|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
81-741 |
0e+00 |
|
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: 1207.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01380 1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSSSN-AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGGSSSGeTQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd01380 161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 320 QMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARD 399
Cdd:cd01380 241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 400 ALAKKIYAHLFDFIVEQINQALHF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd01380 321 ALAKHIYAQLFDWIVDRINKALASpvKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNK-NSLFEKPRMSNSSFIIQHFADKVE 556
Cdd:cd01380 401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 557 YQCEGFLEKNRDTVYDMLVEILRASKFHlcaaffqespvpsspfgamitvksakqviKPntkhfrtTVGNKFRSSLYLLM 636
Cdd:cd01380 481 YQVEGFLEKNRDTVSEEHLNVLKASKNR-----------------------------KK-------TVGSQFRDSLILLM 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 637 ETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEV 716
Cdd:cd01380 525 ETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKT 604
|
650 660
....*....|....*....|....*
gi 568961011 717 CKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01380 605 CENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
62-752 |
0e+00 |
|
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: 963.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 62 NPDILVGENDLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVA 141
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 142 EEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNA-HVEDKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:smart00242 80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVgSVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 221 YTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDR 300
Cdd:smart00242 160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 301 ADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNE-RSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIV 379
Cdd:smart00242 240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 380 TSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:smart00242 320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 460 QQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEK 538
Cdd:smart00242 400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHH-KKHPHFSK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 539 P-RMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpsspfgamitVKSAKQVIKPnt 617
Cdd:smart00242 479 PkKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG------------VSNAGSKKRF-- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 618 khfrTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:smart00242 545 ----QTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQ 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 568961011 698 RYGILMTQQELSLS-DKKEVCKVVLHRLIQDSNQYQFGRTKIFFRAGQVAYLEKLR 752
Cdd:smart00242 621 RYRVLLPDTWPPWGgDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
70-741 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 Cd Length: 674 Bit Score: 916.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 70 NDLTALSYLHEPAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYK-SDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSN---AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF 226
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 227 DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVET 306
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 307 QKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVV 386
Cdd:pfam00063 241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 387 KPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHF-SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNL 465
Cdd:pfam00063 321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKPR-MSN 543
Cdd:pfam00063 401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRlQGE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvKSAKQVIKPNTKHFRTT 623
Cdd:pfam00063 480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN----ESGKSTPKRTKKKRFIT 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:pfam00063 556 VGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILA 635
|
650 660 670
....*....|....*....|....*....|....*....
gi 568961011 704 TQ-QELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:pfam00063 636 PKtWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
12-1181 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 908.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 12 RVWIPDPEEVWKSAEIAK-DYRAGDRVLRLLLEDGmELEyPVDPGSLPPLR-NPDILVGENDLTALSYLHEPAVLHNLRI 89
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDG-ESV-SVKKKVLGNDRiKLPKFDGVDDLTELSYLNEPAVLHNLEK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 90 RFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTV 169
Cdd:COG5022 89 RY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 170 SARYAMRYFATVSKSSSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLEKSRV 247
Cdd:COG5022 168 NAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 248 VFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKIL 327
Cdd:COG5022 248 VHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKIL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 328 AAILHLGNVQVTTVGNERSSVSeDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYA 407
Cdd:COG5022 328 AAILHIGNIEFKEDRNGAAIFS-DNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 408 HLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDF 487
Cdd:COG5022 407 NLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 488 YDNQPVIDLIEAK--MGILELLDEECLLPHGTDENWLQKLYNNF-VNKNSLFEKPRMSNSSFIIQHFADKVEYQCEGFLE 564
Cdd:COG5022 487 FDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRLnKNSNPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLD 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 565 KNRDTVYDMLVEILRASKFHLCAAFFQEspvpsspfgamiTVKSAKQVIKPntkhfrtTVGNKFRSSLYLLMETLNATTP 644
Cdd:COG5022 567 KNKDPLNDDLLELLKASTNEFVSTLFDD------------EENIESKGRFP-------TLGSRFKESLNSLMSTLNSTQP 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 645 HYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM-----TQQELSLSDKKEVCKV 719
Cdd:COG5022 628 HYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSpskswTGEYTWKEDTKNAVKS 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 720 VLHRLIQDSNQYQFGRTKIFFRAGQVAYLEKLRLDKLRQDCIMIQKHVRGWLQRRKFLRERQAALTIQRYFRGQQTVR-- 797
Cdd:COG5022 708 ILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRlv 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 798 ----KAITATALKEAWAAIILQKYCRGYLvrnlyQLIRVATITIqahTRGFLARRRYRKLLQEHKAVILQKYARAWLARR 873
Cdd:COG5022 788 dyelKWRLFIKLQPLLSLLGSRKEYRSYL-----ACIIKLQKTI---KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKK 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 874 RFQNIRRFVLNIQLTYRVQRLQKKLEDQNREnhglVEKLTSLAALRVGD----LEKVQKLEAELEKAATHRH---SYEEK 946
Cdd:COG5022 860 RFSLLKKETIYLQSAQRVELAERQLQELKID----VKSISSLKLVNLELeseiIELKKSLSSDLIENLEFKTeliARLKK 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 947 GRRYRDTVEERLSKLQKHNAELELQRERAEqmLQEKSEELKEKMDKLTrQLFDDVQKEEQQRlvleKGFELKTQAYEKQI 1026
Cdd:COG5022 936 LLNNIDLEEGPSIEYVKLPELNKLHEVESK--LKETSEEYEDLLKKST-ILVREGNKANSEL----KNFKKELAELSKQY 1008
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1027 ESLREEIKALKDERSQL-HHQLEEGQVTSDRlkGEVARLSKQAKTISEFEKEIELLQAQKIDVekhvqSQKREMRERMSe 1105
Cdd:COG5022 1009 GALQESTKQLKELPVEVaELQSASKIISSES--TELSILKPLQKLKGLLLLENNQLQARYKAL-----KLRRENSLLDD- 1080
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961011 1106 vtkqlLESYDIEDVRSRLSVedlehLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEIN 1181
Cdd:COG5022 1081 -----KQLYQLESTENLLKT-----INVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVF 1146
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
81-741 |
0e+00 |
|
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 Cd Length: 633 Bit Score: 821.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMG-DMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd00124 1 AAILHNLRERYARDL-IYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 160 SGESGAGKTVSARYAMRYFATVSKSSSNAH------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQII 233
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGSGSSKSsssassIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 234 GANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEE----FNYTRMGGNTVIEGVNDRADMVETQKT 309
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSyyylNDYLNSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNE--RSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVK 387
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 388 PMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQH--TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNL 465
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNS 544
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 545 SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKfhlcaaffqespvpsspfgamitvksakqvikpntkhfrttv 624
Cdd:cd00124 480 EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 625 gnKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd00124 518 --QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAP 595
|
650 660 670
....*....|....*....|....*....|....*...
gi 568961011 705 Q-QELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd00124 596 GaTEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
81-741 |
0e+00 |
|
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: 743.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01377 1 ASVLHNLRERY-YSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSSSNAH--------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd01377 80 GESGAGKTENTKKVIQYLASVAASSKKKKesgkkkgtLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 233 IGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTL 312
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 313 LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 393 QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQ 472
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 473 EEYMKEDIPWTLIDF-YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMS--NSSFII 548
Cdd:cd01377 400 EEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKksEAHFIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 549 QHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAkqvikpntkhFRtTVGNKF 628
Cdd:cd01377 480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGS----------FR-TVSQLH 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 629 RSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQEL 708
Cdd:cd01377 549 KEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIP 628
|
650 660 670
....*....|....*....|....*....|....
gi 568961011 709 -SLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01377 629 kGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
81-741 |
0e+00 |
|
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: 701.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd01384 1 PGVLHNLKVRY-ELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 160 SGESGAGKTVSARYAMRYFATVSK--SSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANM 237
Cdd:cd01384 80 SGESGAGKTETTKMLMQYLAYMGGraVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 238 RTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKK 317
Cdd:cd01384 160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 318 DFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDS---HLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd01384 240 EEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKsefHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEE 474
Cdd:cd01384 320 TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 475 YMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd01384 400 YTKEEIDWSYIEFVDNQDVLDLIEKKPgGIIALLDEACMFPRSTHETFAQKLYQTLKD-HKRFSKPKLSRTDFTIDHYAG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSspfgamiTVKSAKqvikpntkhFrTTVGNKFRSSLY 633
Cdd:cd01384 479 DVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREG-------TSSSSK---------F-SSIGSRFKQQLQ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDK 713
Cdd:cd01384 542 ELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDE 621
|
650 660
....*....|....*....|....*...
gi 568961011 714 KEVCKVVLHRLiqDSNQYQFGRTKIFFR 741
Cdd:cd01384 622 KAACKKILEKA--GLKGYQIGKTKVFLR 647
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
81-741 |
0e+00 |
|
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: 685.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDmdPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01383 1 PSVLHNLEYRY-SQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDS--PHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSSSNahVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTY 240
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALGGGSSG--IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 241 LLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQ 320
Cdd:cd01383 156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 321 MDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDA 400
Cdd:cd01383 236 EHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 401 LAKKIYAHLFDFIVEQINQALHFSGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKED 479
Cdd:cd01383 316 LAKAIYASLFDWLVEQINKSLEVGKRRTgRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 480 IPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNKNSLFEKPRmsNSSFIIQHFADKVEYQ 558
Cdd:cd01383 396 IDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER--GGAFTIRHYAGEVTYD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 559 CEGFLEKNRDTVYDMLVEILRASKFHLCAAF------FQESPVPSSPFGamitvKSAKQvikpntkhfRTTVGNKFRSSL 632
Cdd:cd01383 473 TSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFaskmldASRKALPLTKAS-----GSDSQ---------KQSVATKFKGQL 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 633 YLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSD 712
Cdd:cd01383 539 FKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQD 618
|
650 660
....*....|....*....|....*....
gi 568961011 713 KKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01383 619 PLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
82-741 |
0e+00 |
|
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: 677.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAEsKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01381 2 GILRNLLIRYRE-KLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVSKSSSnaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYL 241
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS--WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQM 321
Cdd:cd01381 159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 322 DVFKILAAILHLGNVQ--VTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARD 399
Cdd:cd01381 239 DIFKLLAAILHLGNIKfeATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 400 ALAKKIYAHLFDFIVEQINQALHF-SGKQH--TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYM 476
Cdd:cd01381 319 AFVKGIYGRLFIWIVNKINSAIYKpRGTDSsrTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 477 KEDIPWTLIDFYDNQPVIDLI-EAKMGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRM-SNSSFIIQHFADK 554
Cdd:cd01381 399 KEGINWQHIEFVDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGN-NKNYLKPKSdLNTSFGINHFAGV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 555 VEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvKSAKQVIkpntkhfrtTVGNKFRSSLYL 634
Cdd:cd01381 478 VFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS--------ETRKKSP---------TLSSQFRKSLDQ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 635 LMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL------MTQQEL 708
Cdd:cd01381 541 LMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLvpgippAHKTDC 620
|
650 660 670
....*....|....*....|....*....|...
gi 568961011 709 SLSDKKEVCKVVLHrliqDSNqYQFGRTKIFFR 741
Cdd:cd01381 621 RAATRKICCAVLGG----DAD-YQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
82-741 |
0e+00 |
|
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: 676.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01378 2 AINENLKKRF-ENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVSKSSSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd01378 81 ESGAGKTEASKRIMQYIAAVSGGSESevERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd01378 161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 320 QMDVFKILAAILHLGNVQVTTVGNERSSVSeDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSE---TVVKPMTRPQAIN 396
Cdd:cd01378 241 QDSIFRILAAILHLGNIQFAEDEEGNAAIS-DTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAAY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 397 ARDALAKKIYAHLFDFIVEQINQALHFSGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd01378 320 ARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 476 MKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWLQKLyNNFVNKNSLFEKP----RMSNSSFIIQ 549
Cdd:cd01378 400 VREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLTAGdATDQTFLQKL-NQLFSNHPHFECPsghfELRRGEFRIK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQEspvpsspfgamitvksakQVIKPNTKhfR-TTVGNKF 628
Cdd:cd01378 479 HYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE------------------GVDLDSKK--RpPTAGTKF 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 629 RSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGilmtqqel 708
Cdd:cd01378 539 KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK-------- 610
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 568961011 709 SLSDK---------KEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01378 611 LLSPKtwpawdgtwQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
82-741 |
0e+00 |
|
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: 659.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14883 2 GINTNLKVRYK-KDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVSKSSSnaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYL 241
Cdd:cd14883 81 ESGAGKTETTKLILQYLCAVTNNHS--WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 242 LEKSRVVFQSENERNYHIFYQLCASAQQS-EFKH-LKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd14883 159 LEQSRITFQAPGERNYHVFYQLLAGAKHSkELKEkLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 320 QMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSH-LKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINAR 398
Cdd:cd14883 239 QEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEiLKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 399 DALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKE 478
Cdd:cd14883 319 DAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 479 DIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKP--RMSNSSFIIQHFADKV 555
Cdd:cd14883 399 GINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPdrRRWKTEFGVKHYAGEV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 556 EYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFF----QESPVPSSPFGAMITVKSAkqvikpnTKHFRTTVGNKFRSS 631
Cdd:cd14883 478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtypdLLALTGLSISLGGDTTSRG-------TSKGKPTVGDTFKHQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 632 LYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ-QELSL 710
Cdd:cd14883 551 LQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRaRSADH 630
|
650 660 670
....*....|....*....|....*....|.
gi 568961011 711 SDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14883 631 KETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
81-741 |
0e+00 |
|
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: 611.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14872 1 AMIVHNLRKRFKNDQ-IYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSSSNahVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTY 240
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTNG--VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 241 LLEKSRVVFQSENERNYHIFYQLCASAQQSefKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQ 320
Cdd:cd14872 158 LLEKSRVVYQIKGERNFHIFYQLLASPDPA--SRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 321 MDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCE---LLGLETSKVAQWLCNRKI-VTSSETVVKPMTRPQAIN 396
Cdd:cd14872 236 NNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMeIKGCDPTRIPLTPAQATD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 397 ARDALAKKIYAHLFDFIVEQINQALH-FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd14872 316 ACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 476 MKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNF-VNKNSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd14872 396 QSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHaAKSTFVYAEVRTSRTEFIVKHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsspfgamitvksakQVIKPNTKHFRTTVGNKFRSSLY 633
Cdd:cd14872 476 DVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF--------------------PPSEGDQKTSKVTLGGQFRKQLS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSL-SD 712
Cdd:cd14872 536 ALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIAKRVgPD 615
|
650 660
....*....|....*....|....*....
gi 568961011 713 KKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14872 616 DRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
81-741 |
0e+00 |
|
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: 602.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14903 1 AAILYNVKKRFL-RKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 160 SGESGAGKTVSARYAMRYFATVSKSSSNAHVEdKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd14903 80 SGESGAGKTETTKILMNHLATIAGGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEfkHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 320 QMDVFKILAAILHLGNVQVTTVGN--ERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINA 397
Cdd:cd14903 237 QEVLFEVLAGILHLGQLQIQSKPNddEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 398 RDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd14903 317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQHFADKVEY 557
Cdd:cd14903 397 EGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKHYAGPVTY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 558 QCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAKQVIKPNTKhfrTTVGNKFRSSLYLLME 637
Cdd:cd14903 477 ESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALTT---TTVGTQFKDSLNELMT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 638 TLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEVC 717
Cdd:cd14903 554 TIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNTDVPVAERC 633
|
650 660
....*....|....*....|....*
gi 568961011 718 KVVLHRL-IQDSNQYQFGRTKIFFR 741
Cdd:cd14903 634 EALMKKLkLESPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
84-741 |
0e+00 |
|
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: 595.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd01382 4 LNNIRVRYSKDK-IYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 163 SGAGKTVSARYAMRYFaTVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd01382 83 SGAGKTESTKYILRYL-TESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLklgsaeefnytrmggnTVIEGVNDRADMVETQKTFTLLGFKKDFQMD 322
Cdd:cd01382 162 EKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------------LKDPLLDDVGDFIRMDKAMKKIGLSDEEKLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 323 VFKILAAILHLGNVQVTTVGNER---SSVSEDDSH-LKVFCELLGLETSKVAQWLCNRKIVTSSE----TVVK-PMTRPQ 393
Cdd:cd01382 226 IFRVVAAVLHLGNIEFEENGSDSgggCNVKPKSEQsLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLKVEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 394 AINARDALAKKIYAHLFDFIVEQINQALHFSGKQHtFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd01382 306 ANNARDALAKAIYSKLFDHIVNRINQCIPFETSSY-FIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 474 EYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKPRMSNSS------- 545
Cdd:cd01382 385 LYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQKH-KNHFRLSIPRKSKLKihrnlrd 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 546 ---FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvKSAKQVIKPNTKhfrt 622
Cdd:cd01382 464 degFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK--------DSKQKAGKLSFI---- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 623 TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd01382 532 SVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKY 611
|
650 660 670
....*....|....*....|....*....|....*....
gi 568961011 703 MTqQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01382 612 LP-PKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
84-741 |
0e+00 |
|
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: 588.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGES 163
Cdd:cd01385 4 LENLRARFKHGK-IYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 164 GAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLE 243
Cdd:cd01385 83 GSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 244 KSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDV 323
Cdd:cd01385 163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 324 FKILAAILHLGNVQV---TTVGNERSSVSEDDShLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDA 400
Cdd:cd01385 243 FSVLSAVLHLGNIEYkkkAYHRDESVTVGNPEV-LDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 401 LAKKIYAHLFDFIVEQINQAL----HFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYM 476
Cdd:cd01385 322 MAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 477 KEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKlYNNFVNKNSLFEKPRMSNSSFIIQHFADKV 555
Cdd:cd01385 402 KEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVMEPAFIIAHYAGKV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 556 EYQCEGFLEKNRDTVYDMLVEILRASK-----------------------FHLCAAFFQESPVPSS----PFGAMITVKS 608
Cdd:cd01385 481 KYQIKDFREKNLDLMRPDIVAVLRSSSsafvreligidpvavfrwavlraFFRAMAAFREAGRRRAqrtaGHSLTLHDRT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 609 AKQVIKPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPS 688
Cdd:cd01385 561 TKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSV 640
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 568961011 689 RWTYLEFYSRYGILMTQQELSlsdKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01385 641 RYTFQEFITQFQVLLPKGLIS---SKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
82-741 |
0e+00 |
|
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: 572.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14873 2 SIMYNLFQRYKRNQ-IYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSSSNA-------HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQII 233
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELslkektsCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 234 GANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLL 313
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 314 GFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSvseDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFITAGGAQVS---FKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 394 AINARDALAKKIYAHLFDFIVEQINQALHfsGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQ 472
Cdd:cd14873 318 AVDSRDSLAMALYARCFEWVIKKINSRIK--GKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 473 EEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFA 552
Cdd:cd14873 396 LEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHAN-NHFYVKPRVAVNNFGVKHYA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 553 DKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQEspvpsspfgamITVKSAKQVIKPNTKHFRTTVGNKFRSSL 632
Cdd:cd14873 475 GEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEH-----------VSSRNNQDTLKCGSKHRRPTVSSQFKDSL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 633 YLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLsD 712
Cdd:cd14873 544 HSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPE-D 622
|
650 660
....*....|....*....|....*....
gi 568961011 713 KKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14873 623 VRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
82-741 |
0e+00 |
|
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: 571.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMAR----NNRNQS 156
Cdd:cd14890 2 SLLHTLRLRY-ERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 157 IIVSGESGAGKTVSARYAMRYFATVSKSSSN-----------------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFG 219
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQgasgegeaaseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 220 KYTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVND 299
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLR-GECSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 300 RADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVgnERSSVSEDDS---HLKVFCELLGLETSKVAQWLCNR 376
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE--NDTTVLEDATtlqSLKLAAELLGVNEDALEKALLTR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 377 KIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYAN 456
Cdd:cd14890 318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 457 EKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM----GILELLDEECLLpHGTDEN--WLQKLYNNF- 529
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLDDCWRF-KGEEANkkFVSQLHASFg 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 530 -----------VNKNSLFEKPRMSNS-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcaaffqespvps 597
Cdd:cd14890 477 rksgsggtrrgSSQHPHFVHPKFDADkQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS---------------- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 598 spfgamitvksakqvikpnTKHFR-TTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVL 676
Cdd:cd14890 541 -------------------RRSIReVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMM 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961011 677 ETIRISAQSYPSRWTYLEFYSRYGILMTQQElslsDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14890 602 EAIQIRQQGFALREEHDSFFYDFQVLLPTAE----NIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
82-741 |
0e+00 |
|
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: 569.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01387 2 TVLWNLKTRY-ERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVSKSSSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMRTYL 241
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNL-VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQM 321
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 322 DVFKILAAILHLGNV----QVTTVGNERSSVSEDdSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINA 397
Cdd:cd01387 239 SIFRILASVLHLGNVyfhkRQLRHGQEGVSVGSD-AEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 398 RDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd01387 318 RDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 478 EDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKL-YNNFVNKnsLFEKPRMSNSSFIIQHFADKV 555
Cdd:cd01387 398 EQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKChYHHALNE--LYSKPRMPLPEFTIKHYAGQV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 556 EYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQ------ESPVPSSPFGAMITvksakqvIKPNTKhfrtTVGNKFR 629
Cdd:cd01387 476 WYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSshraqtDKAPPRLGKGRFVT-------MKPRTP----TVAARFQ 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 630 SSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQeLS 709
Cdd:cd01387 545 DSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALK-LP 623
|
650 660 670
....*....|....*....|....*....|....
gi 568961011 710 LSDKKEVCKVVLHRL--IQDSNQYQFGRTKIFFR 741
Cdd:cd01387 624 RPAPGDMCVSLLSRLctVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
81-741 |
0e+00 |
|
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: 562.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAESkLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01379 1 DTIVSQLQKRYSRD-QIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSSsNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTY 240
Cdd:cd01379 80 GESGAGKTESANLLVQQLTVLGKAN-NRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 241 LLEKSRVVFQSENERNYHIFYQLCAS-AQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMV---ETQKTFTLLGFK 316
Cdd:cd01379 159 LLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNSGNREkfeEIEQCFKVIGFT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 317 KDFQMDVFKILAAILHLGNVQVTTVGNE----RSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd01379 239 KEEVDSVYSILAAILHIGDIEFTEVESNhqtdKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 393 QAINARDALAKKIYAHLFDFIVEQINQAL----HFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd01379 319 EATDARDAMAKALYGRLFSWIVNRINSLLkpdrSASDEPLS-IGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 469 KLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvnKNSLFEKPRMSNSSFI 547
Cdd:cd01379 398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYWRPKSNALSFG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLcaaffqespvpsspfgamitvksakqvikpntkhFRTTVGNK 627
Cdd:cd01379 476 IHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPL----------------------------------VRQTVATY 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 628 FRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQE 707
Cdd:cd01379 522 FRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWN 601
|
650 660 670
....*....|....*....|....*....|....
gi 568961011 708 LSLSDKKEVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd01379 602 EEVVANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
81-741 |
0e+00 |
|
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: 562.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14904 1 PSILFNLKKRFAASK-PYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 160 SGESGAGKTVSARYAMRYFATVSKSSSNAHVeDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd14904 80 SGESGAGKTETTKIVMNHLASVAGGRKDKTI-AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGN---TVIEGVNDRADMVETQKTFTLLGFK 316
Cdd:cd14904 159 YLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQY--LGDSlaqMQIPGLDDAKLFASTQKSLSLIGLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 317 KDFQMDVFKILAAILHLGNVQVTTVGnERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAIN 396
Cdd:cd14904 237 NDAQRTLFKILSGVLHLGEVMFDKSD-ENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 397 ARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd14904 316 NRDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 476 MKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNK--NSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd14904 396 IREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKkdNESIDFPKVKRTQFIINHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvKSAKQVIKPNtkhfrtTVGNKFRSSLY 633
Cdd:cd14904 476 PVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEG----KSGKGTKAPK------SLGSQFKTSLS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIlMTQQELSLSDK 713
Cdd:cd14904 546 QLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAI-MFPPSMHSKDV 624
|
650 660
....*....|....*....|....*....
gi 568961011 714 KEVCKVVLHRLIQDSN-QYQFGRTKIFFR 741
Cdd:cd14904 625 RRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
81-739 |
0e+00 |
|
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: 550.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY---SGQNMGD---MDPHIFAVAEEAYKQMARNNR- 153
Cdd:cd14901 1 PSILHVLRRRF-AHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehGERRAAGerkLPPHVYAVADKAFRAMLFASRg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 154 ---NQSIIVSGESGAGKTVSARYAMRYFATVS-KSSSNAH------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTE 223
Cdd:cd14901 80 qkcDQSILVSGESGAGKTETTKIIMNYLASVSsATTHGQNaterenVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 224 ISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTV-IEGVNDRAD 302
Cdd:cd14901 160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 303 MVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQ-VTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTS 381
Cdd:cd14901 240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCfVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 382 SETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:cd14901 320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYseSTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 460 QQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSL-FE 537
Cdd:cd14901 400 QQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASFsVS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 538 KPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLcaaffqespVPSspfgamitvksakqvikpnt 617
Cdd:cd14901 480 KLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAF---------LSS-------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 618 khfrtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:cd14901 531 -----TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVH 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 568961011 698 RYGILMTQQElslSDKKEVCKVVLHR---------LIQDSNQYQFGRTKIF 739
Cdd:cd14901 606 TYSCLAPDGA---SDTWKVNELAERLmsqlqhselNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
87-741 |
4.97e-179 |
|
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: 544.35 E-value: 4.97e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 87 LRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMD---PHIFAVAEEAYKQM----ARNNRNQSIIV 159
Cdd:cd14892 7 LRRRY-ERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATASsppPHVFSIAERAYRAMkgvgKGQGTPQSIVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 160 SGESGAGKTVSARYAMRYFATVSKSSS---------NAH--VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDE 228
Cdd:cd14892 86 SGESGAGKTEASKYIMKYLATASKLAKgastskgaaNAHesIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 229 RNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQK 308
Cdd:cd14892 166 DGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKV--FCELLGLETSKVAQWLCNRKIVTSSETVV 386
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVakAAGLLGVDAAELMFKLVTQTTSTARGSVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 387 K-PMTRPQAINARDALAKKIYAHLFDFIVEQINqALH-----------FSGKQHTFIGVLDIYGFETFDVNSFEQFCINY 454
Cdd:cd14892 326 EiKLTAREAKNALDALCKYLYGELFDWLISRIN-ACHkqqtsgvtggaASPTFSPFIGILDIFGFEIMPTNSFEQLCINF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 455 ANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWLQKLYNNFVNK 532
Cdd:cd14892 405 TNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKRkTTDKQLLTIYHQTHLDK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 533 NSLFEKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKfhlcaaffqespvpsspfgamitvksakqv 612
Cdd:cd14892 485 HPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS------------------------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 613 ikpntkhfrttvgnKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTY 692
Cdd:cd14892 535 --------------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQF 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011 693 LEFYSRYGIL--------MTQQELSLSD-KKEVCKVVLHRLiqDSNQYQFGRTKIFFR 741
Cdd:cd14892 601 EEFYEKFWPLarnkagvaASPDACDATTaRKKCEEIVARAL--ERENFQLGRTKVFLR 656
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
81-741 |
2.09e-177 |
|
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: 540.43 E-value: 2.09e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSgQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14888 1 ASILHSLNLRFDIDE-IYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 160 SGESGAGKTVSARYAMRYFATVSKSS--SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN------- 230
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLACAGSEDikKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKskrmsgd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 231 --QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQS-------EFKHLKLG----------------SAEEFNY 285
Cdd:cd14888 159 rgRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAkntglsyEENDEKLAkgadakpisidmssfePHLKFRY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 286 TRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQ-VTTVGNERSSV--SEDDSHLKVFCELL 362
Cdd:cd14888 239 LTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILfENNEACSEGAVvsASCTDDLEKVASLL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 363 GLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHT-FIGVLDIYGFET 441
Cdd:cd14888 319 GVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLlFCGVLDIFGFEC 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 442 FDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDEN 520
Cdd:cd14888 399 FQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVPGGKDQG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 521 WLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKfhlcaaffqeSPVPSSPF 600
Cdd:cd14888 479 LCNKLCQKHKG-HKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK----------NPFISNLF 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 601 GAMItvkSAKQVIKPNTKHFRtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIR 680
Cdd:cd14888 548 SAYL---RRGTDGNTKKKKFV-TVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQ 623
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961011 681 ISAQSYPSRWTYLEFYSRYGILMTQQElslsdKKEVckvvlhrliqdsNQYQFGRTKIFFR 741
Cdd:cd14888 624 VSRAGYPVRLSHAEFYNDYRILLNGEG-----KKQL------------SIWAVGKTLCFFK 667
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-741 |
1.06e-168 |
|
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: 518.03 E-value: 1.06e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14920 2 SVLHNLKDRYY-SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVSKSSSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIG 234
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 235 ANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRADMVETQKTFTLLG 314
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14920 240 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14920 320 DFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNKNSLFEKPRM--SNSSFI 547
Cdd:cd14920 400 EYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQE-QGSHSKFQKPRQlkDKADFC 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE--SPVPSSPFGAMiTVKSAKQVIKPNTKHFRtTVG 625
Cdd:cd14920 479 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdRIVGLDQVTGM-TETAFGSAYKTKKGMFR-TVG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14920 557 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 636
|
650 660 670
....*....|....*....|....*....|....*..
