFGFSLRRTT-----MLDRGpegqVYrrVVHFAEPGAGTKDlalG-LVPGDRLVEINGHNVESKSRDEIV 293
Cdd:cd06709 2 EITLKRGPSG-LGFNIVGGTdqpyiPNDSG----IY--VAKIKEDGAAAID---GrLQEGDKILEINGQSLENLTHQDAV 71
|
90
....*....|....*
gi 1239919865 294 EMIRQSGDSVRLKVQ 308
Cdd:cd06709 72 ELFRNAGEDVKLKVQ 86
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1566-1721 |
9.97e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.01 E-value: 9.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1566 KVKKQLRDLEAKVKDQEEELDEQAGTIQmlEQAKLRLEMEMERMRQTHSKEVESRDEEVEEArqscQKKLKQMEVQLEEE 1645
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNELQKL----EKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1646 YED----KQKVLREKRELESKLTTLSEQVSQRDlESEKRLRKDLKRTKALLAD--AQIMLDHLKNNApsKREIAQLKNQL 1719
Cdd:PRK12704 102 LELlekrEEELEKKEKELEQKQQELEKKEEELE-ELIEEQLQELERISGLTAEeaKEILLEKVEEEA--RHEAAVLIKEI 178
|
..
gi 1239919865 1720 EE 1721
Cdd:PRK12704 179 EE 180
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1563-1907 |
1.36e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.15 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1563 SLAKVKKQLrdleAKVKDQEEELDEQAGTIQMLEQAKLRLEMemermRQTHSKEVESRDEEVEEArqscQKKLKQMEVQL 1642
Cdd:PRK11281 37 TEADVQAQL----DALNKQKLLEAEDKLVQQDLEQTLALLDK-----IDRQKEETEQLKQQLAQA----PAKLRQAQAEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1643 EEEYEDKQKVLREK------RELESKLTTLSEQVSQrdlesekrLRKDLKRTKALLADAQIMLDH----LKNNAPSKREI 1712
Cdd:PRK11281 104 EALKDDNDEETRETlstlslRQLESRLAQTLDQLQN--------AQNDLAEYNSQLVSLQTQPERaqaaLYANSQRLQQI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1713 AQLKNQLEESEFTCAAAvkARKAMEVEMEDLHLQID-------------DIAKAKTAL-EEQLSRLQREKNEIQS----- 1773
Cdd:PRK11281 176 RNLLKGGKVGGKALRPS--QRVLLQAEQALLNAQNDlqrkslegntqlqDLLQKQRDYlTARIQRLEHQLQLLQEainsk 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1774 RLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQL--------EEANK-EKQELQEKLQ---ALQSQVEFLEQSMVDK 1841
Cdd:PRK11281 254 RLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLsqrllkatEKLNTlTQQNLRVKNWldrLTQSERNIKEQISVLK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1842 -SLV-SR----------QEAKIREL-----ETRLE-FE----RTQVKRLESLASRL--KENMEKLTEERDQRTA-AENRE 1896
Cdd:PRK11281 334 gSLLlSRilyqqqqalpSADLIEGLadriaDLRLEqFEinqqRDALFQPDAYIDKLeaGHKSEVTDEVRDALLQlLDERR 413
|
410
....*....|....
gi 1239919865 1897 K--EQ-NKRLQRQL 1907
Cdd:PRK11281 414 EllDQlNKQLNNQL 427
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1501-1692 |
1.37e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1501 AQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQK--VVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKV 1578
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1579 KDQEEELDE---------QAGTIQMLEQAKLRLEMEMERMRQTHSKE---VESRDEEVEEARQSCQKKLKQMEVQLEEEY 1646
Cdd:COG3206 243 AALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239919865 1647 EDKQkvlREKRELESKLTTLSEQVSQ-RDLESE-KRLRKDLKRTKALL 1692
Cdd:COG3206 323 EALQ---AREASLQAQLAQLEARLAElPELEAElRRLEREVEVARELY 367
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1620-1948 |
1.44e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1620 RDEEVEEArQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEsklttlseqvsqrdlESEKRLRKDLKRTKALLADAQIML 1699
Cdd:PRK04863 281 RRVHLEEA-LELRRELYTSRRQLAAEQYRLVEMARELAELN---------------EAESDLEQDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1700 DHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKA----KTALEEQLSRLQREKNEIQsRL 1775
Cdd:PRK04863 345 RQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladyQQALDVQQTRAIQYQQAVQ-AL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1776 EEDQEdMNELMKkhkAAVAQASRDLAQmndLQAQLEEANKEKQELQEKL---QALQSQVEF---LEQSMVDKslVSRQEA 1849
Cdd:PRK04863 424 ERAKQ-LCGLPD---LTADNAEDWLEE---FQAKEQEATEELLSLEQKLsvaQAAHSQFEQayqLVRKIAGE--VSRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1850 K--IRELETRLEFERTQVKRLESLASRLKENMEKLTEERDqrtaAENREKEQNKRLQRQLRDtkeemgelarkEAEASRK 1927
Cdd:PRK04863 495 WdvARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQR----AERLLAEFCKRLGKNLDD-----------EDELEQL 559
|
330 340
....*....|....*....|.
gi 1239919865 1928 KHELEMDLESLEAANQSLQAD 1948
Cdd:PRK04863 560 QEELEARLESLSESVSEARER 580
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1476-1950 |
1.51e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 54.06 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1476 QQVRNHELEKKQRRFDS--ELSQAHEEAQR----EKLQREKLQREkdtLLAEAFSLKQQLeekDMDIAGFTQKVVSleae 1549
Cdd:NF041483 76 QLLRNAQIQADQLRADAerELRDARAQTQRilqeHAEHQARLQAE---LHTEAVQRRQQL---DQELAERRQTVES---- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1550 lqDISSQESKDEASLAKVKKQLRDLeakvkdqeeeLDE-QAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEE-- 1626
Cdd:NF041483 146 --HVNENVAWAEQLRARTESQARRL----------LDEsRAEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAil 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1627 --ARQSCQKKLKQMEVQLEEEyEDKQKVLREKRELES-----KLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQIML 1699
Cdd:NF041483 214 rrARKDAERLLNAASTQAQEA-TDHAEQLRSSTAAESdqarrQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1700 DHLKNNAPS---------KREIAQLKNQ-LEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEE--QLSRLQRE 1767
Cdd:NF041483 293 AKQLASAESaneqrtrtaKEEIARLVGEaTKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTaaQLAKAART 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1768 KNEIQSRLEEDQEDM-----NELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQ--------ELQEKLQALQSQVEFL 1834
Cdd:NF041483 373 AEEVLTKASEDAKATtraaaEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTkeyraktvELQEEARRLRGEAEQL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1835 EQSMVDKSLVSRQEAKireletrlefeRTQVKRLESLASRLKENMEKLTEERDQ--RTAAENREKEQNKRLQR--QLRDT 1910
Cdd:NF041483 453 RAEAVAEGERIRGEAR-----------REAVQQIEEAARTAEELLTKAKADADElrSTATAESERVRTEAIERatTLRRQ 521
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1239919865 1911 KEEMGELARKEAEasRKKHELEMDLESLEAANQSLQADLK 1950
Cdd:NF041483 522 AEETLERTRAEAE--RLRAEAEEQAEEVRAAAERAARELR 559
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1709-1940 |
1.73e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1709 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKK 1788
Cdd:COG1340 21 REEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1789 HKAAVaQASRDLAQMNDLQAQLEEA--------NKEKqELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEF 1860
Cdd:COG1340 101 LAELN-KAGGSIDKLRKEIERLEWRqqtevlspEEEK-ELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1861 ERTQVKRLESLASRLKENMEKLTEERDQ--------------RTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASR 1926
Cdd:COG1340 179 IHKKIKELAEEAQELHEEMIELYKEADElrkeadelhkeiveAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKR 258
|
250
....*....|....
gi 1239919865 1927 KKHELEMDLESLEA 1940
Cdd:COG1340 259 EKEKEELEEKAEEI 272
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1446-1660 |
1.87e-06 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 51.20 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1446 DESQRALQQLKK----KCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQaHEeaqreklqreklqREKDTLLAE 1521
Cdd:pfam15665 10 DEHEAEIQALKEaheeEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQ-HE-------------RMKRQALTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1522 AFSLKQQLEEKDM-DIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL-RDLEAKVKDQEEELDEQAGTIQMLEQAK 1599
Cdd:pfam15665 76 FEQYKRRVEERELkAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFeQEKRKALEELRAKHRQEIQELLTTQRAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239919865 1600 LRLEM-EMERMRQTHSKEVESRDEEVEEarqscqkkLKQMEVQLEEEYEDK---QKVLREkRELE 1660
Cdd:pfam15665 156 SASSLaEQEKLEELHKAELESLRKEVED--------LRKEKKKLAEEYEQKlskAQAFYE-RELE 211
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1558-1683 |
1.98e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 53.22 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1558 SKDEASLAKVkkqLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRqthskevESRDEEVEEARQSCQKKLKQ 1637
Cdd:COG1193 510 GEESIDVEKL---IEELERERRELEEEREEAERLREELEKLREELEEKLEELE-------EEKEEILEKAREEAEEILRE 579
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1239919865 1638 MEVQLEE---EYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKRLRK 1683
Cdd:COG1193 580 ARKEAEElirELREAQAEEEELKEARKKLEELKQELEEKLEKPKKKAKP 628
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
558-693 |
1.99e-06 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 53.59 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 558 LLEAFGNSPTIMNGNATRFSQILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEA------TFNVFYYLLACAD 626
Cdd:cd14894 255 VLEAFGHATTSMNLNSSRFGKMTTLQVafglhPWEFQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILYAMVAGVN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 627 G-----TLRTELHLNHL----------AENNVFGIVplAKPEEKQKAAQQFSKLQTAMKVLGISPDEQKACWLILAAIYH 691
Cdd:cd14894 335 AfpfmrLLAKELHLDGIdcsaltylgrSDHKLAGFV--SKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLW 412
|
..
gi 1239919865 692 LG 693
Cdd:cd14894 413 LG 414
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1527-1826 |
2.03e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1527 QQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKdqeeELDEQAGTIQMLEQAKLRLEMEM 1606
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK----ELREEAQELREKRDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1607 ERMRQTHSKEVESRDEEVEEarqscqkkLKQMEVQLEEEYEDKQKVLREKRELESKLttlseQVSQRDLESEKRLRKDLK 1686
Cdd:COG1340 77 KEERDELNEKLNELREELDE--------LRKELAELNKAGGSIDKLRKEIERLEWRQ-----QTEVLSPEEEKELVEKIK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1687 RTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQR 1766
Cdd:COG1340 144 ELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1767 EKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLaqmndLQAQLEEANKEKQELQEKLQA 1826
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKLRKKQRALK-----REKEKEELEEKAEEIFEKLKK 278
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1792-1973 |
2.17e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1792 AVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEqsmvdkslvsrqeAKIRELETRLEFERTQVKRLESL 1871
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALE-------------ARLEAAKTELEDLEKEIKRLELE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1872 ASRLKENMEKLTEErdQRTAAENREKEQnkrLQRQLRDTKEEMGELARKEAEasrkkheLEMDLESLEAANQSLQADLKL 1951
Cdd:COG1579 68 IEEVEARIKKYEEQ--LGNVRNNKEYEA---LQKEIESLKRRISDLEDEILE-------LMERIEELEEELAELEAELAE 135
|
170 180
....*....|....*....|..
gi 1239919865 1952 AFKRIGDLQAAIEDEMESDENE 1973
Cdd:COG1579 136 LEAELEEKKAELDEELAELEAE 157
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1600-1950 |
2.41e-06 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 52.93 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1600 LRLEMEMERMRQTHSKEVESRDEEVEEARQSCQKKLKQmevQLEEEYEDKQKVLrekrELESKLTTLSEQVSQRDLESEK 1679
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKK---EIDLEYTEAVIAM----GLQERLENLREEFSKANSQDQL 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1680 RLRkdlkrtkALLADAQIMLDHLKNNAPSKREIAQLKNQLEeseftcaaavkarkamevemedlhlQIDDIAKAKTALEE 1759
Cdd:PLN03229 505 MHP-------VLMEKIEKLKDEFNKRLSRAPNYLSLKYKLD-------------------------MLNEFSRAKALSEK 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1760 QlSRLQREKNEIQSRLEE--DQEDMNELMKKHKAAVAQ--ASRDLAQMNDLQAQLEEANKEKQ-ELQEKLQALQSQVEFL 1834
Cdd:PLN03229 553 K-SKAEKLKAEINKKFKEvmDRPEIKEKMEALKAEVASsgASSGDELDDDLKEKVEKMKKEIElELAGVLKSMGLEVIGV 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1835 EQSMVDKSLVSRQE---AKIREL--ETRLEFERT-QVKRLESLASRLKENMEKLTEERDQrtaaenREKEQNKRLQRQLR 1908
Cdd:PLN03229 632 TKKNKDTAEQTPPPnlqEKIESLneEINKKIERViRSSDLKSKIELLKLEVAKASKTPDV------TEKEKIEALEQQIK 705
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1239919865 1909 DTKEEmgelARKEAEASRKKHELEMDLESLEAANQSLQADLK 1950
Cdd:PLN03229 706 QKIAE----ALNSSELKEKFEELEAELAAARETAAESNGSLK 743
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1496-1696 |
3.36e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1496 QAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKdmdiagfTQKVVSLEAELQDIssqeskdEASLAKVKKQLRDLE 1575
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEEL-------NEEYNELQAELEAL-------QAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1576 AKVKDQEEELDEQA----------GTIQMLEQAK---------LRLEMEMERMRQThSKEVESRDEEVEEARQSCQKKLK 1636
Cdd:COG3883 79 AEIEERREELGERAralyrsggsvSYLDVLLGSEsfsdfldrlSALSKIADADADL-LEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239919865 1637 QMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVS--QRDLESEKRLRKDLKRTKALLADAQ 1696
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAaaEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1280-1949 |
4.89e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1280 EEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRAEKEMKELQTQ 1359
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1360 YDALKKQMEVMEMEVmeARLIRAAEINGEVDDDdtggewrlkyeraMREV-DFTKKRLQQEFEDKLEVEQ--QNKRQLE- 1435
Cdd:COG3096 594 IKELAARAPAWLAAQ--DALERLREQSGEALAD-------------SQEVtAAMQQLLEREREATVERDElaARKQALEs 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1436 --RRLgdLQADIDESQRaLQQLkkkCQRLTAEL-----QDTKLH-------LEGQQ-----VRNHELEKKQ--------- 1487
Cdd:COG3096 659 qiERL--SQPGGAEDPR-LLAL---AERLGGVLlseiyDDVTLEdapyfsaLYGPArhaivVPDLSAVKEQlagledcpe 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1488 ---------RRFDSELSQAHEE--------------------------AQREKlQREKLQREKDTL---LAEAFSLKQQL 1529
Cdd:COG3096 733 dlyliegdpDSFDDSVFDAEELedavvvklsdrqwrysrfpevplfgrAAREK-RLEELRAERDELaeqYAKASFDVQKL 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1530 EEKDMDIAGF--TQKVVSL----EAELQDISSQESKDEASLAkvkkQLRDLEAKVKDQEEELDEQAGTIQ-MLEQAKLRL 1602
Cdd:COG3096 812 QRLHQAFSQFvgGHLAVAFapdpEAELAALRQRRSELERELA----QHRAQEQQLRQQLDQLKEQLQLLNkLLPQANLLA 887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1603 EmemermrQTHSKEVESRDEEVEEARQScQKKLKQMEVQLeeeyedkqkvlrekRELESKLTTLseqvsQRDLESEKRLR 1682
Cdd:COG3096 888 D-------ETLADRLEELREELDAAQEA-QAFIQQHGKAL--------------AQLEPLVAVL-----QSDPEQFEQLQ 940
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1683 KDLKRTKALLADAQIMLDHLKNnapskreiaqlknqleeseftcaaaVKARKAmevemedlHLQIDDIAkaktaleeqls 1762
Cdd:COG3096 941 ADYLQAKEQQRRLKQQIFALSE-------------------------VVQRRP--------HFSYEDAV----------- 976
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1763 rlqrekneiqSRLEEDQeDMNELMKkHKAAVAQASRDLA--QMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM-- 1838
Cdd:COG3096 977 ----------GLLGENS-DLNEKLR-ARLEQAEEARREAreQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELee 1044
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1839 ----VDKSLVSRQEAKIRELETRLEFERTQVKRLE-----------SLASRLKENMEKLTEERDQRTAAenreKEQNKRL 1903
Cdd:COG3096 1045 lgvqADAEAEERARIRRDELHEELSQNRSRRSQLEkqltrceaemdSLQKRLRKAERDYKQEREQVVQA----KAGWCAV 1120
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1904 QRQLRDTKEE----MGELARKEAEASRkkhelEMDLESLEAANQSlQADL 1949
Cdd:COG3096 1121 LRLARDNDVErrlhRRELAYLSADELR-----SMSDKALGALRLA-VADN 1164
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1801-1994 |
5.19e-06 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 50.03 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1801 AQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETrlEFERTQvKRLESLASRLKEnME 1880
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAE------VAALNRRIQLLEE--ELERTE-ERLAEALEKLEE-AE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1881 KLTEERDQ-RTAAENREKEQNKR---LQRQLRDTKEEMGELARKEAEASRKKHELEMDLE-------SLEAANQSLQADL 1949
Cdd:pfam00261 71 KAADESERgRKVLENRALKDEEKmeiLEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraeeraeLAESKIVELEEEL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1239919865 1950 KLAFKRIGDLQAAIEDEMES-DENEDLITSLQDMVTKYQKRKNKPE 1994
Cdd:pfam00261 151 KVVGNNLKSLEASEEKASEReDKYEEQIRFLTEKLKEAETRAEFAE 196
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1784-1959 |
5.51e-06 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 49.52 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1784 ELMKKHKAAVAQA------------------SRDLAQMNDLQAQ----LEEANKEKQELQEKLQALQSQVEFLEQSMV-- 1839
Cdd:pfam13851 1 ELMKNHEKAFNEIknyynditrnnlelikslKEEIAELKKKEERneklMSEIQQENKRLTEPLQKAQEEVEELRKQLEny 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1840 --DKSLVSRQEAKIRELEtrleferTQVKRLESLASRLKENMEKLTEERDQRTAAEN---REKEQNKRLQRQLRDTK-EE 1913
Cdd:pfam13851 81 ekDKQSLKNLKARLKVLE-------KELKDLKWEHEVLEQRFEKVERERDELYDKFEaaiQDVQQKTGLKNLLLEKKlQA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1239919865 1914 MGE-LARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDL 1959
Cdd:pfam13851 154 LGEtLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1421-1825 |
5.62e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.94 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1421 EDKLEVEQQNKRQLERRLGDLQADIDESQ--------RALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQRrfdS 1492
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKhtqnvalnKKLSDIKTEYLYELNVLKEKS---------EAELTSKTK---K 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1493 ELSQAHEEAQREKLQREKLQREKDTLLAEA-FSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESkdEASLAKVKKQL 1571
Cdd:NF033838 122 ELDAAFEQFKKDTLEPGKKVAEATKKVEEAeKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKA--ELELVKEEAKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1572 RDLEAKVKDQEEELDEQAGTIQMLEQAKL-RLEMEMERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKq 1650
Cdd:NF033838 200 PRDEEKIKQAKAKVESKKAEATRLEKIKTdREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDK- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1651 kvlREKRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQIMLDHLKNNAPS------KREIAQLKNQLEESEF 1724
Cdd:NF033838 279 ---KENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTntyktlELEIAESDVKVKEAEL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1725 -----------------TCAAAVKARKAMEVEMEDLHLQI---DDIAKAKTALEEQLsrlqREKNEIQSRLEEDQEDMNE 1784
Cdd:NF033838 356 elvkeeakeprneekikQAKAKVESKKAEATRLEKIKTDRkkaEEEAKRKAAEEDKV----KEKPAEQPQPAPAPQPEKP 431
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1239919865 1785 LMKKHKAAVAQASRDLAqmnDLQAQLEEANKEKQELQEKLQ 1825
Cdd:NF033838 432 APKPEKPAEQPKAEKPA---DQQAEEDYARRSEEEYNRLTQ 469
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1606-1952 |
5.63e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 51.68 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1606 MERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQ----LEEEYEDKQKVLREKRELESKLTTLSEQVSQRDLE----- 1676
Cdd:pfam07111 21 LERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEgsqaLSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRleaqa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1677 --------SEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVEMEDLHLQID 1748
Cdd:pfam07111 101 meldalavAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLT-QAHEEALSSLTSKAEGLEKSLN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1749 DIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMN---ELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQ 1825
Cdd:pfam07111 180 SLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEaqvTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1826 ALQSQVEFLE---QSMVdKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEerdQRTAAENREKEQNKR 1902
Cdd:pfam07111 260 DLQATVELLQvrvQSLT-HMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMV---QLKAQDLEHRDSVKQ 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1903 LQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLA 1952
Cdd:pfam07111 336 LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRA 385
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1421-1852 |
6.17e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1421 EDKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKkkcqRLTAelqdTKLHLEGQQVRNHELEKKQRR---FDSELSQA 1497
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFS----RFIG----SHLAVAFEADPEAELRQLNRRrveLERALADH 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1498 HEEAQREKLQREKLQrekdtllaEAFSLKQQLEEKDM--DIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLrdle 1575
Cdd:PRK04863 857 ESQEQQQRSQLEQAK--------EGLSALNRLLPRLNllADETLADRVEEIREQLD----EAEEAKRFVQQHGNAL---- 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1576 akvkdqeEELDEQAGTIQMLEQaklrlemEMERMRQthskevesrdeEVEEARQScQKKLKQ--------MEVQLEEEYE 1647
Cdd:PRK04863 921 -------AQLEPIVSVLQSDPE-------QFEQLKQ-----------DYQQAQQT-QRDAKQqafaltevVQRRAHFSYE 974
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1648 DKQKVLREKRELESKLttlseQVSQRDLESEK-RLRKDLKRTKALLADAQIMLDHLKNNAPSKREI-AQLKNQLEesEFT 1725
Cdd:PRK04863 975 DAAEMLAKNSDLNEKL-----RQRLEQAEQERtRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMlQELKQELQ--DLG 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1726 CAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVA--QASRDLAQM 1803
Cdd:PRK04863 1048 VPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAgwCAVLRLVKD 1127
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1804 NDLQAQL---EEANKEKQEL-------QEKLQALQSQVEFLEQSMVDKSLVSRQEAKIR 1852
Cdd:PRK04863 1128 NGVERRLhrrELAYLSADELrsmsdkaLGALRLAVADNEHLRDVLRLSEDPKRPERKVQ 1186
|
|
| PDZ4_PTPN13-like |
cd06696 |
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ... |
220-307 |
6.68e-06 |
|
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)] and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467182 [Multi-domain] Cd Length: 85 Bit Score: 46.15 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 220 ELELQRRPTGDFGFSLRRTTMldrgPEGQVYRRVVHfaEPgagtkdlALG---LVPGDRLVEINGHNVESKSRDEIVEMI 296
Cdd:cd06696 5 EVTLTKSEKGSLGFTVTKGKD----DNGCYIHDIVQ--DP-------AKSdgrLRPGDRLIMVNGVDVTNMSHTEAVSLL 71
|
90
....*....|.
