|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1445-1780 |
6.99e-174 |
|
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities: AAA1-AAA6). This is the first site (out of four nucleotide binding sites in the dynein motor) where the movement depends on ATP hydrolysis. When this site is nucleotide free or bound to ADP, the microtubule binding domain (MTBD) binds to the microtubule and the linker adopts the straight post-power-stroke conformation. Upon ATP binding and hydrolysis, the MTBD detaches from the microtubule and the linker is primed into the pre-power-stroke conformation. Dynein's AAA+ domains are each divided into an alpha/beta large subdomain designated with an L and and alpha small subdomains designated with an S. This is the AAA1 large (AAA1L) subdomain with the accompanying small subdomain (AAA1S). AAA1L, AAA1S and AAA2L enclose ADP.vanadate (ADP.Vi, ATP-hydrolysis transition state analogue). The AAA1L sensor-I loop, which varies in position depending on dynein's nucleotide state, swings in to contact AAA2L forming the important AAA1 nucleotide-binding site.
Pssm-ID: 463697 [Multi-domain] Cd Length: 327 Bit Score: 537.84 E-value: 6.99e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1445 YTYEYQGNASKLVYTPLTDKCYLTLTQAMKMGLGGNPYGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDVKSMGRIFVG 1524
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1525 LVKCGAWGCFDEFNRLEESVLSAVSMQIQTIQDALKNHRTVCELLGKEVEVNSNSGIFITMNPagkGYGGRQKLPDNLKQ 1604
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNP---GYAGRTELPDNLKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1605 LFRPVAMSHPDNELIAEVILYSEGFKDAKVLSRKLVAIFNLSRELLTPQQHYDWGLRALKTVLRGSGNLLRQlnksgtTQ 1684
Cdd:pfam12774 158 LFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRS------NP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1685 NANESHIVVQALRLNTMSKFTFTDCTRFDALIKDVFPGIELKEVEYDELSAALKQVFEEANYEIIPNQIKKALELYEQLC 1764
Cdd:pfam12774 232 NLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETML 311
|
330
....*....|....*.
gi 1034575401 1765 QRMGVVIVGPSGAGKS 1780
Cdd:pfam12774 312 VRHGVMLVGPTGSGKT 327
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1155-3810 |
5.38e-160 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 560.76 E-value: 5.38e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1155 LPKEQTRFNRVDEDFRSIMTDIKKDNRvTTLTTHAGIRNSLLTILDQLQRCQKSLNEFLEEKRSAFPRFyfIGDDDLLEI 1234
Cdd:COG5245 644 IPHAVHRKMSLVSGVRGIYKRVVSGCE-AINTILEDVGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDR 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1235 LGQSTNPSVIQSHLKKLFAGINSVCFdeKSKHITAMKSLEGEVVPFKNKVPL--SNNVETWLNDlalEMKKTLEQLLkEC 1312
Cdd:COG5245 721 VRELENRVYSYRFFVKKIAKEEMKTV--FSSRIQKKEPFSLDSEAYVGFFRLyeKSIVIRGINR---SMGRVLSQYL-ES 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1313 VttGRSSQGAvDPSLFPSQILC---LAEQIKFTEDVENAIkdhslhqiETQLVnklEQYTNIDTSSEDPGNTESGILELK 1389
Cdd:COG5245 795 V--QEALEIE-DGSFFVSRHRVrdgGLEKGRGCDAWENCF--------DPPLS---EYFRILEKIFPSEEGYFFDEVLKR 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1390 LKALILDIIHNIDVVKQLNQIQVHTTEDWAWKKQLRFYMKSDHTCCVQMVDSEFQYTYEYQGNASKLVYTPLTDKCYLTL 1469
Cdd:COG5245 861 LDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKL 940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1470 TQAMKMGLGGNpygpAGTGKTESVKALGGLLGRQVlvfncdEGIDVKSmgRIFVGLVKCGAWGcFDEFNRLEESVLsAVS 1549
Cdd:COG5245 941 FEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR-TIL 1006
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1550 MQIQTIQDALKNHRTVCELLGKEVEVNSNSGIFITMNPagkgyggRQKLPDNLKQLFRPVAMSHPDNElIAEVilysegf 1629
Cdd:COG5245 1007 VDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE-------RNIVLEIGRRALDMFLSNIPFGA-IKSR------- 1071
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1630 kdAKVLSRKLVAIFNLSRELLTPQQHYDWglRALKTVLRGSGNLLRQLNKSGTTqnaneshiVVQALRLNTMSkftftdc 1709
Cdd:COG5245 1072 --RESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRMLEEKTEYLNK--------ILSITGLPLIS------- 1132
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1710 trfDALIKDvfpgIELKEVEYDEL-SAALKQVFEEANyEIIPNQIKKALELYEQLCQRMGVVIVGPSGAGKSTLWRmlrA 1788
Cdd:COG5245 1133 ---DTLRER----IDTLDAEWDSFcRISESLKKYESQ-QVSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYT---D 1201
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1789 ALCKTGKVVKQYTMNPKAMPRYQLLGHIDMDTREWSDGVLTNSARQVVREpqdvsswiicdgdidpEWIESLNSVLDDNR 1868