gi 568961011 706 Q-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14920 637 AiPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
81-741 |
2.27e-166 |
|
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: 511.52 E-value: 2.27e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14913 1 PAVLYNLKDRYT-SWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVS---------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAatgdlakkkDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTF 310
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQIL-SNKKPELIELLLITTNPYDYPFISqGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 391 RPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14913 319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRM----SNSS 545
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVvkgrAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsSPFGAMITVKSAKQVIKPNTKHFRtTVG 625
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY-------ATFATADADSGKKKVAKKKGSSFQ-TVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14913 551 ALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 568961011 706 Q--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14913 631 AipEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
82-741 |
1.04e-165 |
|
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: 510.27 E-value: 1.04e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14927 2 SVLHNLRRRYS-RWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVS-------------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDE 228
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalgdgpgkkaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 229 RNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQ 307
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI-LSGKKPELQDMLLVSMNPYDYHFCSqGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 308 KTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVK 387
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 388 PMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHV 467
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN--- 543
Cdd:cd14927 400 FILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKkrk 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 544 --SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqESPVPSSpfgamiTVKSAKQVIKPNTKHFR 621
Cdd:cd14927 480 yeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY-ENYVGSD------STEDPKSGVKEKRKKAA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 622 T--TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14927 553 SfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 568961011 700 GILMTQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14927 633 RILNPSAipDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
81-741 |
1.40e-165 |
|
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: 509.13 E-value: 1.40e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14929 1 ASVLHTLRRRY-DHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSSSN----AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGAN 236
Cdd:cd14929 80 GESGAGKTVNTKHIIQYFATIAAMIESkkklGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 237 MRTYLLEKSRVVFQSENERNYHIFYQLCASAQqsEFKHLKLGSA--EEFNYTRMGGNTViEGVNDRADMVETQKTFTLLG 314
Cdd:cd14929 160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKK--ELRDLLLVSAnpSDFHFCSCGAVAV-ESLDDAEELLATEQAMDILG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14929 237 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEE 474
Cdd:cd14929 317 TYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 475 YMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQ---- 549
Cdd:cd14929 397 YRKEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHfelv 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE--SPVPSSPFGAMITVKSAKqvikpntkhFRtTVGNK 627
Cdd:cd14929 477 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENyiSTDSAIQFGEKKRKKGAS---------FQ-TVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 628 FRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL--MTQ 705
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILnpRTF 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 568961011 706 QELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14929 627 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
81-741 |
2.06e-165 |
|
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: 509.00 E-value: 2.06e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14909 1 ASVLHNLRQRY-YAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSS-------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQII 233
Cdd:cd14909 80 GESGAGKTENTKKVIAYFATVGASKktdeaakSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 234 GANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTFTL 312
Cdd:cd14909 160 GADIETYLLEKARVISQQSLERSYHIFYQI-MSGSVPGVKEMCLLSDNIYDYYIVSqGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 313 LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 393 QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQ 472
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 473 EEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN-----SSF 546
Cdd:cd14909 399 EEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpgqqaAHF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 547 IIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvksAKQVIKPNTKHFrTTVGN 626
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQ------AKGGRGKKGGGF-ATVSS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 627 KFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ 706
Cdd:cd14909 552 AYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAG 631
|
650 660 670
....*....|....*....|....*....|....*
gi 568961011 707 ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14909 632 IQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
83-741 |
1.17e-163 |
|
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: 504.56 E-value: 1.17e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP---------IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14907 3 LLINLKKRYQQDK-IFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 154 NQSIIVSGESGAGKTVSARYAMRYFATVS------------------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNS 215
Cdd:cd14907 82 KQAIVISGESGAGKTENAKYAMKFLTQLSqqeqnseevltltssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 216 SRFGKYTEISFDERNQ-IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKL---GSAEEFNYTRMGGN 291
Cdd:cd14907 162 SRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLknqLSGDRYDYLKKSNC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 292 TVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQ---VTTVGNERSSVSeDDSHLKVFCELLGLETSK 368
Cdd:cd14907 242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQfddSTLDDNSPCCVK-NKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 369 VAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSG--KQHTF------IGVLDIYGFE 440
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDekDQQLFqnkylsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 441 TFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTL--IDFYDNQPVIDLIE-AKMGILELLDEECLLPHGT 517
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDkPPIGIFNLLDDSCKLATGT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 518 DENWLQKLYNNFvNKNSLFEKPRMSNS-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvp 596
Cdd:cd14907 481 DEKLLNKIKKQH-KNNSKLIFPNKINKdTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE--- 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 597 sspfGAMITVKSAKQVIKPNTKHFrttVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVL 676
Cdd:cd14907 557 ----DGSQQQNQSKQKKSQKKDKF---LGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVL 629
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961011 677 ETIRISAQSYPSRWTYLEFYSRYGILmtqqelslsdkkevckvvlhrliqdSNQYQFGRTKIFFR 741
Cdd:cd14907 630 ESIRVRKQGYPYRKSYEDFYKQYSLL-------------------------KKNVLFGKTKIFMK 669
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
83-741 |
7.52e-159 |
|
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: 490.36 E-value: 7.52e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDM-DPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14897 3 IVQTLKSRYNKDK-FYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVSkSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYL 241
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLS-PSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRADMVETQKTFT-------LLG 314
Cdd:cd14897 161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILR-DDNRNRPVFNDSEELEYYRQMFHdltnimkLIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 315 F-KKDFQMdVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14897 240 FsEEDISV-IFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 394 AINARDALAKKIYAHLFDFIVEQINQALH----FSGK-QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14897 319 ANDSRDALAKDLYSRLFGWIVGQINRNLWpdkdFQIMtRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 469 KLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNKNSLFEKPRMSNSSFI 547
Cdd:cd14897 399 PRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNRVAFG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsspfgamitvksakqvikpnTKHfrttvgnk 627
Cdd:cd14897 478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF--------------------------TSY-------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 628 FRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQE 707
Cdd:cd14897 524 FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSN 603
|
650 660 670
....*....|....*....|....*....|....
gi 568961011 708 LSLSDKKEVCKVVLHrlIQDSNQYQFGRTKIFFR 741
Cdd:cd14897 604 KVRSDDLGKCQKILK--TAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
82-741 |
3.97e-157 |
|
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: 487.57 E-value: 3.97e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14911 2 SVLHNIKDRYY-SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVS----KSSSNAH------------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEIS 225
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAaskpKGSGAVPhpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 226 FDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRADMVE 305
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 306 TQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETV 385
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 386 VKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFN 464
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 465 LHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN 543
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAKQVIKpntKHFRtT 623
Cdd:cd14911 480 ADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRK---GMFR-T 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14911 556 VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLT 635
|
650 660 670
....*....|....*....|....*....|....*....
gi 568961011 704 TQQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14911 636 PNViPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
81-741 |
1.35e-155 |
|
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: 483.07 E-value: 1.35e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14917 1 PAVLYNLKERYA-SWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVS---------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAaigdrskkdQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTF 310
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQIL-SNKKPELLDMLLITNNPYDYAFISqGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 391 RPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSNSS 545
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRnikgKPEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPfgamitVKSAKQVIKPNTKHfrTTVG 625
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAP------IEKGKGKAKKGSSF--QTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14917 551 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 568961011 706 Q--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14917 631 AipEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
81-741 |
1.62e-153 |
|
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: 478.25 E-value: 1.62e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAY------SGQNM---GDMDPHIFAVAEEAYKQMARN 151
Cdd:cd14908 1 PAILHSLSRRFFRGI-IYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllRSQGIespQALGPHVFAIADRSYRQMMSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 152 NR-NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVE----------DKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:cd14908 80 IRaSQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgeelgklsimDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 221 YTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGS--------AEEFNYTRMGGNT 292
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDgitgglqlPNEFHYTGQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 293 VIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVS---EDDSHLKVFCELLGLETSKV 369
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIaeeGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 370 AQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ--HTFIGVLDIYGFETFDVNSF 447
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 448 EQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLP-HGTDENWLQKL 525
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 526 YNNF-------VNKNSLFEKPRM--SNSSFIIQHFADKVEYQCE-GFLEKNRDTVydmlveilraskfhlcaaffqespv 595
Cdd:cd14908 480 YETYlpeknqtHSENTRFEATSIqkTKLIFAVRHFAGQVQYTVEtTFCEKNKDEI------------------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 596 psspfgamitvksakqvikPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGV 675
Cdd:cd14908 535 -------------------PLTADSLFESGQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGV 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 676 LETIRISAQSYPSRWTYLEFYSRYGILM-TQQELSLSDK-----------KEVCKV-VLHRLIQD--------SNQYQFG 734
Cdd:cd14908 596 LEAVRVARSGYPVRLPHKDFFKRYRMLLpLIPEVVLSWSmerldpqklcvKKMCKDlVKGVLSPAmvsmknipEDTMQLG 675
|
....*..
gi 568961011 735 RTKIFFR 741
Cdd:cd14908 676 KSKVFMR 682
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
83-741 |
3.97e-153 |
|
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: 476.32 E-value: 3.97e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 83 VLHNLRIRFAESkLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQM----ARNNRNQSII 158
Cdd:cd14889 3 LLEVLKVRFMQS-NIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 159 VSGESGAGKTVSARYAMRYFATVSKSssNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMR 238
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELCRG--NSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 239 TYLLEKSRVVFQSENERNYHIFYQLCA--SAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADmvETQKTFTLLGFK 316
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAgiSAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYD--EVCNAMDMVGFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 317 KDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSH-LKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAI 395
Cdd:cd14889 237 EQEEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGwLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 396 NARDALAKKIYAHLFDFIVEQINQAL----HFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLE 471
Cdd:cd14889 317 DARDSIAKVAYGRVFGWIVSKINQLLapkdDSSVELRE-IGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLME 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 472 QEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKPRMSNSSFIIQH 550
Cdd:cd14889 396 QKEYKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKLNIHF-KGNSYYGKSRSKSPKFTVNH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 551 FADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpSSPFGAMITVKSAKQVIKPNTKHFR-TTVGNKFR 629
Cdd:cd14889 475 YAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTAT---RSRTGTLMPRAKLPQAGSDNFNSTRkQSVGAQFK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 630 SSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELS 709
Cdd:cd14889 552 HSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCEPALP 631
|
650 660 670
....*....|....*....|....*....|..
gi 568961011 710 LSdkKEVCKVVLHRliQDSNQYQFGRTKIFFR 741
Cdd:cd14889 632 GT--KQSCLRILKA--TKLVGWKCGKTRLFFK 659
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
82-741 |
8.62e-152 |
|
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: 472.98 E-value: 8.62e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14934 2 SVLDNLRQRYTNMR-IYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVSKSSSNA-----HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGAN 236
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 237 MRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKL-GSAEEFNYTRMGgNTVIEGVNDRADMVETQKTFTLLGF 315
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQG-VTVVDNMDDGEELQITDVAFDVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 316 KKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAI 395
Cdd:cd14934 240 SAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 396 NARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd14934 320 NSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 476 MKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKP-----RMSNSSFIIQ 549
Cdd:cd14934 400 KREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPkggkgKGPEAHFELV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvkSAKQviKPNTKHFrtTVGNKFR 629
Cdd:cd14934 480 HYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG---------SKKQ--KRGSSFM--TVSNFYR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 630 SSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ-EL 708
Cdd:cd14934 547 EQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNViPQ 626
|
650 660 670
....*....|....*....|....*....|...
gi 568961011 709 SLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14934 627 GFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
81-741 |
1.73e-151 |
|
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: 472.30 E-value: 1.73e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14918 1 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSSS---------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTF 310
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPDLIEMLLITTNPYDYAFVSqGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 391 RPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRM----SNSS 545
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvkgkAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsSPFGAMITVKSAKQVIKPNTKHFRtTVG 625
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF-------STYASAEADSGAKKGAKKKGSSFQ-TVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14918 551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 568961011 706 Q--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14918 631 AipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
81-741 |
6.16e-151 |
|
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: 471.08 E-value: 6.16e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14916 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSK----------SSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14916 80 GESGAGKTVNTKRVIQYFASIAAigdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKT 309
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQIL-SNKKPELLDMLLVTNNPYDYAFVSqGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPM 389
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 390 TRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 470 LEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSNS 544
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRnvkgKQEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 545 SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpSSPFGAMITVKSAKQVIKPNTKHFRtTV 624
Cdd:cd14916 479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLF------STYASADTGDSGKGKGGKKKGSSFQ-TV 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 625 GNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL-- 702
Cdd:cd14916 552 SALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnp 631
|
650 660 670
....*....|....*....|....*....|....*....
gi 568961011 703 MTQQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14916 632 AAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
82-741 |
8.95e-151 |
|
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: 470.66 E-value: 8.95e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14932 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVSKSS-----------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEFNYTRM--GGNTVIEGVNDRADMVETQK 308
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCL---EDYSKYRFlsNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHV 467
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNKNSLFEKPR--M 541
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQE-QGNNPKFQKPKklK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 542 SNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESP--VPSSPFGAMitVKSAKQVIKPNTKH 619
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDriVGLDKVAGM--GESLHGAFKTRKGM 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 620 FRtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14932 555 FR-TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 633
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 568961011 700 GILM-TQQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14932 634 EILTpNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
81-741 |
1.34e-150 |
|
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: 470.37 E-value: 1.34e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14912 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSSS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQK 308
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPELIEMLLITTNPYDYPFVSqGEISVASIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14912 239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14912 319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRM----SN 543
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVvkgkAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvKSAKQVIKPNTKHFRtT 623
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAG----GGAKKGGKKKGSSFQ-T 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14912 554 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 633
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 568961011 704 TQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14912 634 ASAipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
81-741 |
2.05e-149 |
|
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: 466.90 E-value: 2.05e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14910 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSSS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:cd14910 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQK 308
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPDLIEMLLITTNPYDYAFVSqGEITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14910 239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14910 319 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN---- 543
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgkve 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvksAKQVIKPNTKHFRtT 623
Cdd:cd14910 479 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGG------GKKGGKKKGSSFQ-T 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14910 552 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 631
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 568961011 704 TQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14910 632 ASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
81-741 |
6.28e-149 |
|
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: 464.90 E-value: 6.28e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFA-ESKLIYTYSGIILVAMNPYKQLPiygDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNN---RNQS 156
Cdd:cd14891 1 AGILHNLEERSKlDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 157 IIVSGESGAGKTVSARYAMRY------------FATVSKSSSNAH-----VEDKVLASNPITEAVGNAKTTRNDNSSRFG 219
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFlttravggkkasGQDIEQSSKKRKlsvtsLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 220 KYTEISF-DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVN 298
Cdd:cd14891 158 KFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 299 DRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQV----TTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLC 374
Cdd:cd14891 238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEALEKVIT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 375 NRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFD-VNSFEQFCIN 453
Cdd:cd14891 318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLIN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 454 YANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFvNK 532
Cdd:cd14891 398 YANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKTH-KR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 533 NSLF--EKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcaaffqespvpsspfgamitvksak 610
Cdd:cd14891 477 HPCFprPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS----------------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 611 qvikpntkhfrttvgNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRW 690
Cdd:cd14891 528 ---------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRV 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 568961011 691 TYLEFYSRYGILMTQQELSL--SDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14891 593 TYAELVDVYKPVLPPSVTRLfaENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
81-741 |
8.30e-148 |
|
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: 462.62 E-value: 8.30e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14923 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVS----------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKT 309
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQI-MSNKKPELIDLLLISTNPFDFPFVSqGEVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPM 389
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 390 TRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 470 LEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSNS 544
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKpakgKAEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 545 SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvkSAKQVIKPNTKHFRtTV 624
Cdd:cd14923 479 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSG-----GSKKGGKKKGSSFQ-TV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 625 GNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd14923 553 SAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNA 632
|
650 660 670
....*....|....*....|....*....|....*....
gi 568961011 705 QQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14923 633 SAipEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
81-741 |
1.22e-147 |
|
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: 462.28 E-value: 1.22e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14915 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSSS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQK 308
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPELIEMLLITTNPYDFAFVSqGEITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14915 239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14915 319 QTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSN 543
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKpakgKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvksAKQVIKPNTKHFRtT 623
Cdd:cd14915 479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGG------GKKGGKKKGSSFQ-T 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14915 552 VSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 631
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 568961011 704 TQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14915 632 ASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
82-741 |
5.85e-147 |
|
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: 460.64 E-value: 5.85e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14921 2 SVLHNLRERYF-SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVSKS-------SSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIG 234
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASShkgkkdtSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 235 ANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEF-NYTRMGGNTVIEGVNDRADMV-ETQKTFTL 312
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLL---EGFnNYTFLSNGFVPIPAAQDDEMFqETLEAMSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 313 LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14921 238 MGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 393 QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLE 471
Cdd:cd14921 318 QADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 472 QEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRM--SNSS 545
Cdd:cd14921 398 QEEYQREGIEWNFIDFgLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGN-HPKFQKPKQlkDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE-SPVPSSPFGAMITVKSAKQVIKPNTKHFRtTV 624
Cdd:cd14921 477 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvDRIVGLDQMAKMTESSLPSASKTKKGMFR-TV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 625 GNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd14921 556 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 635
|
650 660 670
....*....|....*....|....*....|....*...
gi 568961011 705 QQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14921 636 NAiPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
71-791 |
1.67e-146 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 464.12 E-value: 1.67e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 71 DLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:PTZ00014 100 DIGLLPHTNIPCVLDFLKHRY-LKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:PTZ00014 179 GVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRADMVETQK 308
Cdd:PTZ00014 259 GGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKY--INPKCLdVPGIDDVKDFEEVME 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTtvGNERSSVSE----DDSHLKVF---CELLGLETSKVAQWLCNRKIVTS 381
Cdd:PTZ00014 337 SFDSMGLSESQIEDIFSILSGVLLLGNVEIE--GKEEGGLTDaaaiSDESLEVFneaCELLFLDYESLKKELTVKVTYAG 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 382 SETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:PTZ00014 415 NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQK 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 462 QFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR 540
Cdd:PTZ00014 495 NFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGkSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKV 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 541 MSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGamitvksAKQVIkpntkhf 620
Cdd:PTZ00014 575 DSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLA-------KGQLI------- 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 621 rttvGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYG 700
Cdd:PTZ00014 641 ----GSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFK 716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 701 ILmtqqELSLS-----DKKEVCKVVLHRLIQDSNQYQFGRTKIFFR---AGQVAYLEKLRLDKLRQDCIMIQKHVRGWLQ 772
Cdd:PTZ00014 717 YL----DLAVSndsslDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKK 792
|
730
....*....|....*....
gi 568961011 773 RRKFLRERQAALTIQRYFR 791
Cdd:PTZ00014 793 KRKVRKNIKSLVRIQAHLR 811
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-741 |
5.14e-143 |
|
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: 449.93 E-value: 5.14e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14930 2 SVLHNLRERYY-SGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVSKSSSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIG 234
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGrkepgvpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 235 ANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTviEGVNDRADMVETQKTFTLLG 314
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS--SPGQERELFQETLESLRVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14930 239 FSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14930 319 DFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNKNSLFEKPR--MSNSSFI 547
Cdd:cd14930 399 EYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQE-QGGHPKFQRPRhlRDQADFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFF----------QESPVPSSPFGAmitvksakqviKPNT 617
Cdd:cd14930 478 VLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivgleQVSSLGDGPPGG-----------RPRR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 618 KHFRtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:cd14930 547 GMFR-TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 568961011 698 RYGILMTQQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14930 626 RYEILTPNAiPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
83-739 |
1.29e-141 |
|
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: 445.83 E-value: 1.29e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 83 VLHNLRIRFAESkLIYTYSGIILVAMNPYKQLP-IYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYK--QMARNNRNQSII 158
Cdd:cd14880 3 VLRCLQARYTAD-TFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 159 VSGESGAGKTVSARYAMRYFATVSKSSSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14880 82 VSGESGAGKTWTSRCLMKFYAVVAASPTSweshkiaERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEgvndraDMVE-TQKTF 310
Cdd:cd14880 162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNLEE------DCFEvTREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSS---VSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVV- 386
Cdd:cd14880 236 LHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVf 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 387 -KPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHT-FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFN 464
Cdd:cd14880 316 kKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTtFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 465 LHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN 543
Cdd:cd14880 396 AHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSpISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 544 S-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvPSSPfgamitVKSAKQVIKPNTKHFRT 622
Cdd:cd14880 476 EpSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLF-----PANP------EEKTQEEPSGQSRAPVL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 623 TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14880 545 TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL 624
|
650 660 670
....*....|....*....|....*....|....*..
gi 568961011 703 MTQQELSLSDKKEVCKVVLHrliqdSNQYQFGRTKIF 739
Cdd:cd14880 625 RRLRPHTSSGPHSPYPAKGL-----SEPVHCGRTKVF 656
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
81-741 |
1.52e-141 |
|
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: 447.48 E-value: 1.52e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDaiIHAYSGQNMGDMD--PHIFAVAEEAYKQMARNN------ 152
Cdd:cd14895 1 PAFVDYLAQRYGVDQ-VYCRSGAVLIAVNPFKHIPGLYD--LHKYREEMPGWTAlpPHVFSIAEGAYRSLRRRLhepgas 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 153 -RNQSIIVSGESGAGKTVSARYAMRYFATVSK--------SSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTE 223
Cdd:cd14895 78 kKNQTILVSGESGAGKTETTKFIMNYLAESSKhttatsssKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 224 ISF-----DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFK--HLKLGSAEEFNYTRMGGNTVI-E 295
Cdd:cd14895 158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLelQLELLSAQEFQYISGGQCYQRnD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 296 GVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVqvtTVGNERSSVSEDDS---------------------H 354
Cdd:cd14895 238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNV---LFVASSEDEGEEDNgaasapcrlasaspssltvqqH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 355 LKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALhfSGKQHT----- 429
Cdd:cd14895 315 LDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS--PQRQFAlnpnk 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 430 --------FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK- 500
Cdd:cd14895 393 aankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRp 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 501 MGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNS--SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEIL 578
Cdd:cd14895 473 SGIFSLLDEECVVPKGSDAGFARKLYQRLQE-HSNFSASRTDQAdvAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 579 -RASKFHLCAAFfqespvpsSPFGAmiTVKSAKQVIKPNTKHFRTT-----VGNKFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd14895 552 gKTSDAHLRELF--------EFFKA--SESAELSLGQPKLRRRSSVlssvgIGSQFKQQLASLLDVVQQTQTHYIRCIKP 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 653 NDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ---ELSLSDKKEVCKVvlhrliqdsN 729
Cdd:cd14895 622 NDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKnasDATASALIETLKV---------D 692
|
730
....*....|..
gi 568961011 730 QYQFGRTKIFFR 741
Cdd:cd14895 693 HAELGKTRVFLR 704
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-741 |
1.76e-141 |
|
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: 446.08 E-value: 1.76e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14919 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVSKS----SSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANM 237
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASShkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 238 RTYLLEKSRVVFQSENERNYHIFYQLCASAQQsefkHLKLG-SAEEFNYTRM--GGNTVIEGVNDRADMVETQKTFTLLG 314
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGE----HLKTDlLLEPYNKYRFlsNGHVTIPGQQDKDMFQETMEAMRIMG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14919 237 IPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14919 317 DFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNKNSLFEKPRM--SNSSFI 547
Cdd:cd14919 397 EYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQE-QGTHPKFQKPKQlkDKADFC 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE-SPVPSSPFGAMITVKSAKQVIKPNTKHFRtTVGN 626
Cdd:cd14919 476 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvDRIIGLDQVAGMSETALPGAFKTRKGMFR-TVGQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 627 KFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ 706
Cdd:cd14919 555 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 634
|
650 660 670
....*....|....*....|....*....|....*.
gi 568961011 707 -ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14919 635 iPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
82-741 |
5.80e-140 |
|
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: 442.20 E-value: 5.80e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd15896 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVSKS-----------SSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEFNYTRM--GGNTVIEGVNDRADMVETQK 308
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL---ENYNNYRFlsNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHV 467
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIE---AKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN 543
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 544 SS-FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQ--ESPVPSSPFGAMITVKSAkqvIKPNTKHF 620
Cdd:cd15896 478 EAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKdvDRIVGLDKVSGMSEMPGA---FKTRKGMF 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 621 RtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYG 700
Cdd:cd15896 555 R-TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 568961011 701 ILMTQQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd15896 634 ILTPNAiPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
81-739 |
2.32e-139 |
|
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: 439.42 E-value: 2.32e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSG-QNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14876 1 PCVLDFLKHRYLKNQ-IYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 160 SGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd14876 80 SGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRADMVETQKTFTLLGFKKD 318
Cdd:cd14876 160 FLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKF--LNPKCLdVPGIDDVADFEEVLESLKSMGLTEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 319 FQMDVFKILAAILHLGNVQVTT-----VGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14876 238 QIDTVFSIVSGVLLLGNVKITGkteqgVDDAAAISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 394 AINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14876 318 AEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 474 EYMKEDIPWTLIDFYDNQPVID-LIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQHFA 552
Cdd:cd14876 398 LYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSNINFIVVHTI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 553 DKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvKSAK-QVIkpntkhfrttvGNKFRSS 631
Cdd:cd14876 478 GDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG--------KIAKgSLI-----------GSQFLKQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 632 LYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILmtqqELSLS 711
Cdd:cd14876 539 LESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL----DLGIA 614
|
650 660 670
....*....|....*....|....*....|...
gi 568961011 712 -DKKEVCKVVLHRLIQDSN----QYQFGRTKIF 739
Cdd:cd14876 615 nDKSLDPKVAALKLLESSGlsedEYAIGKTMVF 647
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
81-741 |
2.48e-139 |
|
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: 441.64 E-value: 2.48e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAY--------SGQNMGDMDPHIFAVAEEAYKQMARN 151
Cdd:cd14902 1 AALLQALSERF-EHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 152 NR-NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVED--------KVLASNPITEAVGNAKTTRNDNSSRFGKYT 222
Cdd:cd14902 80 ERrNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGsdaveigkRILQTNPILESFGNAQTIRNDNSSRFGKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 223 EISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEF----NYTRMGGNTVIEGVN 298
Cdd:cd14902 160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYellnSYGPSFARKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 299 DRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVS---EDDSHLKVFCELLGLETSKVAQWLCN 375
Cdd:cd14902 240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAvtaASRFHLAKCAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 376 RKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQAL-HFSGKQH--------TFIGVLDIYGFETFDVNS 446
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEInYFDSAVSisdedeelATIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 447 FEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKL 525
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 526 YNNFVNKNslfekprmsnsSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamiT 605
Cdd:cd14902 480 YRYHGGLG-----------QFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSP------G 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 606 VKSAKQVIKPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQS 685
Cdd:cd14902 543 ADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHG 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 686 YPSRWTYLEFYSRYGILMTQQELSLSDKK-------------EVCKVVLHRLIQDSNQ---------------------- 730
Cdd:cd14902 623 YSVRLAHASFIELFSGFKCFLSTRDRAAKmnnhdlaqalvtvLMDRVLLEDGVEREEKnpgaltavtgdgsgtafendcr 702
|
730
....*....|....
gi 568961011 731 ---YQFGRTKIFFR 741
Cdd:cd14902 703 rkdVQVGRTLVFCK 716
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
83-734 |
1.29e-135 |
|
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: 431.71 E-value: 1.29e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQN-MGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14906 3 ILNNLGKRY-KSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSSS---------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNQqqnnnnnnnNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 232 II-GANMRTYLLEKSRVVFQSENER-NYHIFYQLCASAQQSEFKHLKLGS-AEEFNY-------------TRMGGNTVIE 295
Cdd:cd14906 162 KIdGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNdPSKYRYldarddvissfksQSSNKNSNHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 296 GVNDRADMVETQKTFTL-LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVF---CELLGLETSKVAQ 371
Cdd:cd14906 242 NKTESIESFQLLKQSMEsMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvSKLLGYIESVFKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 372 WLCNRKIVTSSETVV--KPMTRPQAINARDALAKKIYAHLFDFIVEQINQ-----------ALHFSGKQHTFIGVLDIYG 438
Cdd:cd14906 322 ALLNRNLKAGGRGSVycRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIFG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 439 FETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGT 517
Cdd:cd14906 402 FENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKGS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 518 DENWLQKLYNNFVNKNSLFEKPrMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQEspvps 597
Cdd:cd14906 482 EQSLLEKYNKQYHNTNQYYQRT-LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQ----- 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 598 spfgamitvksaKQVIKPNTKHFRT---TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACG 674
Cdd:cd14906 556 ------------QITSTTNTTKKQTqsnTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVG 623
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 675 VLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSlSDKKEVCKVVLHRLIQDSNQYQFG 734
Cdd:cd14906 624 VLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRK-NNNNPKLASQLILQNIQSKLKTMG 682
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
83-741 |
5.66e-135 |
|
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: 427.77 E-value: 5.66e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMG-----DMDPHIFAVAEEAYKQMARNNRNQS 156
Cdd:cd14886 3 VIDILRDRFAKDK-IYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 157 IIVSGESGAGKTVSARYAMRYFATVSKSSSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGAN 236
Cdd:cd14886 82 CIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 237 MRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFK 316
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKLFSK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 317 KDFQmDVFKILAAILHLGNVQ---VTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14886 241 NEID-SFYKCISGILLAGNIEfseEGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 394 AINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14886 320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 474 EYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLPHGTDENWLQKLYNNFvnKNSLFEKPRMSNSSFIIQHFA 552
Cdd:cd14886 400 EYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSCKSKI--KNNSFIPGKGSQCNFTIVHTA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 553 DKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSspfgamitvksakqvikPNTKHfrTTVGNKFRSSL 632
Cdd:cd14886 478 ATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNED-----------------GNMKG--KFLGSTFQLSI 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 633 YLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSL-- 710
Cdd:cd14886 539 DQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQna 618
|
650 660 670
....*....|....*....|....*....|..
gi 568961011 711 -SDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14886 619 gEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
83-702 |
1.88e-131 |
|
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: 417.79 E-value: 1.88e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAY---------SGQNMGD--MDPHIFAVAEEAYKQMAR 150
Cdd:cd14900 3 ILSALETRFYAQK-IYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssSTRNKGSdpMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 151 --NNR--NQSIIVSGESGAGKTVSARYAMRYFA---------TVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSR 217
Cdd:cd14900 82 glNGVmsDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 218 FGKYTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKhlklgsaeEFNYTRMggntviegv 297
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK--------RDMYRRV--------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 298 NDRADMVetqktftllGFKKDFQMDVFKILAAILHLGNV--QVTTVGNERSSvseDDSHLKVFCE--------LLGLETS 367
Cdd:cd14900 225 MDAMDII---------GFTPHERAGIFDLLAALLHIGNLtfEHDENSDRLGQ---LKSDLAPSSIwsrdaaatLLSVDAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 368 KVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHF--SGKQHT---FIGVLDIYGFETF 442
Cdd:cd14900 293 KLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMddSSKSHGglhFIGILDIFGFEVF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 443 DVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENW 521
Cdd:cd14900 373 PKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 522 LQKLYNNFVNkNSLFEKPRMSNSS--FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRAskfhlcaaffqespvpssp 599
Cdd:cd14900 453 ASKLYRACGS-HPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVY------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 600 fgamitvksakqvikpntkhfrttvGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETI 679
Cdd:cd14900 513 -------------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAV 567
|
650 660
....*....|....*....|...
gi 568961011 680 RISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14900 568 RVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
81-741 |
5.67e-130 |
|
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: 414.56 E-value: 5.67e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14896 1 SSVLLCLKKRF-HLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSSSNAHVE--DKVLasnPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMR 238
Cdd:cd14896 80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRqpEDVL---PILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKD 318
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 319 FQMDVFKILAAILHLGNVQVTTVGNERSSVSE--DDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAIN 396
Cdd:cd14896 236 ELTAIWAVLAAILQLGNICFSSSERESQEVAAvsSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 397 ARDALAKKIYAHLFDFIVEQINQALHFSGKQHTF--IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEE 474
Cdd:cd14896 316 ARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 475 YMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd14896 396 CQRELLPWVPIPQPPRESCLDLLVDQpHSLLSILDDQTWLSQATDHTFLQKCHYHHGD-HPSYAKPQLPLPVFTVRHYAG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpsspfgamitvkSAKQVIKPNtkhfRTTVGNKFRSSLY 633
Cdd:cd14896 475 TVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEA--------------EPQYGLGQG----KPTLASRFQQSLG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDK 713
Cdd:cd14896 537 DLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDR 616
|
650 660
....*....|....*....|....*...