gi 1239919865 297 RQSGDSVRLKV 307
Cdd:cd06696 72 RAAPKEVTLVL 82
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1414-1916 |
6.72e-06 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 51.45 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1414 KRLQQEFEDKLEVeqqnkrqLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKlhleGQQVRNHELEKKQRrfDSE 1493
Cdd:pfam15964 223 EKLKLLYEAKTEV-------LESQVKSLRKDLAESQKTCEDLKERLKHKESLVAAST----SSRVGGLCLKCAQH--EAV 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1494 LSQAHEEAQREKLQRekLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSleaelqdisSQESKDEASLAKVKK--QL 1571
Cdd:pfam15964 290 LAQTHTNVHMQTIER--LTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQ---------AVQMTEEANFEKTKAliQC 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1572 RDLEAKVKDQEEELDEQAGTiqmlEQAKLRLEMEMERmrqthsKEVESRDEEVEEARQSCQKKLKQMEVQLEeeyedkqK 1651
Cdd:pfam15964 359 EQLKSELERQKERLEKELAS----QQEKRAQEKEALR------KEMKKEREELGATMLALSQNVAQLEAQVE-------K 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1652 VLREKRELESKLTTLSEQVSQRDLESEK---RLRKDLKRTKALLADAQimLDHLKNNAPSKR-------EIAQLKNQLEE 1721
Cdd:pfam15964 422 VTREKNSLVSQLEEAQKQLASQEMDVTKvcgEMRYQLNQTKMKKDEAE--KEHREYRTKTGRqleikdqEIEKLGLELSE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1722 SeftcaaavkaRKAMEVEMEDLHLQIDDIAKaktaLEEQLSRLQREKNeiqsrleedqedmneLMKKHKAAVAQASRDLA 1801
Cdd:pfam15964 500 S----------KQRLEQAQQDAARAREECLK----LTELLGESEHQLH---------------LTRLEKESIQQSFSNEA 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1802 QMNDLQAQLEEankekQELQEKLQALQSQvefleqsmvdkslvsrQEAKIRELETRLEFERTQVKRLESLASRLKENMEK 1881
Cdd:pfam15964 551 KAQALQAQQRE-----QELTQKMQQMEAQ----------------HDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEE 609
|
490 500 510
....*....|....*....|....*....|....*
gi 1239919865 1882 LTEERDQRTAAENREKEQNKRLQRQLRDTKEEMGE 1916
Cdd:pfam15964 610 ITQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEE 644
|
|
| PDZ1_PTPN13_FRMPD2-like |
cd06694 |
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ... |
258-305 |
6.89e-06 |
|
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467180 [Multi-domain] Cd Length: 92 Bit Score: 46.62 E-value: 6.89e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1239919865 258 EPGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRL 305
Cdd:cd06694 38 IPG-GPADKDGRIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPDKVEL 84
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1693-1920 |
6.90e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 51.23 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1693 ADAQI-MLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAK------TALEEQLSRLQ 1765
Cdd:COG0497 140 PDAQReLLDAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAAlqpgeeEELEEERRRLS 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1766 R-EK-----NEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFleqsmv 1839
Cdd:COG0497 220 NaEKlrealQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEF------ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1840 dkslvsrQEAKIRELETRLEfertqvkRLESLASRLKENMEKLTEERDQRTA----AENREkEQNKRLQRQLRDTKEEMG 1915
Cdd:COG0497 294 -------DPERLEEVEERLA-------LLRRLARKYGVTVEELLAYAEELRAelaeLENSD-ERLEELEAELAEAEAELL 358
|
....*
gi 1239919865 1916 ELARK 1920
Cdd:COG0497 359 EAAEK 363
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1479-1606 |
7.73e-06 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 48.39 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1479 RNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEA-FSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQE 1557
Cdd:pfam08614 15 RTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLlAQLREELAELYRSRGELAQRLVDLNEELQELEKKL 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 1558 SKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQML--EQAKLRLEMEM 1606
Cdd:pfam08614 95 REDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLqdELVALQLQLNM 145
|
|
| PDZ2-PTPN13_FRMPD2-like |
cd06792 |
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ... |
273-308 |
8.13e-06 |
|
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of human PTPN13, and related domains. PTPN13, also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1), negatively regulates FAS-mediated apoptosis and NGFR-mediated pro-apoptotic signaling, and may also regulate phosphoinositide 3-kinase (PI3K) signaling. It contains 5 PDZ domains; interaction partners of its second PDZ domain (PDZ2) include the Fas receptor (TNFRSF6) and thyroid receptor-interacting protein 6 (TRIP6). The second PDZ (PDZ2) domain, but not PDZ1 or PDZ3, of FRMPD2 binds to GluN2A and GluN2B, two subunits of N-methyl-d-aspartic acid (NMDA) receptors. Other binding partners of the FRMPDZ2 PDZ2 domain include NOD2, and catenin family members, delta catenin (CTNND2), armadillo repeat gene deleted in velo-cardio-facial syndrome (ARVCF) and p0071 (also known as plakophilin 4; PKP4). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467254 [Multi-domain] Cd Length: 87 Bit Score: 46.05 E-value: 8.13e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1239919865 273 GDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06792 51 GDRLLEVNGVSLEGVTHKQAVECLKNAGQVVTLVLE 86
|
|
| PDZ4_GRIP1-2-like |
cd06686 |
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
220-308 |
8.35e-06 |
|
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467174 [Multi-domain] Cd Length: 99 Bit Score: 46.57 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 220 ELELQRRPTGDFGFSLR----RTTMLDRGPegqvyrrVVHFAEPGAGTKDLALgLVPGDRLVEINGHNVESKSRDEIVEM 295
Cdd:cd06686 9 EVILRGDPLKGFGIQLQggvfATETLSSPP-------LISFIEPDSPAERCGV-LQVGDRVLSINGIPTEDRTLEEANQL 80
|
90
....*....|...
gi 1239919865 296 IRQSGDSVRLKVQ 308
Cdd:cd06686 81 LRDSASKVTLEIE 93
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1622-1940 |
8.78e-06 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 50.83 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1622 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTL----------SEQVSQRDLESEKRLRKDLKRTKAL 1691
Cdd:pfam15070 18 ENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELknqaavppaeEEQPPAGPSEEEQRLQEEAEQLQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1692 LADAQIML-DHLKNNAPSKREIAQLKNQLEESEFTC---AAAVKARKAMeveMEDLHLQIDDIAKAKT---ALEEQLSRL 1764
Cdd:pfam15070 98 LEALAGQLqAQVQDNEQLSRLNQEQEQRLLELERAAerwGEQAEDRKQI---LEDMQSDRATISRALSqnrELKEQLAEL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1765 Q-------REKNEIQSRLEEDQEDMNELMKKhkaaVAQASRDLAQMNDlqaQLEEANKEKQELQEK----LQALQSQVEF 1833
Cdd:pfam15070 175 QngfvkltNENMELTSALQSEQHVKKELAKK----LGQLQEELGELKE---TLELKSQEAQSLQEQrdqyLAHLQQYVAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1834 LEQSMVDKSLVSRQEAKIRELETRLEFERTQVK-RLESLASRLKENMEKLTEERdqrtaaenrekEQNKRLQRQLRDTKE 1912
Cdd:pfam15070 248 YQQLASEKEELHKQYLLQTQLMDRLQHEEVQGKvAAEMARQELQETQERLEALT-----------QQNQQLQAQLSLLAN 316
|
330 340 350
....*....|....*....|....*....|..
gi 1239919865 1913 EMG----ELARKEAEASRKKHELEMDLESLEA 1940
Cdd:pfam15070 317 PGEgdglESEEEEEEAPRPSLSIPEDFESREA 348
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1622-1882 |
8.94e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 51.11 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1622 EEVEEARQSCQKKLKQMEvQLEEEYEdkqKVLREKRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLA------DA 1695
Cdd:COG5185 232 EEALKGFQDPESELEDLA-QTSDKLE---KLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAeytksiDI 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1696 QIMLDHLKNNAPSKREIAQLKNQLEESEftcaAAVKARKA-MEVEMEDLHLQIDDIAKAKTAL--EEQLSRLQREKNEIQ 1772
Cdd:COG5185 308 KKATESLEEQLAAAEAEQELEESKRETE----TGIQNLTAeIEQGQESLTENLEAIKEEIENIvgEVELSKSSEELDSFK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1773 SRLEEDQEDMNELMKKHKAAVAQASRDLA--------QMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLV 1844
Cdd:COG5185 384 DTIESTKESLDEIPQNQRGYAQEILATLEdtlkaadrQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS 463
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1239919865 1845 SRQEAK---IRELETRLEFERTQVKRLESLASRLKENMEKL 1882
Cdd:COG5185 464 RLEEAYdeiNRSVRSKKEDLNEELTQIESRVSTLKATLEKL 504
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1274-1593 |
9.31e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1274 IEVQLSEEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRAEKEM 1353
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1354 KELQTQYDALKKQMevmemevmearliraaeingevddddtggewrlkyeramrevdftkKRLQQEFEDKleveQQNKRQ 1433
Cdd:COG4372 104 ESLQEEAEELQEEL----------------------------------------------EELQKERQDL----EQQRKQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1434 LERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKlhlegQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQR 1513
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALE-----QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1514 EKDTLLAEAfslKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQ 1593
Cdd:COG4372 209 IESLPRELA---EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1675-1975 |
1.09e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 50.19 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1675 LESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMevemedlhlqiddiAKAK 1754
Cdd:pfam15905 59 LELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSL--------------SASV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1755 TALEEQLSRLQREKNEIQSRLEED--QEDMN----ELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQ 1828
Cdd:pfam15905 125 ASLEKQLLELTRVNELLKAKFSEDgtQKKMSslsmELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1829 SQVEFLEQSMVD-KSLVSRQEAKIRELetrlefertqvkrleslaSRLKENMEKLTEERDQrtaAENREKEQNKRLQRQL 1907
Cdd:pfam15905 205 EKLVSTEKEKIEeKSETEKLLEYITEL------------------SCVSEQVEKYKLDIAQ---LEELLKEKNDEIESLK 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1908 RDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKlafKRIGDLQAAIedEMESDENEDL 1975
Cdd:pfam15905 264 QSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLN---AELEELKEKL--TLEEQEHQKL 326
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1276-1642 |
1.17e-05 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 50.67 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1276 VQLSEEQIRSKDEEIQQlrsklekVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRA-EKEMK 1354
Cdd:pfam15964 341 VQMTEEANFEKTKALIQ-------CEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLAlSQNVA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1355 ELQTQYDALKKQMEVMEMEVMEARLIRAAEingEVDDDDTGGEWRLKYERAMREVDFTKKRLQqEFEDK----LEVEQQN 1430
Cdd:pfam15964 414 QLEAQVEKVTREKNSLVSQLEEAQKQLASQ---EMDVTKVCGEMRYQLNQTKMKKDEAEKEHR-EYRTKtgrqLEIKDQE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1431 KRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDT--KLHLEGQqvrnhELEKKQRRFDSEL-SQAHEEAQREK-- 1505
Cdd:pfam15964 490 IEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESehQLHLTRL-----EKESIQQSFSNEAkAQALQAQQREQel 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1506 --------LQREKLQREKDTLLAEAFSLKQQLEEKdmdiagftqkVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAK 1577
Cdd:pfam15964 565 tqkmqqmeAQHDKTVNEQYSLLTSQNTFIAKLKEE----------CCTLAKKLEEITQKSRSEVEQLSQEKEYLQDRLEK 634
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 1578 VKDQEEELDEQAgtIQ---MLEQAKLRLEmEMERMRQTHSKEVE---SRDEEVEEARQSCQKKLKQMEVQL 1642
Cdd:pfam15964 635 LQKRNEELEEQC--VQhgrMHERMKQRLR-QLDKHCQATAQQLVqllSKQNQLFKERQNLTEEVQSLRSQV 702
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1773-2006 |
1.21e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.94 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1773 SRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEankEKQELQEKLQALQSQveFLEQSMVDKSLVSRQ---EA 1849
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCE---EKNALQEQLQAETEL--CAEAEEMRARLAARKqelEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1850 KIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTAAenREKEQnkrlqrqlrdtkeemgeLARKEAEASRKKh 1929
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAA--RQKLQ-----------------LEKVTTEAKIKK- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239919865 1930 eLEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENedlitslqdmvtkYQKRKNKPEGdsdVDSELEDR 2006
Cdd:pfam01576 136 -LEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKS-------------LSKLKNKHEA---MISDLEER 195
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1676-1949 |
1.28e-05 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 49.58 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1676 ESEKRLRKDLKRTKALLADAQimlDHLKNNAPSKREIAQLKNQL-EESEFTCAAAVKARKAMEVEMEDLHLQIDdiaKAK 1754
Cdd:pfam09311 16 EQEAETRDQVKKLQEMLRQAN---DQLEKTMKDKKELEDKMNQLsEETSNQVSTLAKRNQKSETLLDELQQAFS---QAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1755 TALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVaqaSRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFL 1834
Cdd:pfam09311 90 RNFQDQLAVLMDSREQVSDELVRLQKDNESLQGKHSLHV---SLQQAEKFDMPDTVQELQELVLKYREELIEVRTAADHM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1835 EQSMVDKSLVSR-----QEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTAAEnREKeqnkrlQRQLRD 1909
Cdd:pfam09311 167 EEKLKAEILFLKeqiqaEQCLKENLEETLQAEIENCKEEIASISSLKVELERIKAEKEQLENGL-TEK------IRQLED 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1239919865 1910 TKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADL 1949
Cdd:pfam09311 240 LQTTKGSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTEL 279
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1634-1849 |
1.40e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1634 KLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQrdlesekrLRKDLKRTKALLADAQimldhlKNNAPSKREIA 1713
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE--------LQAELEALQAEIDKLQ------AEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1714 QLKNQLEEseftcAAAVKARKAMEVEMEDLHLQ-------------IDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQE 1780
Cdd:COG3883 83 ERREELGE-----RARALYRSGGSVSYLDVLLGsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1781 DMNELMKKHKAAVAQASRDLAQMNDLQAQLEEankEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEA 1849
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSA---EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1771-1989 |
1.52e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.28 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1771 IQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKE----KQELQEKLQALQSQVEFLEQSMvdKSLVSR 1846
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRElesrVAELKEELRQSREKHEELEEKY--KELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1847 QEAKIRELETRLEFERTQVKRLEslasRLKENMEKLTEERDQRTAAENREKEQNKRLQRQlrdtkeemgelaRKEAEASR 1926
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIR----ELEEDIKTLTQRVLERETELERMKERAKKAGAQ------------RKEEEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239919865 1927 KkhELEMDLESLEAANQSLQADLKLAFKRIGdlqaaiEDEMESDENEDLITSLQDMVTKYQKR 1989
Cdd:pfam07888 174 K--QLQAKLQQTEEELRSLSKEFQELRNSLA------QRDTQVLQLQDTITTLTQKLTTAHRK 228
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1578-1915 |
1.59e-05 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 49.68 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1578 VKDQEEELDEQAGTIQMLEQAKLRL---------EMEMER-----MRQTHSKEVESRDEEVEEARQSCQKKL--KQMEVQ 1641
Cdd:pfam15742 1 VSSGEKLKYQQQEEVQQLRQNLQRLqilctsaekELRYERgknldLKQHNSLLQEENIKIKAELKQAQQKLLdsTKMCSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1642 LEEEYED-KQKVlrekRELESKLTTLSEQvsqrdLESEKRLRKDLKRTKALLADAQIMldhlknnapskreIAQLKNQLE 1720
Cdd:pfam15742 81 LTAEWKHcQQKI----RELELEVLKQAQS-----IKSQNSLQEKLAQEKSRVADAEEK-------------ILELQQKLE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1721 ESEFTCAAAVKA--RKAMEVEMEDLhlqIDDIAKAKTAL-EEQLSR--LQREKNEIQS-----RLEEDQEDMNELMKKHK 1790
Cdd:pfam15742 139 HAHKVCLTDTCIleKKQLEERIKEA---SENEAKLKQQYqEEQQKRklLDQNVNELQQqvrslQDKEAQLEMTNSQQQLR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1791 aaVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFL--EQSMVDKSL----------VSRQEAKIRELETRL 1858
Cdd:pfam15742 216 --IQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSSLQQEKEALqeELQQVLKQLdvhvrkynekHHHHKAKLRRAKDRL 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 1859 EFERTQ----VKRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQRQLRDtKEEMG 1915
Cdd:pfam15742 294 VHEVEQrderIKQLENEIGILQQQSEKEKAFQKQVTAQNEILLLEKRKLLEQLTE-QEELI 353
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1561-1904 |
1.68e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1561 EASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQ----AKLRLEMEMERMRQTHS--------KEVESRDEEVEEAR 1628
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQdyqaASDHLNLVQTALRQQEKieryqadlEELEERLEEQNEVV 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1629 QSCQKKLKQMEVQLEEEYEDkqkVLREKRELESKLTTLSEQvSQRDLESEKRLRKdLKRTKALLADAQIMLDHLKNnaps 1708
Cdd:PRK04863 372 EEADEQQEENEARAEAAEEE---VDELKSQLADYQQALDVQ-QTRAIQYQQAVQA-LERAKQLCGLPDLTADNAED---- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1709 krEIAQLKNQLEE-------------------SEFTCAAAVKARKAMEVEMEDLHlqidDIAKAK-------TALEEQLS 1762
Cdd:PRK04863 443 --WLEEFQAKEQEateellsleqklsvaqaahSQFEQAYQLVRKIAGEVSRSEAW----DVARELlrrlreqRHLAEQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1763 RLQREKNEIQSRLEEDQ---EDMNELMKKHKAAVAQA-------SRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVE 1832
Cdd:PRK04863 517 QLRMRLSELEQRLRQQQraeRLLAEFCKRLGKNLDDEdeleqlqEELEARLESLSESVSEARERRMALRQQLEQLQARIQ 596
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1833 FLEQsmvdkslvsrQEAKIRELETRLEFERTQV-------KRLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQ 1904
Cdd:PRK04863 597 RLAA----------RAPAWLAAQDALARLREQSgeefedsQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLS 665
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1563-1973 |
1.72e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.96 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1563 SLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEA--RQSCQKKLKQMEV 1640
Cdd:COG5185 94 LDTKILQEYVNSLIKLPNYEWSADILISLLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETgiIKDIFGKLTQELN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1641 QLEEEYEDKQKVLREKRELESKLTTLSEQVS---QRDLESEKRLRKDLKRTKALLAdaqimldhlknnapsKREIAQLKN 1717
Cdd:COG5185 174 QNLKKLEIFGLTLGLLKGISELKKAEPSGTVnsiKESETGNLGSESTLLEKAKEII---------------NIEEALKGF 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1718 QLEESEftcaaaVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLS-RLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQA 1796
Cdd:COG5185 239 QDPESE------LEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSkRLNENANNLIKQFENTKEKIAEYTKSIDIKKATE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1797 S-RDLAQMNDLQAQLEEAnkeKQELQEKLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFERTQVKRLESLASrL 1875
Cdd:COG5185 313 SlEEQLAAAEAEQELEES---KRETETGIQNLTAEIEQGQESL------TENLEAIKEEIENIVGEVELSKSSEELDS-F 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1876 KENMEKLTEERDQ-RTAAENREKE--------------QNKRLQRQLRDTKEEMGELARK--EAEASRKKHELEMDLESL 1938
Cdd:COG5185 383 KDTIESTKESLDEiPQNQRGYAQEilatledtlkaadrQIEELQRQIEQATSSNEEVSKLlnELISELNKVMREADEESQ 462
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1239919865 1939 E-------AANQSLQADLKLAFKRIGDLQAAIEDEMESDENE 1973
Cdd:COG5185 463 SrleeaydEINRSVRSKKEDLNEELTQIESRVSTLKATLEKL 504
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1464-1836 |
1.77e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1464 AELQDTKLHLEGQQVRNHELEKK---QRRFDSELSQAHEEA-------QREKLQREKLQREKDTLLAeafsLKQQLEEKD 1533
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARElaeLNEAESDLEQDYQAAsdhlnlvQTALRQQEKIERYQADLEE----LEERLEEQN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1534 MDIAGFTQKVVSLEAELQdiSSQESKDEAslakvKKQLRDLEakvkdqeEELDEQ---AGTIQmleQAKLRLEmEMERMR 1610
Cdd:PRK04863 369 EVVEEADEQQEENEARAE--AAEEEVDEL-----KSQLADYQ-------QALDVQqtrAIQYQ---QAVQALE-RAKQLC 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1611 QTHSKEVESRDEEVEEAR---QSCQKKLKQMEVQL----------EEEYEDKQKVLRE------KRELESKLTTLSEQVS 1671
Cdd:PRK04863 431 GLPDLTADNAEDWLEEFQakeQEATEELLSLEQKLsvaqaahsqfEQAYQLVRKIAGEvsrseaWDVARELLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1672 QRDLESEKRLR-KDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaaavkarkAMEVEMEDLHLQIDDI 1750
Cdd:PRK04863 511 LAEQLQQLRMRlSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQE-------------ELEARLESLSESVSEA 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1751 AKAKTALEEQLSRLQREKNEIQSRLEE---DQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQAL 1827
Cdd:PRK04863 578 RERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQAL 657
|
....*....