Cdd:COG5245 1202 ACDYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSKMEYEVE----------------RYVEKTKAEVSSLK 1265
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1869 LLTMPSGERiqfgpnvNFVFETHDlscASPATISRMGMIFLSDEETDLNSLIkSWLRNQPAEYRNN-------------- 1934
Cdd:COG5245 1266 LELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRLSTKGVF-LDELGDTKRYLDEcldffscfeevqke 1334
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1935 ----LENWIGD--YFEKALQWVLKQNDY-VVETSLVGTVMNG--LSHLHGCRDHDEFIINLIRGLGGNLNMKSRLEFTke 2005
Cdd:COG5245 1335 idelSMVFCADalRFSADLYHIVKERRFsGVLAGSDASESLGgkSIELAAILEHKDLIVEMKRGINDVLKLRIFGDKC-- 1412
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2006 vfhwaRESPPDFHKPMDTYYDSTRGRLATY--VLKKPEDLTADDFSNG-----------LTLP---VIQTPDMQRGLDYF 2069
Cdd:COG5245 1413 -----RESTPRFYLISDGDLIKDLNERSDYeeMLIMMFNISAVITNNGsiagfelrgerVMLRkevVIPTSDTGFVDSFS 1487
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2070 KPWLSsdTKQPFILVGPEGCGKGMLLRYAFSQLRSTQIATVHCSAQTTSRHLLQKLSQTcMVISTNTG--RVYRPKDCER 2147
Cdd:COG5245 1488 NEALN--TLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERE-TEYYPNTGvvRLYPKPVVKD 1564
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2148 LVLYLKDINLPKLDKWGTSTLVAFLQQVLTYQGFYDE-NLEWVGLENIQIVASMSAGGRLGRHKLTTRFTSIVRLCSIDY 2226
Cdd:COG5245 1565 LVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSSiAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCY 1644
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2227 PEREQLQTIYGAYLEPVLHKNLKNHSIwgssskIYLLAGSMVQVYEQVRAKFTVDDYSHYFFTPCILTQWVLGLFRYDLE 2306
Cdd:COG5245 1645 PELASLRNIYEAVLMGSYLCFDEFNRL------SEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAET 1718
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2307 GgsSNHPLDYVLEIVAYEARRLFRDKIVGAKELHLFDIILTSVFQGDWGSDILDNMSDSFYVTWGARHNSgaraapgqpl 2386
Cdd:COG5245 1719 R--IDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFG---------- 1786
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2387 pphgkpLGKLNSTDLKDVIKKGLIHYGRDNQNLDILLFHEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTITSLVSHMH 2466
Cdd:COG5245 1787 ------MACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLN 1860
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2467 GAVLFSPKISRGYELKQFKNDLKHVLQLAGIEAQQVVLLLEDYQFVHPTFLEMINSLLSSGEVPGLYTLEELEPLLLPLK 2546
Cdd:COG5245 1861 PRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLR 1940
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2547 DQASQDGFF----GPVFNYFTYRIQQNLHIVL-IMDSANSNFMINCESnPALHKKCQVLWMEGWSNSSMKKIP-EMLFSE 2620
Cdd:COG5245 1941 FVFESTSLEkdteATLTRVFLVYMEENLPVVFsACCSQDTSVLAGIRS-PALKNRCFIDFKKLWDTEEMSQYAnSVETLS 2019
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2621 TGGGEKYNDKKRKEEKKKNSVDPDFLKSFLLIHES-------CKAYGATPSRYMTFLHVYSAISSSKKKELLKRQSHLQA 2693
Cdd:COG5245 2020 RDGGRVFFINGELGVGKGALISEVFGDDAVVIEGRgfeismiEGSLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVE 2099
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2694 GVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQMITVSMQDASEQKTELERLKHRIAEEVVKIEERKNKIDDELK 2773
Cdd:COG5245 2100 GVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKS 2179
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2774 EVQPLVNEAKLAVGNIKPESLSEIRSLRMPPDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVREDIATFD-ARNISKE 2852
Cdd:COG5245 2180 SKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPdEIEFDLE 2259
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2853 IRESVEELLFKNKgSFDPKNAKRASTAAAPLAAWVKANIQYSHVLERIHPLETEQAGLESNLKKTEDRKRKLEELLNSVG 2932
Cdd:COG5245 2260 ARRFREARECSDP-SFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLM 2338
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2933 QKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEELATLPKRAQLAAAFITYLSAAP 3012
Cdd:COG5245 2339 TFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLG 2418
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3013 ESLRKTCLEEWTKSAGLE---KFDLRRFLCTESEQLIWKSEGLP-SDDLSIENALVILQSR-VCPFLIDPSSQATEWLKT 3087
Cdd:COG5245 2419 FLCRAIEFGMSFIRISKEfrdKEIRRRQFITEGVQKIEDFKEEAcSTDYGLENSRIRKDLQdLTAVLNDPSSKIVTSQRQ 2498
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3088 HLKDSRLEVINQQDSNFITALELAVRFGKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEEFRLFLSTR 3167
Cdd:COG5245 2499 MYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSE 2578
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3168 NPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLAKLEESLLETLATSQGNILE 3247
Cdd:COG5245 2579 GRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQ 2658
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3248 NKDLIESLNQTKASSALIQESLKESYKLQISLDQERDAYLPLAESASKMYFIISDLSKINNMYRFSLAAFLRLFQRALQN 3327
Cdd:COG5245 2659 TDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWRRM 2738
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3328 KqdSENTEQRIQSLISSLQHMVYEYICRCLFKAD--------QLMFALHFVRGMHPELfqENEWDTFTGVVVgdmlrkaD 3399
Cdd:COG5245 2739 K--SKYLCAIRYMLMSSEWILDHEDRSGFIHRLDvsfllrtkRFVSTLLEDKNYRQVL--SSCSLYGNDVIS-------H 2807
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3400 SQQKI-RDQLPSWIDQERSWAVATLKialpsLYQTLCFEDAAlwRTYYN--NSMCEQEFPSILAKkvslfqqilvvqalr 3476
Cdd:COG5245 2808 SCDRFdRDVYRALKHQMDNRTHSTIL-----TSNSKTNPYKE--YTYNDswAEAFEVEDSGDLYK--------------- 2865
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3477 pdrlqsamalfacKTLGLKEVSPLPLNLKRLYKETLEIEPIliiispgadpsqeLQELANAERSgecyhqvamgqgqaDL 3556
Cdd:COG5245 2866 -------------FEEGLLELIVGHAPLIYAHKKSLENERN-------------VDRLGSKENE--------------VY 2905
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3557 AIQMLKECARNGDWLCLKNLHLVVSWL-----PVLEKELNTLQPKDTFRLWLTAEVHPNFTPILLQSSLKITYESPPGLK 3631
Cdd:COG5245 2906 AVLNSLFSRKEKSWFEVYNISLSFGWFkryveDVVYPIKASRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETG 2985
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3632 KNLMRTYES-WTPEQISKkdnTHRAHALFSLAWFHAACQERRNYIPQGWTKFYEFSLSDLRAGYNIIDRLF--DGAKDVQ 3708
Cdd:COG5245 2986 CGYADLVEIdRYPFDYTL---VIACDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNILflNHLNARK 3062
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3709 WEFVHGLLENAIYGGRIDNYFDLRVLQSYLKQFF----NSSVID--VFNQRNKKSIFPYSVSlpQSCSILdyraVIEKIP 3782
Cdd:COG5245 3063 WGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGahetSSQILAsvPGGDPELVKFHMEEMC--RSSAFG----VIGQLP 3136
|
2730 2740
....*....|....*....|....*...
gi 1034575401 3783 EDDKPSFFGLPANIARSSQRMISSQVIS 3810
Cdd:COG5245 3137 DLALCAWLMGPCDSEYLKAIVYSSRIDM 3164
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
914-1312 |
4.11e-125 |
|
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic cells, as they can convert energy derived from the hydrolysis of ATP to force and movement along cytoskeletal polymers, such as microtubules. This region is found C-terminal to the dynein heavy chain N-terminal region 1 (pfam08385) in many members of this family. No functions seem to have been attributed specifically to this region.
Pssm-ID: 462462 [Multi-domain] Cd Length: 402 Bit Score: 401.25 E-value: 4.11e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 914 ISKDIESCAQIWAFYEEFQQGFQEMANEDWITFrtKTYLFEEFLMNWHDRLRKVE---EHSVMTVKLQSEVDKYKIVIPI 990
Cdd:pfam08393 4 IKKELEPLKKLWDLVSEWQESLEEWKNGPFSDL--DVEELEEELEEFLKELKKLPkelRDWDVAEELKKKIDDFKKSLPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 991 LKYVRGEHLSPDHWLDLFRLLGLPRGTSLEKLLFGDLLRVadTIVAKAADLKDLNSRAQGEVTIREALRELDLWGVGAVF 1070
Cdd:pfam08393 82 IEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDL--NLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1071 TLIDYEDsqsRTMKLIKDWKDIVNQVGDNRCLLQSLKDSPYYKGFEDKVSIWERKLAELDEYLQNLNHIQRKWVYLEPIF 1150
Cdd:pfam08393 160 ELVPYKD---TGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1151 G----RGALPKEQTRFNRVDEDFRSIMTDIKKDNRVTTLTTHAGIRNSLLTILDQLQRCQKSLNEFLEEKRSAFPRFYFI 1226
Cdd:pfam08393 237 SsediRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1227 GDDDLLEILGQSTNPSVIQSHLKKLFAGINSVCFDEkSKHITAMKSLEGEVVPF-KNKVPLSNNVETWLNDLALEMKKTL 1305
Cdd:pfam08393 317 SNDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE-NKEITGMISKEGEVVPFsKPPVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 1034575401 1306 EQLLKEC 1312
Cdd:pfam08393 396 RDLLKEA 402
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3047-3265 |
3.73e-96 |
|
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the fifth AAA+ domain subdomain AAA5S. Structural analysis reveal that it is the coiled-coil buttress interface. The relative movement of AAA5S together with the stalk (AAA4S), is coupled to rearrangements in the AAA+ ring. Closure of the AAA1 site and the rigid body movement of AAA2-AAA4 force the AAA4/AAA5 interface to close and the AAA6L subdomain to rotate towards the ring centre. The AAA5S subdomain rotates as a unit together with AAA6L, and this movement pulls the buttress relative to the stalk.