gi 568961011 714 KEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14896 617 ERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
82-699 |
8.80e-117 |
|
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: 381.37 E-value: 8.80e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYS---GQNMGDM-------DPHIFAVAEEAYKQMAR 150
Cdd:cd14899 2 SILNALRLRY-ERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhNSQFGDRvtstdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 151 NNRNQSIIVSGESGAGKTVSARYAMRYFATVS----------------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDN 214
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCgtgnnnltnsesisppASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 215 SSRFGKYTEISF-DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQL------CASAQQSEFKHLKLGSAEEFNYTR 287
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 288 MGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNER------------SSVSEDDSHL 355
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGddtvfadearvmSSTTGAFDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 356 KVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGK--------- 426
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 427 ------QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK 500
Cdd:cd14899 401 vddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 501 -MGILELLDEECLLPHGTDENWLQKLYNNFVNKNslfEKPRMSNSS-------FIIQHFADKVEYQCEGFLEKNRDTVYD 572
Cdd:cd14899 481 pIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKN---SHPHFRSAPliqrttqFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 573 MLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAKQVIKPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKP 637
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 568961011 653 NDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14899 638 NDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
83-741 |
7.18e-113 |
|
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: 369.14 E-value: 7.18e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 83 VLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQM-ARNNRNQSIIVS 160
Cdd:cd14875 3 LLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVS----KSSSNAHVEDKVLA----SNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd14875 83 GESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 233 -IGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHL-KLGSAEEFNYTRmGGNTVI------EGVNDRADMV 304
Cdd:cd14875 163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLN-GGNTFVrrgvdgKTLDDAHEFQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 305 ETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVsEDDSHLKVFCELLGLETSKVAQWLcnrkIVTSSET 384
Cdd:cd14875 242 NVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQI-ADETPFLTACRLLQLDPAKLRECF----LVKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 385 VVKPMTRPQ-AINARDALAKKIYAHLFDFIVEQINQALHFSG--KQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:cd14875 317 LVTILANKTeAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 462 QFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR 540
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 541 MS-NSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcAAFFQESPVPSSPFGAmitvksakqvikpntkH 619
Cdd:cd14875 477 STiPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNS-----TDEFIRTLLSTEKGLA----------------R 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 620 FRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14875 536 RKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYF 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 568961011 700 GILMTQQELSL---SDKKEVCKVVL---HRLIQ-DSNQYQFGRTKIFFR 741
Cdd:cd14875 616 YLIMPRSTASLfkqEKYSEAAKDFLayyQRLYGwAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
82-740 |
4.93e-112 |
|
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: 366.10 E-value: 4.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAESkLIYTY-SGIILVAMNPYKQLPIYGDAIIHAY-------SGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14879 5 AITSHLASRFRSD-LPYTRlGSSALVAVNPYKYLSSNSDASLGEYgseyydtTSGSKEPLPPHAYDLAARAYLRMRRRSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 154 NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAH-VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd14879 84 DQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 233 IGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYT-RMGGNTVIEGV--NDRADMVETQKT 309
Cdd:cd14879 164 IGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLaSYGCHPLPLGPgsDDAEGFQELKTA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTT--VGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNR-KIVtSSEtVV 386
Cdd:cd14879 244 LKTLGFKRKHVAQICQLLAAILHLGNLEFTYdhEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKtKLV-RKE-LC 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 387 KPMTRP-QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFD---VNSFEQFCINYANEKLQQ 461
Cdd:cd14879 322 TVFLDPeGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDfATFISLLDFPGFQNRSstgGNSLDQFCVNFANERLHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 462 QFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMG--ILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKP 539
Cdd:cd14879 402 YVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGglLGILDDQTRRMPKKTDEQMLEALRKRFGNHSSFIAVG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 540 RMS----NSSFIIQHFADKVEYQCEGFLEKNRDtvydmlveilraskfHLCAAFfqespvpsspfgaMITVKSAKQvikp 615
Cdd:cd14879 482 NFAtrsgSASFTVNHYAGEVTYSVEGFLERNGD---------------VLSPDF-------------VNLLRGATQ---- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 616 ntkhfrttvgnkFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEF 695
Cdd:cd14879 530 ------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEF 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 568961011 696 YSRYGILMTQQELSLSDKKevckvVLHRLIQDSNQYQFGRTKIFF 740
Cdd:cd14879 598 CERYKSTLRGSAAERIRQC-----ARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
82-702 |
9.59e-109 |
|
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: 354.97 E-value: 9.59e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQlpIYGDAIIHAYSgQNMGDMDPHIFAVAEEAYKQMARNNrNQSIIVSG 161
Cdd:cd14898 2 ATLEILEKRYASGK-IYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFatVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDerNQIIGANMRTYL 241
Cdd:cd14898 77 ESGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 242 LEKSRVVFQSENERNYHIFYQLCASAqqsefkhlKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKdFQm 321
Cdd:cd14898 153 LEKSRVTHHEKGERNFHIFYQFCASK--------RLNIKNDFIDTSSTAGNKESIVQLSEKYKMTCSAMKSLGIAN-FK- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 322 DVFKILAAILHLGNVQVTtvgNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDAL 401
Cdd:cd14898 223 SIEDCLLGILYLGSIQFV---NDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNSM 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 402 AKKIYAHLFDFIVEQINQALHFSGKQHtfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIP 481
Cdd:cd14898 300 ARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGIE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 482 WTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKL--YNN-FVNKNslfekprmSNSSFIIQHFADKVEYQ 558
Cdd:cd14898 378 WPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNgFINTK--------ARDKIKVSHYAGDVEYD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 559 CEGFLEKNRDtvydmlveilrasKFHLcaaffqespvpsSPFGAMITvksakqvikpNTKHFRTTVGNKFRSSLYLLMET 638
Cdd:cd14898 450 LRDFLDKNRE-------------KGQL------------LIFKNLLI----------NDEGSKEDLVKYFKDSMNKLLNS 494
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961011 639 LNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14898 495 INETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
81-741 |
5.17e-102 |
|
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: 341.24 E-value: 5.17e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAES-------KLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14887 1 PNLLENLYQRYNKAyinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 154 NQSIIVSGESGAGKTVSARYAMRYFATVS---KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSefKHLKLGSAEEFNYTrmggntviegvndrADMVETQKTF 310
Cdd:cd14887 161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAA--ATQKSSAGEGDPES--------------TDLRRITAAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLC---NRKIVTSSETVVK 387
Cdd:cd14887 225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADRSHSSEVKClssGLKVTEASRKHLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 388 PMTRP--------------------------------QAINARDALAKKIYAHLFDFIVEQINQALHFSGK--------- 426
Cdd:cd14887 305 TVARLlglppgvegeemlrlalvsrsvretrsffdldGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsded 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 427 -----QHTFIGVLDIYGFETF---DVNSFEQFCINYANEKlqqqfnLHVFKLEQ----EE--YMKEDIPWTLIDFYDNQP 492
Cdd:cd14887 385 tpsttGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANER------LHCFLLEQlilnEHmlYTQEGVFQNQDCSAFPFS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 493 -------------VIDLI-EAKMGILELLDEECLLPH----------GTDENW------------LQKLYNNFVNKNSLF 536
Cdd:cd14887 459 fplastltsspssTSPFSpTPSFRSSSAFATSPSLPSslsslssslsSSPPVWegrdnsdlfyekLNKNIINSAKYKNIT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 537 EKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRAskfhlCAAFFQESPVPSSPFGAMITVKsakqvikpn 616
Cdd:cd14887 539 PALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLA-----CSTYTRLVGSKKNSGVRAISSR--------- 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 617 tkhfRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFY 696
Cdd:cd14887 605 ----RSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELW 680
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 568961011 697 SRYGILMTQQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14887 681 RRYETKLPMALREALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
83-741 |
4.32e-98 |
|
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: 327.74 E-value: 4.32e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLpiygDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd14937 3 VLNMLALRY-KKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 163 SGAGKTVSARYAMRYFatVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd14937 78 SGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTrMGGNTVIEGVNDRADMVETQKTFTLLGFKkDFQMD 322
Cdd:cd14937 156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYI-VNKNVVIPEIDDAKDFGNLMISFDKMNMH-DMKDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 323 VFKILAAILHLGNVQVTTV-GNERSSVSE-DDSHLKVFCE---LLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINA 397
Cdd:cd14937 234 LFLTLSGLLLLGNVEYQEIeKGGKTNCSElDKNNLELVNEisnLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 398 RDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd14937 314 CKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENwLQKLYNNFVNKNSLFEKPRMS-NSSFIIQHFADKVE 556
Cdd:cd14937 394 EDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDES-IVSVYTNKFSKHEKYASTKKDiNKNFVIKHTVSDVT 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 557 YQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvksakqVIKPNTKHFrttvgnKFRSSLYLLM 636
Cdd:cd14937 473 YTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSES-------------LGRKNLITF------KYLKNLNNII 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 637 ETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAqSYPSRWTYLEFYSRYGIL--MTQQELSLSDKK 714
Cdd:cd14937 534 SYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISF-FFQYKYTFDVFLSYFEYLdySTSKDSSLTDKE 612
|
650 660
....*....|....*....|....*..
gi 568961011 715 EVCKVVLHRLiqDSNQYQFGRTKIFFR 741
Cdd:cd14937 613 KVSMILQNTV--DPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
82-741 |
4.90e-95 |
|
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: 319.84 E-value: 4.90e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAY---SGQNMGDMDPHIFAVAEEAYKQMARNNRNQSII 158
Cdd:cd14878 2 SLLYEIQKRFGNNQ-IYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 159 VSGESGAGKTVSARYAMRYFATVSKSSSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF-DERNQIIGANM 237
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTT-FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 238 RTYLLEKSRVVFQSENERNYHIFYQLC--ASAQQSEFKHLKLGSAEEF-NYTRMGGNTVIEGVNDRADMVETQKTFTLLG 314
Cdd:cd14878 160 YTYMLEKSRLVSQPPGQSNFLIFYLLMdgLSAEEKYGLHLNNLCAHRYlNQTMREDVSTAERSLNREKLAVLKQALNVVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14878 240 FSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 395 INARDALAKKIYAHLFDFIVEQINQALH----FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14878 320 EFYRDLLAKSLYSRLFSFLVNTVNCCLQsqdeQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 471 EQEEYMKEDIPWTLIDFYDNQP-VIDLIEAK-MGILELLDEECLLPHGTDENWLQKL--YNNFVNKNSLFEK-------- 538
Cdd:cd14878 400 EQTECVQEGVTMETAYSPGNQTgVLDFFFQKpSGFLSLLDEESQMIWSVEPNLPKKLqsLLESSNTNAVYSPmkdgngnv 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 539 -PRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpsspfgamitvksakqvikpnt 617
Cdd:cd14878 480 aLKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSK------------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 618 khfRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:cd14878 536 ---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLS 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 568961011 698 RYGILMtqqELSLSDKK-----EVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd14878 613 RYKPLA---DTLLGEKKkqsaeERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
82-740 |
1.15e-91 |
|
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: 309.74 E-value: 1.15e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFAESKLiYTYSGIILVAMNPYKQLPiygdAIIHAYSGQNMGDMdPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14881 2 AVMKCLQARFYAKEF-FTNVGPILLSVNPYRDVG----NPLTLTSTRSSPLA-PQLLKVVQEAVRQQSETGYPQAIILSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 162 ESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDErnqiiGANMRT-- 239
Cdd:cd14881 76 TSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-----GALYRTki 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 240 --YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKT-FTLLGFK 316
Cdd:cd14881 151 hcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAcLGILGIP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 317 kdFqMDVFKILAAILHLGNVQVTTvGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAIN 396
Cdd:cd14881 231 --F-LDVVRVLAAVLLLGNVQFID-GGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMSNM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 397 ARDALAKKIYAHLFDFIVEQIN--QALHFSGKQHT---FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLE 471
Cdd:cd14881 307 TRDALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 472 QEEYMKEDIPWTL-IDFYDNQPVIDLIEA-KMGILELLDEECLlPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQ 549
Cdd:cd14881 387 IESCRDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKPQDDRMFGIR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRAskfHLCAaffqespvpsspFGamitvksakqvIKPNTKHFRTTVGNkfr 629
Cdd:cd14881 466 HFAGRVVYDASDFLDTNRDVVPDDLVAVFYK---QNCN------------FG-----------FATHTQDFHTRLDN--- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 630 sslylLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELS 709
Cdd:cd14881 517 -----LLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 568961011 710 LSDKKEV--CKVVL-----HRLIQDSN---QYQFGRTKIFF 740
Cdd:cd14881 592 RVEEKALedCALILqfleaQPPSKLSSvstSWALGKRHIFL 632
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
81-732 |
1.50e-89 |
|
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: 305.29 E-value: 1.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYS-------GQNMGDMDPHIFAVAEEAYKQMARNN 152
Cdd:cd14884 1 PNVLQNLKNRYLKNK-IYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksnsaASAAPFPKAHIYDIANMAYKNMRGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 153 RNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd14884 80 KRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 233 I---------GANMRTYLLEKSRVVFQSENERNYHIFYQL---CASAQQSE------FKHLKLGSAEEFNYTR-MGGNTV 293
Cdd:cd14884 160 QknmfngcfrNIKIKILLLEINRCIAHNFGERNFHVFYQVlrgLSDEDLARrnlvrnCGVYGLLNPDESHQKRsVKGTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 294 IEGVNDRADMVETQK---TFTLL-------GFKKDFQMDVFKILAAILHLGNvqvttvgnerssvseddSHLKVFCELLG 363
Cdd:cd14884 240 LGSDSLDPSEEEKAKdekNFVALlhglhyiKYDERQINEFFDIIAGILHLGN-----------------RAYKAAAECLQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 364 LETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQAlHFSGKQ-------------HTF 430
Cdd:cd14884 303 IEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRN-VLKCKEkdesdnediysinEAI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 431 IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEE 510
Cdd:cd14884 382 ISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAKIFRRLDDITKL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 511 CLLPHG-TDENWLQKLYNNfVNKNSLFEK-------PRMSNSS----------FIIQHFADKVEYQCEGFLEKNRDTVYD 572
Cdd:cd14884 462 KNQGQKkTDDHFFRYLLNN-ERQQQLEGKvsygfvlNHDADGTakkqnikkniFFIRHYAGLVTYRINNWIDKNSDKIET 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 573 MLVEILRASKfhlcaaffqespvpsspfgaMITVKSAkqVIKPNTKHFrTTVGNKFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd14884 541 SIETLISCSS--------------------NRFLREA--NNGGNKGNF-LSVSKKYIKELDNLFTQLQSTDMYYIRCFLP 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 653 NDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRwtylefysrygilMTQQELSLSDKKEVCKVVLHRLIQDSNQYQ 732
Cdd:cd14884 598 NAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHK-------------IPKKETAAALKEQIAKELEKCNSNTDIEYQ 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
83-741 |
4.64e-87 |
|
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: 298.45 E-value: 4.64e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 83 VLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd01386 3 VLHTLRQRYG-ANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 163 SGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd01386 82 SGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRA-DMVETQKTFTLLGFKKDFQM 321
Cdd:cd01386 162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAaAFSKLQAAMKTLGISEEEQR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 322 DVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRK---IVTSSETVVKPMTRPQ----- 393
Cdd:cd01386 242 AIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHlsgGPQQSTTSSGQESPARsssgg 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 394 ----AINARDALAKKIYAHLFDFIVEQINQALhfSGKQHTF--IGVLDIYGFEtfdvN----------SFEQFCINYANE 457
Cdd:cd01386 322 pkltGVEALEGFAAGLYSELFAAVVSLINRSL--SSSHHSTssITIVDTPGFQ----NpahsgsqrgaTFEDLCHNYAQE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 458 KLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDN-QPVIDLI---------------EAKMGILELLDEECLLPHGTDENW 521
Cdd:cd01386 396 RLQLLFHERTFVAPLERYKQENVEVDFDLPELSpGALVALIdqapqqalvrsdlrdEDRRGLLWLLDEEALYPGSSDDTF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 522 LQKLYNNF----VNKNSLFEKPRMSNSSFIIQHF--ADKVEYQCEGFLeknrdtvydmlveilRASKFHLCA----AFFQ 591
Cdd:cd01386 476 LERLFSHYgdkeGGKGHSLLRRSEGPLQFVLGHLlgTNPVEYDVSGWL---------------KAAKENPSAqnatQLLQ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 592 ESpvpSSPFGAmitVKsakqvikpntkhfRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPN------DEKMPFEFDSKR 665
Cdd:cd01386 541 ES---QKETAA---VK-------------RKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPAAGDE 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 666 IVQ------QLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEVC--KVVLHRLIQ----DSNQYQF 733
Cdd:cd01386 602 LLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVAdeRKAVEELLEeldlEKSSYRI 681
|
....*...
gi 568961011 734 GRTKIFFR 741
Cdd:cd01386 682 GLSQVFFR 689
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
93-741 |
3.91e-81 |
|
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: 281.21 E-value: 3.91e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 93 ESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSgQNMGdMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSA 171
Cdd:cd14905 12 KKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN-QRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 172 RYAMRYFATVSKSSSNaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLEKSRVVFQS 251
Cdd:cd14905 90 KIIIQYLLTTDLSRSK-YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 252 ENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAIL 331
Cdd:cd14905 169 KGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFII 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 332 HLGNVQVTTvGNERSSVsEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSEtvvkpmtrpqAINARDALAKKIYAHLFD 411
Cdd:cd14905 249 ILGNVTFFQ-KNGKTEV-KDRTLIESLSHNITFDSTKLENILISDRSMPVNE----------AVENRDSLARSLYSALFH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 412 FIVEQINQALHFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPW-TLIDFYDN 490
Cdd:cd14905 317 WIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISFKDN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 491 QPVIDLIEAKMGILELLDEECllpHGTDENWLQKLyNNFVNKNSLF-EKPrmsnSSFIIQHFADKVEYQCEGFLEKNRDT 569
Cdd:cd14905 396 EESVEMMEKIINLLDQESKNI---NSSDQIFLEKL-QNFLSRHHLFgKKP----NKFGIEHYFGQFYYDVRGFIIKNRDE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 570 VYDML-----------------VEILRASKFHLCAAFFQESPVPSSPFGAMITVKSA-----KQVIKPNTKH------FR 621
Cdd:cd14905 468 ILQRTnvlhknsitkylfsrdgVFNINATVAELNQMFDAKNTAKKSPLSIVKVLLSCgsnnpNNVNNPNNNSggggggGN 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 622 TTVGNKFRSSLYLLMETLNATTP------HYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEF 695
Cdd:cd14905 548 SGGGSGSGGSTYTTYSSTNKAINnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIF 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 568961011 696 YSRYGILMTQQE--LSLSDKKEVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd14905 628 FDRFSFFFQNQRnfQNLFEKLKENDINIDSILPPP--IQVGNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
82-741 |
9.37e-79 |
|
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: 272.90 E-value: 9.37e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYsgqnmgdmdpHIFAVAEEAYKQMARNNRN-QSIIVS 160
Cdd:cd14874 2 GIAQNLHERF-KKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 161 GESGAGKTVSARYAMRYFATVSKSS-SNAHVEdkvlASNPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMR- 238
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKvTTKHSS----AIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKy 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNT--VIEGVNDRADMVETQKTftlLGFK 316
Cdd:cd14874 146 TVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTenIQSDVNHFKHLEDALHV---LGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 317 KDFQMDVFKILAAILHLGNVQVTTVGNerSSVSED------DSHLKVFCELLGLEtskVAQWLcnrKIVTSSETVVKPMT 390
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTKRN--PNVEQDvveignMSEVKWVAFLLEVD---FDQLV---NFLLPKSEDGTTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 391 RPQAINARDALAKKIYAHLFDFIVEQInqALHFSGKQHT-FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14874 295 LNAALDNRDSFAMLIYEELFKWVLNRI--GLHLKCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 470 LEQEEYMKEDIPwtlIDF-----YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKnSLFEKPRMSN 543
Cdd:cd14874 373 DQLVDYAKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDR-SSYGKARNKE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 544 S-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQespvpSSPFGAMITVKSAKQVIKPNTKHfrt 622
Cdd:cd14874 449 RlEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE-----SYSSNTSDMIVSQAQFILRGAQE--- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 623 tvgnkfrsslylLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14874 521 ------------IADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 568961011 703 MTQQELSLSDKKEVCKVVLH-RLIQDSNQYQFGRTKIFFR 741
Cdd:cd14874 589 LPGDIAMCQNEKEIIQDILQgQGVKYENDFKIGTEYVFLR 628
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
83-741 |
1.37e-77 |
|
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: 270.07 E-value: 1.37e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd14882 3 ILEELRHRY-LMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 163 SGAGKTVSARYAMRYFATVSKSSSNahVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRG--ATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 243 EKSRVVFQSENERNYHIFYQLCASAQQSE-FKHLKLGSAEEFNYTRMGGNTVIEGV----NDRADMVETQKTFTLLGFKK 317
Cdd:cd14882 160 EKLRVSTTDGNQSNFHIFYYFYDFIEAQNrLKEYNLKAGRNYRYLRIPPEVPPSKLkyrrDDPEGNVERYKEFEEILKDL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 318 DFQMD----VFKILAAILHLGNVQVttVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14882 240 DFNEEqletVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 394 AINARDALAKKIYAHLFDFIVEQINQALHFS----GKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14882 318 ARDARDVLASTLYSRLVDWIINRINMKMSFPravfGDKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 470 LEQEEYMKEDIPWTLIDFYDNQPVID-LIEAKMGILELLDEECLLPHGTdenwlQKLYNNFVNKNSLFEKPrMSNSSFII 548
Cdd:cd14882 397 SEMLEMEEEDIPTINLRFYDNKTAVDqLMTKPDGLFYIIDDASRSCQDQ-----NYIMDRIKEKHSQFVKK-HSAHEFSV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 549 QHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcaaffqespvpsspfgamiTVKSAKQVIKPNTKHFRTTVGNKF 628
Cdd:cd14882 471 AHYTGRIIYDAREFADKNRDFVPPEMIETMRSS-----------------------LDESVKLMFTNSQVRNMRTLAATF 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 629 RSSLYLLMETL----NATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd14882 528 RATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAF 607
|
650 660 670
....*....|....*....|....*....|....*..
gi 568961011 705 QQELSLSDKKEVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd14882 608 DFDETVEMTKDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
84-699 |
3.43e-66 |
|
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: 239.49 E-value: 3.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQN----------MGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14893 4 LYTLRARYRMEQ-VYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 154 NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAH-----------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYT 222
Cdd:cd14893 83 DQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPdsegasgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 223 EISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQ--SEFKHLKLG-SAEEFNYTRMGGNTVIEGVND 299
Cdd:cd14893 163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMNkCVNEFVMLKQADPLATNFALD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 300 RADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQV---------------TTVGNERSSVSEDDSHLKVFCELLGL 364
Cdd:cd14893 243 ARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggansTTVSDAQSCALKDPAQILLAAKLLEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 365 ETSKVAQWLCNRKIVT--SSETV--VKPMTRPQAINARDALAKKIYAHLFDFIVEQINQAL-----HFSGK----QHTFI 431
Cdd:cd14893 323 EPVVLDNYFRTRQFFSkdGNKTVssLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdRYEKSniviNSQGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 432 GVLDIYGFETFD--VNSFEQFCINYANEK-----LQQQFNLHVFKLEQEEYMKED--IPWTLIDF-YDNQPVIDLIEAK- 500
Cdd:cd14893 403 HVLDMVGFENLTpsQNSFDQLCFNYWSEKvhhfyVQNTLAINFSFLEDESQQVENrlTVNSNVDItSEQEKCLQLFEDKp 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 501 MGILELLDEECLLPHGTDENWLQKLY--NNFV------NKNSLFEKPRMSNSS-----FIIQHFADKVEYQCEGFLEKNR 567
Cdd:cd14893 483 FGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVgglsrpNMGADTTNEYLAPSKdwrllFIVQHHCGKVTYNGKGLSSKNM 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 568 DTVYDMLVEILRASKFHLCAAffqespVPSSPFGAMITVKSAKQVIKpntkhfRTTVGNKFRSSLY-------------- 633
Cdd:cd14893 563 LSISSTCAAIMQSSKNAVLHA------VGAAQMAAASSEKAAKQTEE------RGSTSSKFRKSASsaresknitdsaat 630
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961011 634 -------LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14893 631 dvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
104-227 |
1.33e-44 |
|
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: 159.05 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 104 ILVAMNPYKQLPIYGDA-IIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVS 182
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568961011 183 KSSSNA--------------HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFD 227
Cdd:cd01363 81 FNGINKgetegwvylteitvTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
81-739 |
5.17e-43 |
|
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: 168.86 E-value: 5.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQN-MGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14938 1 PSVLYHLKERF-KNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 160 SGESGAGKTVSARYAMRYFATVSKSS------SNAHVEDKVLAS----------------NPITEAVGNAKTTRNDNSSR 217
Cdd:cd14938 80 SGESGSGKSEIAKNIINFIAYQVKGSrrlptnLNDQEEDNIHNEentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 218 FGKYTEISFDERnQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEefNYTRMGGNTVIEGV 297
Cdd:cd14938 160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIE--NYSMLNNEKGFEKF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 298 NDRAD-MVETQKTFTLLgFKKDFQMD-VFKILAAILHLGNVQVTTV---------------------------GNERSSV 348
Cdd:cd14938 237 SDYSGkILELLKSLNYI-FDDDKEIDfIFSVLSALLLLGNTEIVKAfrkksllmgknqcgqninyetilseleNSEDIGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 349 SEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSeTVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQH 428
Cdd:cd14938 316 DENVKNLLLACKLLSFDIETFVKYFTTNYIFNDS-ILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNIN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 429 TF---IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTL-IDFYDNQPVID-LIEAKMGI 503
Cdd:cd14938 395 INtnyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 504 LELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR---MSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRA 580
Cdd:cd14938 475 LFSLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDditGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 581 SKFHLCAAFFQESPVPSSpfgAMITVKSAKQVIKPNTKHFRTTVGNK-------FRSSLYLLMETLNATTPHYVRCIKPN 653
Cdd:cd14938 555 SENEYMRQFCMFYNYDNS---GNIVEEKRRYSIQSALKLFKRRYDTKnqmavslLRNNLTELEKLQETTFCHFIVCMKPN 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 654 DEK-MPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSrygILMTQQElslsDKKEVCKVVLHRLIQDSNQYQ 732
Cdd:cd14938 632 ESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLS---IFDIKNE----DLKEKVEALIKSYQISNYEWM 704
|
....*..
gi 568961011 733 FGRTKIF 739
Cdd:cd14938 705 IGNNMIF 711
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
187-705 |
1.29e-35 |
|
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: 146.81 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 187 NAHVEDK---VLASNPITEAVGNAKTTRNDNSSRFGKYT--EISFDERN---QIIGANMRTYLLEKSRVVFQ------SE 252
Cdd:cd14894 239 NPHAAKKlsiVLDSNIVLEAFGHATTSMNLNSSRFGKMTtlQVAFGLHPwefQICGCHISPFLLEKSRVTSErgresgDQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 253 NERNYHIFYQLCASAQQSEF-----KHLKLGSAEEFNYTRMG-GNTVIEGVNDRADM----VETQKT----FTLLGFKKD 318
Cdd:cd14894 319 NELNFHILYAMVAGVNAFPFmrllaKELHLDGIDCSALTYLGrSDHKLAGFVSKEDTwkkdVERWQQvidgLDELNVSPD 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 319 FQMDVFKILAAILHLGNVQVT--TVGNE--RSSVSEDDSHLKVfCELLGL-ETSKVAQWLCNRKIV--TSSETVVKPMTR 391
Cdd:cd14894 399 EQKTIFKVLSAVLWLGNIELDyrEVSGKlvMSSTGALNAPQKV-VELLELgSVEKLERMLMTKSVSlqSTSETFEVTLEK 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 392 PQAINARDALAKKIYAHLFDFIVEQINQALHFS-----GKQH------------TFIGVLDIYGFETFDVNSFEQFCINY 454
Cdd:cd14894 478 GQVNHVRDTLARLLYQLAFNYVVFVMNEATKMSalstdGNKHqmdsnasapeavSLLKIVDVFGFEDLTHNSLDQLCINY 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 455 ANEKLQQqfnlhvfKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQ-----KLY-NN 528
Cdd:cd14894 558 LSEKLYA-------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNAQQeekrnKLFvRN 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 529 FVNKNS--LFEKPR-MSNSS-----------FIIQHFADKVEYQCEGFLEKNRDTVY-DMLVEILRASKFHLCAAFFQES 593
Cdd:cd14894 631 IYDRNSsrLPEPPRvLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYaNLLVGLKTSNSSHFCRMLNESS 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 594 PVPSSPFGAMITVKSAKQVIKpNTKHFrttVGnKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRAC 673
Cdd:cd14894 711 QLGWSPNTNRSMLGSAESRLS-GTKSF---VG-QFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQ 785
|
570 580 590
....*....|....*....|....*....|....*....
gi 568961011 674 GV---LETIRISAQSYP----SRWTYLefySRYGILMTQ 705
Cdd:cd14894 786 RLirqMEICRNSSSSYSaidiSKSTLL---TRYGSLLRE 821
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
848-1155 |
6.34e-15 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 80.14 E-value: 6.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 848 RRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNiQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQ 927
Cdd:COG1196 213 ERYQELKAELRELELALLLAKLKELRKELEELEEELS-RLEEELEELQEELEEAEKEIEELKSELEELR-------EELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 928 KLEAELEKAATHRHSYEEKGRRYRDTVEE---RLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTrqLFDDVQKE 1004
Cdd:COG1196 285 ELQEELLELKEEIEELEGEISLLRERLEElenELEELEERLEELKEKIEALKEELEERETLLEELEQLLA--ELEEAKEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1005 EQQRL-VLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQA 1083
Cdd:COG1196 363 LEEKLsALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELE 442
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961011 1084 QKIDVEKHVQSQKREMRERMSEVTKQLLE-SYDIEDVRSRLSvEDLEHLNEDGELWFAYEGLKKATRVLESHF 1155
Cdd:COG1196 443 ELNEELEELEEQLEELRDRLKELERELAElQEELQRLEKELS-SLEARLDRLEAEQRASQGVRAVLEALESGL 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
891-1207 |
6.20e-14 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 77.06 E-value: 6.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 891 VQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELEL 970
Cdd:COG1196 167 VSKYKERKEEAERKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELRELELALLLAKLKELRKELEELEE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 971 QRERAEQMLQEKSEELKEKMDKLT--RQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLE 1048
Cdd:COG1196 247 ELSRLEEELEELQEELEEAEKEIEelKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1049 EGQVTSDRLKGEVARLSKQ----AKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLE-SYDIEDVRSRL 1123
Cdd:COG1196 327 ELKEKIEALKEELEERETLleelEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEiRNELEELKREI 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1124 svEDLEhlnedgelwfayEGLKKATRVLESHFQSQKDcYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTR 1203
Cdd:COG1196 407 --ESLE------------ERLERLSERLEDLKEELKE-LEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAE 471
|
....
gi 568961011 1204 LTSE 1207
Cdd:COG1196 472 LQEE 475
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
893-1200 |
2.01e-13 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 75.52 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 893 RLQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERlsKLQKHNAELELQR 972
Cdd:COG1196 657 RNKRSSLAQKRELKELEEELAELE-------AQLEKLEEELKSLKNELRSLEDLLEELRRQLEEL--ERQLEELKRELAA 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 973 -ERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTqAYEKQIESLREEIKALKDERSQLHHQLEEGQ 1051
Cdd:COG1196 728 lEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALA-KLKEEIEELEEKRQALQEELEELEEELEEAE 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1052 VTSDRLKGEVARLSKQaktISEFEKEIELLQAQKIDVEkhvqSQKREMRERMSEVTKQlLESYDIEDVRSRLSVEDLEHl 1131
Cdd:COG1196 807 RRLDALERELESLEQR---RERLEQEIEELEEEIEELE----EKLDELEEELEELEKE-LEELKEELEELEAEKEELED- 877
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961011 1132 nEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHE 1200
Cdd:COG1196 878 -ELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLET 945
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
837-1199 |
1.03e-12 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 72.87 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 837 IQAHTRGFLARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTY-----RVQRLQKKLEDQNRENHGLVEK 911
Cdd:COG0419 234 IEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELeekieRLEELEREIEELEEELEGLRAL 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 912 LTSLAALR---VGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKE 988
Cdd:COG0419 314 LEELEELLeklKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQE 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 989 KMDKLT--RQLFDDVQ--KEEQQRLVLEKGFELKTqaYEKQIESLREEIKALKdERSQLHHQLEEGQVTSDRLKGEVARL 1064
Cdd:COG0419 394 LKEELAelSAALEEIQeeLEELEKELEELERELEE--LEEEIKKLEEQINQLE-SKELMIAELAGAGEKCPVCGQELPEE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1065 SKQaKTISEFEKEIELLQaQKIDVEKHvqsqKREMRERMSEVTKQL---LESYDIEDVRSRLSVEDLEHLNEDGElwfay 1141
Cdd:COG0419 471 HEK-ELLELYELELEELE-EELSREKE----EAELREEIEELEKELrelEEELIELLELEEALKEELEEKLEKLE----- 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011 1142 EGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRH 1199
Cdd:COG0419 540 NLLEELEELKEKLQLQQLKEELRQLEDRLQELKELLEELRLLRTRKEELEELRERLKE 597
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
890-1207 |
2.23e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.63 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNRENHGLVEKLTSLAALR--VGDLEK---------VQKLEAELEKAATHRHSYEEKgrryRDTVEERL 958
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHELYEEAKakKEELERlkkrltgltPEKLEKELEELEKAKEEIEEE----ISKITARI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 959 SKLQKHNAEL-------------------ELQRERAEQMLQEKSEELK------EKMDKLTRQLFDDVQKEEQQRLVLEK 1013
Cdd:PRK03918 415 GELKKEIKELkkaieelkkakgkcpvcgrELTEEHRKELLEEYTAELKriekelKEIEEKERKLRKELRELEKVLKKESE 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1014 GFELKTQAyeKQIESLREEIKALKDErsqlhhQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhvq 1093
Cdd:PRK03918 495 LIKLKELA--EQLKELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK--- 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1094 sQKREMRERMSEVTKQLLES--YDIEDVRSRLsvEDLEhlnedgELWFAYEGLKKATRVLESHFQSQKDCYE------KE 1165
Cdd:PRK03918 564 -KLDELEEELAELLKELEELgfESVEELEERL--KELE------PFYNEYLELKDAEKELEREEKELKKLEEeldkafEE 634
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568961011 1166 IEGLNFKVVHLSQEINHLQKLFREETdiNESIRHEVTRLTSE 1207
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKKYSEEE--YEELREEYLELSRE 674
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
893-1207 |
4.18e-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: 70.86 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 893 RLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVE---ERLSKLQKHNAELE 969
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 970 LQRERAEQMLQEKSEELKEkmdkltrqlfDDVQKEEQQRLVlekgfelktQAYEKQIESLREEIKALKDERSQLHhqlEE 1049
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAE----------AEAEIEELEAQI---------EQLKEELKALREALDELRAELTLLN---EE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1050 GQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEkHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLE 1129
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-AEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1130 HLNEDGElwfAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEIN--------HLQKLFREETDINESIRHEV 1201
Cdd:TIGR02168 898 ELSEELR---ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeeysltleEAEALENKIEDDEEEARRRL 974
|
....*.