gi 1239919865 1828 QSQVEFLEQ 1836
Cdd:PRK04863 658 DEEIERLSQ 666
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1288-1610 |
2.08e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.15 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1288 EEIQQLRSKL----EKVEkernELRLSNDRLETRISELTSELTDERNTGESASqlldaeaaerlraEKEMKELQTQYDAL 1363
Cdd:pfam00038 4 EQLQELNDRLasyiDKVR----FLEQQNKLLETKISELRQKKGAEPSRLYSLY-------------EKEIEDLRRQLDTL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1364 KKqmevmemevmearliraaeingevddddtggewrlkyERAMREVDFTKKRLQ-QEFEDKLEVEQQNKRQLERRLGDLQ 1442
Cdd:pfam00038 67 TV-------------------------------------ERARLQLELDNLRLAaEDFRQKYEDELNLRTSAENDLVGLR 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1443 ADIDESQRALQQLKKKCQRLTAEL------------------QDTKLHLEGQQVRNHELEKKQRrfdsELSQAHEE-AQR 1503
Cdd:pfam00038 110 KDLDEATLARVDLEAKIESLKEELaflkknheeevrelqaqvSDTQVNVEMDAARKLDLTSALA----EIRAQYEEiAAK 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1504 EKLQREKLQREK-DTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVK-----------KQL 1571
Cdd:pfam00038 186 NREEAEEWYQSKlEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEeryelqladyqELI 265
|
330 340 350
....*....|....*....|....*....|....*....
gi 1239919865 1572 RDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMR 1610
Cdd:pfam00038 266 SELEAELQETRQEMARQLREYQELLNVKLALDIEIATYR 304
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1440-1923 |
2.21e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 49.69 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1440 DLQADIDESQralqQLKKKCQRL---TAELQDTKLHLegqQVRNHELEKKQRRFDSELSQA--------HEEAQREKLQR 1508
Cdd:pfam05622 1 DLSEAQEEKD----ELAQRCHELdqqVSLLQEEKNSL---QQENKKLQERLDQLESGDDSGtpggkkylLLQKQLEQLQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1509 EKLQRE--KDTLLAEAFSLKQQLEE---KDMDIAGFTQKVVSLEAE---LQDISSQESKDEASLAKVKKQLRDLEakvkd 1580
Cdd:pfam05622 74 ENFRLEtaRDDYRIKCEELEKEVLElqhRNEELTSLAEEAQALKDEmdiLRESSDKVKKLEATVETYKKKLEDLG----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1581 qeeELDEQagtIQMLEqaklrlEMEMERMRQTHSKEVESRDEEVEEAR-QSCQKKLKQMEVQLEEEYEDKQKVLREKREL 1659
Cdd:pfam05622 149 ---DLRRQ---VKLLE------ERNAEYMQRTLQLEEELKKANALRGQlETYKRQVQELHGKLSEESKKADKLEFEYKKL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1660 ESKLTTLseqvsQRDLESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLeeseftcaaavkARKAMEVE 1739
Cdd:pfam05622 217 EEKLEAL-----QKEKERLIIERDTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNL------------AAEIMPAE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1740 medlhlqiddiakaktaLEEQLSRLQREKNEIQSRLEEDQEDmnelmkkhkaavaqasrdlaQMNDLQAQLEEANKEKQE 1819
Cdd:pfam05622 280 -----------------IREKLIRLQHENKMLRLGQEGSYRE--------------------RLTELQQLLEDANRRKNE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1820 LQEKLQALQSQVEFLEQsmvdkslvsrqeaKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTAA-ENREKE 1898
Cdd:pfam05622 323 LETQNRLANQRILELQQ-------------QVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKkEQIEEL 389
|
490 500
....*....|....*....|....*
gi 1239919865 1899 QNKRLQRQLRDTKEEMGELARKEAE 1923
Cdd:pfam05622 390 EPKQDSNLAQKIDELQEALRKKDED 414
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1711-1980 |
2.28e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.30 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1711 EIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHK 1790
Cdd:pfam19220 91 RLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1791 AAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFERT-QVKRL 1868
Cdd:pfam19220 171 LLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAeQAERERAEAQLEEAVEAHRAERAsLRMKL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1869 ESLASRLKENMEKLTEERDQ--RTAAENREKEQN--------KRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESL 1938
Cdd:pfam19220 251 EALTARAAATEQLLAEARNQlrDRDEAIRAAERRlkeasierDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEML 330
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 1939 EAANQSLQADLKLAFKRIGDLQAAIE---DEMESDE------NEDLITSLQ 1980
Cdd:pfam19220 331 TKALAAKDAALERAEERIASLSDRIAeltKRFEVERaaleqaNRRLKEELQ 381
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1715-1949 |
2.48e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.51 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1715 LKNQLEESEFTCAAAVKARKAMEVEMEDlhlQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVA 1794
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREK---EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1795 QASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSR--QEAKIRELETRLEFERTQVK 1866
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELermkerAKKAGAQRkeEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1867 RL--------------ESLASRLKENMEKLTeerdQRTAAENREKEQNKRLQRQLRDTKEEmgelarkeAEASRKKHE-L 1931
Cdd:pfam07888 189 SLskefqelrnslaqrDTQVLQLQDTITTLT----QKLTTAHRKEAENEALLEELRSLQER--------LNASERKVEgL 256
|
250
....*....|....*...
gi 1239919865 1932 EMDLESLEAANQSLQADL 1949
Cdd:pfam07888 257 GEELSSMAAQRDRTQAEL 274
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1483-1645 |
2.98e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1483 LEKKQRRFDSELSQAHEEAQREKlqREKLQREKDtllaEAFSLKQQLEEkdmDIAGFTQKVVSLEAELQDISSQESKDEA 1562
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIK--KEALLEAKE----EIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1563 SLAKVKKQLRDLEAKVKDQEEELDEQAGTIQ-MLEQAKLRLE----MEMERMRQTHSKEVEsrdeevEEARQSCQKKLKQ 1637
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEeLIEEQLQELErisgLTAEEAKEILLEKVE------EEARHEAAVLIKE 177
|
....*...
gi 1239919865 1638 MEVQLEEE 1645
Cdd:PRK12704 178 IEEEAKEE 185
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1595-1885 |
3.13e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.38 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1595 LEQAKLRLEMEMERMRQTHSKEVESRDE----EVEEARQ---SCQKKLKQMEVQLE---EEYED-KQKV---LREKRELE 1660
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEPSRLYSlyekEIEDLRRqldTLTVERARLQLELDnlrLAAEDfRQKYedeLNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1661 SKLTTLseqvsQRDLESEKRLRKDL-KRTKALLADaqimLDHLKNNapSKREIAQLKNQLEESEFTCAAAVKARKAMEVE 1739
Cdd:pfam00038 103 NDLVGL-----RKDLDEATLARVDLeAKIESLKEE----LAFLKKN--HEEEVRELQAQVSDTQVNVEMDAARKLDLTSA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1740 MEDLHLQIDDIAkaktaleeQLSRLQREKNeIQSRLEEDQEdmnelmkkhkaavaQASRDLAQMNDLQAQLEEANKEKQE 1819
Cdd:pfam00038 172 LAEIRAQYEEIA--------AKNREEAEEW-YQSKLEELQQ--------------AAARNGDALRSAKEEITELRRTIQS 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1820 LQEKLQALQSQVEFLeqsmvdkslvsrqEAKIRELETRLEFERTQVK----RLESLASRLKENMEKLTEE 1885
Cdd:pfam00038 229 LEIELQSLKKQKASL-------------ERQLAETEERYELQLADYQelisELEAELQETRQEMARQLRE 285
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1415-1595 |
3.22e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1415 RLQQEFEDKLEVEQQNKRQLER---RLGDLQADIDESQRALQQLKKKCQRLTAELQ----DTKLHLEG-------QQVRN 1480
Cdd:PHA02562 217 RKQNKYDELVEEAKTIKAEIEEltdELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfqkVIKMYEKGgvcptctQQISE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1481 HE--LEKKQRRFdSELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQES 1558
Cdd:PHA02562 297 GPdrITKIKDKL-KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
170 180 190
....*....|....*....|....*....|....*..
gi 1239919865 1559 KDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQML 1595
Cdd:PHA02562 376 DNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLL 412
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1615-1830 |
3.33e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1615 KEVESRDEEVEEARQSCQKKLKQMEVQLE---EEYEDKQKVLREKRE----LESKLTTLSEQVSQRDLESEKRLRkDLKR 1687
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEelnEEYNELQAELEALQAeidkLQAEIAEAEAEIEERREELGERAR-ALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1688 TKALLADAQIML------DHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQL 1761
Cdd:COG3883 98 SGGSVSYLDVLLgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1762 SRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQ 1830
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| PDZ2_DLG5-like |
cd06765 |
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
270-308 |
3.70e-05 |
|
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PSZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467246 [Multi-domain] Cd Length: 77 Bit Score: 43.87 E-value: 3.70e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1239919865 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06765 35 LTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLM 73
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1275-1598 |
3.71e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.19 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLSEEQIRSKDEEIQQLRSKLEKVEKERNELRLS----NDRLETRISELTSELTDE-RNTGEsasQLLDAEAAERLRA 1349
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEklgeNAESSKRLNENANNLIKQfENTKE---KIAEYTKSIDIKK 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1350 EKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDTGGEwrlkyeramrevdftkkRLQQEFEDKleVEQQ 1429
Cdd:COG5185 310 ATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLE-----------------AIKEEIENI--VGEV 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1430 NKRQLERRLGDLQADIDESQRAL----QQLKKKCQRLTAELQDTKLHLEGQqvrnheLEKKQRRFDSELSQaHEEAQREK 1505
Cdd:COG5185 371 ELSKSSEELDSFKDTIESTKESLdeipQNQRGYAQEILATLEDTLKAADRQ------IEELQRQIEQATSS-NEEVSKLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1506 LQREKlQREKDTLLAEAFSLKQQLEEKDMDIAgftqkvvSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEE-- 1583
Cdd:COG5185 444 NELIS-ELNKVMREADEESQSRLEEAYDEINR-------SVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEgv 515
|
330
....*....|....*..
gi 1239919865 1584 --ELDEQAGTIQMLEQA 1598
Cdd:COG5185 516 rsKLDQVAESLKDFMRA 532
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1614-1882 |
4.10e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1614 SKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQV----SQRD--LESEKRLRKDLKR 1687
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAqelrEKRDelNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1688 TKALLADAQIMLDHLKNNAP----SKREIAQLKNQLEESEFTCAAAVKARkamEVEMEdLHLQIDDIAKAKTALEEQLsR 1763
Cdd:COG1340 83 LNEKLNELREELDELRKELAelnkAGGSIDKLRKEIERLEWRQQTEVLSP---EEEKE-LVEKIKELEKELEKAKKAL-E 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1764 LQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKsl 1843
Cdd:COG1340 158 KNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL-- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1239919865 1844 vSRQEAKIRELETRLEFERTQVKR---LESLASRLKENMEKL 1882
Cdd:COG1340 236 -QKELRELRKELKKLRKKQRALKRekeKEELEEKAEEIFEKL 276
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1486-1893 |
4.14e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.13 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1486 KQRRFDSElsqaheEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMD-IAGFTQKVVSLEAELQDISSQesKDEASL 1564
Cdd:PLN02939 38 RRRGFSSQ------QKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRtVMELPQKSTSSDDDHNRASMQ--RDEAIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1565 AKVKKQLRdleaKVKDQEEELDEQAGT-IQMLEQAklrlEMEMERMRQTHSKEVESRDEEVEEaRQSCQKKLKQMEVQLE 1643
Cdd:PLN02939 110 AIDNEQQT----NSKDGEQLSDFQLEDlVGMIQNA----EKNILLLNQARLQALEDLEKILTE-KEALQGKINILEMRLS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1644 EEYEDKQKVLREKRELEskltTLSEQVSQRDLESEKRLRKDLKRTKALLADaqimLDHLK-NNAPSKREIAQLKNQL--- 1719
Cdd:PLN02939 181 ETDARIKLAAQEKIHVE----ILEEQLEKLRNELLIRGATEGLCVHSLSKE----LDVLKeENMLLKDDIQFLKAELiev 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1720 EESEFTCAAAVKARKAMEVEMEDLHLQIddiakakTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKH---KAAVAQA 1796
Cdd:PLN02939 253 AETEERVFKLEKERSLLDASLRELESKF-------IVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQvekAALVLDQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1797 SRDLA-QMNDLQAQLEEANKEKQELqEKLQALQSQVefleqsmvdKSLVSRQEAKIRELETrlefertQVKRLESLASRL 1875
Cdd:PLN02939 326 NQDLRdKVDKLEASLKEANVSKFSS-YKVELLQQKL---------KLLEERLQASDHEIHS-------YIQLYQESIKEF 388
|
410
....*....|....*...
gi 1239919865 1876 KENMEKLTEERDQRTAAE 1893
Cdd:PLN02939 389 QDTLSKLKEESKKRSLEH 406
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1287-1467 |
5.15e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1287 DEEIQQLRSKLEKVEKERNELRLSNDrletriseltseLTDERNTGESASQLLDAEAAERLRAEKEMKELQTQYDALKKQ 1366
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNG------------LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1367 MEVMEMEVMEAR--------LIRAAEINGEVDdddtggEWRLKY-------ERAMREVDFTKKRLQQEFEDKLEVEQQNK 1431
Cdd:COG3206 249 LGSGPDALPELLqspviqqlRAQLAELEAELA------ELSARYtpnhpdvIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190
....*....|....*....|....*....|....*.
gi 1239919865 1432 RQLERRLGDLQADIDESQRALQQLKKKCQRLtAELQ 1467
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAEL-RRLE 357
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1775-1965 |
5.38e-05 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 46.91 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1775 LEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEfleqsmvDKSLVSRQEAKIREL 1854
Cdd:pfam12795 11 DEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAE-------AAPKEILASLSLEEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1855 ETRLEFERTQvkrLESLASRLKENMEKLTEERDQRTAAENREKEQNKRLQR------QLRDTKEEMGELARKEAEASRKK 1928
Cdd:pfam12795 84 EQRLLQTSAQ---LQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQirnrlnGPAPPGEPLSEAQRWALQAELAA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1239919865 1929 HELEMDLESLEAANQSLQADL-----KLAFKRIGDLQAAIED 1965
Cdd:pfam12795 161 LKAQIDMLEQELLSNNNRQDLlkarrDLLTLRIQRLEQQLQA 202
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1287-1466 |
5.54e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1287 DEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAAERLRAEKEMKELQT--QYDALK 1364
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1365 KQmevmemEVMEARLIRAAeingevddddtggewrlkyERAMREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQAD 1444
Cdd:COG1579 96 KE------IESLKRRISDL-------------------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|..
gi 1239919865 1445 IDESQRALQQLKKKCQRLTAEL 1466
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1752-2003 |
6.44e-05 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 48.40 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1752 KAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDL-AQMNDLQA-----QLEEANKEKQ--ELQEK 1823
Cdd:pfam15818 21 EAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQLqMKMCALEEekgkyQLATEIKEKEieGLKET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1824 LQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFERTQVKRLE----SLASR---LKENMEKLTEERDQRTAAENRE 1896
Cdd:pfam15818 101 LKALQVSKYSLQKK------VSEMEQKLQLHLLAKEDHHKQLNEIEkyyaTITGQfglVKENHGKLEQNVQEAIQLNKRL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1897 KEQNKRLQRQLRDTKEEM----GELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFkrigDLQAAIEDEME--SD 1970
Cdd:pfam15818 175 SALNKKQESEICSLKKELkkvtSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMEL----ELNKKINEEIThiQE 250
|
250 260 270
....*....|....*....|....*....|...
gi 1239919865 1971 ENEDLITSLQDMVTKYQKrknKPEGDSDVDSEL 2003
Cdd:pfam15818 251 EKQDIIISFQHMQQLLQQ---QTQANTEMEAEL 280
|
|
| PDZ1_harmonin |
cd06737 |
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ... |
218-310 |
6.88e-05 |
|
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467219 [Multi-domain] Cd Length: 85 Bit Score: 43.40 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 218 LRELELQRRPTGDFGFSLRRttmldrGPEGQVYRRVVHFAEPG-AGTKdlalGLVPGDRLVEINGHNVESKSRDEIVEMI 296
Cdd:cd06737 2 LRLVRLDRRGPESLGFSVRG------GLEHGCGLFVSHVSPGSqADNK----GLRVGDEIVRINGYSISQCTHEEVINLI 71
|
90
....*....|....
gi 1239919865 297 RQSgDSVRLKVQPI 310
Cdd:cd06737 72 KTK-KTVSLKVRHV 84
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
1756-1950 |
6.97e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 46.05 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1756 ALEEQLSRLQREKNEIQSRLEE---DQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEankEKQELQEKLQALQSQVe 1832
Cdd:pfam15619 8 ARLHKIKELQNELAELQSKLEElrkENRLLKRLQKRQEKALGKYEGTESELPQLIARHNE---EVRVLRERLRRLQEKE- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1833 fleqsmvdkslvSRQEAKIRELETRLEFERTQVKRLESLAS--RLKENmEKLTEERDQRTAAENREKEQNKRLQRQLRdt 1910
Cdd:pfam15619 84 ------------RDLERKLKEKEAELLRLRDQLKRLEKLSEdkNLAER-EELQKKLEQLEAKLEDKDEKIQDLERKLE-- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1239919865 1911 kEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLK 1950
Cdd:pfam15619 149 -LENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLK 187
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1672-1968 |
7.10e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.61 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1672 QRDLESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE-----MEDLHLQ 1746
Cdd:pfam13868 2 RENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEerkryRQELEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1747 IDDIAKAKtalEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQE-KLQ 1825
Cdd:pfam13868 82 IEEREQKR---QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDeRIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1826 ALQSQVEFLEQsmvdkslvsRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTAAEN---REKEQNKR 1902
Cdd:pfam13868 159 EYLKEKAEREE---------EREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKerqKEREEAEK 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 1903 LQRQLRDTKEE-----MGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEME 1968
Cdd:pfam13868 230 KARQRQELQQAreeqiELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIE 300
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1752-2085 |
7.80e-05 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 48.50 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1752 KAKTALEEQLSRL--------QREKNE-IQSRLEEDQEDMNELMKKHKAAVAQASRD-------------LAQMNDLQAQ 1809
Cdd:PTZ00108 1031 AKKKDLVKELKKLgyvrfkdiIKKKSEkITAEEEEGAEEDDEADDEDDEEELGAAVSydyllsmpiwsltKEKVEKLNAE 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1810 LEEANKEKQELQ---------EKLQALQSQVEFLEQsmvdkslvsrqeakiRELETRLEFERTQVKRLESlASRLKENME 1880
Cdd:PTZ00108 1111 LEKKEKELEKLKnttpkdmwlEDLDKFEEALEEQEE---------------VEEKEIAKEQRLKSKTKGK-ASKLRKPKL 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1881 KLTEERDQRTAAENreKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHElemdlesleaANQSLQADLKLAFKRIGDLQ 1960
Cdd:PTZ00108 1175 KKKEKKKKKSSADK--SKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSG----------SDQEDDEEQKTKPKKSSVKR 1242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1961 AAIEDEMESDENEDLITSLQDMVTKYQKRKNKPE---GDSDVDSELEDRVDGVKSWLSKNKGPSKAASDDgSLKSSRTAL 2037
Cdd:PTZ00108 1243 LKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKrvsAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKK-RLEGSLAAL 1321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 2038 NTSGKEGKG----------VEERPASALSSLSYRKRLTLKDSIGGTGDEDSLFTTLSE 2085
Cdd:PTZ00108 1322 KKKKKSEKKtarkkksktrVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDE 1379
|
|
| PDZ_MPP-like |
cd06726 |
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ... |
273-309 |
7.84e-05 |
|
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1-7 (also known as MAGUK p55 subfamily members 1-7), and related domains. MPPs comprise a subfamily of a larger group of multidomain proteins, namely, membrane-associated guanylate kinases (MAGUKs). MPPs form diverse protein complexes at the cell membranes, which are involved in a wide range of cellular processes, including establishing proper cell structure, polarity and cell adhesion. MPPs have only one PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467208 [Multi-domain] Cd Length: 80 Bit Score: 43.02 E-value: 7.84e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1239919865 273 GDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06726 44 GDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKLIP 80
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1286-1591 |
8.05e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.03 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1286 KDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNTGESASQLLDAEAA---ERLRAEKEMKELQTQYDA 1362
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEqelEESKRETETGIQNLTAEI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1363 LKKQMEVMEMEVMearlIRAA--EINGEVDDDDTGGEWR--LKYERAMREVDFTKKRLQQEFE-DKLEVEQQNKRQLERR 1437
Cdd:COG5185 346 EQGQESLTENLEA----IKEEieNIVGEVELSKSSEELDsfKDTIESTKESLDEIPQNQRGYAqEILATLEDTLKAADRQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1438 LGDLQADIDESQRALQQLKKKCQRLTAELQdtKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREklqREKLQREKDT 1517
Cdd:COG5185 422 IEELQRQIEQATSSNEEVSKLLNELISELN--KVMREADEESQSRLEEAYDEINRSVRSKKEDLNEE---LTQIESRVST 496
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 1518 LLAEAFSLKQQLEEKdmdIAGFTQKVVSLEAELQDiSSQESKDEASLAKVKKQlRDLEAKvKDQEEELDEQAGT 1591
Cdd:COG5185 497 LKATLEKLRAKLERQ---LEGVRSKLDQVAESLKD-FMRARGYAHILALENLI-PASELI-QASNAKTDGQAAN 564
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1755-1929 |
8.21e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.06 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1755 TALEEQLSRLQREKN----EIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQ 1830
Cdd:pfam09787 43 TALTLELEELRQERDllreEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1831 VEFLEQSMVdKSLVSRQEaKIRELETRLEFERTQV--KRLESLA-SRLKENMEKLTEERDQR-TAAENREKEQNKrLQRQ 1906
Cdd:pfam09787 123 LRYLEEELR-RSKATLQS-RIKDREAEIEKLRNQLtsKSQSSSSqSELENRLHQLTETLIQKqTMLEALSTEKNS-LVLQ 199
|
170 180
....*....|....*....|...