Pssm-ID: 463702 [Multi-domain] Cd Length: 222 Bit Score: 310.53 E-value: 3.73e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3047 WKSEGLPSDDLSIENALVILQSRVCPFLIDPSSQATEWLKTHLKDSRLEVINQQDSNFITALELAVRFGKTLIIQEM-DG 3125
Cdd:pfam12781 3 WNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVgEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3126 VEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEEFRLFLSTRNPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHE 3205
Cdd:pfam12781 83 LDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVKKE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3206 KPDLEEQKTKLLQQEEDKKIQLAKLEESLLETLATSQGNILENKDLIESLNQTKASSALI 3265
Cdd:pfam12781 163 RPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
3805-4098 |
1.01e-53 |
|
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein heavy chain. This domain is a complex structure comprising six alpha-helices and an incomplete six-stranded antiparallel beta-barrel. The shape of this domain is distinctively flat, spreading over the AAA1, AAA5 and AAA6 domain.
Pssm-ID: 465677 Cd Length: 301 Bit Score: 191.68 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3805 SSQVISQLRILGRSITAGSKFDREiwSNElSPVLNLWKKLNQnsnlihqKVPPPND----------RQGSPILSFIILEQ 3874
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGGGGGGS--SRE-EIVLELAKDILE-------KLPEPFDieeaeekypvGYEDPLNTVLLQEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3875 FNAIRLVQSVHQSLAALSKVIRGTTLLSSEVQKLASALLNQKCPLAWQSKWEGPEDPL-QYLRGLVARALAIQNWVDKAE 3953
Cdd:pfam18199 74 ERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLgSWIRDLLERLKQLQDWLDDEG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3954 KQAllseTLDLSELFHPDTFLNALRQETARAVGRSVDSLKFVASWKGRLQEAKLQIK------ISGLLLEGCSFDG--NQ 4025
Cdd:pfam18199 154 PPK----VFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSPEEVTEPpedgvyVHGLFLEGARWDRknGC 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034575401 4026 LSEnQLDSPSVSSVLPCFMGWIPQDAcgPYSPDECISLPVYTSAERDR--VVTNIDVPCGGNQDQWIQCGAALFL 4098
Cdd:pfam18199 230 LVE-SEPKELFSPLPVIHLKPVESDK--KKLDENTYECPVYKTSERHStnFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
28-468 |
4.74e-25 |
|
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains to form dimers, and with intermediate chain-light chain complexes to form a basal cargo binding unit. The region featured in this family includes the sequences implicated in mediating these interactions. It is thought to be flexible and not to adopt a rigid conformation.
Pssm-ID: 462457 Cd Length: 560 Bit Score: 113.44 E-value: 4.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 28 VWRQTEHdhYPES-RMLHLLDIIGGSFGRFVQKKLGTLNLWEDPYYLVKESLKAGISICEQWVIVCNHLTGQVWQRYVPH 106
Cdd:pfam08385 128 IWSISRY--YNTSeRMTVLLEKISNQLIEQCKKYLSPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRER 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 107 PWK-NEKYFPETLDKLGKRLEEVLAIRTIHEKFLYFLPASEEKIICLTRVFEP--------FTGLNPVQYNP--YTEPLW 175
Cdd:pfam08385 206 PWDfSERYIFGRFDAFLERLEKILELFETIEQFSKLEKIGGTKGPELEGVIEEileefqeaYKVFKSKTYDIldVSNEGF 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 176 KAAVSQYEKIIAPAEQKIAGKLKNYISEIQdSPQQLLQAFLKYKELVKRPTISKELMLERETLLARLVDSIKDFRLDFEN 255
Cdd:pfam08385 286 DDDYEEFKERIKDLERRLQAFIDQAFDDAR-STESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDK 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 256 rcrgipGDASGPLSGKNLSEVVNSIVWVRQLELKVDDTIKIAEALLSDLpgfrcFHQSAKDLLD-------QLKLYEQEQ 328
Cdd:pfam08385 365 ------QKYNPSPIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLL-----KHAEGKKVIKkynelakKLDEYERLI 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 329 FDDWSRDIqsglsDSRSGLCIEASsrIMELD-SNDGLLKVHYSDRLVILLREVRQLSALGFVIPAKIQQVANIAQKFCKQ 407
Cdd:pfam08385 434 YEAWLKEV-----EEASEGNLKRP--LLVRHpETGKLLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPY 506
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034575401 408 AIILKQVAHFYNSIDQQMIQSQRPMMLQSALAFEQIIKNskagsgGKSQITWDNpKELEGY 468
Cdd:pfam08385 507 AESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEP------GLTTLTWNS-LGIDEY 560
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2680-3032 |
1.25e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2680 KKKELLKRQSHLQAGVSKLNEAKALVDELNRkageqsvlLKTKQDEadaalqmitVSMQDASEQKTELERLKHRIAEEVV 2759