gi 568961011 1202 TRLTSE 1207
Cdd:TIGR02168 975 KRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
850-1079 |
7.31e-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: 70.09 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 850 YRKLLQEHKAVILQKYARAWLARRRFQNIRRfvLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKL 929
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLER--QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 930 EAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQ---MLQEKSEELKEKMDKLTRQLFDDVQ---- 1002
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERledRRERLQQEIEELLKKLEEAELKELQaele 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1003 KEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHH----------QLEEGQVTSD----------RLKGEVA 1062
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlqarldslerLQENLEGFSEgvkallknqsGLSGILG 523
|
250
....*....|....*..
gi 568961011 1063 RLSKQAKTISEFEKEIE 1079
Cdd:TIGR02168 524 VLSELISVDEGYEAAIE 540
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1134 |
8.23e-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: 70.09 E-value: 8.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 847 RRRYRKL-LQEHKAVILQKYarawlaRRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENH-------GLVEKLTSLAAL 918
Cdd:TIGR02168 199 ERQLKSLeRQAEKAERYKEL------KAELRELELALLVLRLEELREELEELQEELKEAEEeleeltaELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 919 RVGDLE---KVQKLEAELEKAATHRHSYEEKGRRYRdtveERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLT- 994
Cdd:TIGR02168 273 RLEVSEleeEIEELQKELYALANEISRLEQQKQILR----ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEe 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 995 -RQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLR-------EEIKALKDERSQLHHQLEEGQVTSDRLKGEV----- 1061
Cdd:TIGR02168 349 lKEELESLEAELEELEAELEELESRLEELEEQLETLRskvaqleLQIASLNNEIERLEARLERLEDRRERLQQEIeellk 428
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011 1062 ----ARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKqllESYDIEDVRSRL-SVEDLEHLNED 1134
Cdd:TIGR02168 429 kleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA---AERELAQLQARLdSLERLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
922-1198 |
1.59e-11 |
|
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: 69.32 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 922 DLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEE-----------RLSKLQKHNAELELQRERAEQMLQEKSEELKEKM 990
Cdd:TIGR02168 187 NLDRLEDILNELERQLKSLERQAEKAERYKELKAElrelelallvlRLEELREELEELQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 991 DKLT----RQLFDDVQKEEQQRLVLEKGFELktQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSK 1066
Cdd:TIGR02168 267 EKLEelrlEVSELEEEIEELQKELYALANEI--SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1067 Q-----------AKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTK-----QLLESY--DIEDVRSRLSVEDL 1128
Cdd:TIGR02168 345 KleelkeeleslEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnneiERLEARleRLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1129 EHL-----NEDGELWFAYEGLKKATRVLESHF----------QSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDI 1193
Cdd:TIGR02168 425 ELLkkleeAELKELQAELEELEEELEELQEELerleealeelREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
....*
gi 568961011 1194 NESIR 1198
Cdd:TIGR02168 505 SEGVK 509
|
|
| HEC1 |
COG5185 |
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ... |
943-1207 |
2.75e-11 |
|
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227512 [Multi-domain] Cd Length: 622 Bit Score: 67.70 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 943 YEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEkSEELKEKMdKLTRQLFDDVQKEEQQRLVLEKGFELKTQAY 1022
Cdd:COG5185 251 YEPSEQELKLGFEKFVHIINTDIANLKTQNDNLYEKIQE-AMKISQKI-KTLREKWRALKSDSNKYENYVNAMKQKSQEW 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1023 -------EKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKgevarlsKQAKTISEFEKEIELLQAQKIDVEKHVQSQ 1095
Cdd:COG5185 329 pgkleklKSEIELKEEEIKALQSNIDELHKQLRKQGISTEQFE-------LMNQEREKLTRELDKINIQSDKLTKSVKSR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1096 KREMRERMSEVTKqLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYE-------GLKKATRVLESHFQSQKDCYEKEIEG 1168
Cdd:COG5185 402 KLEAQGIFKSLEK-TLRQYDSLIQNITRSRSQIGHNVNDSSLKINIEqlfpkgsGINESIKKSILELNDEIQERIKTEEN 480
|
250 260 270
....*....|....*....|....*....|....*....
gi 568961011 1169 LNFKvvhLSQEINHLQKLFREETDINESIRHEVTRLTSE 1207
Cdd:COG5185 481 KSIT---LEEDIKNLKHDINELTQILEKLELELSEANSK 516
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
849-1136 |
2.80e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 68.20 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 849 RYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQR--LQKKLEDQNRENHGLVEKLTSLAALRVGDLEKV 926
Cdd:pfam15921 268 RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmYMRQLSDLESTVSQLRSELREAKRMYEDKIEEL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 927 QK----LEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQmLQEKSEELKEKMDKLTRQLfDDVQ 1002
Cdd:pfam15921 348 EKqlvlANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKR-LWDRDTGNSITIDHLRREL-DDRN 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1003 KEEQQRLVLEKGFELKTQA-YEKQIESLREEIKALkDERSQLHHQLEEgqvTSDRLKGEVARLSKQAKTISEFEKEIEll 1081
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGqMERQMAAIQGKNESL-EKVSSLTAQLES---TKEMLRKVVEELTAKKMTLESSERTVS-- 499
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568961011 1082 qaqkiDVEKHVQSQKREMRERMSEVTKqllesydiedVRSR--LSVEDLEHLNEDGE 1136
Cdd:pfam15921 500 -----DLTASLQEKERAIEATNAEITK----------LRSRvdLKLQELQHLKNEGD 541
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
886-1204 |
4.63e-11 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 67.43 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 886 QLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAathrhsyeekgrryrdtvEERLSKLQKHN 965
Cdd:COG1196 720 ELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESL------------------EEALAKLKEEI 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 966 AELELQRERAEQMLQEKSEELKEkMDKLTRQLFDDVQKEEQQRlvlekgfelktQAYEKQIESLREEIKALKDERSQLHH 1045
Cdd:COG1196 782 EELEEKRQALQEELEELEEELEE-AERRLDALERELESLEQRR-----------ERLEQEIEELEEEIEELEEKLDELEE 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1046 QLEEGQvtsDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSV 1125
Cdd:COG1196 850 ELEELE---KELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEV 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1126 E--DLEHLNEDGELWFAYEGLKKATRVLeshfqsqkdcyEKEIEGL---NFKVVhlsQEINHLQKLFREETDINESIRHE 1200
Cdd:COG1196 927 ElpELEEELEEEYEDTLETELEREIERL-----------EEEIEALgpvNLRAI---EEYEEVEERYEELKSQREDLEEA 992
|
....
gi 568961011 1201 VTRL 1204
Cdd:COG1196 993 KEKL 996
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
848-1079 |
6.28e-11 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 67.05 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 848 RRYRKLLQEHKAVILQKYARAwlaRRRFQNIRRFVLNiqLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQ 927
Cdd:COG1196 785 EEKRQALQEELEELEEELEEA---ERRLDALERELES--LEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 928 KLEAELEKAATHRHSYEEKGRRYRDTVEE---RLSKLQKHNAELELQRERAEQMLqeksEELKEKMDKLtrqlfdDVQKE 1004
Cdd:COG1196 860 ELKEELEELEAEKEELEDELKELEEEKEEleeELRELESELAELKEEIEKLRERL----EELEAKLERL------EVELP 929
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961011 1005 EQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIE 1079
Cdd:COG1196 930 ELEEELEEEYEDTLETELEREIERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELD 1004
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
849-1185 |
2.90e-10 |
|
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: 65.09 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 849 RYRKLLQEhkaviLQKYaRAWLARRRFQNIRRfvlniqltyRVQRLQKKLEDQNREnhglVEKLTslaalrvgdlEKVQK 928
Cdd:TIGR02169 212 RYQALLKE-----KREY-EGYELLKEKEALER---------QKEAIERQLASLEEE----LEKLT----------EEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 929 LEAELEKAATHRhsyEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELkEKMDKLTRQLFDDVQKEEQQR 1008
Cdd:TIGR02169 263 LEKRLEEIEQLL---EELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL-EDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1009 LVLEKgfelKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVarlskqaktiSEFEKEIELLQaQKIDV 1088
Cdd:TIGR02169 339 EELER----EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL----------KDYREKLEKLK-REINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1089 EKHVQSQKREMRERMSEvtkqllesyDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLEShFQSQKDCYEKEIEG 1168
Cdd:TIGR02169 404 LKRELDRLQEELQRLSE---------ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-LAADLSKYEQELYD 473
|
330
....*....|....*..
gi 568961011 1169 LNFKVVHLSQEINHLQK 1185
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQR 490
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
896-1133 |
3.68e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 896 KKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERA 975
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 976 EQmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEkgfelktqAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSD 1055
Cdd:PRK02224 352 DD-LEERAEELREEAAELESELEEAREAVEDRREEIE--------ELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1056 RLKGEVARLSKQAKTISE-FEKEIELLQA-------QKIDVEKHVQSQKrEMRERMSEVTKQLLesyDIEDVRSRLS--V 1125
Cdd:PRK02224 423 ELREREAELEATLRTARErVEEAEALLEAgkcpecgQPVEGSPHVETIE-EDRERVEELEAELE---DLEEEVEEVEerL 498
|
....*...
gi 568961011 1126 EDLEHLNE 1133
Cdd:PRK02224 499 ERAEDLVE 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
890-1129 |
3.70e-10 |
|
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: 64.70 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEK-GRRYRDTVEERLSKLQKHNAEL 968
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlNDLEARLSHSRIPEIQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 969 ELQRERAEQMLQEKSEELKEKmDKLTRQLFDDVQKEEQQRLVLE---KGFELKTQAYEKQIESLREEIKALKDERSQLHH 1045
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRL-TLEKEYLEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1046 QLEEgqvtsdrLKGEVARLSKQaktISEFEKEIELLQAQkIDVEKHVQSQKREMRERMSEVTKQLLESY--DIEDVRSRL 1123
Cdd:TIGR02169 883 RLGD-------LKKERDELEAQ---LRELERKIEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKgeDEEIPEEEL 951
|
....*.
gi 568961011 1124 SVEDLE 1129
Cdd:TIGR02169 952 SLEDVQ 957
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
851-1123 |
7.09e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 851 RKLLQEHKAVILQKYarawlaRRRFQNIRRFVLNI-----QLTYRVQRLQKKLEDQNR--ENHGLVEKLTSL-AALRVGD 922
Cdd:PRK03918 443 RELTEEHRKELLEEY------TAELKRIEKELKEIeekerKLRKELRELEKVLKKESEliKLKELAEQLKELeEKLKKYN 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 923 LEKVQKLEAELEKaaTHRHSYEEKGRryRDTVEERLSKLQkhnaELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQ 1002
Cdd:PRK03918 517 LEELEKKAEEYEK--LKEKLIKLKGE--IKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKELEELGFESVE 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1003 KEEQQRLVLEKGFE--LKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQ---------AKTI 1071
Cdd:PRK03918 589 ELEERLKELEPFYNeyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeyeelREEY 668
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568961011 1072 SEFEKEIELLQAQKIDVEKHVQSQKR---EMRERMSEVTKQLLESYDIEDVRSRL 1123
Cdd:PRK03918 669 LELSRELAGLRAELEELEKRREEIKKtleKLKEELEEREKAKKELEKLEKALERV 723
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
872-1113 |
1.00e-09 |
|
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: 62.83 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 872 RRRFQNIRRFVLNIQLTyRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEE-KGRRY 950
Cdd:pfam17380 359 KRELERIRQEEIAMEIS-RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEaRQREV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 951 RDTVEERLSKLQKHNAElELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYekqiesLR 1030
Cdd:pfam17380 438 RRLEEERAREMERVRLE-EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAM------IE 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1031 EEIKalkdeRSQLHHQLEEGQVTsdrlkgeVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKR---EMRERMSEVT 1107
Cdd:pfam17380 511 EERK-----RKLLEKEMEERQKA-------IYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERsrlEAMEREREMM 578
|
....*.
gi 568961011 1108 KQLLES 1113
Cdd:pfam17380 579 RQIVES 584
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
925-1213 |
1.19e-09 |
|
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: 63.15 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 925 KVQKLEAELEKAAThrhsyEEKGRRYRDTVEERLSKLQKhnaeLELQRERAEQmLQEKSEELKEKMDKLTRQLFDDVQKE 1004
Cdd:TIGR02168 171 KERRKETERKLERT-----RENLDRLEDILNELERQLKS----LERQAEKAER-YKELKAELRELELALLVLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1005 EQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQ 1084
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1085 KIDVEKHVQSQKREMRERMSEVTKQLLE-SYDIEDVRSRLSVedlehlnedgelwfayegLKKATRVLESHFQSQkdcyE 1163
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEElKEELESLEAELEE------------------LEAELEELESRLEEL----E 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 568961011 1164 KEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSENMPLLS 1213
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
892-1208 |
2.28e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 62.09 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 892 QRLQKKLEDQNRENHGLVEKLTSLAALRVGDLE--------KVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQK 963
Cdd:COG0419 192 GQLSELLEDIEDLLEALEEELKELKKLEEIQEEqeeeeleqEIEALEERLAELEEEKERLEELKARLLEIESLELEALKI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 964 HNAELElQRERAEQMLQEKSEELKEKMDKLTRQlfddvQKEEQQRLVLEKgfelKTQAYEKQIESLREEIKALKDERSQL 1043
Cdd:COG0419 272 REEELR-ELERLLEELEEKIERLEELEREIEEL-----EEELEGLRALLE----ELEELLEKLKSLEERLEKLEEKLEKL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1044 HHQLEEGQVTSDRLKGEVARLSKQAKT-ISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKqLLESYDiEDVRSR 1122
Cdd:COG0419 342 ESELEELAEEKNELAKLLEERLKELEErLEELEKELEKALERLKQLEEAIQELKEELAELSAALEE-IQEELE-ELEKEL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1123 LSVE-DLEHLNED-GELWFAYEGLKKATRVLESHFQSQKDCY--EKEIEGLNFKVV--HLSQEINHLQKLFREETDINEs 1196
Cdd:COG0419 420 EELErELEELEEEiKKLEEQINQLESKELMIAELAGAGEKCPvcGQELPEEHEKELleLYELELEELEEELSREKEEAE- 498
|
330
....*....|..
gi 568961011 1197 IRHEVTRLTSEN 1208
Cdd:COG0419 499 LREEIEELEKEL 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
945-1207 |
3.83e-09 |
|
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: 61.24 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 945 EKGRRYRDTVEERLSKLQKHNAELELQRERaeqmLQEKSEElKEKMDKLTRQLfddvQKEEQQRLVLEK-GFELKTQAYE 1023
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLER----LRREREK-AERYQALLKEK----REYEGYELLKEKeALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1024 KQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQA-----KTISEFEKEIELLQAQKIDVEKHVQSQKRE 1098
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvkEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1099 MRERMSEVTKQLLESYDIEdvrsrlsvEDLEHLNEDGELWFA-YEGLKKATRVLESH-----------FQSQKDcYEKEI 1166
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELE--------REIEEERKRRDKLTEeYAELKEELEDLRAEleevdkefaetRDELKD-YREKL 394
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568961011 1167 EGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSE 1207
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
893-1128 |
7.10e-09 |
|
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: 60.47 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 893 RLQKKLEDQNRENHGLVEKLtSLAALRVGDLE-KVQKLEAELEKAATHRHSYEEKGRRY---RDTVEERLSKLQkhnAEL 968
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSI-AEKERELEDAEeRLAKLEAEIDKLLAEIEELEREIEEErkrRDKLTEEYAELK---EEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 969 ELQRERAEQM------LQEKSEELKEKMDKLTRQLFDdvQKEEQQRLVLEKgfelktQAYEKQIESLREEIKALKDERSQ 1042
Cdd:TIGR02169 367 EDLRAELEEVdkefaeTRDELKDYREKLEKLKREINE--LKRELDRLQEEL------QRLSEELADLNAAIAGIEAKINE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1043 LHHQLEEGQvtsDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRErmSEVTKQLLESYdiedVRSR 1122
Cdd:TIGR02169 439 LEEEKEDKA---LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE--AEAQARASEER----VRGG 509
|
....*.
gi 568961011 1123 LSVEDL 1128
Cdd:TIGR02169 510 RAVEEV 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
846-1115 |
7.75e-09 |
|
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: 60.46 E-value: 7.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 846 ARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNI-----QLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRV 920
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 921 GDLEKVQKLEAELEKA----ATHRHSYEEKGRRYRDT------VEERLSKLQKHNAELELQRERAEQMLQEKSE------ 984
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLkeelKALREALDELRAELTLLneeaanLRERLESLERRIAATERRLEDLEEQIEELSEdiesla 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 985 ----ELKEKMDKLTRQL---FDDVQKEEQQRLVLEKGFELKT---QAYEKQIESLREEIKALKDERSQLHHQLEEGQVTS 1054
Cdd:TIGR02168 859 aeieELEELIEELESELealLNERASLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1055 DRLKG-----------------------------EVARLSKQAK--------TISEFEKEIE---LLQAQKIDVEKHVQS 1094
Cdd:TIGR02168 939 DNLQErlseeysltleeaealenkieddeeearrRLKRLENKIKelgpvnlaAIEEYEELKErydFLTAQKEDLTEAKET 1018
|
330 340
....*....|....*....|.
gi 568961011 1095 QKREMRERMSEVTKQLLESYD 1115
Cdd:TIGR02168 1019 LEEAIEEIDREARERFKDTFD 1039
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
862-1189 |
1.13e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 862 LQKYARAW--------LARRRFQNIRRFvlnIQLTYRVQRL----QKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKL 929
Cdd:PRK03918 157 LDDYENAYknlgevikEIKRRIERLEKF---IKRTENIEELikekEKELEEVLREINEISSELPELR-------EELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 930 EAELEKAATHRHSYEEKgrryrdtvEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRqlFDDVQKEEQQRL 1009
Cdd:PRK03918 227 EKEVKELEELKEEIEEL--------EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--LKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1010 VLEK---GFELKTQAYEKQIESLREEIKALKDersqlhhQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKI 1086
Cdd:PRK03918 297 KLSEfyeEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1087 DVEKHVQSQKREMRERMSEVTKQLLE----SYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVL--------ESH 1154
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEKLEKELEElekaKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEH 449
|
330 340 350
....*....|....*....|....*....|....*
gi 568961011 1155 FQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFRE 1189
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
890-1150 |
1.18e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 224259 [Multi-domain] Cd Length: 294 Bit Score: 57.77 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLeaeLEKAATHRHSYEEKGRRYRDTVEERLsklqKHNAELE 969
Cdd:COG1340 14 KRKQLKEEIEELKEKRDELRKEASELAEKRDELNAKVREL---REKAQELREERDEINEEVQELKEKRD----EINAKLQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 970 LQRERAEQMLQEKSE---------ELKEKMDKL-----TRQLFDDVQKEEQQRLV-LEKGFELKTQAYE--KQIESLREE 1032
Cdd:COG1340 87 ELRKEYRELKEKRNEfnlggrsikSLEREIERLekkqqTSVLTPEEERELVQKIKeLRKELEDAKKALEenEKLKELKAE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1033 IKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAktiSEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTK--QL 1110
Cdd:COG1340 167 IDELKKKAREIHEKIQELANEAQEYHEEMIKLFEEA---DELRKEADELHEEFVELSKKIDELHEEFRNLQNELREleKK 243
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568961011 1111 LESYDIEDVRSRLSVEDLEhLNEDGELwfAYEGLKKATRV 1150
Cdd:COG1340 244 IKALRAKEKAAKRREKREE-LKERAEE--IYEKFKRGEKL 280
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
896-1112 |
1.22e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 896 KKLEDQNRENHGLVEKLTSLAALRVG---DLEKVQKLEAEL-----------EKAATHRHSYEEKGRRYRDTVEERLSKL 961
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSlkkELEKLEELKKKLaelekkldeleEELAELLKELEELGFESVEELEERLKEL 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 962 QK-HNAELELQRerAEQMLQEKSEELKEKMDKLTrQLFDDVQKEEQQRLVLEKGFELKTQAY--------EKQIESLREE 1032
Cdd:PRK03918 598 EPfYNEYLELKD--AEKELEREEKELKKLEEELD-KAFEELAETEKRLEELRKELEELEKKYseeeyeelREEYLELSRE 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1033 IKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLE 1112
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFE 754
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
890-1137 |
1.88e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDqnrenhgLVEKLTSLAAlRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKL-------Q 962
Cdd:PRK02224 476 RVEELEAELED-------LEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAeelreraA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 963 KHNAELELQRERAeQMLQEKSEELKEKMDKLTRQLfdDVQKEEQQRL-VLEKGFELKTqAYEKQIESLREEIKALKD--- 1038
Cdd:PRK02224 548 ELEAEAEEKREAA-AEAEEEAEEAREEVAELNSKL--AELKERIESLeRIRTLLAAIA-DAEDEIERLREKREALAElnd 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1039 -------ERSQLHHQLEEgQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKRE------MRERMSE 1105
Cdd:PRK02224 624 errerlaEKRERKRELEA-EFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEleeleeLRERREA 702
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 568961011 1106 V--TKQLLESYDIE---------DVRSRL---SVEDLEH-LNEDGEL 1137
Cdd:PRK02224 703 LenRVEALEALYDEaeelesmygDLRAELrqrNVETLERmLNETFDL 749
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
886-1107 |
1.89e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 59.00 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 886 QLTYRVQRLQKKLEDQNRENH--GLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKgrRYRDTVEERL-SKLQ 962
Cdd:COG0419 563 QLEDRLQELKELLEELRLLRTrkEELEELRERLKELKKKLKELEERLSQLEELLQSLELSEAE--NELEEAEEELeSELE 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 963 KHNAELELQR--ERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKtqAYEKQIESLREEIKALKDER 1040
Cdd:COG0419 641 KLNLQAELEEllQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEELE--QLREELEELLKKLGEIEQLI 718
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568961011 1041 SQLHHQLEEgqvtSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVT 1107
Cdd:COG0419 719 EELESRKAE----LEELKKELEKLEKALELLEELREKLGKAGLRADILRNLLAQIEAEANEILSKLS 781
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
874-1129 |
1.94e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 59.13 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 874 RFQNIRRFVLNIQLTYRvQRLQKKLEDQNRENHGLVEKLTSLAALrvgdLEKVQKLEAELEKAATH--------RHsyEE 945
Cdd:COG3096 276 RHANERRVHLDQALEFR-RELYTSRQQLAAEQYRHVDMSRELAEL----NGAEGDLEADYQAASDHlnlvqtalRQ--QE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 946 KGRRYRDTVEERLSKLQKHNAELELQRERAEQMlQEKSEELKEKMDKLTRQLFD-----DVQK----EEQQRL-VLEKGF 1015
Cdd:COG3096 349 KIERYQADLEELTIRLEEQNEVVEEANERQEEN-EARAEAAELEVDELKSQLADyqqalDVQQtraiQYQQAIaALERAK 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1016 EL--KTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSD--------------RLKGEVAR---------LSKQAKT 1070
Cdd:COG3096 428 ELchLPDLTADSAEEWLETFQAKEEEATEKLLSLEQKMSMAQaahsqfeqayqlvvAIAGELARseawdvareLLREGPD 507
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961011 1071 ISEFEKEIELLQAQKIDVEKHVQSQkREMRERMSEVTKQLLESYDI---EDVRSRLS--VEDLE 1129
Cdd:COG3096 508 QRHLAEQVQPLRMRLSELEQRLRQQ-QSAERLLADFCKRQGKNLDAeelEALHQELEalIESLS 570
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
894-1185 |
2.81e-08 |
|
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: 435008 [Multi-domain] Cd Length: 329 Bit Score: 57.13 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 894 LQKKLEDQNRenHGLVEKLTSLAALRVGDLEK-VQKLEAELEKAathrhsyEEKgrrYRDTVEERLSkLQKHNAELELQR 972
Cdd:pfam15905 65 SQKDLKESKD--QKELEKEIRALVQERGEQDKrLQALEEELEKV-------EAK---LNAAVREKTS-LSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 973 ---ERAEQMLQEKSEE--LKEKMDKLTRQLF---DDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLH 1044
Cdd:pfam15905 132 lelTRVNELLKAKFSEdgTQKKMSSLSMELMklrNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1045 HQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQllesydIEDVRSRLS 1124
Cdd:pfam15905 212 KEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQ------IKDLNEKCK 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961011 1125 VedLEHLNEDgelwfayeglkkatrvLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:pfam15905 286 L--LESEKEE----------------LLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
894-1185 |
5.60e-08 |
|
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: 57.34 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 894 LQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRdTVEERLSKLQKHNAELELQRE 973
Cdd:TIGR04523 157 LNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDNIE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 974 RAEQMLQEKSEELKEKMDKLTrQLFDDVQKEEQQrlVLEKGFELKTQayEKQIESLREEIKALKDERSQLHHQLEegQVT 1053
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLN-QLKDEQNKIKKQ--LSEKQKELEQN--NKKIKELEKQLNQLKSEISDLNNQKE--QDW 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1054 SDRLKGEVA-----------RLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLE--SYdiedvr 1120
Cdd:TIGR04523 309 NKELKSELKnqekkleeiqnQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEnqSY------ 382
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011 1121 sRLSVEDLEHLNEDGELWFayEGLKKATRVLESH---FQSQKDCYEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:TIGR04523 383 -KQEIKNLESQINDLESKI--QNQEKLNQQKDEQikkLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
892-1133 |
5.92e-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: 57.06 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 892 QRLQKKLEDQNREnhglVE---KLTSLAALRVGDLEKVQKLEAELEKAATHRH------SYEEKGRRYRDTVEERLSKLQ 962
Cdd:pfam17380 299 ERLRQEKEEKARE----VErrrKLEEAEKARQAEMDRQAAIYAEQERMAMEREreleriRQEERKRELERIRQEEIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 963 KHNAELE-LQRERaeqmlQEKSEELKEKMDKLTRQlfdDVQKEEQQRLVLEKGFELKtQAYEKQIESLREEIKALKDERS 1041
Cdd:pfam17380 375 SRMRELErLQMER-----QQKNERVRQELEAARKV---KILEEERQRKIQQQKVEME-QIRAEQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1042 -----------QLHHQLE---EGQVTSDRLKGEVARLSKQAKTISE-----FEKEIELLQAQKIDVEKHVQSQKREMRER 1102
Cdd:pfam17380 446 remervrleeqERQQQVErlrQQEEERKRKKLELEKEKRDRKRAEEqrrkiLEKELEERKQAMIEEERKRKLLEKEMEER 525
|
250 260 270
....*....|....*....|....*....|.
gi 568961011 1103 MSEVTKQLLESYDIEDVRSRLSVEDLEHLNE 1133
Cdd:pfam17380 526 QKAIYEEERRREAEEERRKQQEMEERRRIQE 556
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
952-1115 |
6.43e-08 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 55.06 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 952 DTVEERLSKLQKHNAELELQRERAEQMLQEKSEELkEKMDKLTRQLFDDVQKEEQQRLVLEKGF-ELKTQ----AYEKQI 1026
Cdd:COG1579 20 DRLEPRIKEIRKALKKAKAELEALNKALEALEIEL-EDLENQVSQLESEIQEIRERIKRAEEKLsAVKDErelrALNIEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1027 ESLREEIKALKDERSQLHHQLEEGQvtsDRLKGEVARLSKQAKTISEFEKEIELlQAQKIDVEKH-VQSQKREMRERMSE 1105
Cdd:COG1579 99 QIAKERINSLEDELAELMEEIEKLE---KEIEDLKERLERLEKNLAEAEARLEE-EVAEIREEGQeLSSKREELKEKLDP 174
|
170
....*....|
gi 568961011 1106 vtkQLLESYD 1115
Cdd:COG1579 175 ---ELLSEYE 181
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
845-1090 |
6.93e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 56.27 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 845 LARRRYRKLLQEHKAvILQKYARAWLARRRFQNiRRFVLNIQLTYRVQRLQKkLEDQNRENHGLVEKLtsLAAL-RVGDL 923
Cdd:COG4942 56 EQQDQRAKLEKQLKS-LETEIASLEAQLIETAD-DLKKLRKQIADLNARLNA-LEVQEREQRRRLAEQ--LAALqRSGRN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 924 EKVQKL----EAELEKAATHRHSYEEKGRRYR-DTVEERLSKLQKHNAELELQRERAEQMLQEKSEElKEKMDKLtrqlf 998
Cdd:COG4942 131 PPPALLvspeDAQRSVRLAIYYGALNPARAERiDALKATLKQLAAVRAEIAAEQAELTTLLSEQRAQ-QAKLAQL----- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 999 ddvqKEEQQRLvlEKGFELKTQAYEKQIESLREEIKALKDERSQLhhqleEGQVTSDRLKGEVARLSKQAKTISEFEKEI 1078
Cdd:COG4942 205 ----LEERKKT--LAQLNSELSADQKKLEELRANESRLKNEIASA-----EAAAAKAREAAAAAEAAAARARAAEAKRTG 273
|
250
....*....|..