gi 1239919865 1907 LrdtkeEMGELARKEAEASRKKH 1929
Cdd:pfam09787 200 L-----ERMEQQIKELQGEGSNG 217
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1844-2011 |
8.33e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1844 VSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTE-----ERDQRTAAENREKE------QNKRLQRQLRDTKE 1912
Cdd:TIGR02168 167 ISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERqaekaERYKELKAELRELElallvlRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1913 EMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED-----EMESDENEDLITSLQDMVTKYQ 1987
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqqkQILRERLANLERQLEELEAQLE 326
|
170 180
....*....|....*....|....
gi 1239919865 1988 KRKNKPEGDSDVDSELEDRVDGVK 2011
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELK 350
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1738-1869 |
8.36e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.35 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1738 VEMEDLHLQIDdIAKAKTALEEQLSRLQREKNEIQSRLEEDQedmnelmKKHKAAVAQASRDLAQ-----MNDL------ 1806
Cdd:COG1566 74 ARLDPTDLQAA-LAQAEAQLAAAEAQLARLEAELGAEAEIAA-------AEAQLAAAQAQLDLAQrelerYQALykkgav 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239919865 1807 -QAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLE 1869
Cdd:COG1566 146 sQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| PDZ_6 |
pfam17820 |
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins. |
269-308 |
8.58e-05 |
|
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
Pssm-ID: 436067 [Multi-domain] Cd Length: 54 Bit Score: 42.13 E-value: 8.58e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1239919865 269 GLVPGDRLVEINGHNVESKsrDEIVEMIRQSGDS-VRLKVQ 308
Cdd:pfam17820 15 GLRVGDVILAVNGKPVRSL--EDVARLLQGSAGEsVTLTVR 53
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1649-1974 |
8.63e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.00 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1649 KQKVLREKRELESKLTTL-SEQVSQ----RDLESEKRLRKDLKrtkaLLADAQIMLDHLKNNAPSKREIAQLKNQLEESE 1723
Cdd:PRK05771 8 KVLIVTLKSYKDEVLEALhELGVVHiedlKEELSNERLRKLRS----LLTKLSEALDKLRSYLPKLNPLREEKKKVSVKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1724 FTCAAAVKARKAMEVEMEdlhlqIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAqasrdlaqm 1803
Cdd:PRK05771 84 LEELIKDVEEELEKIEKE-----IKELEEEISELENEIKELEQEIERLEPWGNFDLDLSLLLGFKYVSVFV--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1804 ndlqAQLEEANKEKQELQEKlqalQSQVEFLEQSMVDKSLV----SRQEAKIRELETRLEFERTQVKRLESLASRLKENM 1879
Cdd:PRK05771 150 ----GTVPEDKLEELKLESD----VENVEYISTDKGYVYVVvvvlKELSDEVEEELKKLGFERLELEEEGTPSELIREIK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1880 EKLTEerdqrtaaenrekeqnkrLQRQLRDTKEEMGELARKEAEASRKKHE-LEMDLESLEAANQSLQADLKLAF----- 1953
Cdd:PRK05771 222 EELEE------------------IEKERESLLEELKELAKKYLEELLALYEyLEIELERAEALSKFLKTDKTFAIegwvp 283
|
330 340 350
....*....|....*....|....*....|.
gi 1239919865 1954 -KRIGDLQAAIED---------EMESDENED 1974
Cdd:PRK05771 284 eDRVKKLKELIDKatggsayveFVEPDEEEE 314
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1728-1919 |
8.97e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.97 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1728 AAVKARKAMEVEMEDLHlqiDDIAKAKTALEEQLSRLQREKNeiqsRLEEDQEDMNELMKKHKAAVAQASRDLA------ 1801
Cdd:COG1842 20 KAEDPEKMLDQAIRDME---EDLVEARQALAQVIANQKRLER----QLEELEAEAEKWEEKARLALEKGREDLArealer 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1802 ------QMNDLQAQLEEANKEKQELQEKLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFERTQVKRLESLAS-R 1874
Cdd:COG1842 93 kaeleaQAEALEAQLAQLEEQVEKLKEALRQLESKLE-------------ELKAKKDTLKARAKAAKAQEKVNEALSGiD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1239919865 1875 LKENMEKLT--EERDQRTAAEN---REKEQNKRLQRQLRDTKEEMG---ELAR 1919
Cdd:COG1842 160 SDDATSALErmEEKIEEMEARAeaaAELAAGDSLDDELAELEADSEvedELAA 212
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
1783-1933 |
9.59e-05 |
|
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.
Pssm-ID: 464990 [Multi-domain] Cd Length: 181 Bit Score: 45.37 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1783 NELMKKHKAAVAQASRDLAQMNDLQAQLEEankEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQE---AKIRELETRLE 1859
Cdd:pfam16043 6 AELLDQLQALILDLQEELEKLSETTSELSE---RLQQRQKHLEALYQQIEKLEKVKADKEVVEEELdekADKEALASKVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1860 FERTQVKrLESLASRLKENMEKLTE-ERDQRTAAENREKEQNKRLQRQ----LRDTKEE-MGELARKEAEASRKKHELEM 1933
Cdd:pfam16043 83 RDQFDET-LEELNQMLQELLDKLEGqEDAWKKALETLSEELDTKLDRLeldpLKELLERrIKALQKLLQEGSEELDEAEA 161
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1792-1925 |
9.66e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1792 AVAQASRDLAQMNDLQAQLEEANKEKQ-ELQEKL--QALQSQVEFLEQsmvdkslVSRQEAKIRELEtrlefertqvKRL 1868
Cdd:PRK11281 27 ARAASNGDLPTEADVQAQLDALNKQKLlEAEDKLvqQDLEQTLALLDK-------IDRQKEETEQLK----------QQL 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1869 ESLASRLKENMEKLT--EERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARKEAEAS 1925
Cdd:PRK11281 90 AQAPAKLRQAQAELEalKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYN 148
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1641-1853 |
1.04e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 45.83 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1641 QLEEEYEDKQKVLREK-RELESKLTTLSEQVSQ---RDLESEKRLRKDLKRTKALLADAQIMLDhlKNNAPSKREIAQLK 1716
Cdd:pfam04012 15 EGLDKAEDPEKMLEQAiRDMQSELVKARQALAQtiaRQKQLERRLEQQTEQAKKLEEKAQAALT--KGNEELAREALAEK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1717 NQLEESEftcaaavkarKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEedQEDMNELMKKH--KAAVA 1794
Cdd:pfam04012 93 KSLEKQA----------EALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLK--AAKAQEAVQTSlgSLSTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1795 QASRDLAQMNDLQAQLEEANkekqELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRE 1853
Cdd:pfam04012 161 SATDSFERIEEKIEEREARA----DAAAELASAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1339-1605 |
1.14e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 47.38 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1339 LDAEAAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARliraaEINGEV-----------DDDDTGGEWRLKYERAMR 1407
Cdd:pfam05622 199 LSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLR-----ETNEELrcaqlqqaelsQADALLSPSSDPGDNLAA 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1408 EV---DFTKKRLQQEFEDKLEVEQQnKRQLERRLGDLQADIDESQRALQ----QLKKKCQR---LTAELQDTKLHLEGQQ 1477
Cdd:pfam05622 274 EImpaEIREKLIRLQHENKMLRLGQ-EGSYRERLTELQQLLEDANRRKNeletQNRLANQRileLQQQVEELQKALQEQG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1478 VRNHELEKKQRRFDS---ELSQAHEEAQREKLQREKLQREKDTLLAE-AFSLKQQLEEKDMDIAGFTQK----------- 1542
Cdd:pfam05622 353 SKAEDSSLLKQKLEEhleKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAMEERykkyvekaksv 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239919865 1543 VVSLEAELQDISSQEskdeasLAKVKKQLRDLEAKVKDQEEEldeqagtiqmLEQAKLRLEME 1605
Cdd:pfam05622 433 IKTLDPKQNPASPPE------IQALKNQLLEKDKKIEHLERD----------FEKSKLQREQE 479
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1446-1823 |
1.17e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 46.73 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1446 DESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE-EAQREKLQREKLQREKdtllaeafs 1524
Cdd:pfam15905 24 EKSQRFRKQKAAESQPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKElEKEIRALVQERGEQDK--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1525 LKQQLEEKdmdiagftqkVVSLEAELQDISSQESKDEASLAKVKKQLRDLeAKVKDQEEELDEQAGTIQMLEQAKLRLeM 1604
Cdd:pfam15905 95 RLQALEEE----------LEKVEAKLNAAVREKTSLSASVASLEKQLLEL-TRVNELLKAKFSEDGTQKKMSSLSMEL-M 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1605 EMERMRQTHSKEVESRDEEVEEARQSCQKKLK--QMEV-QLEEEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKrL 1681
Cdd:pfam15905 163 KLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEhsKGKVaQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEK-Y 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1682 RKDLKRTKALLADAQimldhlknnapskREIAQLKNQLEESEftcaaavkarkamevemEDLHLQIDDiakaktaLEEQL 1761
Cdd:pfam15905 242 KLDIAQLEELLKEKN-------------DEIESLKQSLEEKE-----------------QELSKQIKD-------LNEKC 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239919865 1762 SRLQREKNEIQSRLEEDQEDMNelmkkhkaavaqasrdlAQMNDLQAQLEEANKEKQELQEK 1823
Cdd:pfam15905 285 KLLESEKEELLREYEEKEQTLN-----------------AELEELKEKLTLEEQEHQKLQQK 329
|
|
| CtpA |
COG0793 |
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
269-309 |
1.18e-04 |
|
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440556 [Multi-domain] Cd Length: 341 Bit Score: 46.79 E-value: 1.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1239919865 269 GLVPGDRLVEINGHNVESKSRDEIVEMIR-QSGDSVRLKVQP 309
Cdd:COG0793 88 GIKPGDIILAIDGKSVAGLTLDDAVKLLRgKAGTKVTLTIKR 129
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1707-1907 |
1.32e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1707 PSKREIaqlKNQLEeseftcaaAVKARKAMEVE-------MEDLHLQIDDIAKAK---TALEEQLSRLQREkneiqsrLE 1776
Cdd:PRK11281 36 PTEADV---QAQLD--------ALNKQKLLEAEdklvqqdLEQTLALLDKIDRQKeetEQLKQQLAQAPAK-------LR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1777 EDQEDMNELMKKHKAAVAQASRDLAqMNDLQAQLEEANKEKQELQEKLQALQSQvefleqsmvdksLVSRQeakireleT 1856
Cdd:PRK11281 98 QAQAELEALKDDNDEETRETLSTLS-LRQLESRLAQTLDQLQNAQNDLAEYNSQ------------LVSLQ--------T 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1857 RLefERTQ------VKRLESLASRLK---ENMEKLTEERDQRTAAENREKEQNKRLQRQL 1907
Cdd:PRK11281 157 QP--ERAQaalyanSQRLQQIRNLLKggkVGGKALRPSQRVLLQAEQALLNAQNDLQRKS 214
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1710-1939 |
1.41e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 45.79 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1710 REIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKH 1789
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1790 KAAVAQASRDLAQMNDLQAQL-------EEANKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFER 1862
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLkeakeiaEEADRKYEEVARKLVVVEGDLERAEER------AELAESKIVELEEELKVVG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239919865 1863 TQVKRLESLAsrlkenmekltEERDQRtaaENREKEQNKRLQRQLRDTKeemgelARKEaEASRKKHELEMDLESLE 1939
Cdd:pfam00261 155 NNLKSLEASE-----------EKASER---EDKYEEQIRFLTEKLKEAE------TRAE-FAERSVQKLEKEVDRLE 210
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1751-2107 |
1.53e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 47.35 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1751 AKAKTALEEQLSR-LQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASR-DLAQMNDLQAQLEEANKEKQELQEKLQALQ 1828
Cdd:PTZ00108 994 KKRKEYLLGKLEReLARLSNKVRFIKHVINGELVITNAKKKDLVKELKKlGYVRFKDIIKKKSEKITAEEEEGAEEDDEA 1073
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1829 SQVEFLEQSMVDKS--------LVSRQEAKIRELETRLEFERTQVKRLESLA---------SRLKENMEKlTEERDQRTA 1891
Cdd:PTZ00108 1074 DDEDDEEELGAAVSydyllsmpIWSLTKEKVEKLNAELEKKEKELEKLKNTTpkdmwledlDKFEEALEE-QEEVEEKEI 1152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1892 AENREKEQNKRL-QRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESD 1970
Cdd:PTZ00108 1153 AKEQRLKSKTKGkASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQK 1232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1971 E-----NEDLITSLQDMVTKYQKRKNKPEGDSDVDSELEDRVDGVKSWLSKNKGPSKAASDDGSLKSSRTALNTSGKEGK 2045
Cdd:PTZ00108 1233 TkpkksSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKK 1312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239919865 2046 GVEERPASALSSLSYRKRLTLKDSIggtgdEDSLFTTLSERAASPERPPRKTCPGPRDELDE 2107
Cdd:PTZ00108 1313 RLEGSLAALKKKKKSEKKTARKKKS-----KTRVKQASASQSSRLLRRPRKKKSDSSSEDDD 1369
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1709-1927 |
1.58e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 46.61 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1709 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIddiakakTALEEQLSRLQREKNEiQSRLEEDQEDMNELMKK 1788
Cdd:PRK11637 67 QQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQI-------DELNASIAKLEQQQAA-QERLLAAQLDAAFRQGE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1789 HKAAVAQASRDLAQMND-LQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDK-----SLVSRQEAKIRELE-TRLEFE 1861
Cdd:PRK11637 139 HTGLQLILSGEESQRGErILAYFGYLNQARQETIAELKQTREELAAQKAELEEKqsqqkTLLYEQQAQQQKLEqARNERK 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1862 RTqvkrLESLASRLKENMEKLTEERDQRTAAENR----EKEQNKRLQRQLRdtkeEMGELARKEAEASRK 1927
Cdd:PRK11637 219 KT----LTGLESSLQKDQQQLSELRANESRLRDSiaraEREAKARAEREAR----EAARVRDKQKQAKRK 280
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1634-1928 |
1.77e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1634 KLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQRdleSEKRlRKDLKRTKALLADAQIMLDHLKNNAPskrEIA 1713
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKEL---AEKR-DELNAQVKELREEAQELREKRDELNE---KVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1714 QLKNQLEEseftcaAAVKARKAMEvEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRlEEDQEDMNELMKKhkaav 1793
Cdd:COG1340 75 ELKEERDE------LNEKLNELRE-ELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTE-VLSPEEEKELVEK----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1794 aqaSRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKS-LVSRQEAKIRELETRLEFERTQVKRLESLA 1872
Cdd:COG1340 142 ---IKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAeEAQELHEEMIELYKEADELRKEADELHKEI 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1239919865 1873 SRLKENMEKLTEERDQRTAAENREKEQNKRLQRQLRDT-KEEMGELARKEAEASRKK 1928
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALkREKEKEELEEKAEEIFEK 275
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1271-1365 |
1.79e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1271 RPLIEVQLSEEQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERntgesasqlldAEAAERLRAE 1350
Cdd:COG2433 396 EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR-----------SEERREIRKD 464
|
90
....*....|....*
gi 1239919865 1351 KEMKELQTQYDALKK 1365
Cdd:COG2433 465 REISRLDREIERLER 479
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1275-1585 |
1.83e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLSEEQIRskdEEIQQLRSKLEKVEKERNELRlsndrletrisELTSELTDERNTGESASQLLDAEAAErLRAEK--- 1351
Cdd:COG1340 5 ELSSSLEELE---EKIEELREEIEELKEKRDELN-----------EELKELAEKRDELNAQVKELREEAQE-LREKRdel 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1352 --EMKELQTQYDALKKQmevmemevmearlirAAEINGEVDDddtggewrLKYERAMREVD-FTKKRLQQEFEdKLEVEQ 1428
Cdd:COG1340 70 neKVKELKEERDELNEK---------------LNELREELDE--------LRKELAELNKAgGSIDKLRKEIE-RLEWRQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1429 QNK-------RQLERRLGDLQADIDESQRALQQlKKKCQRLTAELQdtklhlegqqvrnhELEKKQRRFDSELSQAHEEA 1501
Cdd:COG1340 126 QTEvlspeeeKELVEKIKELEKELEKAKKALEK-NEKLKELRAELK--------------ELRKEAEEIHKKIKELAEEA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1502 QREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQES--KDEASLAKVKKQLRDLEAKVK 1579
Cdd:COG1340 191 QELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKklRKKQRALKREKEKEELEEKAE 270
|
....*.
gi 1239919865 1580 DQEEEL 1585
Cdd:COG1340 271 EIFEKL 276
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1811-1926 |
2.08e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1811 EEANKEKQELQEKLQALQSQVEFLEqsmvdkslvsrqeAKIRELETRLEFERTQVKRLESLASRLKENMEKltEERDQRt 1890
Cdd:COG2433 402 EHEERELTEEEEEIRRLEEQVERLE-------------AEVEELEAELEEKDERIERLERELSEARSEERR--EIRKDR- 465
|
90 100 110
....*....|....*....|....*....|....*.
gi 1239919865 1891 AAENREKEqNKRLQRQLRDTKEEMGELARKEAEASR 1926
Cdd:COG2433 466 EISRLDRE-IERLERELEEERERIEELKRKLERLKE 500
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1499-1929 |
2.14e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1499 EEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDmdiagfTQKVVSLEAELQDiSSQESKDEaslakvkkqlrdlEAKV 1578
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPN------EHNSYEEDSELKP-SGQGGLDE-------------EEAF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1579 KDQEEELDEQagTIQMLEQAKLRlEMEMERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDkQKVLREKRE 1658
Cdd:pfam02029 65 LDRTAKREER--RQKRLQEALER-QKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE-ETEIREKEY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1659 LESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQIMLDhlknnapskreiaqlknqleeseftcaaavKARKAMEV 1738
Cdd:pfam02029 141 QENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDE------------------------------KIKKEKKV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1739 EMEDLHLqiddiakaktaleeqlsrLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEeANKEKQ 1818
Cdd:pfam02029 191 KYESKVF------------------LDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLE-AEQKLE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1819 ELQEKLQALQSQvEFleqsmvdkslvsrQEAKIRELETRLEfertqvkrLESLASRLKENMEKLTEERDQRTAAenrEKE 1898
Cdd:pfam02029 252 ELRRRRQEKESE-EF-------------EKLRQKQQEAELE--------LEELKKKREERRKLLEEEEQRRKQE---EAE 306
|
410 420 430
....*....|....*....|....*....|.
gi 1239919865 1899 QNKRLQRQLRDTKEEMgELARKEAEASRKKH 1929
Cdd:pfam02029 307 RKLREEEEKRRMKEEI-ERRRAEAAEKRQKL 336
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1811-1933 |
2.16e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 42.98 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1811 EEANKEKQELQEKLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKL------TE 1884
Cdd:pfam20492 2 EEAEREKQELEERLKQYEEETKKAQEEL------EESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLeesaemEA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1239919865 1885 ERDQRTAAENREKEQNKRLQRQlrdtkeemgELARKEAEASRKKHELEM 1933
Cdd:pfam20492 76 EEKEQLEAELAEAQEEIARLEE---------EVERKEEEARRLQEELEE 115
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1410-1587 |
2.24e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.96 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1410 DFTKKRLQ------QEFEDKLEVEQQN----KRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKLHLEgqqvr 1479
Cdd:pfam15905 148 DGTQKKMSslsmelMKLRNKLEAKMKEvmakQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETE----- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1480 nhelekKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMD----IAGFTQKVVSLEAELQDISS 1555
Cdd:pfam15905 223 ------KLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQElskqIKDLNEKCKLLESEKEELLR 296
|
170 180 190
....*....|....*....|....*....|..
gi 1239919865 1556 QESKDEASLakvKKQLRDLEAKVKDQEEELDE 1587
Cdd:pfam15905 297 EYEEKEQTL---NAELEELKEKLTLEEQEHQK 325
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1671-1942 |
2.41e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.98 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1671 SQRDLESEKRLRKDLKRTKALLADAQImldhlknnapSKREIAQLKNQLEEseftcaAAVKARKAMEvemEDLHLQIDDI 1750
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDA----------SKQRAAAYQKALDD------APAELRELRQ---ELAALQAKAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1751 AKAKTALEEQ-LSRLQREKNEIQSRLEEDQEDMNELMKkhkaavaqasrdlaQMNDLQAQLEEANKEKQELQEKLQALQS 1829
Cdd:pfam12795 69 AAPKEILASLsLEELEQRLLQTSAQLQELQNQLAQLNS--------------QLIELQTRPERAQQQLSEARQRLQQIRN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1830 QvefLEQSMVDKSLVSrqEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTAaenrekeQNKRLQRQLRD 1909
Cdd:pfam12795 135 R---LNGPAPPGEPLS--EAQRWALQAELAALKAQIDMLEQELLSNNNRQDLLKARRDLLTL-------RIQRLEQQLQA 202
|
250 260 270
....*....|....*....|....*....|...