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKEELER--------LKKRLTG---------LTPEKLEKELEELEKAKEEIEEEIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2760 KIEERKNKIDDELKEVQPLVNEAKLAVG---------------NIKPESLSEIRSLRMPPDVIRDILEGVLRLMgifdts 2824
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKEL------ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2825 wVSMKSFLAKRgvREDIATfdaRNISKEIRESVEELlfknkGSFDPKNAKrastaaaplaawvKANIQYSHVLERIHPLE 2904
Cdd:PRK03918 483 -RELEKVLKKE--SELIKL---KELAEQLKELEEKL-----KKYNLEELE-------------KKAEEYEKLKEKLIKLK 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2905 TEQAGLESNLKKTEDRKRKLEELLNsvgqKVSELKEkfqsrtsEAAKLEAEVSK-AQETIKAAEVLINQLDREHKRWN-- 2981
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLAELEK----KLDELEE-------ELAELLKELEElGFESVEELEERLKELEPFYNEYLel 607
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034575401 2982 ----AQVVEITEELATLPKRAQLAAAFITYLSAAPESLRKTcLEEWTKSAGLEKF 3032
Cdd:PRK03918 608 kdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE-LEELEKKYSEEEY 661
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2679-2996 |
2.48e-08 |
|
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: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2679 SKKKELLKRQshLQAGVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQmitvsmqDASEQKTELERLKHRIAEEV 2758
Cdd:TIGR02169 680 RERLEGLKRE--LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ-------EEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2759 VKIEERKNKIDDELKEVQPL---VNEAKLAVGNIKPE-SLSEIRSLRmppDVIRDILEGVLRLMGIFDtswvSMKSFLAK 2834
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELeedLHKLEEALNDLEARlSHSRIPEIQ---AELSKLEEEVSRIEARLR----EIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2835 RGVREDIAtfdarniSKEIRESVEELLfknkgsfdpknakrastaaaplaawvKANIQYSHVLERIHPLETEQAGLESNL 2914
Cdd:TIGR02169 824 LTLEKEYL-------EKEIQELQEQRI--------------------------DLKEQIKSIEKEIENLNGKKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2915 KKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIK----AAEVLINQLDrEHKRWNAQVVEITEE 2990
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSelkaKLEALEEELS-EIEDPKGEDEEIPEE 949
|
....*.
gi 1034575401 2991 LATLPK 2996
Cdd:TIGR02169 950 ELSLED 955
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1722-1793 |
9.75e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.88 E-value: 9.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034575401 1722 GIELKEVEydelsaalKQVFEEANYEIIPNQIkkalelyeqlcqrmgVVIVGPSGAGKSTLWRMLRAALCKT 1793
Cdd:COG2401 35 GVELRVVE--------RYVLRDLNLEIEPGEI---------------VLIVGASGSGKSTLLRLLAGALKGT 83
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1482-1522 |
2.71e-03 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 41.50 E-value: 2.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1034575401 1482 YGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDV------KSMGRIF 1522
Cdd:cd19481 32 YGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKyvgeseKNLRKIF 78
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1769-1785 |
4.60e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.52 E-value: 4.60e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1445-1780 |
6.99e-174 |
|
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities: AAA1-AAA6). This is the first site (out of four nucleotide binding sites in the dynein motor) where the movement depends on ATP hydrolysis. When this site is nucleotide free or bound to ADP, the microtubule binding domain (MTBD) binds to the microtubule and the linker adopts the straight post-power-stroke conformation. Upon ATP binding and hydrolysis, the MTBD detaches from the microtubule and the linker is primed into the pre-power-stroke conformation. Dynein's AAA+ domains are each divided into an alpha/beta large subdomain designated with an L and and alpha small subdomains designated with an S. This is the AAA1 large (AAA1L) subdomain with the accompanying small subdomain (AAA1S). AAA1L, AAA1S and AAA2L enclose ADP.vanadate (ADP.Vi, ATP-hydrolysis transition state analogue). The AAA1L sensor-I loop, which varies in position depending on dynein's nucleotide state, swings in to contact AAA2L forming the important AAA1 nucleotide-binding site.