gi 568961011 1079 ELLQAQKIDVEK 1090
Cdd:COG4942 274 ETYKPTAPEKML 285
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
866-1133 |
7.12e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 866 ARAWLarrRFQNIRRFVLNIQLTYRvQRLQKKLEDQNRENHGLVEKLTSLAALRvgdlEKVQKLEAELEKAATHRHS--- 942
Cdd:PRK04863 271 AADYM---RHANERRVHLEEALELR-RELYTSRRQLAAEQYRLVEMARELAELN----EAESDLEQDYQAASDHLNLvqt 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 943 ---YEEKGRRYRDTVEERLSKLQKHNAELELQRERAEqMLQEKSEELKEKMDKLTRQLFDDVQK-EEQQRLVLEkgFELK 1018
Cdd:PRK04863 343 alrQQEKIERYQADLEELEERLEEQNEVVEEADEQQE-ENEARAEAAEEEVDELKSQLADYQQAlDVQQTRAIQ--YQQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1019 TQAYEKQ-----------------IESLREEIKALKDERSQLHHQLEEGQVTSD----------RLKGEVARL--SKQAK 1069
Cdd:PRK04863 420 VQALERAkqlcglpdltadnaedwLEEFQAKEQEATEELLSLEQKLSVAQAAHSqfeqayqlvrKIAGEVSRSeaWDVAR 499
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961011 1070 -TISEFEKEIEL------LQAQKIDVEKHVQSQKREMReRMSEVTKQLLESYDIEDVRSRLSVE---DLEHLNE 1133
Cdd:PRK04863 500 eLLRRLREQRHLaeqlqqLRMRLSELEQRLRQQQRAER-LLAEFCKRLGKNLDDEDELEQLQEEleaRLESLSE 572
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
884-1185 |
9.87e-08 |
|
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: 428520 [Multi-domain] Cd Length: 660 Bit Score: 56.28 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 884 NIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrvgdlekvQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQK 963
Cdd:pfam05557 50 NQELQKRIRLLEKREAEAEEALREQAELNRLK-----------KKNLEALNKKLNEKESQLADAREVISCLKNELSELRR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 964 --HNAELELQRERAE-QMLQEKSEELKEKMDKLTrQLFDDVQKeeQQRLVLEKgfELKTQAYEKQIESLREEIKALKDER 1040
Cdd:pfam05557 119 qiQRQELELSSTNSElEELQERLDLQKAKAQEAE-QLRQNLEA--QQSSLAEA--EQRIKELEFEIQSQEQDSEIVKNSK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1041 SQLhHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQ----------AQKIDVEKHVQSQKREMRERMSEVTKQL 1110
Cdd:pfam05557 194 SEL-ARIPELERELERLREHNKHLNENIENKLLLKEEVEDLKrklereegyrEELATLELEKEKLEQELKSWEKLAQDTG 272
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011 1111 LESYDIEDVRSR---LSVEDLEHLNEDGELWFAYEGLKKATRVLeshfQSQKDCYEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:pfam05557 273 LNLRSPEDLSRRieqLQQREITLKEENSSLTSSARQLEKAQREL----EQELAQYLKNIEDLNKKLKRHKALVRRLQR 346
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
988-1193 |
1.02e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 988 EKMDKLTRQL--FDDVQKEEQQRLVLEKGFELKTQAYEKQI---ESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVA 1062
Cdd:PRK03918 145 ESREKVVRQIlgLDDYENAYKNLGEVIKEIKRRIERLEKFIkrtENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1063 RLSKQAKTISEFEKEIELLQAQKIDVEKHVQS---QKREMRERMSEVTKQllesydIEDVRSRlsVEDLEHLNEDGELWF 1139
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGSKRKleeKIRELEERIEELKKE------IEELEEK--VKELKELKEKAEEYI 296
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568961011 1140 AYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDI 1193
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL 350
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
846-1090 |
1.13e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 56.31 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 846 ARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLtyRVQRLQKKLEDQNRENhgLVEKLTSLAalrvgdlEK 925
Cdd:COG0419 499 LREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLEN--LLEELEELKEKLQLQQ--LKEELRQLE-------DR 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 926 VQKLEAELEKAATHRHSYE--EKGRRYRDTVEERLSKLQKHNAELE-----LQRERAEQMLQEKSEELKEKMDKL----- 993
Cdd:COG0419 568 LQELKELLEELRLLRTRKEelEELRERLKELKKKLKELEERLSQLEellqsLELSEAENELEEAEEELESELEKLnlqae 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 994 -TRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESL--REEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKT 1070
Cdd:COG0419 648 lEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEekLEELEQLEEELEQLREELEELLKKLGEIEQLIEELESRKAE 727
|
250 260
....*....|....*....|
gi 568961011 1071 ISEFEKEIELLQAQKIDVEK 1090
Cdd:COG0419 728 LEELKKELEKLEKALELLEE 747
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
851-1137 |
1.45e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 224259 [Multi-domain] Cd Length: 294 Bit Score: 54.69 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 851 RKLLQEH--KAVILQKYARAWLARRRFQN--IRRFVLNIQ--------LTYRVQRLQKKLEDQNRENHGL---VEKLTSL 915
Cdd:COG1340 19 KEEIEELkeKRDELRKEASELAEKRDELNakVRELREKAQelreerdeINEEVQELKEKRDEINAKLQELrkeYRELKEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 916 AALRVGDLEKVQKLEAELEKaathrhsyEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSE--ELKEKMDKL 993
Cdd:COG1340 99 RNEFNLGGRSIKSLEREIER--------LEKKQQTSVLTPEEERELVQKIKELRKELEDAKKALEENEKlkELKAEIDEL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 994 TRQLFDdvQKEEQQRLVLEkgfelkTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISE 1073
Cdd:COG1340 171 KKKARE--IHEKIQELANE------AQEYHEEMIKLFEEADELRKEADELHEEFVELSKKIDELHEEFRNLQNE---LRE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961011 1074 FEKEIELLQAQKIDVEKhvQSQKREMRERMSEVTKQLLESydiedvrSRLSVEDLEHLNEDGEL 1137
Cdd:COG1340 240 LEKKIKALRAKEKAAKR--REKREELKERAEEIYEKFKRG-------EKLTTEELLLLQKAGLV 294
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
890-1192 |
1.96e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNRenhglVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRryrdtvEERLSKLQKHNAELE 969
Cdd:PTZ00121 1379 KADAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK------ADEAKKKAEEAKKAD 1447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 970 LQRERAEQmlQEKSEELKEKMDKLTRQlfDDVQKEEQQRlvlEKGFELKTQAYE--KQIESLR--EEIKALKDE--RSQL 1043
Cdd:PTZ00121 1448 EAKKKAEE--AKKAEEAKKKAEEAKKA--DEAKKKAEEA---KKADEAKKKAEEakKKADEAKkaAEAKKKADEakKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1044 HHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDV--EKHVQSQKREMRERMSEVTKQlLESYDIEDVRS 1121
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaeEAKKAEEDKNMALRKAEEAKK-AEEARIEEVMK 1599
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961011 1122 RLSVEDL---EHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETD 1192
Cdd:PTZ00121 1600 LYEEEKKmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
864-1126 |
2.27e-07 |
|
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: 55.13 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 864 KYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLE--DQNRENHGLVEKLTSLAALRvgDLEKVQKL-EAELEKAAThr 940
Cdd:pfam17380 259 RYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEkmEQERLRQEKEEKAREVERRR--KLEEAEKArQAEMDRQAA-- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 941 hSYEEKGRRYRDTvEERLSKLQKHNAELELQRERAEQMLQEKSeelkeKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQ 1020
Cdd:pfam17380 335 -IYAEQERMAMER-ERELERIRQEERKRELERIRQEEIAMEIS-----RMRELERLQMERQQKNERVRQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1021 AYEKQieslrEEIKALKDERSQLHHQLEEG-QVTSDRLKGEVAR-LSKQAKTISEFEKEIELLQAQ-------KIDVEKH 1091
Cdd:pfam17380 408 EEERQ-----RKIQQQKVEMEQIRAEQEEArQREVRRLEEERAReMERVRLEEQERQQQVERLRQQeeerkrkKLELEKE 482
|
250 260 270
....*....|....*....|....*....|....*..
gi 568961011 1092 VQSQKREMRERMSEVTKQLLESYD--IEDVRSRLSVE 1126
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQamIEEERKRKLLE 519
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
896-1213 |
2.58e-07 |
|
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.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 54.86 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 896 KKLEDQNRENHGLVEKLtslaalrvgdLEKVQKLEAELekaATHRHSYEEkgrrYRDTVEERLSKLQKHNAELE------ 969
Cdd:pfam06160 110 DELLESEEKNREEVEEL----------KDKYRELRKTL---LANRFSYGP----AIDELEKQLAEIEEEFSQFEeltesg 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 970 --LQRERAEQMLQEKSEELKEKMDKLTrQLFDDVQKEEQQRL---------VLEKGFELKTQAYEKQIESLREEIKALKd 1038
Cdd:pfam06160 173 dyLEAREVLEKLEEETDALEELMEDIP-PLYEELKTELPDQLeelkegyreMEEEGYALEHLNVDKEIQQLEEQLEENL- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1039 ersqlhHQLEEGQVtsDRLKGEVARLSKQAKTISE-FEKEIEllqAQKiDVEKHvQSQKREMRERMSEVTKQLLESYDIE 1117
Cdd:pfam06160 251 ------ALLENLEL--DEAEEALEEIEERIDQLYDlLEKEVD---AKK-YVEKN-LPEIEDYLEHAEEQNKELKEELERV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1118 DVRSRLSVEDLEHLNE-DGELwfayEGLKKATRVLESHFQSQKDCY----------EKEIEGLNFKVVHLSqeiNHLQKL 1186
Cdd:pfam06160 318 QQSYTLNENELERVRGlEKQL----EELEKRYDEIVERLEEKEVAYselqeeleeiLEQLEEIEEEQEEFK---ESLQSL 390
|
330 340 350
....*....|....*....|....*....|....
gi 568961011 1187 FREETDINESIR------HEVTRLTS-ENMPLLS 1213
Cdd:pfam06160 391 RKDELEAREKLDefklelREIKRLVEkSNLPGLP 424
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
890-1115 |
2.70e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNRENHGLVEKLTSLAAlrvgdlEKVQKLEAELEKAATHRHSYEEKGR--RYRDTVEERLSKLQKHNAE 967
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKA------EEAKKAEEAKIKAEELKKAEEEKKKveQLKKKEAEEKKKAEELKKA 1655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 968 LELQRERAEQmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLE---KGFELKTQAYE--KQIESLREEIKALKDERSQ 1042
Cdd:PTZ00121 1656 EEENKIKAAE-EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeakKAEELKKKEAEekKKAEELKKAEEENKIKAEE 1734
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961011 1043 LHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhvQSQKREMRERMSEVTKQLLESYD 1115
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
890-1112 |
2.95e-07 |
|
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: 55.03 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNRENHGLVEKLTSLAaLRVGDLE--------KVQKLEAELEKAathRHSYEEKGRRYRDTVEErLSKL 961
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKE-LIIKNLDntresletQLKVLSRSINKI---KQNLEQKQKELKSKEKE-LKKL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 962 QKHNAELELQreraEQMLQEKSEELKEKMDKLTRQLfddVQKEEQ----QRLVLEKGFELKTQAYEKQIESLREEIKALK 1037
Cdd:TIGR04523 502 NEEKKELEEK----VKDLTKKISSLKEKIEKLESEK---KEKESKisdlEDELNKDDFELKKENLEKEIDEKNKEIEELK 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1038 DERSQLHHQLEEGQVTSDRLKGEVARLSKQ----AKTISEFEKEIELLQAQKIDVE---KHVQSQKREMRERMSEVTKQL 1110
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEieekEKKISSLEKELEKAKKENEKLSsiiKNIKSKKNKLKQEVKQIKETI 654
|
..
gi 568961011 1111 LE 1112
Cdd:TIGR04523 655 KE 656
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
898-1207 |
4.32e-07 |
|
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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 54.40 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 898 LEDQN----RENHGLVEKLTSLAALRVGDLEKV---QKLEAELEKAATH---RHSYEEKGR----RYRDTVEERLSKLQK 963
Cdd:pfam01576 143 LEDQNnklqKERKLLEERISEFTSNLAEEEEKSkslNKLKNKHEAMISDledRLKKEEKGRqeleKAKRKLEGESSDLQE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 964 HNAELELQRERAEQMLQEKSEELKEKMDKLTR------QLFDDVQKEEQQRLVLEKGFELKTQA---YEKQIESLREEIK 1034
Cdd:pfam01576 223 QIAELQAQIAELRAQLAKKEEELQAALARLEEetaqknAALKKLRELEAQLSELQEDLESERAArakAEKQRRDLGEELE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1035 ALKDE--------------RSQ-------LHHQLE------EGQVTSDRLKG-----------EVARLSKQA-------- 1068
Cdd:pfam01576 303 ALKTEledtldttaaqqelRSKreqevteLKKALEeetrshEAQLQEMRQKHtqaleelteqlEQAKRNKASlekakqal 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1069 -KTISEFEKEIELLQAQKIDVE---KHVQSQKREMRERMSEVTKQLLEsydIEDVRSRLSVEdLEHLNED-GELWFAYEG 1143
Cdd:pfam01576 383 eSENAELQAELRSLQQAKQDSEhkrKKLEGQLQELQSRLSESERQRAE---LAEKLSKLQSE-LESVSSLlNEAEGKNIK 458
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568961011 1144 LKKATRVLESHFQSQKDCYEKEI-EGLNF--KVVHLSQEINHLQKLFREETDINESIRHEVTRLTSE 1207
Cdd:pfam01576 459 LSKDVSSLESQLQDTQELLQEETrQKLNLssRLRQLEDEKNSLQEQLEEEEEAKRNVERQLQTLQAQ 525
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
896-1210 |
7.11e-07 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 226883 [Multi-domain] Cd Length: 570 Bit Score: 53.53 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 896 KKLEDQNRENHG----LVEKLTSLAALRVGDL-EKVQKLEAELEKAATHRHSYE---EKGrryrDTVEER--LSKLQKHN 965
Cdd:COG4477 131 VESEEKNSEEIDhvleLYEELRRDVLANRHQYgEAAPELEKKLENIEEELSQFVeltSSG----DYIEARevLEEAEEHM 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 966 AELELQRERAEQMLQEKSEELKEKMDKLtrqlfddvqkEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLhh 1045
Cdd:COG4477 207 IALRSIMERIPSLLAELQTELPGQLQDL----------KAGYRDMKEEGYHLEHVNIDSRLERLKEQLVENSELLTQL-- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1046 QLEEGQVTSDRLKGEVARLSKQaktiseFEKEIEllqAQKIDVEKHvqSQKREMRERMSEVTKQLLEsyDIEDVRS--RL 1123
Cdd:COG4477 275 ELDEAEEELGLIQEKIESLYDL------LEREVE---AKNVVEENL--PILPDYLEKAKENNEHLKE--EIERVKEsyRL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1124 SVEDL-------EHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINES 1196
Cdd:COG4477 342 AETELgsvrkfeKELKELESVLDEILENIEAQEVAYSELQDNLEEIEKALTDIEDEQEKVQEHLTSLRKDELEARENLER 421
|
330
....*....|....*...
gi 568961011 1197 IR---HEVTR-LTSENMP 1210
Cdd:COG4477 422 LKsklHEIKRyMEKSNLP 439
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
894-1213 |
8.83e-07 |
|
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: 53.49 E-value: 8.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 894 LQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELElQRE 973
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQ-------QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK-ELE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 974 RAEQMLQEKSEELK-EKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEK---QIESLREEIKALKDERSQLHHQLEE 1049
Cdd:TIGR04523 288 KQLNQLKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQlneQISQLKKELTNSESENSEKQRELEE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1050 GQVTSDRLKGEvarlskqaktISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEV-----TKQLLESyDIEDVRSRLS 1124
Cdd:TIGR04523 368 KQNEIEKLKKE----------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIkklqqEKELLEK-EIERLKETII 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1125 -----VEDLEhlNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINEsirh 1199
Cdd:TIGR04523 437 knnseIKDLT--NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE---- 510
|
330
....*....|....
gi 568961011 1200 EVTRLTSENMPLLS 1213
Cdd:TIGR04523 511 KVKDLTKKISSLKE 524
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1013-1207 |
1.62e-06 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 52.79 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1013 KGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHV 1092
Cdd:COG1196 670 KELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEEL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1093 QSQKREMRERMSEVTKQLLEsydIEDVRSRLSvEDLEHLNEDGElwfAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFK 1172
Cdd:COG1196 750 EEELEELQERLEELEEELES---LEEALAKLK-EEIEELEEKRQ---ALQEELEELEEELEEAERRLDALERELESLEQR 822
|
170 180 190
....*....|....*....|....*....|....*
gi 568961011 1173 VVHLSQEINHLQKLFREETDINESIRHEVTRLTSE 1207
Cdd:COG1196 823 RERLEQEIEELEEEIEELEEKLDELEEELEELEKE 857
|
|
| DUF812 |
pfam05667 |
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of ... |
892-1115 |
1.78e-06 |
|
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of unknown function.
Pssm-ID: 428574 [Multi-domain] Cd Length: 601 Bit Score: 52.32 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 892 QRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKV-----QKLEAELEKAATHRHSYEEKGRRYRDTVE-ERLSKLQKHN 965
Cdd:pfam05667 246 TKLLKRIAEQLRSAALASTEATSGASRSKQDLAELlssfgGSSTTDTNLTKGSRFTHTEKLQFTNEEAPaATSSPPTKAE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 966 AELELQRERAEQM--LQEKSEELKEKMDKL----------TRQLFDDVQKEEQQRLVLEKGFELKTQAY------EKQIE 1027
Cdd:pfam05667 326 TEEELQQQREEELeeLQEQLEELESSIEELekeikklessIKQVEEELEELKEQNEELEKQYKVKKKTLdllpdaEENIA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1028 SLREEIKALKDERSQLHHQLEEGQVTsdrLKGEVARLsKQAKTISEFEKEielLQAQKIdvekhvqsqkREMRERMSEVT 1107
Cdd:pfam05667 406 KLQALVEASAQRLVELAGQWEKHRVP---LIEEYRAL-KEAKSNKESESQ---RKLEEI----------KELREKIKEVA 468
|
250
....*....|....*...
gi 568961011 1108 ----------KQLLESYD 1115
Cdd:pfam05667 469 eearskeelyKQLVAEYE 486
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
886-1200 |
2.35e-06 |
|
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: 52.28 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 886 QLTYRVQRLQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKhn 965
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQLTSERKQRASLK-------EQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK-- 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 966 aELELQRERAEQmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLR--EEIKALKDERSQL 1043
Cdd:TIGR00618 603 -LSEAEDMLACE-QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALsiRVLPKELLASRQL 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1044 HHQLEEG---QVTSDR--LKGEVARLSKQAKTISEFEKEIELLQ----AQKIDVEK----HVQSQKREMRERmSEVTKQL 1110
Cdd:TIGR00618 681 ALQKMQSekeQLTYWKemLAQCQTLLRELETHIEEYDREFNEIEnassSLGSDLAAredaLNQSLKELMHQA-RTVLKAR 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1111 LESYDIEDVRSRLSV---EDLEHLNEDGELWF-AYEGLKKATRVLESHFQSQKDCYEKEiegLNFKVVHLSQEINHLQKL 1186
Cdd:TIGR00618 760 TEAHFNNNEEVTAALqtgAELSHLAAEIQFFNrLREEDTHLLKTLEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSR 836
|
330
....*....|....
gi 568961011 1187 FREETDINESIRHE 1200
Cdd:TIGR00618 837 LEEKSATLGEITHQ 850
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
883-1213 |
2.41e-06 |
|
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: 51.94 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 883 LNIQLTYRVQRLQKKLEDQNRE-NHGLVEKLTSlaalrvgDLEKVQKLEAELEKAATHRhsyeekgrryrdtvEERLSKL 961
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQkEQDWNKELKS-------ELKNQEKKLEEIQNQISQN--------------NKIISQL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 962 QKHNAELELQRERAEQMLQEKSEELKEKMDKLtRQLFDDVQ--KEEQQRLVLEKG-FELKTQAYEKQIESLREEIKALKD 1038
Cdd:TIGR04523 341 NEQISQLKKELTNSESENSEKQRELEEKQNEI-EKLKKENQsyKQEIKNLESQINdLESKIQNQEKLNQQKDEQIKKLQQ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1039 ERSQLHHQLEEGQVTSDRLKGEVARLSKQ-----------AKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVT 1107
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknlDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1108 KQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQS-----QKDCYEKEIEGLNFKVVHLSQEINH 1182
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKS 579
|
330 340 350
....*....|....*....|....*....|....
gi 568961011 1183 L---QKLFREETDINESIRHEVTRLTSENMPLLS 1213
Cdd:TIGR04523 580 LkkkQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
853-1113 |
2.73e-06 |
|
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: 429718 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 853 LLQEHKAVILQK---YARAWLARRRFQNIRRfvlniQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRvgdlekvQKL 929
Cdd:pfam07888 46 LLQAQEAANRQRekeKERYKRDREQWERQRR-----ELESRVAELKEELRQSREKVEELEEKYKELSRSG-------EEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 930 EAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKmdkltRQLFDDVQKEEQQRL 1009
Cdd:pfam07888 114 AEEKDALLAQRAESEARIRELEEDIKTLTQRVLERETELERMKERVKKAGAQRKEEEAER-----KQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1010 VLEKGF-ELKTQAYEK--QIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKi 1086
Cdd:pfam07888 189 SLSKEFqELRNSLAQRdtQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQR- 267
|
250 260
....*....|....*....|....*..
gi 568961011 1087 dveKHVQSQKREMRERMSEVTKQLLES 1113
Cdd:pfam07888 268 ---DRTQAELHQARLQAAQLTLQLADA 291
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
932-1208 |
3.12e-06 |
|
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: 51.90 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 932 ELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEK-----SEELKEKMDKLTRQLFDDVQKEEQ 1006
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKkaleyYQLKEKLELEEEYLLYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1007 QRLVL------------EKGFELKTQAYEKQIESLREEIKALKDERSQ----LHHQLEEGQVTSDRLKGEVARLSKqakt 1070
Cdd:pfam02463 237 ERIDLlqellrdeqeeiESSKQEIEKEEEKLAQVLKENKEEEKEKKLQeeelKLLAKEEEELKSELLKLERRKVDD---- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1071 isefEKEIELLQAQKIDVEKHVQSQKREMRERmsevtKQLLESYDIEDVRSRLSVEDLEHLNEDGELwfAYEGLKKATRV 1150
Cdd:pfam02463 313 ----EEKLKESEKEKKKAEKELKKEKEEIEEL-----EKELKELEIKREAEEEEEEELEKLQEKLEQ--LEEELLAKKKL 381
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011 1151 LESHFQSQKDCYEKEIEGLNFKVvhlsQEINHLQKLFREETDINESIRHEVTRLTSEN 1208
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEE----KEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
924-1084 |
4.23e-06 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 426264 [Multi-domain] Cd Length: 170 Bit Score: 48.42 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 924 EKVQKLEAELEKAAthrhsyeekgRRYRDTVEERLSKLQKH-NAELELQRERAE-------QMLQEKSEELKEKMDKLTR 995
Cdd:pfam01442 6 TYAEELQEQLGPVA----------QELVDRLEKETEALRERlQKDLEEVRAKLEpyleelqAKLQQNVEELRQRLEPYTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 996 QLFDDVQK--EEQQRLVLEKGFELKTQAyEKQIESLREEIKALKDE-RSQLHHQLEEGQVTSDRLKGEV-ARLSKQAKTI 1071
Cdd:pfam01442 76 ELRKRLNAdaEELQEKLAPYGEELRERL-EQNVDALRARLAPYAEElRQKLAERLEELKESLAPYAEEVqAQLSQRLQEL 154
|
170
....*....|....
gi 568961011 1072 SE-FEKEIELLQAQ 1084
Cdd:pfam01442 155 REkLEPQAEDLREK 168
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
897-1118 |
4.39e-06 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 49.72 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 897 KLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAE 976
Cdd:pfam06008 41 QIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 977 QMLQEKSEELKEKMDklTRQLFDDVQKEEQQrlvLEKGFELKTQAyEKQIESLREEIKALKDersQLHHQLEEgqvTSDR 1056
Cdd:pfam06008 121 SRMLAEAQRMLGEIR--SRDFGTQLQNAEAE---LKAAQDLLSRI-QTWFQSPQEENKALAN---ALRDSLAE---YEAK 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961011 1057 LKGEVARLSK-QAKTisefeKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIED 1118
Cdd:pfam06008 189 LSDLRELLREaAAKT-----RDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTARDSLD 246
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
891-1118 |
4.54e-06 |
|
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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 51.31 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 891 VQRLQKKLEDQNRENHGlveKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQkhNAELEL 970
Cdd:pfam01576 403 SEHKRKKLEGQLQELQS---RLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ--DTQELL 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 971 QRE---------RAEQM------LQEKSEELKEKMDKLTR-------QLFDDVQKEEQQRLVLEKGFELKTQaYEKQIES 1028
Cdd:pfam01576 478 QEEtrqklnlssRLRQLedeknsLQEQLEEEEEAKRNVERqlqtlqaQLSDLKKKLEEDAGAVEALEEGRKR-LQRELEA 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1029 L--REEIKA-----LKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRE 1101
Cdd:pfam01576 557 LtqRLEEKAaaydkLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKET 636
|
250
....*....|....*..
gi 568961011 1102 RMSEVTKQLLESYDIED 1118
Cdd:pfam01576 637 KALSLARALEEALDAKE 653
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
944-1213 |
4.89e-06 |
|
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: 434960 [Multi-domain] Cd Length: 1050 Bit Score: 51.04 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 944 EEKGRRYRDT-VEERLSKLQKHNAELELQREraeqMLQEKSEEL----KEKMDKLTRQLFDDVQKEEQqrlvlEKG-FEL 1017
Cdd:pfam15818 15 ELRMRREAETqYEEQIGKIIVETQELKWQKE----TLQNQKETLakqhKEAMAVFKKQLQMKMCALEE-----EKGkYQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1018 KTQAYEKQIESLREEIKALkdersqlhhqleegqvtsdrlkgEVARLSKQaKTISEFEKEIELLQAQKIDVEKhvqsQKR 1097
Cdd:pfam15818 86 ATEIKEKEIEGLKETLKAL-----------------------QVSKYSLQ-KKVSEMEQKVQLHLLAKEDHHK----QLN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1098 EMRERMSEVTKQL---------LESYDIEDVR--SRLSVedlehLNE--DGELWFAYEGLKKATRVL-ESHFQSQkdcYE 1163
Cdd:pfam15818 138 EIEKYYATITGQFglvkenhekLEQNVQEAIQlnKRLSA-----LNKkqESEICSLKKELKKVTSDLiKSKVTCQ---YK 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 568961011 1164 KEIEGLNFKVVHlsQEINHLQKLFREETDINESIRHEVTRLTSENMPLLS 1213
Cdd:pfam15818 210 MGEENINLTIKE--QKFQELQERLNMELELNKKINEEITHIQEEKQDIII 257
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
934-1127 |
6.86e-06 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 48.78 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 934 EKAATHRHSYEEKGRRYRDT---VEERLSKLQKHNAELELQRERAEQ---MLQEKSEELKEKMDKLTRQLFDdvQKEEQQ 1007
Cdd:pfam00769 2 EEAEREKQELEERLKQYEEEtrkAQEELEESEETAELLEEKLRVAEEeaeLLEQKAQEAEEEKERLEESAEM--EAEEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1008 RLvlekgfELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKgevarlskqaktisefEKEIELLQAQKID 1087
Cdd:pfam00769 80 QL------ERELREAQEEVARLEEESERKEEEAERLQEELEEAREEEEEAK----------------EKLLAASTSPSHH 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568961011 1088 VEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVED 1127
Cdd:pfam00769 138 HSEESENEDDEEEEESYEGGSAELSNDGDMDQLSDRIEEE 177
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
924-1209 |
7.06e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 924 EKVQKLEAELEKAATHRHSYEE--KGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKltRQLFDDV 1001
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEakKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK--KKAEEAK 1570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1002 QKEEQQRLVLEKGFELKtQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGE----------VARLSKQAKTI 1071
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAK-KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeekkkveqlKKKEAEEKKKA 1649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1072 SEFEKEIELLQAQKIDVEKHVQSQKREMRE-RMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDgELWFAyEGLKKATRV 1150
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE-EKKKA-EELKKAEEE 1727
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1151 LESHF-QSQKDCYEKEIEGLNFKVVHlsQEINHLQKLFREETDINESIRHEVTRLTSENM 1209
Cdd:PTZ00121 1728 NKIKAeEAKKEAEEDKKKAEEAKKDE--EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
893-1120 |
7.11e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 50.49 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 893 RLQKKLEDQNREnhglvekLTSLAALRVGDLEKVQKLEA-----ELEKAAThRHSYEEKGRRYRDTVEER---LSKLQKH 964
Cdd:pfam15921 594 QLEKEINDRRLE-------LQEFKILKDKKDAKIRELEArvsdlELEKVKL-VNAGSERLRAVKDIKQERdqlLNEVKTS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 965 NAELELQRERAEQM---LQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEK-------------GFELKTQAYEKQIES 1028
Cdd:pfam15921 666 RNELNSLSEDYEVLkrnFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdghamkvamGMQKQITAKRGQIDA 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1029 LREEIKAL--------------KDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISE----FEKEIELLQAQKIDVEK 1090
Cdd:pfam15921 746 LQSKIQFLeeamtnankekhflKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEkvanMEVALDKASLQFAECQD 825
|
250 260 270
....*....|....*....|....*....|
gi 568961011 1091 HVQSQKREmrermsEVTKQLLESYDIEDVR 1120
Cdd:pfam15921 826 IIQRQEQE------SVRLKLQHTLDVKELQ 849
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
923-1124 |
9.78e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 923 LEKVQKLEAELEKAATHRhSYEEKGRRYRD--TVEERLSKLQKHNAELElQRERAEQMLQekseelkekmdkltrQLFDD 1000
Cdd:PRK04863 479 YQLVRKIAGEVSRSEAWD-VARELLRRLREqrHLAEQLQQLRMRLSELE-QRLRQQQRAE---------------RLLAE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1001 VQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEgqvtsdrLKGEVARLSKQAKTISEFEKEIEL 1080
Cdd:PRK04863 542 FCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ-------LQARIQRLAARAPAWLAAQDALAR 614
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568961011 1081 LQAQ-------KIDVEKHVQSQKRemRERMSEVTKQLLES--YDIEDVRSRLS 1124
Cdd:PRK04863 615 LREQsgeefedSQDVTEYMQQLLE--RERELTVERDELAArkQALDEEIERLS 665
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
892-1167 |
1.06e-05 |
|
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: 49.97 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 892 QRLQKKLEDQNRENHGLVEKLTslaalrvgDLEKVQKLEAELEKAathrhsyeeKGRRYRDTVEERLSKLQKHNAELELQ 971
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRA--------RIEELRAQEAVLEET---------QERINRARKAAPLAAHIKAVTQIEQQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 972 RERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLV--LEKGFELKTQAYEKQIeSLREEIKALKDERSQLHHQLEE 1049
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtLHSQEIHIRDAHEVAT-SIREISCQQHTLTQHIHTLQQQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1050 GQVTSDRLKGEVARLSK---QAKTISEFEKEIELLQAQKIDVEKHVQSQKR--EMRERMSEVTKQLLESYDIEDVRSRLS 1124
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDIlqrEQATIDTRTSAFRDLQGQLAHAKKQQELQQRyaELCAAAITCTAQCEKLEKIHLQESAQS 467
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568961011 1125 VEDLEHLNEDGELWFAYEGLKKATR--VLESHFQSQKDCYEKEIE 1167
Cdd:TIGR00618 468 LKEREQQLQTKEQIHLQETRKKAVVlaRLLELQEEPCPLCGSCIH 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
890-1079 |
1.13e-05 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 50.10 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLE-KVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAEL 968
Cdd:COG1196 341 ERETLLEELEQLLAELEEAKEELEEKLSALLEELEeLFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 969 ELQRERAEQMLQEKSE------ELKEKMDKLTRQLFDDVQKEEQQRLVLEKgFELKTQAYEKQIESLREEIKALKDERSQ 1042
Cdd:COG1196 421 EDLKEELKELEAELEElqteleELNEELEELEEQLEELRDRLKELERELAE-LQEELQRLEKELSSLEARLDRLEAEQRA 499
|
170 180 190
....*....|....*....|....*....|....*..