gi 1239919865 1910 TKEEMGELARKEAEASRKkhELEMDLESLEAAN 1942
Cdd:pfam12795 203 LQELLNEKRLQEAEQAVA--QTEQLAEEAAGDH 233
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1731-1882 |
2.42e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 45.82 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1731 KARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQasrdlAQMNDLQAQL 1810
Cdd:cd22656 114 EAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIAR-----KEIKDLQKEL 188
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239919865 1811 EEANKE-KQELQEKLQALQSQVEFLEQSMvdkslvsRQEAKIRELETRLEferTQVKRLESLASRLKENMEKL 1882
Cdd:cd22656 189 EKLNEEyAAKLKAKIDELKALIADDEAKL-------AAALRLIADLTAAD---TDLDNLLALIGPAIPALEKL 251
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1756-1962 |
2.48e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1756 ALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDlqaqleEANKEKQELQEKLQALQSQVEFLE 1835
Cdd:pfam12128 255 SAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRD------ELNGELSAADAAVAKDRSELEALE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1836 -----------------QSMVD--KSLVSRQEAKIRELETRL-----EFERTQVKRLESLA---SRLKENMEKLTEERD- 1887
Cdd:pfam12128 329 dqhgafldadietaaadQEQLPswQSELENLEERLKALTGKHqdvtaKYNRRRSKIKEQNNrdiAGIKDKLAKIREARDr 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1888 QRTAAEN----REKEQNKRLQRQLRDTKEEMGELARKEAEASRK------KHELEMDLESLEAANQSLQADLKLAFKRIG 1957
Cdd:pfam12128 409 QLAVAEDdlqaLESELREQLEAGKLEFNEEEYRLKSRLGELKLRlnqataTPELLLQLENFDERIERAREEQEAANAEVE 488
|
....*
gi 1239919865 1958 DLQAA 1962
Cdd:pfam12128 489 RLQSE 493
|
|
| PDZ3_DLG5-like |
cd06767 |
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
269-308 |
2.64e-04 |
|
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467248 [Multi-domain] Cd Length: 82 Bit Score: 41.54 E-value: 2.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1239919865 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06767 42 GLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLVQ 81
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1452-1633 |
2.64e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.28 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1452 LQQLKKKCQRLTAELQdTKLHLEGQQV-RNHELEKKQRRFDSELSQAHEeaqreklqrEKLQREKDTLLaeafSLKQQLE 1530
Cdd:pfam07111 483 LEQLREERNRLDAELQ-LSAHLIQQEVgRAREQGEAERQQLSEVAQQLE---------QELQRAQESLA----SVGQQLE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1531 EKDMDIAGFTQKVVSLEAEL---QDISSQESKDEasLAKVKKQLRDLEAKVKDQ-EEELDEQAGTIQMLEQAKLRLEMEM 1606
Cdd:pfam07111 549 VARQGQQESTEEAASLRQELtqqQEIYGQALQEK--VAEVETRLREQLSDTKRRlNEARREQAKAVVSLRQIQHRATQEK 626
|
170 180
....*....|....*....|....*..
gi 1239919865 1607 ERMRQTHSKEVESRDEEVEEARQSCQK 1633
Cdd:pfam07111 627 ERNQELRRLQDEARKEEGQRLARRVQE 653
|
|
| PDZ5_DrPTPN13-like |
cd23060 |
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ... |
220-307 |
2.83e-04 |
|
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of Danio rerio Ptpn13, and related domains. Protein-tyrosine phosphatases (PTPs) dephosphorylate phosphotyrosyl residues in proteins that are phosphorylated by protein tyrosine kinases (PTKs). Danio rerio Ptpn13 is a classical non-receptor-like PTP. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467273 [Multi-domain] Cd Length: 80 Bit Score: 41.57 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 220 ELELQRRPTGDFGFSLRRttmldrGPEGQ-VYRRVVHfaePGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd23060 1 QIELEKPANGGLGFSLVG------GEGGSgIFVKSIS---PG-GVADRDGRLQVGDRLLQVNGESVIGLSHSKAVNILRK 70
|
....*....
gi 1239919865 299 SGDSVRLKV 307
Cdd:cd23060 71 AKGTVQLTV 79
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1710-1900 |
3.12e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 44.36 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1710 REIAQLKNQLEESEFTCAAAVKARKAMEVE-----MEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNE 1784
Cdd:cd00176 7 RDADELEAWLSEKEELLSSTDYGDDLESVEallkkHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1785 LMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQvefleQSMVDKSLVSRQEAKIRELETRLEFERTQ 1864
Cdd:cd00176 87 RWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE-----DLGKDLESVEELLKKHKELEEELEAHEPR 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1239919865 1865 VKRLESLASRLKENMEKLTEERDQRTAAENREKEQN 1900
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEE 197
|
|
| PDZ2_Par3-like |
cd23058 |
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ... |
260-307 |
3.15e-04 |
|
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP, Drosophila Bazooka) and related domains. Par3 is a scaffold protein involved in organizing cell polarity across animals. Par3 binds numerous molecules both for its recruitment to one pole of the cell and for downstream contributions to polarized cell function. It regulates cell polarity by targeting the Par complex proteins Par6 and atypical protein kinase C (aPKC) to specific cortical sites. Physical interactions between Par3 and the Par complex include Par3 PDZ domain 1 binding to the Par6 PDZ domain, Par3 PDZ domain 1 and PDZ domain 3 binding the Par6's PDZ-binding motif, and an interaction with an undefined region of aPKC that requires both Par3 PDZ2 and PDZ3. The PDZ domains of Par3 have also been implicated as potential phosphoinositide signaling integrators, since its second PDZ domain binds to phosphoinositides, and the third PDZ interacts with phosphoinositide phosphatase PTEN. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par3 family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467271 [Multi-domain] Cd Length: 93 Bit Score: 41.86 E-value: 3.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 260 GAGTKDlalG-LVPGDRLVEINGHNVESKSRDEIVEMIRQS--GDSVRLKV 307
Cdd:cd23058 43 GAAIQD---GrLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTklGGTVSLVV 90
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1536-1773 |
3.20e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1536 IAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQaklrlememermrqthsk 1615
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1616 EVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESK-LTTLSEQVSQRD--LESEKRLRKDLKRTKALL 1692
Cdd:COG3883 66 EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSEsFSDFLDRLSALSkiADADADLLEELKADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1693 ADAQIMLDHLKNnapskrEIAQLKNQLEESEftcAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQ 1772
Cdd:COG3883 146 EAKKAELEAKLA------ELEALKAELEAAK---AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
.
gi 1239919865 1773 S 1773
Cdd:COG3883 217 A 217
|
|
| PDZ_syntrophin-like |
cd06801 |
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ... |
270-308 |
3.32e-04 |
|
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of syntrophins (including alpha-1-syntrophin, beta-1-syntrophin, beta-2-syntrophin, gamma-1-syntrophin, and gamma-2-syntrophin), and related domains. Syntrophins play a role in recruiting various signaling molecules into signaling complexes and help provide appropriate spatiotemporal regulation of signaling pathways. They function in cytoskeletal organization and maintenance; as components of the dystrophin-glycoprotein complex (DGC), they help maintain structural integrity of skeletal muscle fibers. They link voltage-gated sodium channels to the actin cytoskeleton and the extracellular matrix, and control the localization and activity of the actin reorganizing proteins such as PI3K, PI(3,4)P2 and TAPP1. Through association with various cytoskeletal proteins within the cells, they are involved in processes such as regulation of focal adhesions, myogenesis, calcium homeostasis, and cell migration. They also have roles in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This syntrophin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467262 [Multi-domain] Cd Length: 83 Bit Score: 41.41 E-value: 3.32e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1239919865 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06801 44 LFVGDAILSVNGENLEDATHDEAVQALKNAGDEVTLTVK 82
|
|
| PDZ_rhophilin-like |
cd06712 |
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
219-307 |
3.32e-04 |
|
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of rhophilin-1, rhophilin-2, and related domains. Rhophilin-1 (RHPN1, also known as GTP-Rho-binding protein 1) and rhophilin-2 (RHPN2, also known as GTP-Rho-binding protein 2) are Rho-GTP binding proteins involved in cytoskeletal dynamics. Rhophilin-2 inhibits RhoA's activity to induce F-actin stress fibers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This rhophilin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467196 [Multi-domain] Cd Length: 78 Bit Score: 41.42 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 219 RELELQRRpTGDFGFSLRrttmldrGpEGQVyrrVVHFAEPGaGTKDLAlGLVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd06712 2 RTVHLTKE-EGGFGFTLR-------G-DSPV---QVASVDPG-SCAAEA-GLKEGDYIVSVGGVDCKWSKHSEVVKLLKS 67
|
90
....*....|
gi 1239919865 299 SG-DSVRLKV 307
Cdd:cd06712 68 AGeEGLELQV 77
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1765-1944 |
3.40e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.71 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1765 QREKNEIQSRLEEDQEDMNELMKKHkaaVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEfleqsmvdkslv 1844
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREE---LELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAA------------ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1845 sRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTAAENR--EKEQNKRLQRQLRdtKEEMGELARKEA 1922
Cdd:pfam15709 418 -QERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRlmEMAEEERLEYQRQ--KQEAEEKARLEA 494
|
170 180
....*....|....*....|..
gi 1239919865 1923 EASRKKHELEMDLESLEAANQS 1944
Cdd:pfam15709 495 EERRQKEEEAARLALEEAMKQA 516
|
|
| DUF1633 |
pfam07794 |
Protein of unknown function (DUF1633); This family contains sequences derived from a group of ... |
1568-1774 |
3.65e-04 |
|
Protein of unknown function (DUF1633); This family contains sequences derived from a group of hypothetical proteins expressed by Arabidopsis thaliana. These sequences are highly similar and the region concerned is about 100 residues long.
Pssm-ID: 116408 [Multi-domain] Cd Length: 698 Bit Score: 46.03 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1568 KKQLRDLEAKVK-DQEEELDEQAgtiQMLEQAKLRLEMEMermrqTHSKEVESRDEEveearqscqkKLKQMEVQLEEEY 1646
Cdd:pfam07794 457 ERAIREEDPHLGaDQDREVRFGA---EGIVPGIERLKIEL-----STSKDLEKGYAE----------KIGFMEMEFGGLE 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1647 EDKQKVLREKRELESKLTTLSEQVsqRDLESEKR-LRKDLKRTKALLADAQI-MLDHLKNNAPSKREIAQLKNQleesef 1724
Cdd:pfam07794 519 ADKQMARNQIHRLEEKKDELSKKV--LDLTSIAQgAKKAVHDAKVELAAAYLkLLAGIKDKWVAKKEFTVLEGQ------ 590
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1725 tcAAAVKARKAMevemedlhlqIDDIAKAKTALEEQLSRLQREKNEIQSR 1774
Cdd:pfam07794 591 --AAEVESNLAL----------IDQITKAAIDLTLEKPRFQAEIDDLEAR 628
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1399-1663 |
3.80e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 45.41 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1399 RLKYERAMREVDfTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQadideSQRA-LQQLKKKCQRLTAELQDTKLHLEGQQ 1477
Cdd:pfam15558 16 RHKEEQRMRELQ-QQAALAWEELRRRDQKRQETLERERRLLLQQ-----SQEQwQAEKEQRKARLGREERRRADRREKQV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1478 VRNHE-----LEKKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFT------------ 1540
Cdd:pfam15558 90 IEKESrwreqAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKrqlkereeqkkv 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1541 -----QKVVSLEAELQDISSQESKDEASL-----AKVKKQLRDLEAKVKDQEEELDEQAGTI-QMLEQAKLRLEmEMERM 1609
Cdd:pfam15558 170 qennlSELLNHQARKVLVDCQAKAEELLRrlsleQSLQRSQENYEQLVEERHRELREKAQKEeEQFQRAKWRAE-EKEEE 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1610 RQTHSKE-VESRDEEVEEARQSCQKKLK---QMEVQLEEEYEDKQKVLREKRELESKL 1663
Cdd:pfam15558 249 RQEHKEAlAELADRKIQQARQVAHKTVQdkaQRARELNLEREKNHHILKLKVEKEEKC 306
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1638-2000 |
4.01e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 45.48 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1638 MEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKrlrkDLKRTKALLADAQIMLDHLKNN-APSKREIAQLK 1716
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEE----DLKRQNAVLQEAQVELDALQNQlALARAEMENIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1717 NQLEESEFTCAAAV-KARKAMEVEMEDLHLQIDDIAKA-----KTALEEQLSR-------LQREKNEIQSRLEEDQEDMN 1783
Cdd:pfam03528 82 AVATVSENTKQEAIdEVKSQWQEEVASLQAIMKETVREyevqfHRRLEQERAQwnqyresAEREIADLRRRLSEGQEEEN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1784 ---------ELMKKHKAAVAQASRDLAQMNDLQAQLEEANKE-----KQELQEKLQALQSQVEFLEQSM----VDKSLVS 1845
Cdd:pfam03528 162 ledemkkaqEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKEleaskMKELNHYLEAEKSCRTDLEMYVavlnTQKSVLQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1846 RQEAKIR----ELETRLEFERTQ-------------------------VKRLESLASRLKENMEKLTEERDQRTAAENRE 1896
Cdd:pfam03528 242 EDAEKLRkelhEVCHLLEQERQQhnqlkhtwqkandqflesqrllmrdMQRMESVLTSEQLRQVEEIKKKDQEEHKRART 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1897 KEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKL----AFKRIGDLqaaIEDEMESDEN 1972
Cdd:pfam03528 322 HKEKETLKSDREHTVSIHAVFSPAGVETSAPLSNVEEQINSAHGSVHSLDTDVVLgagdSFNKQEDP---FKEGLRRAQS 398
|
410 420
....*....|....*....|....*...
gi 1239919865 1973 EDLITSLQDMVTKYQKRKNKPEGDSDVD 2000
Cdd:pfam03528 399 TDSLGSSSSLQHKFLGHNQKAKSAGNLD 426
|
|
| PDZ1_L-delphilin-like |
cd06743 |
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ... |
269-299 |
4.08e-04 |
|
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467225 [Multi-domain] Cd Length: 76 Bit Score: 41.11 E-value: 4.08e-04
10 20 30
....*....|....*....|....*....|.
gi 1239919865 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQS 299
Cdd:cd06743 36 GLQPGDQILELDGQDVSSLSCEAIIALARRC 66
|
|
| PDZ_MPP3-MPP4-MPP7-like |
cd06799 |
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ... |
269-309 |
4.27e-04 |
|
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP3, MPP4, and MPP7, and related domains. MPP3 (also known as MAGUK p55 subfamily member 3, erythrocyte membrane protein p55, or EMP55), MPP4 (also known as MAGUK p55 subfamily member 4 or Discs large homolog 6), and MPP7 (also known as MAGUK p55 subfamily member 7) are membrane-associated guanylate kinase (MAGUK)-like proteins. MPP3 is part of a cell adhesion protein complex including tumor suppressor CADM1 and actin-binding protein 4.1B. Participation in the Crumbs cell polarity complex has also been demonstrated for MPP7 in epithelial cells, and for MPP3 and MPP4 in the retina. MPP4 is needed for proper localization of plasma membrane calcium ATPases and maintenance of calcium homeostasis at the rod photoreceptor synaptic terminals. Binding partners of the MPP3 PDZ domain include nectin-3, serotonin 5-hydroxytryptamine, 5-HT(2C) receptor, and a cell adhesion protein, TSLC1 (tumor suppressor in lung cancer 1); fragments of MPP4 having the PDZ domain bind CRB (PDZ-SH3-GUK) and GABA transporter GAT1 (PDZ-SH3). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467260 [Multi-domain] Cd Length: 81 Bit Score: 41.07 E-value: 4.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1239919865 269 GLV-PGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06799 40 GLIhVGDELREVNGISVEGKDPEEVIQILANSQGPITFKLIP 81
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1432-1655 |
4.64e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.97 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1432 RQLERRLGDLQADIDESQRALQQLK-----KKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFdseLSQAHEEAQREKL 1506
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDygddlESVEALLKKHEALEAELAAHEERVEALNELGEQL---IEEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1507 QREKLQREKDTLLAEAFSLKQQLEEKdMDIAGFTQKVVSLEAELQDISSQESKDE--ASLAKVKKQLRDLeakvKDQEEE 1584
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLEEKEAALASEDlgKDLESVEELLKKH----KELEEE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 1585 LDEQagtiqmleqaklrlEMEMERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLRE 1655
Cdd:cd00176 155 LEAH--------------EPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| PDZ1_PTPN13-like |
cd23072 |
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ... |
259-309 |
4.87e-04 |
|
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467285 [Multi-domain] Cd Length: 92 Bit Score: 41.32 E-value: 4.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1239919865 259 PGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKV-QP 309
Cdd:cd23072 39 PG-GPADLDGRLKPGDRLISVNDVSLEGLSHDAAVEILQNAPEDVTLVVsQP 89
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
1720-1937 |
5.05e-04 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 44.82 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1720 EESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTA-LEEQLSRLQREKNEIQSRLEEDQE-DMNELMKKHKaavaqas 1797
Cdd:pfam09755 74 QEEEFISNTLLKKIQALKKEKETLAMNYEQEEEFLTNdLSRKLTQLRQEKVELEQTLEQEQEyQVNKLMRKIE------- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1798 RDLAQMNDLQAQLEEANKEKQELQEKL-QALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFERT------------- 1863
Cdd:pfam09755 147 KLEAETLNKQTNLEQLRREKVELENTLeQEQEALVNRLWKRM------DKLEAEKRLLQEKLDQPVSappsprdstsegd 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1864 -------QVKRLESLASRLKENMEKL----TEERDQRTAAENREKEQNKRLQRQLRDTKEEMGELARK--EAEASrkkhe 1930
Cdd:pfam09755 221 taqnltaHIQYLRKEVERLRRQLATAqqehTEKMAQYAQEERHIREENLRLQRKLQLEMERREALCRHlsESESS----- 295
|
....*..
gi 1239919865 1931 LEMDLES 1937
Cdd:pfam09755 296 LEMDEER 302
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1477-1772 |
5.25e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.32 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1477 QVRNHELEKKQrrfdSELSQAHEEAQREKLQREKLQREkdtllaeafslkqqleekdmdiAGFTQKVVSLEAELQDISSq 1556
Cdd:PRK05035 437 EIRAIEQEKKK----AEEAKARFEARQARLEREKAARE----------------------ARHKKAAEARAAKDKDAVA- 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1557 eskdeASLAKVK-KQLRDLEAKVKDQEEELDEQAgtiqMLEQAKLRLEMEMERMRQTHSKEVES-RDEEVEEA--RQSCQ 1632
Cdd:PRK05035 490 -----AALARVKaKKAAATQPIVIKAGARPDNSA----VIAAREARKAQARARQAEKQAAAAADpKKAAVAAAiaRAKAK 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1633 KKLKQMEVQLEEEYEDKQK------VLREKRELESKLTTLSEQVSQRDLESEKRLRKD--LKRTKALLADAQIMLDHLKN 1704
Cdd:PRK05035 561 KAAQQAANAEAEEEVDPKKaavaaaIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAaaIARAKAKKAEQQANAEPEEP 640
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1705 NAPSKREIAqlknqleesefTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTAleEQLSRLQREKNEIQ 1772
Cdd:PRK05035 641 VDPRKAAVA-----------AAIARAKARKAAQQQANAEPEEAEDPKKAAVA--AAIARAKAKKAAQQ 695
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1576-1826 |
6.38e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1576 AKVKDQEEElDEQAgtiqmlEQAKLRLEMEMERMRqthsKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKvlre 1655
Cdd:PRK05035 436 AEIRAIEQE-KKKA------EEAKARFEARQARLE----REKAAREARHKKAAEARAAKDKDAVAAALARVKAKKA---- 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1656 kRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQimldhlKNNAPSKREIAqlknqleeseftcaAAV---KA 1732
Cdd:PRK05035 501 -AATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAA------AAADPKKAAVA--------------AAIaraKA 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1733 RKAMEVEMEDLHLQIDDIAKAKTALEeqLSRLQREKNEiQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEE 1812
Cdd:PRK05035 560 KKAAQQAANAEAEEEVDPKKAAVAAA--IARAKAKKAA-QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAE 636
|
250
....*....|....
gi 1239919865 1813 ANKEKQELQEKLQA 1826
Cdd:PRK05035 637 PEEPVDPRKAAVAA 650
|
|
| Phage_HK97_TLTM |
pfam06120 |
Tail length tape measure protein; This family consists of the tail length tape measure protein ... |
1714-1929 |
6.87e-04 |
|
Tail length tape measure protein; This family consists of the tail length tape measure protein from bacteriophage HK97 and related sequences from Escherichia coli O157:H7.