Pssm-ID: 463697 [Multi-domain] Cd Length: 327 Bit Score: 537.84 E-value: 6.99e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1445 YTYEYQGNASKLVYTPLTDKCYLTLTQAMKMGLGGNPYGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDVKSMGRIFVG 1524
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1525 LVKCGAWGCFDEFNRLEESVLSAVSMQIQTIQDALKNHRTVCELLGKEVEVNSNSGIFITMNPagkGYGGRQKLPDNLKQ 1604
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNP---GYAGRTELPDNLKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1605 LFRPVAMSHPDNELIAEVILYSEGFKDAKVLSRKLVAIFNLSRELLTPQQHYDWGLRALKTVLRGSGNLLRQlnksgtTQ 1684
Cdd:pfam12774 158 LFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRS------NP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1685 NANESHIVVQALRLNTMSKFTFTDCTRFDALIKDVFPGIELKEVEYDELSAALKQVFEEANYEIIPNQIKKALELYEQLC 1764
Cdd:pfam12774 232 NLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETML 311
|
330
....*....|....*.
gi 1034575401 1765 QRMGVVIVGPSGAGKS 1780
Cdd:pfam12774 312 VRHGVMLVGPTGSGKT 327
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1155-3810 |
5.38e-160 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 560.76 E-value: 5.38e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1155 LPKEQTRFNRVDEDFRSIMTDIKKDNRvTTLTTHAGIRNSLLTILDQLQRCQKSLNEFLEEKRSAFPRFyfIGDDDLLEI 1234
Cdd:COG5245 644 IPHAVHRKMSLVSGVRGIYKRVVSGCE-AINTILEDVGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDR 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1235 LGQSTNPSVIQSHLKKLFAGINSVCFdeKSKHITAMKSLEGEVVPFKNKVPL--SNNVETWLNDlalEMKKTLEQLLkEC 1312
Cdd:COG5245 721 VRELENRVYSYRFFVKKIAKEEMKTV--FSSRIQKKEPFSLDSEAYVGFFRLyeKSIVIRGINR---SMGRVLSQYL-ES 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1313 VttGRSSQGAvDPSLFPSQILC---LAEQIKFTEDVENAIkdhslhqiETQLVnklEQYTNIDTSSEDPGNTESGILELK 1389
Cdd:COG5245 795 V--QEALEIE-DGSFFVSRHRVrdgGLEKGRGCDAWENCF--------DPPLS---EYFRILEKIFPSEEGYFFDEVLKR 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1390 LKALILDIIHNIDVVKQLNQIQVHTTEDWAWKKQLRFYMKSDHTCCVQMVDSEFQYTYEYQGNASKLVYTPLTDKCYLTL 1469
Cdd:COG5245 861 LDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKL 940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1470 TQAMKMGLGGNpygpAGTGKTESVKALGGLLGRQVlvfncdEGIDVKSmgRIFVGLVKCGAWGcFDEFNRLEESVLsAVS 1549
Cdd:COG5245 941 FEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR-TIL 1006
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1550 MQIQTIQDALKNHRTVCELLGKEVEVNSNSGIFITMNPagkgyggRQKLPDNLKQLFRPVAMSHPDNElIAEVilysegf 1629
Cdd:COG5245 1007 VDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE-------RNIVLEIGRRALDMFLSNIPFGA-IKSR------- 1071
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1630 kdAKVLSRKLVAIFNLSRELLTPQQHYDWglRALKTVLRGSGNLLRQLNKSGTTqnaneshiVVQALRLNTMSkftftdc 1709
Cdd:COG5245 1072 --RESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRMLEEKTEYLNK--------ILSITGLPLIS------- 1132
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1710 trfDALIKDvfpgIELKEVEYDEL-SAALKQVFEEANyEIIPNQIKKALELYEQLCQRMGVVIVGPSGAGKSTLWRmlrA 1788
Cdd:COG5245 1133 ---DTLRER----IDTLDAEWDSFcRISESLKKYESQ-QVSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYT---D 1201
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1789 ALCKTGKVVKQYTMNPKAMPRYQLLGHIDMDTREWSDGVLTNSARQVVREpqdvsswiicdgdidpEWIESLNSVLDDNR 1868
Cdd:COG5245 1202 ACDYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSKMEYEVE----------------RYVEKTKAEVSSLK 1265
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1869 LLTMPSGERiqfgpnvNFVFETHDlscASPATISRMGMIFLSDEETDLNSLIkSWLRNQPAEYRNN-------------- 1934
Cdd:COG5245 1266 LELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRLSTKGVF-LDELGDTKRYLDEcldffscfeevqke 1334
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1935 ----LENWIGD--YFEKALQWVLKQNDY-VVETSLVGTVMNG--LSHLHGCRDHDEFIINLIRGLGGNLNMKSRLEFTke 2005
Cdd:COG5245 1335 idelSMVFCADalRFSADLYHIVKERRFsGVLAGSDASESLGgkSIELAAILEHKDLIVEMKRGINDVLKLRIFGDKC-- 1412
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2006 vfhwaRESPPDFHKPMDTYYDSTRGRLATY--VLKKPEDLTADDFSNG-----------LTLP---VIQTPDMQRGLDYF 2069
Cdd:COG5245 1413 -----RESTPRFYLISDGDLIKDLNERSDYeeMLIMMFNISAVITNNGsiagfelrgerVMLRkevVIPTSDTGFVDSFS 1487
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2070 KPWLSsdTKQPFILVGPEGCGKGMLLRYAFSQLRSTQIATVHCSAQTTSRHLLQKLSQTcMVISTNTG--RVYRPKDCER 2147
Cdd:COG5245 1488 NEALN--TLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERE-TEYYPNTGvvRLYPKPVVKD 1564
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2148 LVLYLKDINLPKLDKWGTSTLVAFLQQVLTYQGFYDE-NLEWVGLENIQIVASMSAGGRLGRHKLTTRFTSIVRLCSIDY 2226
Cdd:COG5245 1565 LVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSSiAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCY 1644
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2227 PEREQLQTIYGAYLEPVLHKNLKNHSIwgssskIYLLAGSMVQVYEQVRAKFTVDDYSHYFFTPCILTQWVLGLFRYDLE 2306