gi 568961011 1043 LHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIE 1079
Cdd:COG1196 500 SQGVRAVLEALESGLPGVYGPVAELIKVKEKYETALE 536
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
886-1180 |
1.27e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 49.71 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 886 QLTYRVQRLQKKLEDQNRenhgLVEKLTSLAALRVGDLE-KVQKLEAELEKAATHRhsyeekgRRYRDTVEERLSKLQKH 964
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNE----LHEKQKFYLRQSVIDLQtKLQEMQMERDAMADIR-------RRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 965 NAELELQRERAEQMLQEKSEELkekmDKLTRQLF--DDVQKEEQQRLVlekGFElktQAYEKQIESlreeikalKDERSQ 1042
Cdd:pfam15921 151 VHELEAAKCLKEDMLNDSNTQI----EQLRKMMLshEGVLQEIRSILV---DFE---EASGKKIYE--------HDSMST 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1043 LHHQ---------LEEGQVTSDRLKGEVARLSKQAKTI-SEFEKEIELLQAQKID-VEKHVQSQKRE---MRERMSEVTK 1108
Cdd:pfam15921 213 IHFRslgsaiskiLRELDTEISYLKGRIFPVEDQLEALkSESQNKIELLLQQHQDrIEQLISEHEVEitgLTEKASSARS 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568961011 1109 QllesydIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEI 1180
Cdd:pfam15921 293 Q------ANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
955-1106 |
1.33e-05 |
|
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: 49.44 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 955 EERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMD-KLT-----RQLFDDVQKEEQQRLVLEKGFE-LKTQAY--EKQ 1025
Cdd:pfam10174 337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEeKSTlageiRDLKDMLDVKERKINVLQKKIEnLQEQLRdkDKQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1026 IESLREEIKALKDERSQ-------LHHQLEEGQVTSDRLKGEVARLSKqaktisEFEKEIELLQAQKIDVEKHVQSQKRE 1098
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNtdtalttLEEALSEKERIIERLKEQREREDR------ERLEELESLKKENKDLKEKVSALQPE 490
|
....*...
gi 568961011 1099 MRERMSEV 1106
Cdd:pfam10174 491 LTEKESSL 498
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
845-1137 |
1.53e-05 |
|
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: 49.58 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 845 LARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrvgdLE 924
Cdd:pfam02463 185 LAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES-------SK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 925 KVQKLEAELEKaatHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKE 1004
Cdd:pfam02463 258 QEIEKEEEKLA---QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1005 EQ--QRLVLEKGFELKTQAYEKQIESLREEIKAL---KDERSQLHHQLEEGQVTSDRLKGEVarLSKQAKTISEFEKEIE 1079
Cdd:pfam02463 335 EEieELEKELKELEIKREAEEEEEEELEKLQEKLeqlEEELLAKKKLESERLSSAAKLKEEE--LELKSEEEKEAQLLLE 412
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011 1080 LLQAQKIDVEKHVQSQKREmrermSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGEL 1137
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEI-----LEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
941-1117 |
1.78e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 225288 [Multi-domain] Cd Length: 652 Bit Score: 48.93 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 941 HSYEEKGRRyrdtVEERLSKLQKhnaelELQRERAEQM------LQEKSEELKEKmdkltRQLFDDVQKEEQQRlVLEKG 1014
Cdd:COG2433 355 LAYKPKLEK----VERKLPELGI-----WKDVERIKALvirgypLAEALSKVKEE-----ERPREKEGTEEEER-REITV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1015 FELKTQAYEKQIESLREEIKALKDErsqlhhqLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQs 1094
Cdd:COG2433 420 YEKRIKKLEETVERLEEENSELKRE-------LEELKREIEKLESELERFRREVRDKVRKDREIRARDRRIERLEKELE- 491
|
170 180
....*....|....*....|...
gi 568961011 1095 QKREMRERMSEVTKQLLESYDIE 1117
Cdd:COG2433 492 EKKKRVEELERKLAELRKMRKLE 514
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
627-652 |
3.41e-05 |
|
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: 45.80 E-value: 3.41e-05
10 20
....*....|....*....|....*.
gi 568961011 627 KFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd01363 145 IINESLNTLMNVLRATRPHFVRCISP 170
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
924-1167 |
3.56e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 924 EKVQKLEaELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAEL-----------ELQRERAEQMlqEKSEELKEKMDK 992
Cdd:PTZ00121 1561 EEKKKAE-EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEkkmkaeeakkaEEAKIKAEEL--KKAEEEKKKVEQ 1637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 993 LTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLR--EEIKALKDERSQLHHQLEEgqvtsdrlKGEVARLSKQAKT 1070
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKkaEEAKKAEEDEKKAAEALKK--------EAEEAKKAEELKK 1709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1071 ISEFEKEiellQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRlsveDLEHLNEDGELWfAYEGLKKATRV 1150
Cdd:PTZ00121 1710 KEAEEKK----KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK----KIAHLKKEEEKK-AEEIRKEKEAV 1780
|
250
....*....|....*..
gi 568961011 1151 LESHFQSQKDCYEKEIE 1167
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVD 1797
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is ... |
890-1009 |
3.74e-05 |
|
MAP7 (E-MAP-115) family; The organisation of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilizing protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 428577 [Multi-domain] Cd Length: 153 Bit Score: 45.01 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNR-----ENHGLVEKLTSLAAlrvgdlEKVQKLEAELEKAATHRH-SYEEKGRRYRDTVEERLSKLQK 963
Cdd:pfam05672 21 RQAREQREREEQERlekeeEERLRREELRRRAE------EERARREEEARRLEEERKrEEEERQRKAEEEAEEKEQREKE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568961011 964 HNAELELQRERAEQMLQEKSEELKEKMDKLTrqlfddvQKEEQQRL 1009
Cdd:pfam05672 95 EQERLQKQKEEAEAKAREEAERQRQEREKIM-------QQEEQERL 133
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
922-1129 |
3.93e-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: 433539 [Multi-domain] Cd Length: 341 Bit Score: 47.22 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 922 DLEKVQKLEAELEKAATHRHSY----EEKGRRYRDTVEERlsklqKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQL 997
Cdd:pfam13868 4 NSDELRELNSKLLAAKCNKERDaqieEKKRIKAEEKEEER-----RLDEMMEEERERALEEEEEKEEERKEERKQYRQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 998 FDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREE----IKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQA-KTIS 1072
Cdd:pfam13868 79 EEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEdqaeAEEKLEKQRQLREEIDEFNEEQAKWKELEKEEEKEEdLRIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961011 1073 EFEKEIELLQAQKidvEKHVQSQKREMRERMSEVTKQLLESYD----IEDVRSRLSVEDLE 1129
Cdd:pfam13868 159 EYLKEKAEREEER---EAERREIKEEKEREIARLRAQQEKAQDekaeRDELRAKLYQEEQE 216
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
896-1204 |
3.96e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.91 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 896 KKLEDQNRENHGLVEKLtslaalrvgdLEKVQKLEAELekaATHRHSYeekGRRYrDTVEERLSKLQKHNAELE------ 969
Cdd:PRK04778 129 QELLESEEKNREEVEQL----------KDLYRELRKSL---LANRFSF---GPAL-DELEKQLENLEEEFSQFVeltesg 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 970 --LQRERAEQMLQEKSEELKEKMDKLTrQLFDDVQKEEQQRL---------VLEKGFELKTQAYEKQIESLREEIKALKD 1038
Cdd:PRK04778 192 dyVEAREILDQLEEELAALEQIMEEIP-ELLKELQTELPDQLqelkagyreLVEEGYHLDHLDIEKEIQDLKEQIDENLA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1039 ERSQLhhqleegqvtsdrlkgEVARLSKQAKTISE--------FEKEIEllqAQKiDVEKHvQSQKREMRERMSEVTKQL 1110
Cdd:PRK04778 271 LLEEL----------------DLDEAEEKNEEIQEridqlydiLEREVK---ARK-YVEKN-SDTLPDFLEHAKEQNKEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1111 L-------ESY-----DIEDVRSRLsvEDLEHLNEDgelwfayegLKKATRVLESH---FQSQKDCYEKEIEGLnfKVVH 1175
Cdd:PRK04778 330 KeeidrvkQSYtlnesELESVRQLE--KQLESLEKQ---------YDEITERIAEQeiaYSELQEELEEILKQL--EEIE 396
|
330 340 350
....*....|....*....|....*....|.
gi 568961011 1176 LSQE--INHLQKLFREETDINESIRHEVTRL 1204
Cdd:PRK04778 397 KEQEklSEMLQGLRKDELEAREKLERYRNKL 427
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
924-1086 |
4.04e-05 |
|
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: 47.83 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 924 EKVQKLEAELE--KAATHRHSYE--EKGRRYRDTVEERLSKLQKHNAELELQRERAEQmlQEKSEELKEKMDKLTRQLFD 999
Cdd:pfam09731 294 REIDQLSKKLAelKKREEKHIERalEKQKEELDKLAEELSARLEEVRAADEAQLRLEF--EREREEIRESYEEKLRTELE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1000 DVQKEEQQRLvlekGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEgqvtsdrLKGEVARLSKQAKTISEFEKEIe 1079
Cdd:pfam09731 372 RQAEAHEEHL----KDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNE-------LLANLKGLEKATSSHSEVEDEN- 439
|
....*..
gi 568961011 1080 lLQAQKI 1086
Cdd:pfam09731 440 -RKAQQL 445
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
913-1106 |
4.07e-05 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 47.71 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 913 TSLAALRVGD------LEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEEL 986
Cdd:COG4372 57 ATLAILFLLNrnlrsgVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 987 KEkMDKLTRQlfddvQKEEQQRLvlekgfelKTQAYEKQieSLREEIKALKDERSQLhhqleegQVTSDRLKGEVARLSK 1066
Cdd:COG4372 137 QE-LARLTKQ-----AQDLQTRL--------KTLAEQRR--QLEAQAQSLQASQKQL-------QASATQLKSQVLDLKL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568961011 1067 QAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEV 1106
Cdd:COG4372 194 RSAQIEQEAQNLATRANAAQARTEELARRAAAAQQTAQAI 233
|
|
| Lipoprotein_7 |
pfam01540 |
Adhesin lipoprotein; This family consists of the p50 and variable adherence-associated antigen ... |
926-1139 |
4.46e-05 |
|
Adhesin lipoprotein; This family consists of the p50 and variable adherence-associated antigen (Vaa) adhesins from Mycoplasma hominis. M. hominis is a mycoplasma associated with human urogenital diseases, pneumonia, and septic arthritis. An adhesin is a cell surface molecule that mediates adhesion to other cells or to the surrounding surface or substrate. The Vaa antigen is a 50-kDa surface lipoprotein that has four tandem repetitive DNA sequences encoding a periodic peptide structure, and is highly immunogenic in the human host. p50 is also a 50-kDa lipoprotein, having three repeats A,B and C, that may be a tetramer of 191-kDa in its native environment.
Pssm-ID: 110537 [Multi-domain] Cd Length: 353 Bit Score: 47.39 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 926 VQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAEL-ELQRERAE--QMLQEKSEELKEKM---DKLTRQL-- 997
Cdd:pfam01540 92 ISKLSAAVENAKNEKKAIDDKNAQIAKELAERNAKIQSNIEELkKINNEAFElsKTVNKTIAEVEKKFkipKDFKEQLen 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 998 -FDDVQKEEQQRLVLEKGFELKTQAYEKQIESLRE-------EIK--------ALKDERSQLHhQLEEGQVTSDRLKGEV 1061
Cdd:pfam01540 172 fADDLLDKSRQIDEFTTVTSTQEGFTLAELESFKEitttwfnGMKsewarvldAWKNELTEIN-SIIKGVEELKKLSHEI 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961011 1062 ARLSKQA-KTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGELWF 1139
Cdd:pfam01540 251 SEFSNSVkKTISELEKKFKIDDKTNKEEAKKFKNELENFADQLLNKSHEIDKFVTVTSARGDFSLSELESFKSFNTTWF 329
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
894-1136 |
6.01e-05 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227606 [Multi-domain] Cd Length: 833 Bit Score: 47.33 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 894 LQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSY--EEKGRRYRDTVEERLSKLQKHNAELELQ 971
Cdd:COG5281 357 LAAKLAAEKLARVTAQGALNARLKLAQDDLTQAELNYAAADQAANQEGALnaREDEAEVLSTQEERRDILKNLLADAEKR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 972 RERAEQMLQEKSEELKEKMDKLTRQLFDDV-QKEEQQRLvlekgfelKTQAYEKQIESLREEIKALKDERSQLhHQLEEG 1050
Cdd:COG5281 437 TARQEELNKALAKAKILQADKAAKAYQEDIlQREAQSRG--------KTAAAERSQEQMTAALKALLAFQQQI-ADLSGA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1051 QVTSDRLKGEVARLSKQAKTISEfEKEIELLQAQKIDvekhvQSQKREmrerMSEVTKQLLESYDIEDVRSRLSVEDLEH 1130
Cdd:COG5281 508 KEKASDQKSLLWKAEEQYALLKE-EAKQRQLQEQKAL-----LEHKKE----TLEYTSQLAELLDQQADRFELSAQAAGS 577
|
....*.
gi 568961011 1131 LNEDGE 1136
Cdd:COG5281 578 QKERGS 583
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
881-1043 |
6.80e-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: 435008 [Multi-domain] Cd Length: 329 Bit Score: 46.35 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 881 FVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAathrHSYEEKGRRYR---DTVEER 957
Cdd:pfam15905 176 MAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITEL----SCVSEQVEKYKldiAQLEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 958 LSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLtrqlfddvqKEEQQRLVLEkgFELKTQAYEKQIESLREEIKALK 1037
Cdd:pfam15905 252 LKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLL---------ESEKEELLRE--YEEKEQTLNAELEELKEKLTLEE 320
|
....*.
gi 568961011 1038 DERSQL 1043
Cdd:pfam15905 321 QEHQKL 326
|
|
| JMY |
pfam15871 |
Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is ... |
890-1051 |
7.26e-05 |
|
Junction-mediating and -regulatory protein; JMY, Junction-mediating and -regulatory protein is also a WASP homolog-associated protein with actin, membranes and microtubules. This middle region is the coiled-coil region that putatively binds microtubules to the scaffold. This ability to interact with microtubules plays a role in membrane tubulation.
Pssm-ID: 434985 Cd Length: 298 Bit Score: 46.18 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNRENHglvEKLTSLAALRVGDLEKVQKLEAELEKaathrhSYEEKGRRYRDTV----EERLSKLQKHN 965
Cdd:pfam15871 129 RVEALQKEAEEWQRRAE---EAVDSIQDITVNYFKETVKALKAMQK------QMEQDQKRFGKAAwasaAPRLEKLKYML 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 966 AELELQRERAEQM-LQEKSEELKEKMDKLTrqlfddvQKEEQQRLV--LE-KGFELKTQAYEKQIESLREEIKALKDERS 1041
Cdd:pfam15871 200 AKETLQLMRAKELcLNQKRAEIKKEMESLD-------EGEGAVAVVdeLEiQYYELQLELYEVQLEILKNEELLLTAQLD 272
|
170
....*....|
gi 568961011 1042 QLHHQLEEGQ 1051
Cdd:pfam15871 273 SLRRQIKEKQ 282
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
895-1206 |
8.60e-05 |
|
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: 47.02 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 895 QKKLEDQNRENHGLVEKLTSLAALRVGDLE----KVQKLEAELEKAATHRHSYEEKGRRYRDTVE-ERL--SKLQKHNAE 967
Cdd:pfam05483 417 DEKLLDEKKQFEKIAEELKGKEQELIFLLQarekEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkEKLknIELTAHCDK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 968 LELQRERAEQMLQEKSEELKEKMDKLtrqlfDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDErsqLHHQL 1047
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDI-----INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDE---VKCKL 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1048 EEGQVTSDRLKGEVARLSKQAKTI----SEFEKEIEllqaQKIDVEKHVQSQKREMRERMSEVTKQlLESYDIEDVRSRL 1123
Cdd:pfam05483 569 DKSEENARSIEYEVLKKEKQMKILenkcNNLKKQIE----NKNKNIEELHQENKALKKKGSAENKQ-LNAYEIKVNKLEL 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1124 SVEDLEHlnedgelwfayeglkkatrvlesHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFRE----ETDINESIRH 1199
Cdd:pfam05483 644 ELASAKQ-----------------------KFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavklQKEIDKRCQH 700
|
....*..
gi 568961011 1200 EVTRLTS 1206
Cdd:pfam05483 701 KIAEMVA 707
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
884-1110 |
8.81e-05 |
|
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: 45.50 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 884 NIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrvgdlekvqKLEAELEKAATHRhsyeeKGRRYRDtVEERLSKLQK 963
Cdd:pfam17078 19 NLQLTVQSQNLLSKLEIAQQKESKFLENLASL------------KHENDNLSSMLNR-----KERRLKD-LEDQLSELKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 964 HNAELELQ----RERAEQmLQEKSEELKEKMDKLTRQLfdDVQKEEQQRLvlekgfelkTQAYEKQIESLREEIKALKDE 1039
Cdd:pfam17078 81 SYEELTESnkqlKKRLEN-SSASETTLEAELERLQIQY--DALVDSQNEY---------KDHYQQEINTLQESLEDLKLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1040 rsqLHHQLEE-GQVTSDRLKGEVARLS------KQAKTISEfEKEIELLQ-----AQKIDVEKHVQSQKrEMRERMSEVT 1107
Cdd:pfam17078 149 ---NEKQLENyQQRISSNDKDIDTKLDsynnkfKNLDNIYV-NKNNKLLTkldslAQLLDLPSWLNLYP-ESRNKILEYA 223
|
...
gi 568961011 1108 KQL 1110
Cdd:pfam17078 224 EKM 226
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
911-1160 |
8.91e-05 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 434726 [Multi-domain] Cd Length: 520 Bit Score: 46.77 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 911 KLTSLAALRVGDLEKVQKL--EAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKhnaelelQRERAEQMLQEKSEELKE 988
Cdd:pfam15450 187 KLCSFLQKSFLALEKRMKAseSTRLKAESSLREELEGKWQKLQELTEERLRALTG-------QLEQEEGHLLEQCRGLDE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 989 KMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESL----REEIKALKDE----RSQLHHQLEEGQVTSDRLKGE 1060
Cdd:pfam15450 260 AVVQLTKFVRQNQVSLNRVLLAEQKARDAKGQLEESRAGELasymQESLEAMQLAgdlaRRETQAALELLQEKSQVLEHS 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1061 VARLSKQAKTISEF--------------------EKEIELLQAQKIDVEKHVQSQK------REMRERMSEVTKQllesy 1114
Cdd:pfam15450 340 VAELVTQLKDLSDHflalswrldlqeqtlglklsEAQEEWEGAERRSLEKLAQWQKevpahlREVQEKVDSLPRQ----- 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 568961011 1115 dIEDVRSRL----SVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKD 1160
Cdd:pfam15450 415 -IEAVSDKCvlhkSDSDLKISAEGKAREFEVKALRQELATLLSSVQLLKE 463
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
870-1100 |
9.80e-05 |
|
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: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 870 LARRRFQNIRrfvLN-IQLTYRVQRLQKKLEDQ-NRENHGLVEKLTSLAA-LRVGDLEKVQKLEAELEKAATHRhsyEEK 946
Cdd:pfam12128 643 FARTALKNAR---LDlRRLFDEKQSEKDKKNKAlAERKDSANERLNSLEAqLKQLDKKHQAWLEEQKEQKREAR---TEK 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 947 GRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLtrqlfdDVqkEEQQRLVLEKGFELKTQAYEkQI 1026
Cdd:pfam12128 717 QAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASL------GV--DPDVIAKLKREIRTLERKIE-RI 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1027 ESLREEIKALKD--------ERSQLHHQLEEGQVTSDRLKGEVARLSKQAKT-ISEFEKEIELLQAQKIDVEKHVQSQKR 1097
Cdd:pfam12128 788 AVRRQEVLRYFDwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTKLrRAKLEMERKASEKQQVRLSENLRGLRC 867
|
...
gi 568961011 1098 EMR 1100
Cdd:pfam12128 868 EMS 870
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
960-1131 |
1.00e-04 |
|
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: 45.78 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 960 KLQKHNAELELQRERAEQMLQEkSEELKEKMDKLtrqlfDDVQKEEQQRLVlekgfelktqAYEKQIESLREEIKALKDE 1039
Cdd:smart00787 120 QLVKTFARLEAKKMWYEWRMKL-LEGLKEGLDEN-----LEGLKEDYKLLM----------KELELLNSIKPKLRDRKDA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1040 RSQLHHQLEEG-----QVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQS---QKREMRERMSEVTKQLL 1111
Cdd:smart00787 184 LEEELRQLKQLedeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDltnKKSELNTEIAEAEKKLE 263
|
170 180
....*....|....*....|...
gi 568961011 1112 ES--YDIEDVRS-RLSVEDLEHL 1131
Cdd:smart00787 264 QCrgFTFKEIEKlKEQLKLLQSL 286
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
924-1082 |
1.07e-04 |
|
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: 430106 [Multi-domain] Cd Length: 176 Bit Score: 44.15 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 924 EKVQKLEAELEKAATHRHSYE-EKGRRYRDTVEERLSKLQKHNAEL-ELQRERAE--QMLQEKSEELKEKMDKLTRQlfd 999
Cdd:pfam08614 21 AENAALQSEPESVPPSTSSSTaSASPVQSASIQSLEQLLAQLREELaELYRSRGElaQQLVDLNEELQELEKKLRED--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1000 dvqkeeqqrlvlekgfelktqayEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVA----RLSKQAKTISEFE 1075
Cdd:pfam08614 98 -----------------------ERRLAELEAERAQLEEKLRDREEELREKRKLNQDLQDELValqlQLNMAEEKLRKLE 154
|
....*...
gi 568961011 1076 KE-IELLQ 1082
Cdd:pfam08614 155 KEnRELVE 162
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1015-1205 |
1.08e-04 |
|
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: 46.59 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1015 FELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVA-----------RLSKQAKTISEFEKEIELLQA 1083
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEqlrkeleelsrQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1084 QKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSvEDLEHLNEDGELW-FAYEGLKKATRVLESHFQSQkdcy 1162
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE-AQIEQLKEELKALrEALDELRAELTLLNEEAANL---- 822
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568961011 1163 EKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLT 1205
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
924-1100 |
1.11e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 924 EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELelqRERAEQMLQEKSEELKEKMDKLTRQLfddvqk 1003
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEAQQAIKEAKKEADEIIKEL------ 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1004 eeqQRLVLEKGFELKTQAYE---KQIESLREEIKALKDERSQLHHQLEEGQ---VTSDRLKGEVARLSKQAKTISEF--- 1074
Cdd:PRK00409 594 ---RQLQKGGYASVKAHELIearKRLNKANEKKEKKKKKQKEKQEELKVGDevkYLSLGQKGEVLSIPDDKEAIVQAgim 670
|
170 180 190
....*....|....*....|....*....|.
gi 568961011 1075 -----EKEIELLQAQKIDVEKHVQSQKREMR 1100
Cdd:PRK00409 671 kmkvpLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
957-1085 |
1.13e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 224755 [Multi-domain] Cd Length: 225 Bit Score: 45.00 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 957 RLSKLQKHNA-ELELQRERAEQMLQEKSEELKEKMDKLT----------RQLFDDVQKEEQQRLVLEKGFEL-KTQAYEK 1024
Cdd:COG1842 6 RLKDLVKANInELLDKAEDPEKMLEQAIRDMESELAKARqalaqaiarqKQLERKLEEAQARAEKLEEKAELaLQAGNED 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961011 1025 QIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISEFEKEIELLQAQK 1085
Cdd:COG1842 86 LAREALEEKQSLEDLAKALEAELQQAEEQVEKLKKQLAALEQK---IAELRAKKEALKARK 143
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
890-1104 |
1.16e-04 |
|
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: 46.60 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNRENHGLVEKLTSLAAlrvgDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELE 969
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIEQ----KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 970 LQRERAEQMLQEKSEELKEkmdkltrqlfddvqkeeqqrlvlekgfelktqaYEKQIESLREEIKALKDERSQLHHQLEE 1049
Cdd:TIGR02169 868 EELEELEAALRDLESRLGD---------------------------------LKKERDELEAQLRELERKIEELEAQIEK 914
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568961011 1050 GQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhVQSQKREMRERMS 1104
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIR 968
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
875-1208 |
1.51e-04 |
|
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: 46.58 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 875 FQNIRRFVLNIQLTYR-VQRLQKKLED--QNRENHGLVEKLTSLAALRvGDLEKVQKLEAELEKAATHRHSYEEKGRRYR 951
Cdd:TIGR01612 1442 FKNADENNENVLLLFKnIEMADNKSQHilKIKKDNATNDHDFNINELK-EHIDKSKGCKDEADKNAKAIEKNKELFEQYK 1520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 952 DTVEERLSKLqkhnAELELQ------RERAEQMLQE----------KSEELKEKMDKLTRQLF---DDVQKEEQQ----- 1007
Cdd:TIGR01612 1521 KDVTELLNKY----SALAIKnkfaktKKDSEIIIKEikdahkkfilEAEKSEQKIKEIKKEKFrieDDAAKNDKSnkaai 1596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1008 --RLVLEKgFE---LKTQAYEKQIESLREEIKALKDERSQL-----HHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKE 1077
Cdd:TIGR01612 1597 diQLSLEN-FEnkfLKISDIKKKINDCLKETESIEKKISSFsidsqDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKE 1675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1078 IELLQAQ----KIDVEKHVQSQKREMRERMSEV----------TKQLLESyDIEDVRSRLSVEDLEHLNEDGElwfayeg 1143
Cdd:TIGR01612 1676 LDELDSEiekiEIDVDQHKKNYEIGIIEKIKEIaiankeeiesIKELIEP-TIENLISSFNTNDLEGIDPNEK------- 1747
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961011 1144 lkkatrvLESHFQSQKDCYEKEIEGLNFKVvhlsqeiNHLQKLFREETDINEsIRHevTRLTSEN 1208
Cdd:TIGR01612 1748 -------LEEYNTEIGDIYEEFIELYNIIA-------GCLETVSKEPITYDE-IKN--TRINAQN 1795
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
741-1184 |
1.54e-04 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 46.38 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 741 RAGQVAYLEKLRLDKLRQDCIMIQK---HVRGWLQRRKFLRERQAAltiqryFRGQQTVRKAITAtalkeAWAAIILqky 817
Cdd:COG4717 418 RAGDEAREEKIAANSQVIDKEEVCNlydRRDTAWQKQRFLREKQTA------FERQKTEHTKIIA-----LRLAGML--- 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 818 cRGYLVRNLYQLIrvATITIQAHTRGFLarrryrkllqehKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKK 897
Cdd:COG4717 484 -LVALSRLLTSLI--FQIIFAVAQIVFL------------SAEIKSSSRAVREEKAAVTDIPEELARLLITDELPELAVD 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 898 LEDQNRENHGLVEKLTSLAALRvgdlEKVQKLEAELEKAATHRHSYEEKGRRYRDT-----------VEERLS------K 960
Cdd:COG4717 549 LLVQSRIRQHWQQLRKALDQLE----AAYEALEGRFAAAEAAMAEWQSEWEEALDElglsrelspeqQLDILStmkdlkK 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 961 LQKHNAELELQRERaeqmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELktqayEKQIESLREEIKALKDER 1040
Cdd:COG4717 625 LMQKKAELTHQVAR----LREEQAAFEERVEGLLAVLEAQFIDLSTLFCVQRLRVAA-----ELQKEEARLALEGNIERT 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1041 SQLHHQLEEgqvtsdrlkgevarlskqakTISEFEKEIE-LLQAQKIDVE-------KHVQsQKREMRERMSEVTKQLLE 1112
Cdd:COG4717 696 KELNDELRA--------------------ELELHRKEILdLFDCGTADTEdafreaaREEQ-QLTQRESRLESLEAQLEG 754
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568961011 1113 SYDiedvrSRLSVEDLEHLNEDGELWFAYEglkkatrvleshfQSQKDCYEKEIEGLNFKVVHLSQEINHLQ 1184
Cdd:COG4717 755 VAA-----EAYELSASLDQRELKEEELALL-------------EEAIDALDEEVEELHAQVAALSRQIAQLE 808
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
929-1030 |
1.54e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.26 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 929 LEAELEKAATHRHSYEEKGRRyrdTVEERLSK-LQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDD-----VQ 1002
Cdd:cd16269 187 LQADQALTEKEKEIEAERAKA---EAAEQERKlLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEqeralES 263
|
90 100
....*....|....*....|....*...
gi 568961011 1003 KEEQQRLVLEKGFELKTQAYEKQIESLR 1030
Cdd:cd16269 264 KLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| COG4026 |
COG4026 |
Uncharacterized protein, contains TOPRIM domain, potential nuclease [General function ... |
861-1042 |
1.72e-04 |
|
Uncharacterized protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 226513 [Multi-domain] Cd Length: 290 Bit Score: 44.90 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 861 ILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAAlrvgdleKVQKLEAELEKAATHR 940
Cdd:COG4026 107 LVRKELKNALVRAGLKTLQRVPEYMDLKEDYEELKEKLEELQKEKEELLKELEELEA-------EYEEVQERLKRLEVEN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 941 HSYEEKgrryRDTVEERLSKLQKHNAELELQRERAEQMLQEK--SEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGF--- 1015
Cdd:COG4026 180 SRLEEM----LKKLPGEVYDLKKRWDELEPGVELPEEELISDlvKETLNLAPKDIEGQGYIYAEDEKEVEILLGTVYiaa 255
|
170 180
....*....|....*....|....*....
gi 568961011 1016 ELKTQAYE--KQIESLREEIKALKDERSQ 1042
Cdd:COG4026 256 PSREDAVEelEIIKEAIEEVIPEIDEEGE 284
|
|
| COG4026 |
COG4026 |
Uncharacterized protein, contains TOPRIM domain, potential nuclease [General function ... |
970-1086 |
1.97e-04 |
|
Uncharacterized protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 226513 [Multi-domain] Cd Length: 290 Bit Score: 44.90 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 970 LQRERAEQMLQEKSEELKEKmdkltrqlFDDVQKEEQQrlVLEKGFELktqayEKQIESLREEIKALKDERSQLHHQLee 1049
Cdd:COG4026 124 LQRVPEYMDLKEDYEELKEK--------LEELQKEKEE--LLKELEEL-----EAEYEEVQERLKRLEVENSRLEEML-- 186
|
90 100 110
....*....|....*....|....*....|....*..
gi 568961011 1050 gqvtsDRLKGEVARLSKQaktISEFEKEIELLQAQKI 1086
Cdd:COG4026 187 -----KKLPGEVYDLKKR---WDELEPGVELPEEELI 215
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
890-1204 |
1.99e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNRENHGLVEKLTSLAALrvgdLEKVQKLEAELEKAATHRHSYEEKGRRYRDtVEERLSKLQkhNAELE 969
Cdd:PRK01156 219 EIERLSIEYNNAMDDYNNLKSALNELSSL----EDMKNRYESEIKTAESDLSMELEKNNYYKE-LEERHMKII--NDPVY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 970 LQRERAEQMLQEKSEelKEKMDKLTRQLFDDVQKEEQQRLVLEkgfelktqayekQIESLREEIKALKDERSQLHHQLEE 1049
Cdd:PRK01156 292 KNRNYINDYFKYKND--IENKKQILSNIDAEINKYHAIIKKLS------------VLQKDYNDYIKKKSRYDDLNNQILE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1050 GQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLE-SYDIE--DVRSRLSVE 1126
Cdd:PRK01156 358 LEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDiSSKVSslNQRIRALRE 437
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011 1127 DLEHLNEDGELwfaYEGLKKATrVLESHFQSQKDcyEKEIEGLNFKVVHLSQEINHLQklfREETDINESIRHEVTRL 1204
Cdd:PRK01156 438 NLDELSRNMEM---LNGQSVCP-VCGTTLGEEKS--NHIINHYNEKKSRLEEKIREIE---IEVKDIDEKIVDLKKRK 506
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
894-1185 |
2.01e-04 |
|
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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 45.92 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 894 LQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAathrHSYEEKGRRYRDTVEERLSKLQkhnAELELQRE 973
Cdd:pfam01576 375 LEKAKQALESENAELQAELRSLQQAKQDSEHKRKKLEGQLQEL----QSRLSESERQRAELAEKLSKLQ---SELESVSS 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 974 RAEQmLQEKSEELKEKMDKLTRQLFDD---VQKEEQQRLvlekgfelktqayekqieSLREEIKALKDERSQLHHQLEEg 1050
Cdd:pfam01576 448 LLNE-AEGKNIKLSKDVSSLESQLQDTqelLQEETRQKL------------------NLSSRLRQLEDEKNSLQEQLEE- 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1051 qvtsdrlkGEVARlskqaktiSEFEKEIELLQAQKIDVEKHVQsQKREMRERMSEVTKQLLEsyDIEDVRSRLSvedleh 1130
Cdd:pfam01576 508 --------EEEAK--------RNVERQLQTLQAQLSDLKKKLE-EDAGAVEALEEGRKRLQR--ELEALTQRLE------ 562
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568961011 1131 lnedgELWFAYEGLKKATRVLeshfqsqkdcyEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:pfam01576 563 -----EKAAAYDKLEKTKNRL-----------QQELDDLLVDLDHQRQLVSNLEK 601
|
|
| K-box |
pfam01486 |
K-box region; The K-box region is commonly found associated with SRF-type transcription ... |
973-1048 |
2.03e-04 |
|
K-box region; The K-box region is commonly found associated with SRF-type transcription factors see pfam00319. The K-box is a possible coiled-coil structure. Possible role in multimer formation.