Pssm-ID: 428779 [Multi-domain] Cd Length: 295 Bit Score: 44.07 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1714 QLKNQLEESEFTCAAAVKARKAMEVEMEdLHLQIDDIAKAKTALEEQ--LSRLQREKNE--------IQSRLEEDQEDMN 1783
Cdd:pfam06120 41 QKQEQARQSALEYAATIDQVRANLNKMT-LPETADNSGKTKESLAAQnkLVDEQRQKVEglksaiagYQQMLASPGPSIN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1784 ELMKKHKAAVAQASRDLAQMNDL----QAQLEEANKEKQELQEKLQALQSQVEFL--EQSMVDKSLvsRQEAKIRELETR 1857
Cdd:pfam06120 120 GYLINHLISQEDAVKSLAAAQDElsveQSRLNELSKKSEEIQSALKAVESQRDFLirQQSAAQNNM--RHSLLMVNAEHS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1858 lEFERTQ-------VKRLESLASRLKENMEKLTEERDQRTAAENREKEQN-----KRLQRQLRDTKEEMGELARKEAEAS 1925
Cdd:pfam06120 198 -EFNRIMsagnqilTNRLALVNSPMRIPAAPLSEKQQDFIQKSERDKELSaltgeARVIRQAEFAADDIGLLNKPEFADN 276
|
....
gi 1239919865 1926 RKKH 1929
Cdd:pfam06120 277 RQKY 280
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1658-1940 |
6.97e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.90 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1658 ELESKLTTLSEQVSQRDLESEKrlrKDLKRTKALladaqIMLDHLKNNAPSKREiaQLKNQLE-ESEFTCAAAVKARKAM 1736
Cdd:pfam15964 325 EAQQRESSAYEQVKQAVQMTEE---ANFEKTKAL-----IQCEQLKSELERQKE--RLEKELAsQQEKRAQEKEALRKEM 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1737 EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDmnelMKKHKAAVAQASRDLA-QMNDLQAQLEEANK 1815
Cdd:pfam15964 395 KKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQ----LASQEMDVTKVCGEMRyQLNQTKMKKDEAEK 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1816 EKQELQEKlqaLQSQVEFLEQsmvdkslvsrqeaKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDqrtaaenr 1895
Cdd:pfam15964 471 EHREYRTK---TGRQLEIKDQ-------------EIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLG-------- 526
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1239919865 1896 EKEQNKRLQRQLRDTKEE-MGELARKEA-EASRKKHELEMDLESLEA 1940
Cdd:pfam15964 527 ESEHQLHLTRLEKESIQQsFSNEAKAQAlQAQQREQELTQKMQQMEA 573
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1401-1577 |
6.97e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 43.36 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1401 KYERAMREV-----DFTKK--RLQQEFEDKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQD---TK 1470
Cdd:pfam13851 5 NHEKAFNEIknyynDITRNnlELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENyekDK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1471 LHLEGQQVRNHELEKKQRrfdsELSQAHEEaqreKLQR-EKLQREKDTLLAE----AFSLKQQLEEKDMDIAgftQKVVS 1545
Cdd:pfam13851 85 QSLKNLKARLKVLEKELK----DLKWEHEV----LEQRfEKVERERDELYDKfeaaIQDVQQKTGLKNLLLE---KKLQA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1239919865 1546 L-------EAELQDISSQESKDEASLAKVKKQLRD-LEAK 1577
Cdd:pfam13851 154 LgetlekkEAQLNEVLAAANLDPDALQAVTEKLEDvLESK 193
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1277-1660 |
7.34e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.68 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1277 QLSEEQIR---SKDEeiqqLRSKLEKVEKERNELRLSNDrletrisELTSeLTDErntgesASQLLDAEAAERLRAEKeM 1353
Cdd:pfam05622 70 QLQEENFRletARDD----YRIKCEELEKEVLELQHRNE-------ELTS-LAEE------AQALKDEMDILRESSDK-V 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1354 KELQTQYDALKKQMEVMEMEVMEARLIRaaEINGEVDDDDTGGEWRLKYERAMREVDFTKKRLQQEFEDKLEVEQQNKRQ 1433
Cdd:pfam05622 131 KKLEATVETYKKKLEDLGDLRRQVKLLE--ERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1434 LERRLGDLQADIDesqrALQQLKkkcQRLTAE---LQDTKLHLEGQQVRNHELEKKQRRFDSElSQAHEEAQREKLQ--- 1507
Cdd:pfam05622 209 LEFEYKKLEEKLE----ALQKEK---ERLIIErdtLRETNEELRCAQLQQAELSQADALLSPS-SDPGDNLAAEIMPaei 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1508 REKLQRekdtLLAEAFSLKQQLEEKDmdiagfTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDE 1587
Cdd:pfam05622 281 REKLIR----LQHENKMLRLGQEGSY------RERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQE 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1588 QAGTIQMLEQAKLRLEMEMERMRQTHSkEVESRDEEVEEARQSCQKKLKQMEVQLEE-----EYEDKQKVLREKRELE 1660
Cdd:pfam05622 351 QGSKAEDSSLLKQKLEEHLEKLHEAQS-ELQKKKEQIEELEPKQDSNLAQKIDELQEalrkkDEDMKAMEERYKKYVE 427
|
|
| PDZ5_MUPP1-like |
cd06669 |
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ... |
269-311 |
8.13e-04 |
|
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467157 [Multi-domain] Cd Length: 98 Bit Score: 40.67 E-value: 8.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1239919865 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQSG-DSVRLKV-QPIP 311
Cdd:cd06669 54 RLLPGDRLVFVNDVSLENASLDEAVQALKSAPpGTVRIGVaKPLP 98
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1288-1782 |
8.14e-04 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 44.67 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1288 EEIQQLRSKLEKVEKERnelrlsnDRLETRISELTSELTDERNTGESASQLLDAEAA----ERLRAEKEMKELQTQYDAL 1363
Cdd:pfam15070 29 QKMQQLSEQVRTLREEK-------ERSVSQVQELETSLAELKNQAAVPPAEEEQPPAgpseEEQRLQEEAEQLQKELEAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1364 kkqmevmemevmearlirAAEINGEVDDDDTggewrlkyeramrevdftKKRLQQEFEDKL-EVEQQNKRQLE------R 1436
Cdd:pfam15070 102 ------------------AGQLQAQVQDNEQ------------------LSRLNQEQEQRLlELERAAERWGEqaedrkQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1437 RLGDLQADIDESQRALQQLKKKCQRLtAELQD-------------TKLHLEgQQVRNhELEKKQRRFDSELSQAHEEAQR 1503
Cdd:pfam15070 146 ILEDMQSDRATISRALSQNRELKEQL-AELQNgfvkltnenmeltSALQSE-QHVKK-ELAKKLGQLQEELGELKETLEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1504 EKLQREKLQREKDTLLAE----AFSLKQQLEEKDMdiagfTQKVVSLEAELQD-ISSQESKDEASLAKVKKQLRD----L 1574
Cdd:pfam15070 223 KSQEAQSLQEQRDQYLAHlqqyVAAYQQLASEKEE-----LHKQYLLQTQLMDrLQHEEVQGKVAAEMARQELQEtqerL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1575 EAKVKDQEEEldeQAGTIQMLEQAK---LRLEMEMERMRQTH---SKEVESRDEEVE---EARQSCQKKLKQMEVQLEEE 1645
Cdd:pfam15070 298 EALTQQNQQL---QAQLSLLANPGEgdgLESEEEEEEAPRPSlsiPEDFESREAMVAffnSALAQAEEERAELRRQLKEQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1646 YedkqkvlREKRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLadaQIMLDHLKNNAPS-KREIAQLKNQLEESEF 1724
Cdd:pfam15070 375 K-------RRCRRLAQQAAPAQEEPEHEAHAPGTGGDSVPVEVHQAL---QVAMEKLQSRFTElMQEKADLKERVEELEH 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 1725 TCAaavkarkamevemeDLHLQIDDIAKAKTALEEQ---LSRLQREKNEIQSRLEEDQEDM 1782
Cdd:pfam15070 445 RCI--------------QLSGETDTIGEYIALYQSQraiLKQRHREKEEYISRLAQDKEEM 491
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1275-1496 |
8.44e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1275 EVQLSEEQIRSKDEEIQQLRSKLEKVEKERNElRLSNDRLETRISELTSELTDERNT-GESASQLLDAEAAERlRAEKEM 1353
Cdd:PRK11281 88 QLAQAPAKLRQAQAELEALKDDNDEETRETLS-TLSLRQLESRLAQTLDQLQNAQNDlAEYNSQLVSLQTQPE-RAQAAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1354 KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDTggewRLKYERAMREVDFTKKRLQQEFEDKLEVEQQnkrQ 1433
Cdd:PRK11281 166 YANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNA----QNDLQRKSLEGNTQLQDLLQKQRDYLTARIQ---R 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239919865 1434 LERRLGDLQADIdeSQRALQQLKKKCQRltAELQDtklhlEGQQVRNHELEKKQRRFDSELSQ 1496
Cdd:PRK11281 239 LEHQLQLLQEAI--NSKRLTLSEKTVQE--AQSQD-----EAARIQANPLVAQELEINLQLSQ 292
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1740-1831 |
8.56e-04 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 44.29 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1740 MEDLHLQIDDIAKAKTALE--------EQLSRLQREKNEIQSRLEEDQEDMNEL---MKKHKAAVAQASRDLAQMNDLQA 1808
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAkrgfpldvDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKE 80
|
90 100
....*....|....*....|...
gi 1239919865 1809 QLEEANKEKQELQEKLQALQSQV 1831
Cdd:PRK05431 81 EIKALEAELDELEAELEELLLRI 103
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1546-1848 |
8.89e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1546 LEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQthskEVESRDEEVE 1625
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE----EAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1626 EARQScQKKLKQMEVQLEEEYEDKQKVL----REKRELESKLTTLSEQVSQRDLESEKRLRKDLKRTKALLadaqimLDH 1701
Cdd:COG4372 119 ELQKE-RQDLEQQRKQLEAQIAELQSEIaereEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL------LKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1702 LKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEmedlHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQED 1781
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA----KLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239919865 1782 MNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQE 1848
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1432-1611 |
9.43e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.98 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1432 RQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDtklhLEGQqvrnHELEKKQRRfdSELSQAHEEAQREKLQREKL 1511
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE----LEAQ----QQEEAESSR--EQLQELEEQLATERSARREA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1512 QREKDTLLAEAFSLKQQLEEKDMDIAGftqKVVSLEAELQDISSQ-ESKDEASLAKvkkqlRDLEAKVKDQEEELDEQAG 1590
Cdd:pfam09787 113 EAELERLQEELRYLEEELRRSKATLQS---RIKDREAEIEKLRNQlTSKSQSSSSQ-----SELENRLHQLTETLIQKQT 184
|
170 180
....*....|....*....|.
gi 1239919865 1591 TIQMLEQAKLRLEMEMERMRQ 1611
Cdd:pfam09787 185 MLEALSTEKNSLVLQLERMEQ 205
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1716-1893 |
9.58e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1716 KNQLEESEFTCAAAVK-ARKAMEVEMEDLHLQI-DDIAKAKTALEEQLsrlQREKNEIQsRLEEDQEDMNELMKKHKAAV 1793
Cdd:PRK12704 30 EAKIKEAEEEAKRILEeAKKEAEAIKKEALLEAkEEIHKLRNEFEKEL---RERRNELQ-KLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1794 AQASRDLAQMNDLQAQLEEANKEKQELQEKLQalQSQVEFLEQSMvdkSLvSRQEAK---IRELETRLEFERtqvkrles 1870
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELI--EEQLQELERIS---GL-TAEEAKeilLEKVEEEARHEA-------- 171
|
170 180 190
....*....|....*....|....*....|....
gi 1239919865 1871 lASRLKENMEKLTEERD-----------QRTAAE 1893
Cdd:PRK12704 172 -AVLIKEIEEEAKEEADkkakeilaqaiQRCAAD 204
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1752-1916 |
9.67e-04 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 41.51 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1752 KAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQELQEKLQALQSQV 1831
Cdd:pfam10473 3 KKQLHVLEKLKESERKADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1832 EFLEQSmvdkslvsrqeakireletrLEFERTQVKRLESLASRLKENMEKLTEERDQrtaaenrEKEQNKRLQRQLRDTK 1911
Cdd:pfam10473 83 ENLTKE--------------------LQKKQERVSELESLNSSLENLLEEKEQEKVQ-------MKEESKTAVEMLQTQL 135
|
....*
gi 1239919865 1912 EEMGE 1916
Cdd:pfam10473 136 KELNE 140
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1760-1949 |
9.71e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1760 QLSRLQREKNEIQSRLEEDQEDMNEL---MKKHKAAVAQASRdlaQMNDLQAQLEEANKEKQELQEKLQALQSQvefleQ 1836
Cdd:PRK11637 48 QLKSIQQDIAAKEKSVRQQQQQRASLlaqLKKQEEAISQASR---KLRETQNTLNQLNKQIDELNASIAKLEQQ-----Q 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1837 SMVDKSLVSRQEAKIRE-----LETRLEFERTQVK-RLESLASRL----KENMEKLTEERDQrTAAENREKEQNKRLQRQ 1906
Cdd:PRK11637 120 AAQERLLAAQLDAAFRQgehtgLQLILSGEESQRGeRILAYFGYLnqarQETIAELKQTREE-LAAQKAELEEKQSQQKT 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1239919865 1907 LRDTKEEMgELARKEAEASRKKhelemDLESLEAANQSLQADL 1949
Cdd:PRK11637 199 LLYEQQAQ-QQKLEQARNERKK-----TLTGLESSLQKDQQQL 235
|
|
| PDZ_SYNPO2-like |
cd10820 |
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ... |
269-308 |
1.01e-03 |
|
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNPO2, SYNPO2L, and related domains. SYNPO2 (also known as genethonin-2, myopodin) is a cytoskeleton adaptor protein. It participates in chaperone-assisted selective autophagy (CASA), a mechanism for the disposal of misfolded and damaged proteins and provides a link between the CASA chaperone complex and a membrane-tethering and fusion machinery that generates autophagosome membranes. The SYNPO2 PPxY motif binds CASA cochaperone BCL2-associated athanogene 3 (BAG3) and the SYNPO2 PDZ domain binds vacuolar protein sorting 18 homolog (VPS18). There are three isoforms of SYNPO2, which possess an amino-terminal PDZ domain (SYNPO2a, b, c); the short isoform SYNPO2d, lacks the PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNPO2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467264 [Multi-domain] Cd Length: 78 Bit Score: 39.98 E-value: 1.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1239919865 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd10820 39 GLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQLLIK 78
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1504-1655 |
1.04e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.59 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1504 EKLQREKLQREKDTLLAEAFSLKQQLEEKdmdIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLRDLEAKVKDQEE 1583
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEP---LQKAQEEVEELRKQLE----NYEKDKQSLKNLKARLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239919865 1584 ELDeqagtiqMLEQAKLRLEMEMERMRQthskevesRDEE-VEEARQSCQKK---LKQMEVQLEEEYEDKQKVLRE 1655
Cdd:pfam13851 107 EHE-------VLEQRFEKVERERDELYD--------KFEAaIQDVQQKTGLKnllLEKKLQALGETLEKKEAQLNE 167
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1431-1648 |
1.06e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1431 KRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTK-----LHLEGQQvrnHELEKKQRRFDSELSQAHEEAQREK 1505
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglVDLSEEA---KLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1506 LQREKLQREKDTLLAEAFSLKQqleekDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ---- 1581
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaqri 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239919865 1582 ----EEELDEQAGTIQMLEQAKLRLEmemERMRQTHSKEVESRD--EEVEEARQ---SCQKKLKQMEVQLEEEYED 1648
Cdd:COG3206 315 laslEAELEALQAREASLQAQLAQLE---ARLAELPELEAELRRleREVEVARElyeSLLQRLEEARLAEALTVGN 387
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1656-1830 |
1.13e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1656 KRELESKLTTLseqvsQRDLeseKRLRKDLKRTKALLADAQIMLDHLKnnapskREIAQLKNQleeseftcaaavkarka 1735
Cdd:smart00787 146 KEGLDENLEGL-----KEDY---KLLMKELELLNSIKPKLRDRKDALE------EELRQLKQL----------------- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1736 mEVEMEDLHLQIDDIAKAKtaleeqLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEAN- 1814
Cdd:smart00787 195 -EDELEDCDPTELDRAKEK------LKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRg 267
|
170
....*....|....*....
gi 1239919865 1815 ---KEKQELQEKLQALQSQ 1830
Cdd:smart00787 268 ftfKEIEKLKEQLKLLQSL 286
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1413-1671 |
1.18e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1413 KKRLQQEFEDKLE----VEQQNKR--QLERRLGDLQADIDESQRALQQLKKKCQRLTAElQDTKLHLEGQQVRNHELEKK 1486
Cdd:PRK11281 58 DKLVQQDLEQTLAlldkIDRQKEEteQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE-TLSTLSLRQLESRLAQTLDQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1487 QRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEAFSLKQQLeeKDMDIAG----FTQKVVsLEAELQDISSQESKDEA 1562
Cdd:PRK11281 137 LQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLL--KGGKVGGkalrPSQRVL-LQAEQALLNAQNDLQRK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1563 SLAkVKKQLRDLEAKVKD----QEEELDEQAGTIQMLEQAKlRLEMEMERMRQTHSKEVESRDE-------EVEEARQSC 1631
Cdd:PRK11281 214 SLE-GNTQLQDLLQKQRDyltaRIQRLEHQLQLLQEAINSK-RLTLSEKTVQEAQSQDEAARIQanplvaqELEINLQLS 291
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1239919865 1632 QKKLKQMevqlEEEYEDKQKVLREKRELESKLTT---LSEQVS 1671
Cdd:PRK11281 292 QRLLKAT----EKLNTLTQQNLRVKNWLDRLTQSernIKEQIS 330
|
|
| PDZ2_MAGI-1_3-like |
cd06732 |
PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
216-308 |
1.36e-03 |
|
PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467214 [Multi-domain] Cd Length: 82 Bit Score: 39.84 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 216 PALRELELQRRPTGdFGFslrrtTMLDRgPEGQVYRRVVhfAEPGAGtkdlalGLVPGDRLVEINGHNVESKSRDEIVEM 295
Cdd:cd06732 1 PELVTVPIVKGPMG-FGF-----TIADS-PQGQRVKQIL--DPQRCR------GLQEGDLIVEINGQNVQNLSHAQVVDV 65
|
90
....*....|....*
gi 1239919865 296 IRQS--GDSVRLKVQ 308
Cdd:cd06732 66 LKECpkGSEVTLLVQ 80
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1549-1778 |
1.37e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1549 ELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMErmrqthskEVESRDEEVEEar 1628
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE--------EVEARIKKYEE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1629 qscqkklKQMEVQLEEEYEDKQKvlrekrELESklttlseqvsqrdlesekrlrkdLKRTKALLADaqimldhlknnaps 1708
Cdd:COG1579 81 -------QLGNVRNNKEYEALQK------EIES-----------------------LKRRISDLED-------------- 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1709 krEIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAktaLEEQLSRLQREKNEIQSRLEED 1778
Cdd:COG1579 111 --EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEAEREELAAKIPPE 175
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
1849-1974 |
1.45e-03 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 40.84 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1849 AKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRTAAEnrekEQNKRLQRQLRDTKEEMGELARKEAEASRKK 1928
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELE----AEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1239919865 1929 HELEMDLESLEAANQSLQADLKlafKRIGDLQAAIEDEMESDENED 1974
Cdd:pfam04871 77 DDLLLLLGDLEEKVEKYKARLK---ELGEEVLSDDEDDDEDDEEDD 119
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1556-1911 |
1.54e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 43.90 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1556 QESKD-EASLAKVKKQLRDLEAKVKDQEEeldeqagTIQMLEQAKLRLEMEMERMRQThsKEVESRDEEVEEARQSCQKK 1634
Cdd:pfam13166 89 EESIEiQEKIAKLKKEIKDHEEKLDAAEA-------NLQKLDKEKEKLEADFLDECWK--KIKRKKNSALSEALNGFKYE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1635 LKQMEVQLEE--EYEDKQKVLREKRELESKLTTLSEQ---------VSQRDLESEKRLRKDLKRTKALLADAQIMLDHLK 1703
Cdd:pfam13166 160 ANFKSRLLREieKDNFNAGVLLSDEDRKAALATVFSDnkpeiapltFNVIDFDALEKAEILIQKVIGKSSAIEELIKNPD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1704 NNAPSKREIAQLKNQLEESEFtC--------AAAVKAR--KAMEVEMEDLHLQIDDIAKAKTALEEQL----------SR 1763
Cdd:pfam13166 240 LADWVEQGLELHKAHLDTCPF-CgqplpaerKAALEAHfdDEFTEFQNRLQKLIEKVESAISSLLAQLpavsdlasllSA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1764 LQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLaQMNDLQAQLEEANKEKQELQEklqalqsqvefleqsmvdksL 1843
Cdd:pfam13166 319 FELDVEDIESEAEVLNSQLDGLRRALEAKRKDPFKSI-ELDSVDAKIESINDLVASINE--------------------L 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1844 VSRQEAKIRELET-----RLEFERTQVKRLESLASRLKENM-------EKLTEERDQRTAAENREKEQNKRLQRQLRDTK 1911
Cdd:pfam13166 378 IAKHNEITDNFEEeknkaKKKLRLHLVEEFKSEIDEYKDKYaglekaiNSLEKEIKNLEAEIKKLREEIKELEAQLRDHK 457
|
|
| PDZ_ARHGEF11-12-like |
cd23069 |
PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
219-308 |
1.55e-03 |
|
PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ARHGEF11, ARHGEF12, and related domains. This subfamily includes the GEFs (guanine exchange factors) ARHGEF11 (Rho guanine nucleotide exchange factor 11, known as PDZ-RhoGEF) and ARHGEF12 (Rho guanine nucleotide exchange factor 12, also known as leukemia-associated RhoGEF). GEFs activate Rho GTPases by promoting GTP binding. ARHGEF11/12 are regulators of G protein signaling (RGS) domain-containing GEFs; the RGS domain mediates their binding to and activation of Galpha (and Gq also in the case of ARHGEF12), in response to G-protein coupled receptor activation. ARHGEF11 and 12 are involved in serum-signaling, and regulate Yes-Associated Protein (YAP1)-dependent transcription. The ARHGEF12 PDZ domain binds plexin-B1 and the receptor tyrosine kinase insulin-like growth factor receptor (IGF-R1) beta-subunit. ARHGEF12 also interacts with glutamate receptor delta-1(GluD1), a postsynaptic organizer of inhibitory synapses in cortical pyramidal neurons. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ARHGEF11-12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467282 [Multi-domain] Cd Length: 76 Bit Score: 39.30 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 219 RELELQRRPTGdFGFslrrTTMLDRgpegQVYrrVVHFAEPGAGTKdlaLGLVPGDRLVEINGHNVESKSRDEIVEMIRq 298
Cdd:cd23069 2 RCVVIQRDENG-YGL----TVSGDN----PVF--VQSVKEGGAAYR---AGVQEGDRIIKVNGTLVTHSNHLEVVKLIK- 66
|
90
....*....|
gi 1239919865 299 SGDSVRLKVQ 308
Cdd:cd23069 67 SGSYVALTLL 76
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1541-1884 |
1.57e-03 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 43.67 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1541 QKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMER-MRQTHSKEVES 1619
Cdd:pfam15450 20 QWVADLQAEVVSLRGHKERCEHATLSLLRELLQVRAHVQLQDSELKQLRQEVQQAARAPEKEALEFPGpQNQNQMQALDK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1620 RDEEVEEA------RQSCQK------------KLKQMEVQLEEEYEDK---------------QKVLREKRELESKLTTL 1666
Cdd:pfam15450 100 RLVEVREAltqirrKQALQDserkgaeqeanlRLTKLTGKLKQEEQGReaacsalqksqeeasQKVDHEVARMQAQVTKL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1667 SEQVSQRDLESEKRLRKDLKrtKALLADAQIMldhlkNNAPSKREIAQlKNQLEESEftcaaaVKARKAMEVEMEDLHLQ 1746
Cdd:pfam15450 180 GEEMSLRFLKREAKLCSFLQ--KSFLALEKRM-----KASESTRLKAE-SSLREELE------GRWQKLQELTEERLRAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1747 IDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNE-LMKKHKAAVAQASRDLAQMNDLQAQLEE-----------AN 1814
Cdd:pfam15450 246 QGQREQEEGHLLEQCRGLDAAVVQLTKFVRQNQVSLNRvLLAEQKARDAKGQLEESQAGELASYVQEnleavqlagelAQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1815 KEKQE----LQEKLQALQSQVEFLEQSMVDKS----------LVSRQEAKIRELETRLEFERTQVKRLESLASRLKENME 1880
Cdd:pfam15450 326 QETQGalelLQEKSQVLEGSVAELVRQVKDLSdhflalswrlDLQEQTLGLKLSEAKKEWEGAERKSLEDLAQWQKEVAA 405
|
....
gi 1239919865 1881 KLTE 1884
Cdd:pfam15450 406 HLRE 409
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
1741-1834 |
1.57e-03 |
|
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.