Cdd:COG5245 1645 PELASLRNIYEAVLMGSYLCFDEFNRL------SEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAET 1718
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2307 GgsSNHPLDYVLEIVAYEARRLFRDKIVGAKELHLFDIILTSVFQGDWGSDILDNMSDSFYVTWGARHNSgaraapgqpl 2386
Cdd:COG5245 1719 R--IDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFG---------- 1786
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2387 pphgkpLGKLNSTDLKDVIKKGLIHYGRDNQNLDILLFHEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTITSLVSHMH 2466
Cdd:COG5245 1787 ------MACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLN 1860
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2467 GAVLFSPKISRGYELKQFKNDLKHVLQLAGIEAQQVVLLLEDYQFVHPTFLEMINSLLSSGEVPGLYTLEELEPLLLPLK 2546
Cdd:COG5245 1861 PRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLR 1940
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2547 DQASQDGFF----GPVFNYFTYRIQQNLHIVL-IMDSANSNFMINCESnPALHKKCQVLWMEGWSNSSMKKIP-EMLFSE 2620
Cdd:COG5245 1941 FVFESTSLEkdteATLTRVFLVYMEENLPVVFsACCSQDTSVLAGIRS-PALKNRCFIDFKKLWDTEEMSQYAnSVETLS 2019
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2621 TGGGEKYNDKKRKEEKKKNSVDPDFLKSFLLIHES-------CKAYGATPSRYMTFLHVYSAISSSKKKELLKRQSHLQA 2693
Cdd:COG5245 2020 RDGGRVFFINGELGVGKGALISEVFGDDAVVIEGRgfeismiEGSLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVE 2099
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2694 GVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQMITVSMQDASEQKTELERLKHRIAEEVVKIEERKNKIDDELK 2773
Cdd:COG5245 2100 GVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKS 2179
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2774 EVQPLVNEAKLAVGNIKPESLSEIRSLRMPPDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVREDIATFD-ARNISKE 2852
Cdd:COG5245 2180 SKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPdEIEFDLE 2259
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2853 IRESVEELLFKNKgSFDPKNAKRASTAAAPLAAWVKANIQYSHVLERIHPLETEQAGLESNLKKTEDRKRKLEELLNSVG 2932
Cdd:COG5245 2260 ARRFREARECSDP-SFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLM 2338
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2933 QKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEELATLPKRAQLAAAFITYLSAAP 3012
Cdd:COG5245 2339 TFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLG 2418
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3013 ESLRKTCLEEWTKSAGLE---KFDLRRFLCTESEQLIWKSEGLP-SDDLSIENALVILQSR-VCPFLIDPSSQATEWLKT 3087
Cdd:COG5245 2419 FLCRAIEFGMSFIRISKEfrdKEIRRRQFITEGVQKIEDFKEEAcSTDYGLENSRIRKDLQdLTAVLNDPSSKIVTSQRQ 2498
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3088 HLKDSRLEVINQQDSNFITALELAVRFGKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEEFRLFLSTR 3167
Cdd:COG5245 2499 MYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSE 2578
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3168 NPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLAKLEESLLETLATSQGNILE 3247
Cdd:COG5245 2579 GRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQ 2658
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3248 NKDLIESLNQTKASSALIQESLKESYKLQISLDQERDAYLPLAESASKMYFIISDLSKINNMYRFSLAAFLRLFQRALQN 3327
Cdd:COG5245 2659 TDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWRRM 2738
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3328 KqdSENTEQRIQSLISSLQHMVYEYICRCLFKAD--------QLMFALHFVRGMHPELfqENEWDTFTGVVVgdmlrkaD 3399
Cdd:COG5245 2739 K--SKYLCAIRYMLMSSEWILDHEDRSGFIHRLDvsfllrtkRFVSTLLEDKNYRQVL--SSCSLYGNDVIS-------H 2807
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3400 SQQKI-RDQLPSWIDQERSWAVATLKialpsLYQTLCFEDAAlwRTYYN--NSMCEQEFPSILAKkvslfqqilvvqalr 3476
Cdd:COG5245 2808 SCDRFdRDVYRALKHQMDNRTHSTIL-----TSNSKTNPYKE--YTYNDswAEAFEVEDSGDLYK--------------- 2865
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3477 pdrlqsamalfacKTLGLKEVSPLPLNLKRLYKETLEIEPIliiispgadpsqeLQELANAERSgecyhqvamgqgqaDL 3556
Cdd:COG5245 2866 -------------FEEGLLELIVGHAPLIYAHKKSLENERN-------------VDRLGSKENE--------------VY 2905
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3557 AIQMLKECARNGDWLCLKNLHLVVSWL-----PVLEKELNTLQPKDTFRLWLTAEVHPNFTPILLQSSLKITYESPPGLK 3631
Cdd:COG5245 2906 AVLNSLFSRKEKSWFEVYNISLSFGWFkryveDVVYPIKASRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETG 2985
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3632 KNLMRTYES-WTPEQISKkdnTHRAHALFSLAWFHAACQERRNYIPQGWTKFYEFSLSDLRAGYNIIDRLF--DGAKDVQ 3708
Cdd:COG5245 2986 CGYADLVEIdRYPFDYTL---VIACDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNILflNHLNARK 3062
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3709 WEFVHGLLENAIYGGRIDNYFDLRVLQSYLKQFF----NSSVID--VFNQRNKKSIFPYSVSlpQSCSILdyraVIEKIP 3782
Cdd:COG5245 3063 WGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGahetSSQILAsvPGGDPELVKFHMEEMC--RSSAFG----VIGQLP 3136
|
2730 2740
....*....|....*....|....*...