Pssm-ID: 426286 [Multi-domain] Cd Length: 91 Bit Score: 41.29 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 973 ERAEQMLQEKSEELKEKMDKLTRQL------------FDDVQKEEQQrlvLEKGF----ELKTQAYEKQIESLREEIKAL 1036
Cdd:pfam01486 3 ENEQENWQQEAAKLKKEIENLQRSQrhllgedlsslsLKELQQLEQQ---LEKSLkrirSRKNQLLLEQIEELKKKERIL 79
|
90
....*....|..
gi 568961011 1037 KDERSQLHHQLE 1048
Cdd:pfam01486 80 QEENKELRKKLE 91
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
852-1166 |
2.09e-04 |
|
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: 45.81 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 852 KLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEA 931
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKS 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 932 ELEKAATHRHSYEEKGRR---YRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRqlfddvqKEEQQR 1008
Cdd:TIGR00606 865 KTNELKSEKLQIGTNLQRrqqFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISS-------KETSNK 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1009 LVlekgfelktqayEKQIESLREEIKALKDERSQLHHQLEEGQvtSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDV 1088
Cdd:TIGR00606 938 KA------------QDKVNDIKEKVKNIHGYMKDIENKIQDGK--DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLM 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1089 EKHVQSQKREMRERMSEVTKQLLESyDIEDVRSRLSVEDLEhLNEDG--ELWFAYEGLKKATRVL---ESHFQSQKDCYE 1163
Cdd:TIGR00606 1004 RQDIDTQKIQERWLQDNLTLRKREN-ELKEVEEELKQHLKE-MGQMQvlQMKQEHQKLEENIDLIkrnHVLALGRQKGYE 1081
|
...
gi 568961011 1164 KEI 1166
Cdd:TIGR00606 1082 KEI 1084
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
890-1129 |
2.21e-04 |
|
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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 45.54 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNRENHGLVEKLTSLAalrvgdlekvQKLEAELEKAAthrhSYEEKGRRYRDTVEERLSKLQKHNAELE 969
Cdd:pfam01576 20 KQQKAESELKELEKKHQQLCEEKNILA----------EQLQAETELFA----EAEEMRARLAARKQELEEILHELEARLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 970 LQRERAEQMLQEKsEELKEKMDKLTRQLfdDVQKEEQQRLVLEKgfelktQAYEKQIESLREEIKALKDERSQLH---HQ 1046
Cdd:pfam01576 86 EEEERSQQLQNEK-KKMQQHIQDLEEQL--EEEEAARQKLQLEK------VTTEAKIKKMEEDILLLEDQNNKLQkerKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1047 LEE--GQVTSDRLKGE--VARLS----KQAKTISEFEKEIELLQAQKIDVEKhvqsQKREMRERMSEVTKQLLE-SYDIE 1117
Cdd:pfam01576 157 LEEriSEFTSNLAEEEekSKSLNklknKHEAMISDLEDRLKKEEKGRQELEK----AKRKLEGESSDLQEQIAElQAQIA 232
|
250
....*....|..
gi 568961011 1118 DVRSRLSVEDLE 1129
Cdd:pfam01576 233 ELRAQLAKKEEE 244
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
921-1112 |
2.72e-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: 434873 [Multi-domain] Cd Length: 521 Bit Score: 44.94 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 921 GDLEKVQKLEAELEKAATHRHSYEEKGRRYR---DTVEERLSKLQKHNAELELQR-------ERAEQMLQEKSEELKEKM 990
Cdd:pfam15709 306 GNMESEEERSEEDPSKALLEKREQEKASRDRlraERAEMRRLEVERKRREQEEQRrlqqeqlERAEKMREELELEQQRRF 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 991 D--KLTRQLFDDvqkEEQQRLVLEKGFELKTQAYE----KQIESLREEIKALKDERSQlhHQLEEGQVTSDRLKGEVARL 1064
Cdd:pfam15709 386 EeiRLRKQRLEE---ERQRQEEEERKQRLQLQAAQerarQQQEEFRRKLQELQRKKQQ--EEAERAEAEKQRQKELEMQL 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568961011 1065 SKQAKTISEFEKEIEL-LQAQKIDVEKHVQSQKREMRERMSEVTKQLLE 1112
Cdd:pfam15709 461 AEEQKRLMEMAEEERLeYQRQKQEAEEKARLEAEERRQKEEEAARLALE 509
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
887-1060 |
2.75e-04 |
|
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: 45.48 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 887 LTYRVQRLQKKLEDQNRENHGLVEKLTSLAA-LRVGDLeKVQKLEAELEKAathRHSYEEKGRRYRDTVEER-------L 958
Cdd:pfam05483 599 LKKQIENKNKNIEELHQENKALKKKGSAENKqLNAYEI-KVNKLELELASA---KQKFEEIIDNYQKEIEDKkiseeklL 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 959 SKLQKHNA----ELELQRErAEQMLQEKSEELKEKMDKLTRQlFDDVQKEEQQRLVLEKGfelKTQAYEKQIESLREEIK 1034
Cdd:pfam05483 675 EEVEKAKAiadeAVKLQKE-IDKRCQHKIAEMVALMEKHKHQ-YDKIIEERDSELGLYKN---KEQEQSSAKAALEIELS 749
|
170 180
....*....|....*....|....*.
gi 568961011 1035 ALKDERSQLHHQLEEGQVTSDRLKGE 1060
Cdd:pfam05483 750 NIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
890-1130 |
2.80e-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: 45.21 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNRENHGLVEklTSLAALRvGDL----EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQkhn 965
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWK--EKRDELN-GELsaadAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQ--- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 966 AELELQRER------AEQMLQEKSEELKEKMD-KLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKA--- 1035
Cdd:pfam12128 354 SELENLEERlkaltgKHQDVTAKYNRRRSKIKeQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAgkl 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1036 -LKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhVQSQKREMRERMSEVTKQL-LES 1113
Cdd:pfam12128 434 eFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVER-LQSELRQARKRRDQASEALrQAS 512
|
250
....*....|....*..
gi 568961011 1114 YDIEDVRSRLsvEDLEH 1130
Cdd:pfam12128 513 RRLEERQSAL--DELEL 527
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
954-1109 |
2.96e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 954 VEERLSKLQKHNAE------LELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIE 1027
Cdd:PRK12704 24 VRKKIAEAKIKEAEeeakriLEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1028 SLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEiellQAQKIDVEKhvqsQKREMRERMSEVT 1107
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE----EAKEILLEK----VEEEARHEAAVLI 175
|
..
gi 568961011 1108 KQ 1109
Cdd:PRK12704 176 KE 177
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
924-1112 |
2.99e-04 |
|
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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 45.15 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 924 EKVQKLEAELEkaathrhsyeEKGRRYRDTVEERLSKLQKHNAELELQRErAEQM---LQEKSEELKEKMDKLTRQLfdD 1000
Cdd:pfam01576 19 EKQQKAESELK----------ELEKKHQQLCEEKNILAEQLQAETELFAE-AEEMrarLAARKQELEEILHELEARL--E 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1001 VQKEEQQRLVLEKgfelktQAYEKQIESLREEIKALKDERSQLhhQLEegQVTSDrlkgevarlskqAKtISEFEKEIEL 1080
Cdd:pfam01576 86 EEEERSQQLQNEK------KKMQQHIQDLEEQLEEEEAARQKL--QLE--KVTTE------------AK-IKKMEEDILL 142
|
170 180 190
....*....|....*....|....*....|..
gi 568961011 1081 LQAQKIDVEKhvqsQKREMRERMSEVTKQLLE 1112
Cdd:pfam01576 143 LEDQNNKLQK----ERKLLEERISEFTSNLAE 170
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
979-1185 |
3.41e-04 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 43.22 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 979 LQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEkgfelktQAYEKQIESLREEIKALKDERSQLHHQLEEGQvtsdrlk 1058
Cdd:pfam14988 9 LAKKTEEKQKKIEKLWNQYVQECEEIERRRQELA-------SRYTQQTAELQTQLLQKEKEQASLKKELQALR------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1059 gEVARLSKQAktisefEKEIELLQAQKIDVEKHVQSQKREMRERMSEvTKQLLESyDIEDVRSRLSVEDLEHlnedgELW 1138
Cdd:pfam14988 75 -PFAKLKESQ------EREIQDLEEEKEKVRAETAEKDREAHLQFLK-EKALLEK-QLQELRILELGERATR-----ELK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568961011 1139 FAYEGLK-KATRVLESHFQSQKdcyeKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:pfam14988 141 RKAQALKlAAKQALSEFCRSIK----RENRQLQKELLQLIQETQALEA 184
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
747-1079 |
4.95e-04 |
|
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: 44.58 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 747 YLEKLRLDKLRQDCIMIQKHVRGWLQRRKFLRERQAALTIQRYFRGQQTVRKAITATALKEAWAAIILQKYCRGYLVRNL 826
Cdd:pfam02463 695 LRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 827 yQLIRVATITIQAHTRGFLARRRYRKLLQEHKAVILQKYARAWLarRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENH 906
Cdd:pfam02463 775 -ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL--EEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 907 GLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQE----- 981
Cdd:pfam02463 852 AEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEaeill 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 982 ----KSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKtqayEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRL 1057
Cdd:pfam02463 932 kyeeEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL----GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007
|
330 340
....*....|....*....|..
gi 568961011 1058 KGEVARLsKQAKTISEFEKEIE 1079
Cdd:pfam02463 1008 IRAIIEE-TCQRLKEFLELFVS 1028
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
885-1104 |
4.98e-04 |
|
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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 44.38 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 885 IQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrVGDLEKVQKLEAELEKAathRHSYEEKGRRYRDTVEERLSKLQK- 963
Cdd:pfam01576 639 LSLARALEEALDAKEELERQNKQLRAEMEDL----VSSKDDVGKNVHELERS---KRALEQQVEEMKTQLEELEDELQAt 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 964 HNAELEL---------QRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQR---LVLEKGFELKTQAYEKQIESL-- 1029
Cdd:pfam01576 712 EDAKLRLevnmqalkaQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRaqaVAAKKKLELDLKELEAQIEAAnk 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1030 -REE-IKALKDERSQ---LHHQLEEGQVTSDRLKGEVARLSKQAKTIsefekEIELLQAQKI-----DVEKHVQSQKREM 1099
Cdd:pfam01576 792 gRDEaVKQLKKLQAQmkdLQRELDEARASRDEIFAQSKESEKKLKSL-----EAELLQLQEDlaaaeRARRQAQQERDEL 866
|
....*
gi 568961011 1100 RERMS 1104
Cdd:pfam01576 867 AEEIA 871
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
890-1128 |
5.36e-04 |
|
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: 44.43 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNREnhgLVEKLTSLAALRvgdlEKVQKLEAELEKAATHRhsyeekgrryrDTVEERLSKLQKHNAELE 969
Cdd:pfam10174 395 KINVLQKKIENLQEQ---LRDKDKQLAGLK----ERVKSLQTDSSNTDTAL-----------TTLEEALSEKERIIERLK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 970 LQRERAEQMLQEKSE-------ELKEKMDKLTRQLFDdvqKEEQQRLVLEKGFELKTQAYEK--QIESLREEIKALKDER 1040
Cdd:pfam10174 457 EQREREDRERLEELEslkkenkDLKEKVSALQPELTE---KESSLIDLKEHASSLASSGLKKdsKLKSLEIAVEQKKEEC 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1041 SQLHHQLEEGQVT----------SDRLK-----------------GEVARL-----------SKQAKTISEFEKEIELL- 1081
Cdd:pfam10174 534 SKLENQLKKAHNAeeavrtnpeiNDRIRlleqevarykeesgkaqAEVERLlgilrevenekNDKDKKIAELESLTLRQm 613
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568961011 1082 --QAQKIDVEKHVQSQKRemRERMSEVTKQLLESYDIEDVRSRLSVEDL 1128
Cdd:pfam10174 614 keQNKKVANIKHGQQEMK--KKGAQLLEEARRREDNLADNSQQLQLEEL 660
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
924-1200 |
5.75e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 924 EKVQKLEaELEKAATHRHSYE-EKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLtrqlfddvQ 1002
Cdd:PTZ00121 1543 EEKKKAD-ELKKAEELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA--------K 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1003 KEEQQRLvleKGFELKTQAYE-KQIESLREEIKALKDERSQLHHQLEEGQVtsdrlkgevaRLSKQAKTISEFEKEIELL 1081
Cdd:PTZ00121 1614 KAEEAKI---KAEELKKAEEEkKKVEQLKKKEAEEKKKAEELKKAEEENKI----------KAAEEAKKAEEDKKKAEEA 1680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1082 QAQKIDVEKHVQSQKREMRE-RMSEVTKQLLEsydiEDVRSRLSVEDLEHLNEdgelwFAYEGLKKatrvlESHFQSQKD 1160
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEaKKAEELKKKEA----EEKKKAEELKKAEEENK-----IKAEEAKK-----EAEEDKKKA 1746
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568961011 1161 CYEKEIEGLNFKVVHLSQEINHLQKLFREETD--INESIRHE 1200
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEavIEEELDEE 1788
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
887-1201 |
7.29e-04 |
|
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: 43.90 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 887 LTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDT---VEERLSKLQK 963
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEydrVEKELSKLQR 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 964 HNAELELQRE---------RAEQMLQEKS---------------------------------------------EELKE- 988
Cdd:TIGR02169 491 ELAEAEAQARaseervrggRAVEEVLKASiqgvhgtvaqlgsvgeryataievaagnrlnnvvveddavakeaiELLKRr 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 989 -----------KMDKLTRQL-----------------FDD---------------VQKEE-------QQRLV------LE 1012
Cdd:TIGR02169 571 kagratflplnKMRDERRDLsilsedgvigfavdlveFDPkyepafkyvfgdtlvVEDIEaarrlmgKYRMVtlegelFE 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1013 K------------GFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISEFEKEIEL 1080
Cdd:TIGR02169 651 KsgamtggsraprGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK---IGEIEKEIEQ 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1081 LQAQkidvEKHVQSQKREMRERMSEvTKQLLESYD--IEDVRSRLS------------VEDLE-HLNEDG--ELWFAYEG 1143
Cdd:TIGR02169 728 LEQE----EEKLKERLEELEEDLSS-LEQEIENVKseLKELEARIEeleedlhkleeaLNDLEaRLSHSRipEIQAELSK 802
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011 1144 LKKATRVLESHFQSqkdcYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEV 1201
Cdd:TIGR02169 803 LEEEVSRIEARLRE----IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
954-1208 |
7.47e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 43.98 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 954 VEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDkltrqlfddvQKEEQQRLVLEKgfelKTQAYEKQIESLREEI 1033
Cdd:COG0419 183 AKAKIEELEGQLSELLEDIEDLLEALEEELKELKKLEE----------IQEEQEEEELEQ----EIEALEERLAELEEEK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1034 KALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISEFEKEIELLQAQKIDVEkhvqsQKREMRERMSEVTKQLLES 1113
Cdd:COG0419 249 ERLEELKARLLEIESLELEALKIREEELRELERL---LEELEEKIERLEELEREIE-----ELEEELEGLRALLEELEEL 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1114 YD-IEDVRSRLS--VEDLEHLNEDGELWFAYEG-LKKATRVLESHFQSQKDCYEKEIEGLNFKV----VHLSQEINHLQK 1185
Cdd:COG0419 321 LEkLKSLEERLEklEEKLEKLESELEELAEEKNeLAKLLEERLKELEERLEELEKELEKALERLkqleEAIQELKEELAE 400
|
250 260
....*....|....*....|...
gi 568961011 1186 LFREETDINESIRHEVTRLTSEN 1208
Cdd:COG0419 401 LSAALEEIQEELEELEKELEELE 423
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
924-1085 |
7.74e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 924 EKVQKLEAELEKaathrhsyeekgrryrdTVEERLSKLQKhnaeLELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQK 1003
Cdd:PRK12704 64 EEIHKLRNEFEK-----------------ELRERRNELQK----LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1004 EEQqrlVLEKGFELKtQAYEKQIESLrEEIKAL-KDE-RSQLHHQLEEgqvtsdRLKGEVARLskqaktISEFEKEIElL 1081
Cdd:PRK12704 123 QQE---LEKKEEELE-ELIEEQLQEL-ERISGLtAEEaKEILLEKVEE------EARHEAAVL------IKEIEEEAK-E 184
|
....
gi 568961011 1082 QAQK 1085
Cdd:PRK12704 185 EADK 188
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
884-1058 |
8.26e-04 |
|
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: 43.66 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 884 NIQLTYRVQRLQKKL---EDQNRENHGLVEKLtsLAALRVGDLEKVQKLE--AELEKAATHRHSYEEKGRRYRDTVEERL 958
Cdd:pfam10174 553 NPEINDRIRLLEQEVaryKEESGKAQAEVERL--LGILREVENEKNDKDKkiAELESLTLRQMKEQNKKVANIKHGQQEM 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 959 SKlqKHNAELELQRERAEQM----LQEKSEELKEKMDKlTRQLFDDVQKE---EQQRLV----------------LEKGF 1015
Cdd:pfam10174 631 KK--KGAQLLEEARRREDNLadnsQQLQLEELMGALEK-TRQELDATKARlssTQQSLAekdghltnlraerrkqLEEIL 707
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1016 ELKTQAYEKQI-----------------ESLREEIKALKDERSQLHHQLEegQVTSDRLK 1058
Cdd:pfam10174 708 EMKQEALLAAIsekdaniallelssskkKKTQEEVMALKREKDRLVHQLK--QQTQNRMK 765
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
943-1122 |
8.33e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 43.17 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 943 YEEKGRRYRDTvEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFD----DVQKEEQQRLVLE------ 1012
Cdd:COG4942 47 IAALEKKIREQ-QDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARlnalEVQEREQRRRLAEqlaalq 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1013 -----------------KGFELKTQAYEKQIESLREEIKALKDERSQLHHQ---LEEGQVTSDRLKGE-VARLSKQAKTI 1071
Cdd:COG4942 126 rsgrnpppallvspedaQRSVRLAIYYGALNPARAERIDALKATLKQLAAVraeIAAEQAELTTLLSEqRAQQAKLAQLL 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568961011 1072 SEFEKEIELLQAQKidvEKHvQSQKREMRERMSEVtKQLLESYDIEDVRSR 1122
Cdd:COG4942 206 EERKKTLAQLNSEL---SAD-QKKLEELRANESRL-KNEIASAEAAAAKAR 251
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
852-1127 |
8.84e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.88 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 852 KLLQEHKAVILQKYA--RAWL------ARRRFQNIRRFVLNIqltyrvqrLQKKLEDQNRENHGLVEKLTSLAALRVGDL 923
Cdd:PTZ00108 980 DILKEFYLVRLDLYKkrKEYLlgklerELARLSNKVRFIKHV--------INGELVITNAKKKDLVKELKKLGYVRFKDI 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 924 EKVQK---LEAELEKAATHRHSYEEKGRRYRDTVEE------------RLSKLQKHNAELELQRERAEQMLQEKSEEL-K 987
Cdd:PTZ00108 1052 IKKKSekiTAEEEEGAEEDDEADDEDDEEELGAAVSydyllsmpiwslTKEKVEKLNAELEKKEKELEKLKNTTPKDMwL 1131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 988 EKMDKLTRQLFDDVQKEEQQRLVLEKgFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRlKGEVARLSKQ 1067
Cdd:PTZ00108 1132 EDLDKFEEALEEQEEVEEKEIAKEQR-LKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSK-RVDSDEKRKL 1209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1068 AKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVED 1127
Cdd:PTZ00108 1210 DDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEG 1269
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
999-1207 |
8.99e-04 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 43.47 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 999 DDVQKE-EQQRLVLEKGFELKTQAyEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKE 1077
Cdd:COG4372 77 DDIRPQlRALRTELGTAQGEKRAA-ETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAQDLQTRLKT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1078 IELLQAQKIDVEKHVQSQKREMRERMSEVTKQllesydiedvRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHfQS 1157
Cdd:COG4372 156 LAEQRRQLEAQAQSLQASQKQLQASATQLKSQ----------VLDLKLRSAQIEQEAQNLATRANAAQARTEELARR-AA 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568961011 1158 QKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSE 1207
Cdd:COG4372 225 AAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQE 274
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
886-1206 |
9.07e-04 |
|
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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 43.61 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 886 QLTYRVQRLQKKLEDQNRENhglvekltSLAALRVGDLE-KVQKLEAELEKAathrhsyeEKGRryrdtvEERLSKLQKH 964
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQR--------AQAVAAKKKLElDLKELEAQIEAA--------NKGR------DEAVKQLKKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 965 NAEL-ELQRE-------RAEQMLQEKSEELKEK-MDKLTRQLFDDVQKEEQQRLVLEK-----GFELKTQAYEKQieSLR 1030
Cdd:pfam01576 804 QAQMkDLQREldearasRDEIFAQSKESEKKLKsLEAELLQLQEDLAAAERARRQAQQerdelAEEIASGNSGKS--ALL 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1031 EEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTIS-EFEKEIELLQAQKiDVEKHVQSQKREMRERMSEVTKQ 1109
Cdd:pfam01576 882 DEKRRLEARIAQLEEELEEEQSNTELLNDRLRKLTLQVEQLTtELAAERSTSQKSE-SARQQLERQNKELKAKLQEMEGT 960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1110 L----------LESyDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHfQSQKDCYEKEIEGLNFKVVHL--- 1176
Cdd:pfam01576 961 VkskykssiaaLEA-KIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDE-RRNADQYKDQAEKGNSRLKQLkrq 1038
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568961011 1177 -------SQEIN----HLQKLFREETDINESIRHEVTRLTS 1206
Cdd:pfam01576 1039 leeaeeeASRANaarrKLQRELDDATESAEAMNREVTTLRS 1079
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
887-1110 |
9.53e-04 |
|
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 characteristic 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: 43.13 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 887 LTYRVQRLQKKLEDQNRENHGLVEKLTSLAALrvgdlekVQKLEAELEKAATHRHSYEEKGRRYR---DTVEERLSKLQK 963
Cdd:pfam19220 88 LVARLAKLEAALREAEAAKEELRIELRDKTAQ-------AEALERQLAAETEQNRALEEENKALReeaQAAEKALQRAEG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 964 HNAELELQRERAEQ---MLQEKSEELKEKMDKLTRQLFDDVQK--EEQQRL-VLEKGFELKTQAYEKQIESLREEIKALK 1037
Cdd:pfam19220 161 ELATARERLALLEQenrRLQALSEEQAAELAELTRRLAELETQldATRARLrALEGQLAAEQAERERAEAQLEEAVEAHR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1038 DERSQLHHQLEEGQ---VTSDRLKGEVA---------------RLSKQAKTISEFEKEIELLQAQKIDVE---KHVQSQK 1096
Cdd:pfam19220 241 AERASLRMKLEALTaraAATEQLLAEARnqlrdrdeairaaerRLKEASIERDTLERRLAGLEADLERRTqqfQEMQRAR 320
|
250
....*....|....
gi 568961011 1097 REMRERMSEVTKQL 1110
Cdd:pfam19220 321 AELEERAEMLTKAL 334
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
855-1068 |
1.02e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 224755 [Multi-domain] Cd Length: 225 Bit Score: 41.92 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 855 QEHKAVILQKYARAwlARRRFQNIRRFVlnIQLTYRVQRLQKKLEDQNRENHGLVEKltSLAALRVGD-------LEKVQ 927
Cdd:COG1842 22 AEDPEKMLEQAIRD--MESELAKARQAL--AQAIARQKQLERKLEEAQARAEKLEEK--AELALQAGNedlareaLEEKQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 928 KLEaelEKAATHRHSYEEKgRRYRDTVEERLSKLQKHNAELELQRERAeqMLQEKSEELKEKMDKLTR--------QLFD 999
Cdd:COG1842 96 SLE---DLAKALEAELQQA-EEQVEKLKKQLAALEQKIAELRAKKEAL--KARKAAAKAQEKVNRSLGggssssamAAFE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961011 1000 DVqkeEQQRLVLEKGFELKTQAYEKQIESLREEIKalkdersqlhhQLEEGQVTSDRLKGEVARLSKQA 1068
Cdd:COG1842 170 RM---EEKIEEREARAEAAAELAEGSGDDLDKEFA-----------QAGAQSAVDSRLAALKARMKGPA 224
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
952-1189 |
1.06e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 224259 [Multi-domain] Cd Length: 294 Bit Score: 42.75 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 952 DTVEERLSKLQKHNAELELQRERAEQmLQEKSEELKEKMDKLTRQLfddvqkeeqqRLVLEKGFELKTQAYEkqiesLRE 1031
Cdd:COG1340 6 DKLDELELKRKQLKEEIEELKEKRDE-LRKEASELAEKRDELNAKV----------RELREKAQELREERDE-----INE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1032 EIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQK------IDVEKHVQSQKREMRERMSE 1105
Cdd:COG1340 70 EVQELKEKRDEINAKLQELRKEYRELKEKRNEFNLGGRSIKSLEREIERLEKKQqtsvltPEEERELVQKIKELRKELED 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1106 VTKQLLESYDIEDVRSR---LSVEDLEHLNEDGELwfAYEGLKKATRVLESHfqSQKDCYEKEIEGLNFKVVHLSQEINH 1182
Cdd:COG1340 150 AKKALEENEKLKELKAEideLKKKAREIHEKIQEL--ANEAQEYHEEMIKLF--EEADELRKEADELHEEFVELSKKIDE 225
|
....*..
gi 568961011 1183 LQKLFRE 1189
Cdd:COG1340 226 LHEEFRN 232
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
895-1052 |
1.18e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 434695 [Multi-domain] Cd Length: 258 Bit Score: 42.24 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 895 QKKLEDQNREnhglVEKLTSLAALRVGDLEK-VQKLEAELEKAATHRHSYeekgRRYRD--------TVEERLSKLQKHN 965
Cdd:pfam15397 62 KKQLQQAKAE----LQEWEEKEESKLNKLEQqLEQLNAKIQKTQEELNFL----STYKDkeypvkavQIANLVRQLQQLK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 966 AELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQ---QRLVLEKgfELKTQAYEKQIESLREEIKALKDERSQ 1042
Cdd:pfam15397 134 DSQQDELDELEEMRREVLESLSRKIQKKKEKILSSLAEKTQspyQESLLQK--TRDNQVMLKEIEQFREFIDELEEEIPK 211
|
170
....*....|
gi 568961011 1043 LHHQLEEGQV 1052
Cdd:pfam15397 212 LKAEVQQLQA 221
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
878-1069 |
1.26e-03 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 43.09 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 878 IRRFVLNIQLTyRVQRLQKKLEDQNRE-NHGLVEKLTSLAALRvgdlEKVQKLEAELEKAATHRHSYEEKgrryRDTVEE 956
Cdd:COG4372 102 TEREAARSELQ-KARQEREAVRQELAAaRQNLAKAQQELARLT----KQAQDLQTRLKTLAEQRRQLEAQ----AQSLQA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 957 RLSKLQKHNAELELQRE----RAEQMLQEKSE--ELKEKMDKLTRQLfddvQKEEQQRLVLEKgfelKTQAYEKQIESLR 1030
Cdd:COG4372 173 SQKQLQASATQLKSQVLdlklRSAQIEQEAQNlaTRANAAQARTEEL----ARRAAAAQQTAQ----AIQQRDAQISQKA 244
|
170 180 190
....*....|....*....|....*....|....*....
gi 568961011 1031 EEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAK 1069
Cdd:COG4372 245 QQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQ 283
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
891-1101 |
1.32e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 434695 [Multi-domain] Cd Length: 258 Bit Score: 41.86 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 891 VQRLQKKLEDQNRENHGLVEKLTSL---AALRVGDL----EKVQKLEAELEKaathrhSYEEKGRRYRDTVEERLSKLQK 963
Cdd:pfam15397 8 LEELKKHEDFLTKLNLELIKAIQDTedsTALKVRKLlqqyEKFGTIISILEY------SNKKQLQQAKAELQEWEEKEES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 964 HNAELELQRERAEQMLQEKSEE---LKEKMDK-----------LTRQLfDDVQKEEQ-QRLVLEKGFELKTQAYEKQIES 1028
Cdd:pfam15397 82 KLNKLEQQLEQLNAKIQKTQEElnfLSTYKDKeypvkavqianLVRQL-QQLKDSQQdELDELEEMRREVLESLSRKIQK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961011 1029 LREEIKALKDERSQLHHQ--LEEGQVTSDRLKGEVARlskQAKTISEFEKEIELLQAQkidVEKhVQSQKREMRE 1101
Cdd:pfam15397 161 KKEKILSSLAEKTQSPYQesLLQKTRDNQVMLKEIEQ---FREFIDELEEEIPKLKAE---VQQ-LQAQRQEPRE 228
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
859-1043 |
1.39e-03 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 42.82 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 859 AVILQKYARAWLAR------RRFQNIRRFvLNIQLTYRVQRLQ--KKLEDQNRENHGLVE--KLTSLAALRVGDL-EKVQ 927
Cdd:COG3206 171 AKLANALAQAYLADqleaqlEAFRRASDS-LDERLEELRARLQeaEAQVEDFRAQHGLTDaaRGQLLSEQQLSALnTQLQ 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 928 KLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLT---RQLfDDVQKE 1004
Cdd:COG3206 250 SARARLAQAEARLASLLQLLPLGREAAALREVLESPTIQDLRQQYAQVRQQIADLSTELGAKHPQLValeAQL-AELRQQ 328
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568961011 1005 EQQRLV-LEKGFELKTQAYEKQIESLREEIKALKDERSQL 1043
Cdd:COG3206 329 IAAELRqILASLPNELALLEQQEAALEKELAQLKGRLSKL 368
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
886-1130 |
1.39e-03 |
|
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: 42.82 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 886 QLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKgrryRDTVEERL------- 958
Cdd:pfam07111 335 QLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQ----TASAEEQLkfvvnam 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 959 ----SKLQKHNAELE--------------------------LQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQR 1008
Cdd:pfam07111 411 sstqIWLETTMTRVEqavaripslsnrlsyavrkvhtikglMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREER 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1009 LVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLE-EGQVTSDRLKG-----EVARLSKQAKTISEFEKEIELLQ 1082
Cdd:pfam07111 491 NRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEqELQRAQESLASvgqqlEVARQGQQESTEEAASLRQELTQ 570
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568961011 1083 AQKI---DVEKHVQSQKREMRERMSEVTKQLLESYDiEDVRSRLSVEDLEH 1130
Cdd:pfam07111 571 QQEIygqALQEKVAEVETRLREQLSDTKRRLNEARR-EQAKAVVSLRQIQH 620
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
852-1261 |
1.44e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 852 KLLQEHKAVILQKYARAWLARRRFQNIRRfvlNIQLTYRVQRLQKKLEDQNRENHGlVEKLTSLAALRVGDLEKvqKLEA 931
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKK---AEEEKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAK--KAEE 1672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 932 ELEKAATHRHSYEEKGRRYRDTV--EERLSKLQKHNAELELQRERAEQMLQE------KSEELKEKMDkltrqlfDDVQK 1003
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKkeAEEAKKAEELKKKEAEEKKKAEELKKAeeenkiKAEEAKKEAE-------EDKKK 1745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1004 EEQQRlvLEKGFELKTQAYEKQIESLREEIKALKDErsqlhhQLEEGQVTSD-RLKGEVARLSKQAKtiSEFEKEIELLQ 1082
Cdd:PTZ00121 1746 AEEAK--KDEEEKKKIAHLKKEEEKKAEEIRKEKEA------VIEEELDEEDeKRRMEVDKKIKDIF--DNFANIIEGGK 1815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1083 AQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGElwFAYEGLKKA---TRVLESHFQSQ- 1158
Cdd:PTZ00121 1816 EGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEAD--FNKEKDLKEddeEEIEEADEIEKi 1893
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1159 -KDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESiRHEVTRLTSENMpllsvmcfsatCGNAGYSPASEIAEDHT 1237
Cdd:PTZ00121 1894 dKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEET-REEIIKISKKDM-----------CINDFSSKFCDYMKDNI 1961
|
410 420
....*....|....*....|....*..