Pssm-ID: 464384 [Multi-domain] Cd Length: 261 Bit Score: 42.69 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1741 EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMNDLQAQLEEANKekqEL 1820
Cdd:pfam14932 70 EALEESLEEIREATEDLEAELQELQKTKQLKINRLNKLQAQASSLSQGLRALVAEEEEAAKQLEELQEELAALNA---KT 146
|
90
....*....|....
gi 1239919865 1821 QEKLQALQSQVEFL 1834
Cdd:pfam14932 147 NNVLQSLQSEVKEL 160
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1262-1513 |
1.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1262 AWWKLFTTVRPLIEVQLSEEQIRSKDEEIQQLRS----------KLEKVEKERNELRLSNDRLETRISELTSELTD---- 1327
Cdd:COG4913 649 ALQRLAEYSWDEIDVASAEREIAELEAELERLDAssddlaaleeQLEELEAELEELEEELDELKGEIGRLEKELEQaeee 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1328 -------ERNTGESASQLLDAEAAERLRAEKE-------MKELQTQYDALKKQMEVMEMevmeaRLIRA-----AEINGE 1388
Cdd:COG4913 729 ldelqdrLEAAEDLARLELRALLEERFAAALGdaverelRENLEERIDALRARLNRAEE-----ELERAmrafnREWPAE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1389 VDDDDTGGEWRLKYeRAMREvdftkkRLQQ----EFEDKLevEQQNKRQLERRLGDLQADIDESQR-ALQQLKkkcqRLT 1463
Cdd:COG4913 804 TADLDADLESLPEY-LALLD------RLEEdglpEYEERF--KELLNENSIEFVADLLSKLRRAIReIKERID----PLN 870
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1464 AELQ------DTKLHLEGQQVRNHELEKKQRRFD--SELSQAHEEAQREKlQREKLQR 1513
Cdd:COG4913 871 DSLKripfgpGRYLRLEARPRPDPEVREFRQELRavTSGASLFDEELSEA-RFAALKR 927
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1816-1946 |
1.61e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 41.14 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1816 EKQELQEKLQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFERTQVKRLESlasRLKENMEKLTEERDQRTAAENr 1895
Cdd:pfam12718 8 EAENAQERAEELEEKVKELEQENLEK------EQEIKSLTHKNQQLEEEVEKLEE---QLKEAKEKAEESEKLKTNNEN- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 1896 ekeqnkrLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQ 1946
Cdd:pfam12718 78 -------LTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALE 121
|
|
| PDZ2_MUPP1-like |
cd06667 |
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ... |
259-307 |
1.61e-03 |
|
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467155 [Multi-domain] Cd Length: 80 Bit Score: 39.57 E-value: 1.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1239919865 259 PGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06667 31 PG-GVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSHVRLVV 78
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1625-1790 |
1.65e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 43.88 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1625 EEARQSCQKKLKQMEVQLEEEYEDKQKvLREKRElesKLTTLSEQVSQRDLESEKRLRKDLKRTKALLADAQimlDHLKN 1704
Cdd:pfam10168 553 DLAREEIQKRVKLLKLQKEQQLQELQS-LEEERK---SLSERAEKLAEKYEEIKDKQEKLMRRCKKVLQRLN---SQLPV 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1705 NAPSKREIAQLKNQLEESEFTCAAAVK-ARKAMEVemedlhlQIDDIAKAKTALEE---QLSRLQREKneIQSRLEEDQE 1780
Cdd:pfam10168 626 LSDAEREMKKELETINEQLKHLANAIKqAKKKMNY-------QRYQIAKSQSIRKKsslSLSEKQRKT--IKEILKQLGS 696
|
170
....*....|
gi 1239919865 1781 DMNELMKKHK 1790
Cdd:pfam10168 697 EIDELIKQVK 706
|
|
| PDZ2_Dlg1-2-4-like |
cd06724 |
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ... |
258-308 |
1.81e-03 |
|
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467207 [Multi-domain] Cd Length: 85 Bit Score: 39.56 E-value: 1.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 258 EPGAGTKDLALGLvpGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06724 37 EGGAAQKDGRLQV--GDKLLAVNDVSLEEVTHEEAVAALKNTSDVVYLKVA 85
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1787-1930 |
1.96e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1787 KKHKAAVAQASRDLAQMndlqaqLEEANKEKQELQeKLQALQSQVEFLE-QSMVDKSLVSRqEAKIRELETRLEFERTQV 1865
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRI------LEEAKKEAEAIK-KEALLEAKEEIHKlRNEFEKELRER-RNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239919865 1866 -KRLESLASR------LKENMEKLTEERDQRTA-AENREKEQNKRLQRQLRDTKEEMGELARKEAEaSRKKHE 1930
Cdd:PRK12704 99 dRKLELLEKReeelekKEKELEQKQQELEKKEEeLEELIEEQLQELERISGLTAEEAKEILLEKVE-EEARHE 170
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
1547-1945 |
2.12e-03 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 43.31 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1547 EAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQthskevESRDEEVEE 1626
Cdd:pfam09730 19 ESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRD------EIKEYKVRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1627 ARQscqkklkqmevqleeeyedkqkvLREKRELESKLTTLSEQVS---QRDLESE------KRLRKDLKRTKALLADA-- 1695
Cdd:pfam09730 93 ARL-----------------------LQDYSELEEENISLQKQVSvlkQNQVEFEglkheiTRKEEETELLNSQLEEAir 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1696 --QIMLDHLKNNAPSKREIAQLKNQL--EESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQL------SRLQ 1765
Cdd:pfam09730 150 lrEIAERQLDEALETLKTEREQKNSLrkELSHYMTLNDFDYVSHLSISLDGLKFSEDEGAGTEPNNDGEAmdggenGGGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1766 REKNEIQSRLEEDQED-------------MNEL----MKKHKAAVAQASRD----LAQMNDLQAQLEEANKEKQELQEKL 1824
Cdd:pfam09730 230 LKNSGLDNRTSTPRKSevfppapslvsdlLSELniseIQKLKQQLIQVEREkvslLSTLQESQKQLEQAKGALSEQQEKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1825 QALQSQVEFLEQSMVDKSLVS--RQEAKIRELETRLEFErTQVKRLESLASRLKENMEKLTEERDQRTAA-------ENR 1895
Cdd:pfam09730 310 NRLTENLEAMRGLQASKERQDalDSEKDRDSHEDGDYYE-VDINGPEILECKYRVAVEEAGELREELKALkaryntlEER 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1239919865 1896 EKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESL-EAANQSL 1945
Cdd:pfam09730 389 YKEEKTRWEAEAQDLAEKIRQLEKASHQDQERIAHLEKELGKTrKVAGESE 439
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1418-1553 |
2.14e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.66 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1418 QEFEDKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKKKCQRLTAELQdtklhlEGQQVrnheLEKKQRRFDSELSQA 1497
Cdd:pfam02841 179 QEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQK------EEEQM----MEAQERSYQEHVKQL 248
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239919865 1498 HEEAQREklqREKLQREKDTLLAeafslKQQLEEKDMDIAGFTQKVVSLEAELQDI 1553
Cdd:pfam02841 249 IEKMEAE---REQLLAEQERMLE-----HKLQEQEELLKEGFKTEAESLQKEIQDL 296
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1432-1877 |
2.30e-03 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 43.28 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1432 RQLERRLGDLQADI-------DESQRALQQLKKKCQRLTA--ELQDTKLHLEGQQVRN--HELEKKQRRFDSELSQAHEE 1500
Cdd:pfam15450 16 KQLEQWVADLQAEVvslrghkERCEHATLSLLRELLQVRAhvQLQDSELKQLRQEVQQaaRAPEKEALEFPGPQNQNQMQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1501 AQREKL--QREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKvVSLEAELQDISS---QESKDEASlAKVKKQLRDLE 1575
Cdd:pfam15450 96 ALDKRLveVREALTQIRRKQALQDSERKGAEQEANLRLTKLTGK-LKQEEQGREAACsalQKSQEEAS-QKVDHEVARMQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1576 AKVKDQEEE-----LDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQ 1650
Cdd:pfam15450 174 AQVTKLGEEmslrfLKREAKLCSFLQKSFLALEKRMKASESTRLKAESSLREELEGRWQKLQELTEERLRALQGQREQEE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1651 KVLREK-RELESKLTTLSEQVSQ------RDLESEKRLRKdlkrTKALLADAQImlDHLKNNAPSKREIAQLKNQLEESE 1723
Cdd:pfam15450 254 GHLLEQcRGLDAAVVQLTKFVRQnqvslnRVLLAEQKARD----AKGQLEESQA--GELASYVQENLEAVQLAGELAQQE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1724 FTCAAAV--KARKAMEVEMEDLHLQIDDIAKAKTALEeqlSRLQREKNEIQSRLEEDQEDMNELMKKhkaavaqasrdla 1801
Cdd:pfam15450 328 TQGALELlqEKSQVLEGSVAELVRQVKDLSDHFLALS---WRLDLQEQTLGLKLSEAKKEWEGAERK------------- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1802 QMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMV----DKSLVSRQEAKIRELEtrLEFERTQVKRLESLASRLKE 1877
Cdd:pfam15450 392 SLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVlhksDSDLKISAEGKAREFE--VEAMRQELAALLSSVQLLKE 469
|
|
| PDZ4_DLG5-like |
cd06766 |
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
254-308 |
2.49e-03 |
|
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467247 [Multi-domain] Cd Length: 81 Bit Score: 38.91 E-value: 2.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239919865 254 VHFAEPGAGTKDLAlGLVPGDRLVEINGHNVESKSRDEI-VEMIRQSgDSVRLKVQ 308
Cdd:cd06766 28 VEDVEDDSPAKGPD-GLVPGDLILEYNSVDMRNKTAEEAyLEMLKPA-ETVTLKVQ 81
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1757-1946 |
2.51e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 43.13 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1757 LEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMND----LQAQLEEANKEKQELQEKLQAlqsQVE 1832
Cdd:pfam15070 34 LSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAGPSEeeqrLQEEAEQLQKELEALAGQLQA---QVQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1833 FLEQSmvdKSLVSRQEAKIRELETRLEFERTQVKRLEslasRLKENME--KLTeerDQRTAAENRE-KEQNKRLQRQ-LR 1908
Cdd:pfam15070 111 DNEQL---SRLNQEQEQRLLELERAAERWGEQAEDRK----QILEDMQsdRAT---ISRALSQNRElKEQLAELQNGfVK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1239919865 1909 DTKEEM-------------GELARKEAEASRKKHEL--EMDLESLEAanQSLQ 1946
Cdd:pfam15070 181 LTNENMeltsalqseqhvkKELAKKLGQLQEELGELkeTLELKSQEA--QSLQ 231
|
|
| RseP |
COG0750 |
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ... |
269-308 |
2.84e-03 |
|
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];
Pssm-ID: 440513 [Multi-domain] Cd Length: 349 Bit Score: 42.38 E-value: 2.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1239919865 269 GLVPGDRLVEINGHNVEskSRDEIVEMIRQS-GDSVRLKVQ 308
Cdd:COG0750 145 GLQPGDRIVAINGQPVT--SWDDLVDIIRASpGKPLTLTVE 183
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1742-1831 |
2.92e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 42.41 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1742 DLHLQIDDIAKAKTALEEQLSRLQREKNEIQSrleeDQEDMNELMKKHKAAVAQASrDLAQMN--DLQAQLEEANKEKQE 1819
Cdd:TIGR04320 262 KLATAQADLAAAQTALNTAQAALTSAQTAYAA----AQAALATAQKELANAQAQAL-QTAQNNlaTAQAALANAEARLAK 336
|
90
....*....|..
gi 1239919865 1820 LQEKLQALQSQV 1831
Cdd:TIGR04320 337 AKEALANLNADL 348
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1526-2002 |
3.03e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.28 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1526 KQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKqLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLeME 1605
Cdd:PTZ00440 480 KDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKN-IEDYYITIEGLKNEIEGLIELIKYYLQSIETL-IK 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1606 MERMRQTHSKEVESRDEEVEE----------ARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELESKLTTLSEQVSQRDL 1675
Cdd:PTZ00440 558 DEKLKRSMKNDIKNKIKYIEEnvdhikdiisLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDL 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1676 ES-EKRLRKDLKRTKALLadaqimldhlkNNAPSKREIAQLKNQLEE-----SEFTCAAAVKARKAMEVEMEDLHLQIDD 1749
Cdd:PTZ00440 638 QElLDELSHFLDDHKYLY-----------HEAKSKEDLQTLLNTSKNeyeklEFMKSDNIDNIIKNLKKELQNLLSLKEN 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1750 IAKA-----KTALEEQLSRLQREKNEIQSRLEEDQEDMNELmKKHKAAVAQASRDL---AQMNDLQA-----QLEEANKE 1816
Cdd:PTZ00440 707 IIKKqlnniEQDISNSLNQYTIKYNDLKSSIEEYKEEEEKL-EVYKHQIINRKNEFilhLYENDKDLpdgknTYEEFLQY 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1817 KQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFERTQVKRlesLASRLKENMEKLTEERDQRTAAENR 1895
Cdd:PTZ00440 786 KDTILNKENKISNDINILKENKKNnQDLLNSYNILIQKLEAHTEKNDEELKQ---LLQKFPTEDENLNLKELEKEFNENN 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1896 EK---------EQNKRLQ---------RQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKlafKRIG 1957
Cdd:PTZ00440 863 QIvdniikdieNMNKNINiiktlniaiNRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNLL---NNLN 939
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1239919865 1958 DLQAAIEDEMESDENEDLITSLQDMVTKYQKRKNKPEGDSDVDSE 2002
Cdd:PTZ00440 940 KEKEKIEKQLSDTKINNLKMQIEKTLEYYDKSKENINGNDGTHLE 984
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1738-1832 |
3.21e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.25 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1738 VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQM-NDLQAQLEEANKE 1816
Cdd:pfam03938 5 VDMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKeQELQQLQQKAQQE 84
|
90
....*....|....*..
gi 1239919865 1817 -KQELQEKLQALQSQVE 1832
Cdd:pfam03938 85 lQKKQQELLQPIQDKIN 101
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1781-1885 |
3.25e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 40.59 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1781 DMNELMKKHKAAVAQAsrdlAQMNDLQAQLE-EANKEKQELQEKLQALQSQVEFLEQSMVDKslvsrQEAKIRELETrlE 1859
Cdd:COG2825 30 DVQRILQESPEGKAAQ----KKLEKEFKKRQaELQKLEKELQALQEKLQKEAATLSEEERQK-----KERELQKKQQ--E 98
|
90 100
....*....|....*....|....*.
gi 1239919865 1860 FERTQVKRLESLASRLKENMEKLTEE 1885
Cdd:COG2825 99 LQRKQQEAQQDLQKRQQELLQPILEK 124
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1312-1466 |
3.88e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1312 DRLETRISELTSELTDERNTGESASQLLDAEAAERLRAEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDD 1391
Cdd:PRK09039 56 DRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG--------RAGELAQELDS 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239919865 1392 DDTGGewrlkyERAMREVDftkkRLQQEFEdkleveqqnkrQLERRLGDLQADIDESQRALQQLKKKCQRLTAEL 1466
Cdd:PRK09039 128 EKQVS------ARALAQVE----LLNQQIA-----------ALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1425-1578 |
4.42e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1425 EVEQQNKRQLERRLGDLQADIDesqralqQLKKKCQRLTAELQDTKLHLEGQQVrnhELEKKQRRFDSELSQAHEEAQRE 1504
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAK-------KYQDKAAKVVDKLTDFENQTEKDQT---ALETLEKALKDLLTDEGGAIARK 179
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1505 KLqrEKLQREKDTLLAE-AFSLKQQLEEkdmdiagftqkvvsLEAELQDISSQESKDE---ASLAKVKKQLRDLEAKV 1578
Cdd:cd22656 180 EI--KDLQKELEKLNEEyAAKLKAKIDE--------------LKALIADDEAKLAAALrliADLTAADTDLDNLLALI 241
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1432-1687 |
4.43e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1432 RQLERRLGDLQADIDESQRALQQLKKKCQRLT-AELQdtklhlEGQQVrnhELEKKQRRfdseLSQAheeaqrEKLqREK 1510
Cdd:COG0497 168 RALKKELEELRADEAERARELDLLRFQLEELEaAALQ------PGEEE---ELEEERRR----LSNA------EKL-REA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1511 LQR------EKD----TLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSqeskdeaslakvkkQLRDLEAKVKD 1580
Cdd:COG0497 228 LQEalealsGGEggalDLLGQALRALERLAEYDPSLAELAERLESALIELEEAAS--------------ELRRYLDSLEF 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1581 QEEELDEqagtiqmLEQaklRLEmEMERMRQTHSKEVesrdEEVEEARQSCQKKLKQMEvQLEEEYEDKQKvlrEKRELE 1660
Cdd:COG0497 294 DPERLEE-------VEE---RLA-LLRRLARKYGVTV----EELLAYAEELRAELAELE-NSDERLEELEA---ELAEAE 354
|
250 260
....*....|....*....|....*..
gi 1239919865 1661 SKLTTLSEQVSQRDLESEKRLRKDLKR 1687
Cdd:COG0497 355 AELLEAAEKLSAARKKAAKKLEKAVTA 381
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1400-1659 |
4.47e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1400 LKYERAMREvdftKKRLQQEFEDKLEVEQQNKRQLERRLGDLQADIDESQRALQQLK-KKCQRLTAELQDTKLHLEGQQV 1478
Cdd:pfam13868 91 EEYEEKLQE----REQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKeLEKEEEREEDERILEYLKEKAE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1479 RNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEAfSLKQQLEEKDMDIAGFTQKVVSLEAELQdissqes 1558
Cdd:pfam13868 167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKL-YQEEQERKERQKEREEAEKKARQRQELQ------- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1559 kdeASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQT-HSKEVESRDEEVEEAR-QSCQKKLK 1636
Cdd:pfam13868 239 ---QAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLeHRRELEKQIEEREEQRaAEREEELE 315
|
250 260
....*....|....*....|...