gi 568961011 1238 ---RCGYFFRLTICCGFASFLLLWPNH 1261
Cdd:PTZ00121 1962 ssgNCSDEERKELCCSISDFCLKYFDH 1988
|
|
| RmuC |
COG1322 |
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and ... |
890-1069 |
1.62e-03 |
|
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and repair];
Pssm-ID: 224241 [Multi-domain] Cd Length: 448 Bit Score: 42.38 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNRENH--GLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEErlsKLQKHNAE 967
Cdd:COG1322 16 NLAFIRQLLLRLGRLEQmlGELAAVLEQLLLLLAFRAEAEQLRTFARSLQALNLELIQELNELKARLQQ---QLLQSREQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 968 LELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQrlvLEKGFELKTQAYEKQiesLREEIKALKDERSQLHHQL 1047
Cdd:COG1322 93 LQLLIESLAQLSSEFQELANEIFEELNRRLAELNQQNLKQ---LLKPLREVLEKFREQ---LEQRIHESAEERSTLLEEI 166
|
170 180
....*....|....*....|..
gi 568961011 1048 EEGQvtsdrlkGEVARLSKQAK 1069
Cdd:COG1322 167 DRLL-------GEIQQLAQEAG 181
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
838-1054 |
1.64e-03 |
|
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: 434789 [Multi-domain] Cd Length: 374 Bit Score: 42.34 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 838 QAHTRGFLARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVlniqlTYRVQRLQKKLEDQNRENhglVEKLTSLA- 916
Cdd:pfam15558 108 QEKLERAAQEAEQRKQCQEQNLKEKEEELQALREQNGLQLQERLE-----QACHKRQLKELEEQKKVQ---ENNLSELLn 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 917 --ALRVgDLEKVQKLEAELEKAAT---HRHSYEekgrRYRDTVEERLSKL----QKHNAELELQRERAEQMLQEKSEELK 987
Cdd:pfam15558 180 hqARKV-LVDCQAKAEELLRRLSLeqsLQRSQE----NYEQLVEERHRELrekaQKEEEQFQRAKLRAEEKEEEQQEHKE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 988 ---EKMDKLTRQ--------LFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKAL---KDERSQLHHQ-----LE 1048
Cdd:pfam15558 255 alaELADQKIQQarsvahktVQDKAQRARELNLEREKNHHLLKLKVEKEEECHREGIKEAikkKEQRSEQISRekeatLE 334
|
....*.
gi 568961011 1049 EGQVTS 1054
Cdd:pfam15558 335 EARKTA 340
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242); |
904-1036 |
1.73e-03 |
|
Uncharacterized protein family (UPF0242);
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 40.96 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 904 ENHGLVEKLTSLAALrvgDLEKVQKLEAELEKaathRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKS 983
Cdd:pfam06785 66 EKSFLEEKEAKLTEL---DAEGFKILEETLEE----LQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFR 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568961011 984 EELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFElKTQAYEKQIESLREEIKAL 1036
Cdd:pfam06785 139 LESEEQLAEKQLLINEYQQTIEEQRSVLEKRQD-QIENLESKVRDLNYEIKTL 190
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
923-1189 |
1.74e-03 |
|
Intermediate filament protein;
Pssm-ID: 425436 [Multi-domain] Cd Length: 313 Bit Score: 41.82 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 923 LEKVQKLEAE---LEKAATHRhsYEEKGRR-------YRDTVEE---RLSKLQKHNAELELQRERaeqmLQEKSEELKEK 989
Cdd:pfam00038 17 IDKVRFLEQQnkdLETKISEL--RQKKGAEpsrlyslYEREIRElrrQLDTLTVERARLQLELDN----LRLAAEDFRQK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 990 MDK---LTRQLFDDVQkeeQQRLVLEKGFELKTQAyEKQIESLREEIKALK----DERSQLHHQLEEGQVTsdrLKGEVA 1062
Cdd:pfam00038 91 YEDelnLRQSAEADIV---GLRKDLDEATLARVDL-EMKIESLKEELAFLKknheEEVRELQSQVSDTQVN---VEMDAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1063 RLSKQAKTISEFEKEIELLQAQ-KIDVEKHVQSQKREMRERmSEVTKQLLESYDIEDVRSRLSVEDLEHlnedgELwfay 1141
Cdd:pfam00038 164 RKLDLTSALAEIRAQYEEIAEKnREEAEEWYQSKLEELQQA-AARNGDALRSAKEEITELRRQIQSLEI-----EL---- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568961011 1142 EGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINH----LQKLFRE 1189
Cdd:pfam00038 234 QSLKKQKASLERQLAETEERYELQLADYQELISELEAELQQirqeMARQLRE 285
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
886-1199 |
1.79e-03 |
|
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: 42.73 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 886 QLTYRVQRLQKKLEDQNRENHGLVEKLTSLA-----ALRVGDLE-KVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLS 959
Cdd:TIGR00606 595 KLNKELASLEQNKNHINNELESKEEQLSSYEdklfdVCGSQDEEsDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTD 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 960 KLQ----------KHNAELELQRERAEQMLQEKSEELKEkmdklTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESL 1029
Cdd:TIGR00606 675 ENQsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKS-----TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPEL 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1030 REEIKALKDERSQLHHQLEEgqvtSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQ 1109
Cdd:TIGR00606 750 RNKLQKVNRDIQRLKNDIEE----QETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQ 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1110 LLESyDIEDVRSRL-----SVEDLEHLNEDGELWFAYegLKKATRVLESH-------------FQSQKDCYEKEIEGLNF 1171
Cdd:TIGR00606 826 QVNQ-EKQEKQHELdtvvsKIELNRKLIQDQQEQIQH--LKSKTNELKSEklqigtnlqrrqqFEEQLVELSTEVQSLIR 902
|
330 340
....*....|....*....|....*...
gi 568961011 1172 KVVHLSQEINHLQKLFREETDINESIRH 1199
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
896-1202 |
1.88e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 896 KKLEDQNRENHGLVEKLTSLAAlrvgDLEKVQKL--------------------EAELEKAATHR-------HSYEEKGR 948
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSF----DVQKLQRLhqafsrfigshlavafeadpEAELRQLNRRRveleralADHESQEQ 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 949 RYR---DTVEERLSKLQKHNAELELQrerAEQMLQEKSEELKEKMDKLtrqlfddvqkEEQQRLVLEKGFELktQAYEKQ 1025
Cdd:PRK04863 862 QQRsqlEQAKEGLSALNRLLPRLNLL---ADETLADRVEEIREQLDEA----------EEAKRFVQQHGNAL--AQLEPI 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1026 IESLR---EEIKALKDERSQLHHQLEEGQVTSDRLKGEVARL-----SKQAKTISEFEKEIELLQAQkidvEKHVQSQKR 1097
Cdd:PRK04863 927 VSVLQsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEMLAKNSDLNEKLRQR----LEQAEQERT 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1098 EMRERMSEVTKQLLEsYD--IEDVRSRLSV-EDL--EHLNEDGELWFAY-EGLKKATRVLE-------SHFQSQKDCYEK 1164
Cdd:PRK04863 1003 RAREQLRQAQAQLAQ-YNqvLASLKSSYDAkRQMlqELKQELQDLGVPAdSGAEERARARRdelharlSANRSRRNQLEK 1081
|
330 340 350
....*....|....*....|....*....|....*...
gi 568961011 1165 EIeglnfkvVHLSQEINHLQKLFREETDINESIRHEVT 1202
Cdd:PRK04863 1082 QL-------TFCEAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
983-1084 |
1.89e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 983 SEEL--KEK-MDKLTRQLfddvqKEEQQRLVLEKgfeLKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKG 1059
Cdd:PRK09039 45 SREIsgKDSaLDRLNSQI-----AELADLLSLER---QGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100
....*....|....*....|....*....
gi 568961011 1060 EVARLSKQ---AKTIS-EFEKEIELLQAQ 1084
Cdd:PRK09039 117 RAGELAQEldsEKQVSaRALAQVELLNQQ 145
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
886-1123 |
2.21e-03 |
|
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: 434815 [Multi-domain] Cd Length: 193 Bit Score: 40.65 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 886 QLTYRVQRLQKKLEDQNRENHglvekltslaalrvgDLEKVQKLEaelEKAAthrhsyeekgRRYRDTVEERLSKLQKHN 965
Cdd:pfam15619 15 ELQNELAELQRKLEELRKENK---------------LLKRLQRRQ---EKAL----------GKYEDTESELPQLIARHN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 966 AELELQRERaeqmlqekseeLKEKMDKLTRQlfddvqkeeqqrlvlekgfELKTQAYEKQIESLREEIKALKD------- 1038
Cdd:pfam15619 67 EEVRVLRER-----------LRRSQEKERDL-------------------ERKLKEKEAELLRLRDELKKLKKlsedknl 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1039 -ERSQLHHQLEEGQvtsdrlkgevARLSKQAKTISEFEKEIELLQAQkidVEKHVQSQKREMRERMSEVTKQLLEsydIE 1117
Cdd:pfam15619 117 aEREELQKKLAQLE----------AKLEEKEEKIQELERKLELEEKN---FRRQLAAEKKKHKEAQEEVKILQEE---IE 180
|
....*.
gi 568961011 1118 DVRSRL 1123
Cdd:pfam15619 181 RLQQKL 186
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
923-1049 |
2.29e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 225288 [Multi-domain] Cd Length: 652 Bit Score: 42.38 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 923 LEKVQKLEAELEKAATHRHSYEEKGrryrdTVEERLSKLQKHNAELElqRERAEqmLQEKSEELKEKMDKLTRQLfDDVQ 1002
Cdd:COG2433 394 LSKVKEEERPREKEGTEEEERREIT-----VYEKRIKKLEETVERLE--EENSE--LKRELEELKREIEKLESEL-ERFR 463
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568961011 1003 KEEQQrlvlEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEE 1049
Cdd:COG2433 464 REVRD----KVRKDREIRARDRRIERLEKELEEKKKRVEELERKLAE 506
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
949-1133 |
2.55e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 41.16 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 949 RYRDTVEERLSKL-----QKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQrlvlekgFELKTQAYE 1023
Cdd:PRK06669 37 RLREEEEEQVEQLreeanDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEASSIIEKLQMQ-------IEREQEEWE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1024 KQIESLREEIKALKdersqlhhqLEEG-QVTSDRLKGEVARLSKQA-----KTISEFEKEIELLQAQKIDV-----EKHV 1092
Cdd:PRK06669 110 EELERLIEEAKAEG---------YEEGyEKGREEGLEEVRELIEQLnkiieKLIKKREEILESSEEEIVELaldiaKKVI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568961011 1093 QSQKREMRERMSEVTKQLLESY-DIEDVRSRLSVEDLEHLNE 1133
Cdd:PRK06669 181 KEISENSKEIALALVKELLKEVkDATDITIRVNPEDYEYVKE 222
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
892-1109 |
2.75e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 430780 [Multi-domain] Cd Length: 302 Bit Score: 41.47 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 892 QRLQKKLEDQNRENHGLVEKLTSLAALRvgdlEKVQKLEAELEKaatHRHSYEEKGRRYRDTVEERLSKLQKH------- 964
Cdd:pfam09728 42 KKLKKKQDQLQKEKDQLQSELSKAILAK----SKLEKLCRELQK---QNKKLKEESKKLAKEEEEKRKELSEKfqatlkd 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 965 -NAELELQRERAEQMLQEkSEELKEKMDKLTRQL------FDDV--QKEEQQRLVLEK----GFELKTQAYEKQIESLRE 1031
Cdd:pfam09728 115 iQDKMEEKSEPNNKLREE-NEELREKLKSLIEQYelreehFEKLlkTKELEVQLAEAKlqqaTEEEEKKAQEKEVAKARE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1032 ---EIKALKDERSQLHHQLEE-----GQVTS---------DRLKGEVARLSKQAKTiseFEKEIELLQAQKIDVEKHVQS 1094
Cdd:pfam09728 194 lkaQVQTLSETEKELREQLNLyvekfEEFQDtlnksnevfTTFKKEMEKMSKKIKK---LEKENLTWKRKWEKSNKALLE 270
|
250
....*....|....*
gi 568961011 1095 QKREMRERMSEVTKQ 1109
Cdd:pfam09728 271 MAEERQKLKEELEKL 285
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
890-1037 |
2.79e-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: 39.60 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 890 RVQRLQKKLEDQNRENHGLVEKLTSLAAlrvgdleKVQKLEAELEKAathrhsyEEKGRRYRDTVEERlSKLQKHNAELE 969
Cdd:pfam12718 15 RAEELEEKVKELEQENLEKEQEIKSLTH-------KNQQLEEEVEKL-------EEQLKEAKEKAEES-EKLKTNNENLT 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011 970 LQRERAEQMLQEKSEELKEKMDKLtRQLfdDVQKEEQQRLVleKGFELKTQAYEKQIESLREEIKALK 1037
Cdd:pfam12718 80 RKIQLLEEELEESDKRLKETTEKL-RET--DVKAEHLERKV--QALEQERDEWEKKYEELEEKYKEAK 142
|
|
| DHR10 |
pfam18595 |
Designed helical repeat protein 10 domain; Repeat proteins composed of multiple tandem copies ... |
926-995 |
2.91e-03 |
|
Designed helical repeat protein 10 domain; Repeat proteins composed of multiple tandem copies of a modular structure unit1 are widespread in nature and have critical roles in molecular recognition, signaling, and other essential biological processes. This entry describes a MazG related domain also designated as Designed helical repeat protein 10 (DHR10). This domain is also found at the N-terminal region of Nuf2 proteins pfam03800.
Pssm-ID: 436606 [Multi-domain] Cd Length: 117 Bit Score: 38.73 E-value: 2.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961011 926 VQKLEAELEKAATHRHSYEEKGRRYRDTV--EERLSK-LQKHNAELElqreRAEQMLQEKSEELKEKMDKLTR 995
Cdd:pfam18595 49 LAKLEEAKKKLKELRDALEEKEIELRELErrEERLQRqLENAQEKLE----RLREQAEEKREAAQARLEELRE 117
|
|
| Ax_dynein_light |
pfam10211 |
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ... |
970-1048 |
3.34e-03 |
|
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organisms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.
Pssm-ID: 431138 [Multi-domain] Cd Length: 187 Bit Score: 39.87 E-value: 3.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961011 970 LQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQqrlvLEKGFELKTQAYEKQIEslrEEIKALKDERSQLHHQLE 1048
Cdd:pfam10211 115 LQAEQGKSELEKKIADLEEEKEELEKQVAELKAKCEA----IEKREEERRQAEEKKHA---EEIAFLKKTNQQLKAQLE 186
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
831-851 |
3.54e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 425778 Cd Length: 21 Bit Score: 35.76 E-value: 3.54e-03
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
954-1109 |
3.58e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 41.25 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 954 VEERLSKLQKH----NAELELQRERAEQmLQEKSEELKEKMDKLTRQLF---DDVQKEEQQRLVLEKGFELKTQAYEKQI 1026
Cdd:COG4942 36 DDKQLKQIQKEiaalEKKIREQQDQRAK-LEKQLKSLETEIASLEAQLIetaDDLKKLRKQIADLNARLNALEVQEREQR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1027 ESLREEIKALKdeRSQLHHQLEEGQVTSDRLKGEvaRLSKQ--------AKTISEFEKEIELLQAQKIDVEkhvqSQKRE 1098
Cdd:COG4942 115 RRLAEQLAALQ--RSGRNPPPALLVSPEDAQRSV--RLAIYygalnparAERIDALKATLKQLAAVRAEIA----AEQAE 186
|
170
....*....|.
gi 568961011 1099 MRERMSEVTKQ 1109
Cdd:COG4942 187 LTTLLSEQRAQ 197
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
968-1129 |
3.67e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 968 LELQRERA-------EQMLQEKSEELkekmDKLTRQLFDDVQKEEQQRLvlekgfelktQAYEKQIESLREEIKALKDER 1040
Cdd:PRK02224 164 LEEYRERAsdarlgvERVLSDQRGSL----DQLKAQIEEKEEKDLHERL----------NGLESELAELDEEIERYEEQR 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1041 SQLHHQLEEGQVTsdrlkgeVARLSKQAKTISEFEKEIELLQAQKIDVEKhvqsQKREMRERMSEVTKQLLE-SYDIEDV 1119
Cdd:PRK02224 230 EQARETRDEADEV-------LEEHEERREELETLEAEIEDLRETIAETER----EREELAEEVRDLRERLEElEEERDDL 298
|
170
....*....|
gi 568961011 1120 RSRLSVEDLE 1129
Cdd:PRK02224 299 LAEAGLDDAD 308
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
830-851 |
3.99e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 35.76 E-value: 3.99e-03
|
| DUF874 |
pfam05917 |
Helicobacter pylori protein of unknown function (DUF874); This family consists of several ... |
886-1038 |
4.06e-03 |
|
Helicobacter pylori protein of unknown function (DUF874); This family consists of several hypothetical proteins specific to Helicobacter pylori. The function of this family is unknown.
Pssm-ID: 283549 [Multi-domain] Cd Length: 398 Bit Score: 40.99 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 886 QLTYRVQRLQKKLEDQNRENHGLVEKLTS-----LAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRyrdtVEERLSK 960
Cdd:pfam05917 81 ELDDKVQDKSKQAEKENQINWWKYSGLTIaasllLAACSAGDTDEQIELEQEKKEAENAEDRANKNGIE----LEQEKQK 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011 961 LQKHNAELELQRERAEQMLQeKSEELKEKMDKltrqlfdDVQKEEQQRlvlekgfelktqayEKQIESLREEIKALKD 1038
Cdd:pfam05917 157 TNKSGIELANNQIKAEQEQQ-KTEQEKQKAEK-------EAIELEQEK--------------QKTIKTQRDLIKEQKD 212
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
910-1135 |
4.09e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 41.80 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 910 EKLTSLAALRVGDLEKVQKLEAELEKAAThRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQ-EKSEELKE 988
Cdd:COG3096 442 EWLETFQAKEEEATEKLLSLEQKMSMAQA-AHSQFEQAYQLVVAIAGELARSEAWDVARELLREGPDQRHLaEQVQPLRM 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 989 KMDKLTRQLFDDVQKEE-------QQRLVLE-KGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEgqvtsdrLKGE 1060
Cdd:COG3096 521 RLSELEQRLRQQQSAERlladfckRQGKNLDaEELEALHQELEALIESLSDSVSNAREQRMALRQEQEQ-------LQSR 593
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961011 1061 VARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSvEDLEHLNEDG 1135
Cdd:COG3096 594 IQSLMQRAPVWLAAQNALEQLSEQSGEEFTDSQDVTEYMQQLLEREREATVERDELGARKNALD-EEIERLSQPG 667
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
924-1198 |
4.13e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 924 EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMlQEKSEELKEKMDKLTRQLFDDVQK 1003
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA-EKKKEEAKKKADAAKKKAEEKKKA 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1004 EEQQRLVLE---KGFELKTQAYEKQIEslrEEIKALKDER---SQLHHQLEEGQVTSD-RLKGEVARLSKQAKTISEFEK 1076
Cdd:PTZ00121 1394 DEAKKKAEEdkkKADELKKAAAAKKKA---DEAKKKAEEKkkaDEAKKKAEEAKKADEaKKKAEEAKKAEEAKKKAEEAK 1470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1077 EIELLQAQKIDVEKHVQSQKR--EMRERMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEgLKKATRVlesh 1154
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE-AKKAEEK---- 1545
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568961011 1155 fqsqkdcyEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIR 1198
Cdd:PTZ00121 1546 --------KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
961-1030 |
4.14e-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: 397124 [Multi-domain] Cd Length: 297 Bit Score: 40.73 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 961 LQKHNAELELQRERAEQML--QEKSEE-----LKEKMDKLTRQLFDDVQ-----KEEQQRLVLEKGFELKTQAYEKQIES 1028
Cdd:pfam02841 216 AEAEQELLREKQKEEEQMMeaQERSYQehvkqLIEKMEAEREQLLAEQErmlehKLQEQEELLKEGFKTEAESLQKEIQD 295
|
..
gi 568961011 1029 LR 1030
Cdd:pfam02841 296 LK 297
|
|
| COG4487 |
COG4487 |
Uncharacterized protein, contains DUF2130 domain [Function unknown]; |
892-1085 |
4.67e-03 |
|
Uncharacterized protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 226889 [Multi-domain] Cd Length: 438 Bit Score: 40.96 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 892 QRLQKKLEDQNRENHGLV-EKLTSLAALRVGDLEKVQKLEAELEKAATHRHSyEEKGRRYRDTVEERlsklQKHNAELEL 970
Cdd:COG4487 34 QEDQSRILNTLEEFEKEAnEKRAQYRSAKKKELSQLEEQLINQKKEQKNLFN-EQIKQFELALQDEI----AKLEALELL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 971 QRERaEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAyEKQIESlreeikALKDERSQLHHQLEEG 1050
Cdd:COG4487 109 NLEK-DKELELLEKELDELSKELQKQLQNTAEIIEKKRENNKNEERLKFEN-EKKLEE------SLELEREKFEEQLHEA 180
|
170 180 190
....*....|....*....|....*....|....*
gi 568961011 1051 QVTSDRLKGEVARLSKQAktISEFEKEIELLQAQK 1085
Cdd:COG4487 181 NLDLEFKENEEQRESKWA--ILKKLKRRAELGSQQ 213
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
923-1169 |
4.98e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.25 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 923 LEKVQKLEAELEKAAT---HRHSYEEKGRRYR----DTVEERLSKLQKHNAELELQRERAEqmLQEKSEELKEKMDKLT- 994
Cdd:cd16269 61 LQELLDLHAACEKEALevfMKRSFKDEDQKFQkklmEQLEEKKEEFCKQNEEASSKRCQAL--LQELSAPLEEKISQGSy 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 995 -----RQLF-DDVQK-EEQQRLVLEKGFELK--TQAYEKQIESLREEIkaLKDERSQLHHQLEEgqvtsdrlkgEVARLS 1065
Cdd:cd16269 139 svpggYQLYlEDREKlVEKYRQVPRKGVKAEevLQEFLQSKEAEAEAI--LQADQALTEKEKEI----------EAERAK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1066 KQAKtisefEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLEsyDIEDVRSRLSvEDLEHLnedgelwfayegLK 1145
Cdd:cd16269 207 AEAA-----EQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEE--ERENLLKEQE-RALESK------------LK 266
|
250 260
....*....|....*....|....
gi 568961011 1146 KATRVLESHFQSQKDCYEKEIEGL 1169
Cdd:cd16269 267 EQEALLEEGFKEQAELLQEEIRSL 290
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
894-1130 |
5.52e-03 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 40.98 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 894 LQKKLEDQNRENHGLVEKLTSLAALRV--GDLEKVQKLEAEL-EKAATHRH---SYEEKGRRYRDTV---EERLSKLQKH 964
Cdd:COG4717 207 YHKLLESRRAEHARLAELRSELRADRDhiRALRDAVELWPRLqEWKQLEQEltrRREELATFPRDGVlrlEKREAHLQKT 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 965 NAELELQRERAEQM--LQEKSEELKEKMdkltrqLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIK---ALKDE 1039
Cdd:COG4717 287 EAEIDALLVRLAELkdLASQLIPAKEAV------LQALVRLHQQLSEIKASAFELTETLAGIEADLRDKEEAagnGFEAE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1040 RSQLHHQLEEGQVTSDR---LKGEVARLSKQAKTISEFEKEIELLQAQKI-DVEKHVQSQKrEMRERMSEVTKQLLESYD 1115
Cdd:COG4717 361 RVHDLRSLECMLRYQSSqreLKQTEAAYCKRLDEKRLFEDEAEEEARQRLaDDEEEVRAGD-EAREEKIAANSQVIDKEE 439
|
250
....*....|....*
gi 568961011 1116 IEDVRSRLSVEDLEH 1130
Cdd:COG4717 440 VCNLYDRRDTAWQKQ 454
|
|
| GimC |
COG1382 |
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; |
923-1046 |
5.71e-03 |
|
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 224300 [Multi-domain] Cd Length: 119 Bit Score: 38.06 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 923 LEKVQKLEAELEKAATHRhsyeekgrryrDTVEERLSKLQKHNAELELQRERAEqmLQEKSEELKEKMDKltrqlfDDVQ 1002
Cdd:COG1382 12 LAQLQQLQQQLQKVILQK-----------QQLEAQLKEIEKALEELEKLDEDAP--VYKKVGNLLVKVSK------EEAV 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568961011 1003 KEEQQRLVLekgFELKTQAYEKQIESLREEIKALKDERSQLHHQ 1046
Cdd:COG1382 73 DELEERKET---LELRIKTLEKQEEKLQERLEELQSEIQKALGD 113
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
891-1049 |
5.89e-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: 39.74 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 891 VQRLQKKLEDQNRE---NHGLVEKLTSLA-ALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNA 966
Cdd:cd00176 35 VEALLKKHEALEAElaaHEERVEALNELGeQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 967 ELELQRERAEQMLQEKSEELKEKMDKLTRQL--FDDVQKE------------EQQRLVLEKGFELKTQAYEKQIESLREE 1032
Cdd:cd00176 115 ADDLEQWLEEKEAALASEDLGKDLESVEELLkkHKELEEEleaheprlkslnELAEELLEEGHPDADEEIEEKLEELNER 194
|
170
....*....|....*..
gi 568961011 1033 IKALKDERSQLHHQLEE 1049
Cdd:cd00176 195 WEELLELAEERQKKLEE 211
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
1003-1183 |
6.02e-03 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 40.04 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1003 KEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQ 1082
Cdd:COG1579 3 NNNLKSLLAIQKLDLEKDRLEPRIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAEEKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1083 A------QKIDVEKHVQSQKREMRERMSEVTkqllesyDIEDVRSRLSVEdlehlnedgelwfaYEGLKKATRVLESHFQ 1156
Cdd:COG1579 83 SavkderELRALNIEIQIAKERINSLEDELA-------ELMEEIEKLEKE--------------IEDLKERLERLEKNLA 141
|
170 180
....*....|....*....|....*..
gi 568961011 1157 SQKDCYEKEIEGLNFKVVHLSQEINHL 1183
Cdd:COG1579 142 EAEARLEEEVAEIREEGQELSSKREEL 168
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
896-1107 |
6.32e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 896 KKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSyeekgrRYRDTVEERLSKLQKHNAELELQRERA 975
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA------RKQNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 976 EQmLQEKSEELKEKMDKLTRQLFDDVQKEEQ-QRLV--LEKGFELKTQAyeKQIESLREEIKALKDERSQLHHQLEEGQV 1052
Cdd:PHA02562 244 LN-LVMDIEDPSAALNKLNTAAAKIKSKIEQfQKVIkmYEKGGVCPTCT--QQISEGPDRITKIKDKLKELQHSLEKLDT 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568961011 1053 TSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVT 1107
Cdd:PHA02562 321 AIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
983-1208 |
7.29e-03 |
|
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: 40.77 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 983 SEELKEK-MDKLTRQLFDDVQKEEQQRLVLEKGFELKtqayEKQIESLREEIKALKDERSQLhhqleegqvtSDRLKGEV 1061
Cdd:TIGR04523 30 KQDTEEKqLEKKLKTIKNELKNKEKELKNLDKNLNKD----EEKINNSNNKIKILEQQIKDL----------NDKLKKNK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1062 ARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDvrsrlsveDLEHLNEDgelwfaY 1141
Cdd:TIGR04523 96 DKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK--------ELEKLNNK------Y 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1142 EGLKKATRVLEshfqSQKDCYEKEIEGLNFKVVHLSQEINHLQ-KLFREETDI--NESIRHEVTRLTSEN 1208
Cdd:TIGR04523 162 NDLKKQKEELE----NELNLLEKEKLNIQKNIDKIKNKLLKLElLLSNLKKKIqkNKSLESQISELKKQN 227
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
948-1050 |
7.71e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 223571 [Multi-domain] Cd Length: 557 Bit Score: 40.28 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 948 RRYRDTVEERLSKLQKHNAELEL--QRERAEQMLQEKSEELKEKMDKLTRQLfddvqkeEQQRLVLEKGFElktqayekq 1025
Cdd:COG0497 314 RKYGVTIEDLLEYLDKIKEELAQldNSEESLEALEKEVKKLKAELLEAAEAL-------SAIRKKAAKELE--------- 377
|
90 100
....*....|....*....|....*
gi 568961011 1026 iESLREEIKALKDERSQLHHQLEEG 1050
Cdd:COG0497 378 -KEVTAELKALAMEKARFTVELKPL 401
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
899-1037 |
8.21e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 225288 [Multi-domain] Cd Length: 652 Bit Score: 40.46 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 899 EDQNRENHGLVEKltslAALRVGDLEKV-QKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQ--KHNAELELQRERA 975
Cdd:COG2433 400 EERPREKEGTEEE----ERREITVYEKRiKKLEETVERLEEENSELKRELEELKREIEKLESELErfRREVRDKVRKDRE 475
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961011 976 EQMLQEKSEEL-KEKMDKLTR--QLFDDVQKEEQQRLVLEKGFELKTQAYEK----QIESLREEIKALK 1037
Cdd:COG2433 476 IRARDRRIERLeKELEEKKKRveELERKLAELRKMRKLELSGKGTPVKVVEKltleAIEEAEEEYGIKE 544
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
980-1113 |
8.82e-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: 38.05 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 980 QEKSEELKEKMdkltRQLFDDVQKEEQQRLVLEKgfelKTQAYEKQIESLREEIKALKDERSQLHH------------QL 1047
Cdd:pfam12718 13 QERAEELEEKV----KELEQENLEKEQEIKSLTH----KNQQLEEEVEKLEEQLKEAKEKAEESEKlktnnenltrkiQL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961011 1048 --EEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhvqsqkremreRMSEVTKQLLES 1113
Cdd:pfam12718 85 leEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEK-----------KYEELEEKYKEA 141
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1023-1109 |
9.19e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961011 1023 EKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKtisEFEKEIELLQAQKIDVEKHVQSQKREMRER 1102
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAA---ELEEKQQELEAQLEQLQEKAAETSQERKQK 217
|
....*..
gi 568961011 1103 MSEVTKQ 1109
Cdd:PRK11448 218 RKEITDQ 224
|
|
|