gi 1239919865 1637 QMEVQLEEEYEDKQKVLREKREL 1659
Cdd:pfam13868 316 EGERLREEEAERRERIEEERQKK 338
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1572-1928 |
4.72e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.99 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1572 RDLEAKVKDQEEELDEqagTIQMLEQAKLRLEMEMERMRQThskEVESRDEEVEEArqscQKKLKQmevqleeeYEDKQK 1651
Cdd:pfam04108 52 EGLEKVLNELKKDFKQ---LLKDLDAALERLEETLDKLRNT---PVEPALPPGEEK----QKTLLD--------FIDEDS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1652 VLREKRELESKLTTLSEQVsqrdleseKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaaavk 1731
Cdd:pfam04108 114 VEILRDALKELIDELQAAQ--------ESLDSDLKRFDDDLRDLQKELESLSSPSESISLIPTLLKELESLE-------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1732 arKAMEVEMEDLHLQIDDIAKAKTALEEqlsrlqrEKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQmndLQAQLE 1811
Cdd:pfam04108 178 --EEMASLLESLTNHYDQCVTAVKLTEG-------GRAEMLEVLENDARELDDVVPELQDRLDEMENNYER---LQKLLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1812 EANKEKQELQEKLQALQsqvEFleqsmvdKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENME-------KLTE 1884
Cdd:pfam04108 246 QKNSLIDELLSALQLIA---EI-------QSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREFYEgfpsaygSLLL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1239919865 1885 ERDqrtaaenREKEQNKRLQRQLRDTKEEMGELARKEAEAsRKK 1928
Cdd:pfam04108 316 EVE-------RRREWAEKMKKILRKLAEELDRLQEEERKR-REK 351
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1415-1589 |
4.73e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1415 RLQQEFEDKLEVEQQNKRQLERRLGDLQADIDESQRALQQLKKkcQRLTAELQDTKlhlEGQQVRNHELEKKQRrfdsel 1494
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEK--ERLAAQEQKKQ---AEEAAKQAALKQKQA------ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1495 sqahEEAQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVS-----LEAELQDISSQESKDEASLAKVKK 1569
Cdd:PRK09510 135 ----EEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAeakkkAEAEAAAKAAAEAKKKAEAEAKKK 210
|
170 180
....*....|....*....|
gi 1239919865 1570 QLRDLEAKVKDQEEELDEQA 1589
Cdd:PRK09510 211 AAAEAKKKAAAEAKAAAAKA 230
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1425-1678 |
4.76e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1425 EVEQQnKRQLERRLgDLQADIDESQRALQQLKKKCQR----LTAELQDTKLHLEGQQVRNHELEKKQRRFdSELSQAHEE 1500
Cdd:PRK10246 607 EHERQ-LRLLSQRH-ELQGQIAAHNQQIIQYQQQIEQrqqqLLTALAGYALTLPQEDEEASWLATRQQEA-QSWQQRQNE 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1501 AQREKLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRD-LEAKVK 1579
Cdd:PRK10246 684 LTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTaLQASVF 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1580 DQEEE-----LDEQagTIQMLEQAKLRLEMEMERMR-------QTHSKEVESRDEEVEEAR--QSCQKKLKQMEVQLEE- 1644
Cdd:PRK10246 764 DDQQAflaalLDEE--TLTQLEQLKQNLENQRQQAQtlvtqtaQALAQHQQHRPDGLDLTVtvEQIQQELAQLAQQLREn 841
|
250 260 270
....*....|....*....|....*....|....*..
gi 1239919865 1645 ---EYEDKQKvLREKRELESKLTTLSEQVSQRDLESE 1678
Cdd:PRK10246 842 ttrQGEIRQQ-LKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1281-1644 |
4.83e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.94 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1281 EQIRSKDEEIQQLRSKLEKVEKERNELRLSNDRLETRISELTSELTDERNtGESASQLLDA-----EAAERLRAEK-EMK 1354
Cdd:pfam05701 70 EELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQGIADEAS-VAAKAQLEVAkarhaAAVAELKSVKeELE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1355 ELQTQYDALKKQMEVMEMEVMEArLIRAAEINGEVDDddtggewrlkyerAMREVDFTKKRLQQEFEDKLEVE------- 1427
Cdd:pfam05701 149 SLRKEYASLVSERDIAIKRAEEA-VSASKEIEKTVEE-------------LTIELIATKESLESAHAAHLEAEehrigaa 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1428 ---QQNKRQLERRLGDLQadiDESQRALQQ------LKKKCQRLTAELQDTKLHL----EGQQVRNHELEKKQRRFDSEL 1494
Cdd:pfam05701 215 larEQDKLNWEKELKQAE---EELQRLNQQllsakdLKSKLETASALLLDLKAELaaymESKLKEEADGEGNEKKTSTSI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1495 SQAHEEAQRE----KLQREKLQREKDTLLAEAFSLKQQLEEKDMDIAGFTQK-------VVSLEAELQDISSQeskdeas 1563
Cdd:pfam05701 292 QAALASAKKEleevKANIEKAKDEVNCLRVAAASLRSELEKEKAELASLRQRegmasiaVSSLEAELNRTKSE------- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1564 LAKVKKQLRDLEAKVKDQEEELDEQAgtiQMLEQAKLRLEMEMERMRQTHskevesrdEEVEEARQSCQKklkqMEVQLE 1643
Cdd:pfam05701 365 IALVQAKEKEAREKMVELPKQLQQAA---QEAEEAKSLAQAAREELRKAK--------EEAEQAKAAAST----VESRLE 429
|
.
gi 1239919865 1644 E 1644
Cdd:pfam05701 430 A 430
|
|
| PDZ_PDLIM-like |
cd06753 |
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
269-308 |
4.85e-03 |
|
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDLIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467235 [Multi-domain] Cd Length: 79 Bit Score: 37.89 E-value: 4.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1239919865 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06753 39 NLRPGDVILAINGESTEGMTHLEAQNKIKAATGSLSLTLE 78
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1434-1538 |
4.99e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 39.34 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1434 LERRLGDLQADIDESQRALQQLKKKCQRLTAELQDTKlhLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQ-REKLQ 1512
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEAR--AEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQaKAEIE 105
|
90 100
....*....|....*....|....*.
gi 1239919865 1513 REKDTLLAEafsLKQQLEEKDMDIAG 1538
Cdd:cd06503 106 QEKEKALAE---LRKEVADLAVEAAE 128
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
1800-1885 |
5.06e-03 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 38.74 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1800 LAQMNDLQAQLEEANKEKQELQEKLQALQSQVEFLEQS--------MVDKSLVSR-QEAKIRELETRLEFERTQVKRLES 1870
Cdd:pfam01920 1 INKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLdedtkvykLIGDVLVKQdKEEVKEQLEERKETLEKEIKTLEK 80
|
90
....*....|....*
gi 1239919865 1871 LASRLKENMEKLTEE 1885
Cdd:pfam01920 81 QLEKLEKELEELKEE 95
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1847-1955 |
5.16e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1847 QEAKIRELETRLEFERTQVKRLESLASRLKENMEklteERDQRTAaenREKEQNKRLQRQLRDTKEEMGELARKEAEASR 1926
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELE----EKDERIE---RLERELSEARSEERREIRKDREISRLDREIER 476
|
90 100 110
....*....|....*....|....*....|..
gi 1239919865 1927 KKHELE---MDLESLEAANQSLQADLKLAFKR 1955
Cdd:COG2433 477 LERELEeerERIEELKRKLERLKELWKLEHSG 508
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1443-1567 |
5.29e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1443 ADIDESQRALQQLKKKCQRLTAElQDtklhlEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQRekdtllaea 1522
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKE-QD-----EASFERLAELRDELAELEEELEALKARWEAEKELIEEIQE--------- 475
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1239919865 1523 fsLKQQLEEKDMDIAGFTQKVVSLEAELQDISS--QESKDEASLAKV 1567
Cdd:COG0542 476 --LKEELEQRYGKIPELEKELAELEEELAELAPllREEVTEEDIAEV 520
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1540-1637 |
5.30e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.49 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1540 TQKVVSLEAELQDISSQeskDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTiqMLEQAKLRLEMEMERMRQTHSKEVES 1619
Cdd:smart00935 6 VQKILQESPAGKAAQKQ---LEKEFKKRQAELEKLEKELQKLKEKLQKDAAT--LSEAAREKKEKELQKKVQEFQRKQQK 80
|
90
....*....|....*...
gi 1239919865 1620 RDEEVEEARQSCQKKLKQ 1637
Cdd:smart00935 81 LQQDLQKRQQEELQKILD 98
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1731-1836 |
5.37e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 39.09 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1731 KARKAMEVEM------EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQMN 1804
Cdd:pfam13863 4 KKREMFLVQLaldakrEEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIK 83
|
90 100 110
....*....|....*....|....*....|..
gi 1239919865 1805 DLQAQLEEANKEKQELQEKLQALQSQVEFLEQ 1836
Cdd:pfam13863 84 KLTAQIEELKSEISKLEEKLEEYKPYEDFLEK 115
|
|
| PDZ5_GRIP1-2-like |
cd06682 |
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
270-308 |
5.40e-03 |
|
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family domain PDZ5 is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467170 [Multi-domain] Cd Length: 85 Bit Score: 38.09 E-value: 5.40e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1239919865 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06682 46 LEPGDKLLAIDNIRLDNCSMEDAAQILQQAEDIVKLKIR 84
|
|
| PDZ2_APBA1_3-like |
cd06793 |
PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, ... |
273-309 |
5.42e-03 |
|
PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, APBA3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of APBA1, APBA2, APBA3, and related domains. The APBA/X11/Mint protein family includes three members: neuron specific APBA1 (also known as X11alpha and Mint1) and APBA2 (also known as X11beta and Mint2), and the ubiquitously expressed APBA3 (also known as X12gamma and Mint3). They are involved in regulating neuronal signaling, trafficking, and plasticity. They contain two PDZ domains (PDZ1 and PDZ2) which bind a variety of proteins: Arf GTPases (APBA1 and APBA2 PDZ2) and neurexin (APBA1 and APBA2 PDZ1 and 2) which are involved in vesicle docking and exocytosis; alpha1B subunit of N-type Ca2+ channel (APBA1 PDZ1) that is involved in ion channels; KIF17 (APBA1 PDZ1) that is involved in transport and traffic; and Alzheimer's disease related proteins, APP (APBA3 PDZ2), CCS (APBA1 PDZ2), NF-kappa-B/p65 (APBA2 PDZ2), presenilin-1 (APBA1 and APBA2 PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This APBA1,3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467255 [Multi-domain] Cd Length: 78 Bit Score: 37.77 E-value: 5.42e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1239919865 273 GDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06793 42 GHRIIEINGQSVVATPHEKIVQLLSNSVGEIHMKTMP 78
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1439-1583 |
5.44e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1439 GDLQADIDESQRALQQLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFDSELSQAhEEAQREKLQREKLQREKDTL 1518
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQ---AAEQERLKQLEKERLAAQEQKKQA-EEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239919865 1519 LAEAFSLKQQLEEKDMDIAGftqKVVSLEAELQDISSQESKDEaslAKVKKQLrDLEAKVKDQEE 1583
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAA---KKAAAEAKKKAEAEAAKKAA---AEAKKKA-EAEAAAKAAAE 198
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1282-1393 |
5.61e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1282 QIRSKDEEIQQLRSKLEKVEKERNELRLSND--------RLETRISELTSELTDERNTGESASQLLDAEAAERLRAEK-- 1351
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDeasferlaELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQry 484
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1239919865 1352 -EMKELQTQYDALKKQmevmemEVMEARLIRAaeingEVDDDD 1393
Cdd:COG0542 485 gKIPELEKELAELEEE------LAELAPLLRE-----EVTEED 516
|
|
| YwqH |
COG5899 |
Spore coat protein YwqH [Cell cycle control, cell division, chromosome partitioning]; |
1739-1867 |
5.93e-03 |
|
Spore coat protein YwqH [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444601 Cd Length: 134 Bit Score: 39.23 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1739 EMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNELMKKH--------KAAVAQASRDLAQ--MNDLQA 1808
Cdd:COG5899 3 YISTLNLILSSLSSKLAEKEEQIERLKRAKKELEQEQKEFSDEIRSILKPElnstwtgsLADDFDKIREEAKtaYYKIVN 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 1809 qlEEANKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFERTQVKR 1867
Cdd:COG5899 83 --DQYSEYIQSIEEKIFSLENEIESLQNE------ASSLLHKGEKAADELGDKIRKLKG 133
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1615-1819 |
6.64e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 41.37 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1615 KEVESRDEEVEEARQSCQKKLKQMEVQL-------EEEYEDKQKVLREKRELESKLTTLSEQVSQRDLESEKRLRKDLKR 1687
Cdd:TIGR02794 71 KKLEQQAEEAEKQRAAEQARQKELEQRAaaekaakQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1688 TKALLADAqimldhlKNNAPSKREIAQLKNQLEESefTCAAAVKARKAMEVEMEDLHLQiddiAKAKTALEEQlSRLQRE 1767
Cdd:TIGR02794 151 QAEEEAKA-------KAAAEAKKKAEEAKKKAEAE--AKAKAEAEAKAKAEEAKAKAEA----AKAKAAAEAA-AKAEAE 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1239919865 1768 KneiqsrleedqedmnelmKKHKAAVAQASRDLAQMNDLQAQLEEANKEKQE 1819
Cdd:TIGR02794 217 A------------------AAAAAAEAERKADEAELGDIFGLASGSNAEKQG 250
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1432-1646 |
6.88e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.51 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1432 RQLERRLGDLQADIDESQRALQQLKKKCQRLtaelqdtklhlegqqvrnhelekkqrrfdseLSQAHEEAQREKLQREKL 1511
Cdd:cd00176 36 EALLKKHEALEAELAAHEERVEALNELGEQL-------------------------------IEEGHPDAEEIQERLEEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1512 QREKDTLLAEAFSLKQQLEEKdMDIAGFTQKVVSLEAELQDISSQESKDE--ASLAKVKKQLRDLeakvKDQEEELDEQA 1589
Cdd:cd00176 85 NQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLEEKEAALASEDlgKDLESVEELLKKH----KELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1239919865 1590 GTIQMLEQAKLRLEmemERMRQTHSKEVESRDEEVEEARQSCQKKLKQMEVQLEEEY 1646
Cdd:cd00176 160 PRLKSLNELAEELL---EEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1738-1831 |
6.99e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1738 VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQSRLEEDQEDMNElmkkhKAAVAQASRDLAQMNDLQAQLEEANKEK 1817
Cdd:smart00935 4 VDVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQK-----DAATLSEAAREKKEKELQKKVQEFQRKQ 78
|
90
....*....|....
gi 1239919865 1818 QELQEKLQALQSQV 1831
Cdd:smart00935 79 QKLQQDLQKRQQEE 92
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1901-1995 |
7.09e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1901 KRLQRQLRDTKEEM-GELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEdLITSL 1979
Cdd:pfam03938 18 KAAQAQLEKKFKKRqAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQE-LLQPI 96
|
90
....*....|....*.
gi 1239919865 1980 QDMVTKYQKRKNKPEG 1995
Cdd:pfam03938 97 QDKINKAIKEVAKEKG 112
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1740-1907 |
7.28e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 40.49 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1740 MEDLHLQIDDIAKAKTALEEQ----LSRLQREKN------EIQSRLEEDQEDMNELMKKHKAAVaqasRDLA-QMNDLQA 1808
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQsqnlLSKLEIAQQkeskflENLASLKHENDNLSSMLNRKERRL----KDLEdQLSELKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1809 QLEEANKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEAK------IRELETRLE-FERTQVKRLESLASRL 1875
Cdd:pfam17078 81 SYEELTESNKQLKKRLENSSASETTLEAELerlqiqYDALVDSQNEYKdhyqqeINTLQESLEdLKLENEKQLENYQQRI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1239919865 1876 KENM----EKLTEERDQRTAAENREKEQNKRLQRQL 1907
Cdd:pfam17078 161 SSNDkdidTKLDSYNNKFKNLDNIYVNKNNKLLTKL 196
|
|
| PDZ2_GRIP1-2-like |
cd06681 |
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
270-308 |
8.04e-03 |
|
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467169 [Multi-domain] Cd Length: 89 Bit Score: 37.60 E-value: 8.04e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1239919865 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06681 49 IKPGDRLLSVDGISLHGATHAEAMSILKQCGQEATLLIE 87
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1768-2004 |
8.15e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1768 KNEIQSRLEE--DQEDMNELMKKHKAAVAQASRDLAQ-------MNDLQAQLEEANKEKQELQEKLQALQSQveflEQSM 1838
Cdd:PRK11281 38 EADVQAQLDAlnKQKLLEAEDKLVQQDLEQTLALLDKidrqkeeTEQLKQQLAQAPAKLRQAQAELEALKDD----NDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1839 VDKSLVSRQeakIRELETRLEFERTQV----KRLESLASRL------KENMEKLTEERDQRTAAENREKEQNKRLQRQLR 1908
Cdd:PRK11281 114 TRETLSTLS---LRQLESRLAQTLDQLqnaqNDLAEYNSQLvslqtqPERAQAALYANSQRLQQIRNLLKGGKVGGKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1909 DTKEEM--GELARKEAEASRKKHELEMD--LESLEAANQSL-QADLKLAFKRIGDLQAAIedemesdeNEDLITSLQDMV 1983
Cdd:PRK11281 191 PSQRVLlqAEQALLNAQNDLQRKSLEGNtqLQDLLQKQRDYlTARIQRLEHQLQLLQEAI--------NSKRLTLSEKTV 262
|
250 260
....*....|....*....|...
gi 1239919865 1984 TKYQKRK--NKPEGDSDVDSELE 2004
Cdd:PRK11281 263 QEAQSQDeaARIQANPLVAQELE 285
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1549-1836 |
8.38e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1549 ELQDISSQESKDEASLAKVKKQLRDL-------EAKVKDQEEELDEQAGTIQMLEQAKLRLE-----MEMERMRQTHSKE 1616
Cdd:pfam15905 60 ELKKKSQKNLKESKDQKELEKEIRALvqergeqDKRLQALEEELEKVEAKLNAAVREKTSLSasvasLEKQLLELTRVNE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1617 VEsrdeEVEEARQSCQKKLK--QMEV-QLEEEYEDKQKVLREKRE-LESKLttlseQVSQRDLESekrlrkdlkrtkall 1692
Cdd:pfam15905 140 LL----KAKFSEDGTQKKMSslSMELmKLRNKLEAKMKEVMAKQEgMEGKL-----QVTQKNLEH--------------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1693 adaqimldhlknnapSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAK---TALEEQLSRLQREKN 1769
Cdd:pfam15905 196 ---------------SKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKldiAQLEELLKEKNDEIE 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239919865 1770 EIQSRLEEDQEDMNELMKKHKAAVAQASRDLAQM-NDLQAQLEEANKEKQELQEKLQALQSQVEFLEQ 1836
Cdd:pfam15905 261 SLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELlREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1747-1882 |
8.81e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1747 IDDIAKAKTALEEQLSRLQREKNEIQsrLEEDQEDMNELMKKHKAAVAQASrdlaqmnDLQAQLEEANKEKQELQEKLQA 1826
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERE--LTEEEEEIRRLEEQVERLEAEVE-------ELEAELEEKDERIERLERELSE 452
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239919865 1827 LQSQvefLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKL 1882
Cdd:COG2433 453 ARSE---ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLE 505
|
|
| PDZ3_MAGI-1_3-like |
cd06733 |
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
223-300 |
9.20e-03 |
|
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467215 [Multi-domain] Cd Length: 85 Bit Score: 37.59 E-value: 9.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239919865 223 LQRRPTGdFGFSLRRTTmldrGPEGQVYrrVVHFAEPGAGTKDlalG-LVPGDRLVEINGHNVESKSRDEIVEMIRQSG 300
Cdd:cd06733 6 LRRQETG-FGFRILGGT----EEGSQVS--IGAIVPGGAADLD---GrLRTGDELLSVDGVNVVGASHHKVVDLMGNAA 74
|
|
| PDZ_MAST2 |
cd23074 |
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 2; PDZ (PSD-95 ... |
226-310 |
9.41e-03 |
|
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 2; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST2 (also known as microtubule-associated serine/threonine kinase-205 kD, MAST205) , and related domains. MAST2 belongs to the MAST family kinases, which include MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain. MAST2 may function to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Binding partners of MAST2 include beta2-syntrophin, TNF receptor-associated factor 6 (TRAF6), cAMP-regulated phosphoprotein (ARPP-16), Na+/H+ exchanger NHE3 (SLC9A3) and PTEN. MAST2 is also associated with microtubules of the spermatid manchette. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST2 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467287 [Multi-domain] Cd Length: 93 Bit Score: 37.68 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 226 RPTGDFGFSLR--RTTMLDRGPEgQVYRRVVHFAEPGAGTKdlaLGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSV 303
Cdd:cd23074 9 RAGKKYGFTLRaiRVYMGDSDVY-TVHHMVWHVEDGGPASE---AGLRQGDLITHVNGEPVHGLVHTEVVELILKSGNKV 84
|
....*..
gi 1239919865 304 RLKVQPI 310
Cdd:cd23074 85 SISTTPL 91
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1585-1829 |
9.77e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.05 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1585 LDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEVESR---DEEVEEARQSCQKKLKQMEVQLEEEYED-KQKVLREKRELE 1660
Cdd:pfam04012 17 LDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQkqlERRLEQQTEQAKKLEEKAQAALTKGNEElAREALAEKKSLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1661 SKLTTLSEQVSQRdLESEKRLRKDLKRTKAlladaqimldhlknnapskrEIAQLKNQLEeseftcaaAVKARKAMevem 1740
Cdd:pfam04012 97 KQAEALETQLAQQ-RSAVEQLRKQLAALET--------------------KIQQLKAKKN--------LLKARLKA---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239919865 1741 edlhlqiddiAKAKTALEEQLSRLQREKNEIQ-SRLEEDQEDMnelmkkhkAAVAQASRDLAQMNDLQAQLEEANKEKQE 1819
Cdd:pfam04012 144 ----------AKAQEAVQTSLGSLSTSSATDSfERIEEKIEER--------EARADAAAELASAVDLDAKLEQAGIQMEV 205
|
250
....*....|
gi 1239919865 1820 LQEKLQALQS 1829
Cdd:pfam04012 206 SEDVLARLKA 215
|
|
| HsdS |
COG0732 |
Restriction endonuclease S subunit [Defense mechanisms]; |
1485-1524 |
9.80e-03 |
|
Restriction endonuclease S subunit [Defense mechanisms];
Pssm-ID: 440496 [Multi-domain] Cd Length: 88 Bit Score: 37.35 E-value: 9.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1239919865 1485 KKQRRFDSELSQAHEEAQREKLQREKLQREKDTLLAEAFS 1524
Cdd:COG0732 43 EEQKRIVEILDSLFDKIAALEKEIEKLKELRDALLPKLFT 82
|
|
| |