gi 1034575401 3783 EDDKPSFFGLPANIARSSQRMISSQVIS 3810
Cdd:COG5245 3137 DLALCAWLMGPCDSEYLKAIVYSSRIDM 3164
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
914-1312 |
4.11e-125 |
|
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic cells, as they can convert energy derived from the hydrolysis of ATP to force and movement along cytoskeletal polymers, such as microtubules. This region is found C-terminal to the dynein heavy chain N-terminal region 1 (pfam08385) in many members of this family. No functions seem to have been attributed specifically to this region.
Pssm-ID: 462462 [Multi-domain] Cd Length: 402 Bit Score: 401.25 E-value: 4.11e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 914 ISKDIESCAQIWAFYEEFQQGFQEMANEDWITFrtKTYLFEEFLMNWHDRLRKVE---EHSVMTVKLQSEVDKYKIVIPI 990
Cdd:pfam08393 4 IKKELEPLKKLWDLVSEWQESLEEWKNGPFSDL--DVEELEEELEEFLKELKKLPkelRDWDVAEELKKKIDDFKKSLPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 991 LKYVRGEHLSPDHWLDLFRLLGLPRGTSLEKLLFGDLLRVadTIVAKAADLKDLNSRAQGEVTIREALRELDLWGVGAVF 1070
Cdd:pfam08393 82 IEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDL--NLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1071 TLIDYEDsqsRTMKLIKDWKDIVNQVGDNRCLLQSLKDSPYYKGFEDKVSIWERKLAELDEYLQNLNHIQRKWVYLEPIF 1150
Cdd:pfam08393 160 ELVPYKD---TGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1151 G----RGALPKEQTRFNRVDEDFRSIMTDIKKDNRVTTLTTHAGIRNSLLTILDQLQRCQKSLNEFLEEKRSAFPRFYFI 1226
Cdd:pfam08393 237 SsediRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1227 GDDDLLEILGQSTNPSVIQSHLKKLFAGINSVCFDEkSKHITAMKSLEGEVVPF-KNKVPLSNNVETWLNDLALEMKKTL 1305
Cdd:pfam08393 317 SNDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE-NKEITGMISKEGEVVPFsKPPVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 1034575401 1306 EQLLKEC 1312
Cdd:pfam08393 396 RDLLKEA 402
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3047-3265 |
3.73e-96 |
|
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the fifth AAA+ domain subdomain AAA5S. Structural analysis reveal that it is the coiled-coil buttress interface. The relative movement of AAA5S together with the stalk (AAA4S), is coupled to rearrangements in the AAA+ ring. Closure of the AAA1 site and the rigid body movement of AAA2-AAA4 force the AAA4/AAA5 interface to close and the AAA6L subdomain to rotate towards the ring centre. The AAA5S subdomain rotates as a unit together with AAA6L, and this movement pulls the buttress relative to the stalk.
Pssm-ID: 463702 [Multi-domain] Cd Length: 222 Bit Score: 310.53 E-value: 3.73e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3047 WKSEGLPSDDLSIENALVILQSRVCPFLIDPSSQATEWLKTHLKDSRLEVINQQDSNFITALELAVRFGKTLIIQEM-DG 3125
Cdd:pfam12781 3 WNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVgEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3126 VEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEEFRLFLSTRNPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHE 3205
Cdd:pfam12781 83 LDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVKKE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3206 KPDLEEQKTKLLQQEEDKKIQLAKLEESLLETLATSQGNILENKDLIESLNQTKASSALI 3265
Cdd:pfam12781 163 RPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
3805-4098 |
1.01e-53 |
|
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein heavy chain. This domain is a complex structure comprising six alpha-helices and an incomplete six-stranded antiparallel beta-barrel. The shape of this domain is distinctively flat, spreading over the AAA1, AAA5 and AAA6 domain.
Pssm-ID: 465677 Cd Length: 301 Bit Score: 191.68 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3805 SSQVISQLRILGRSITAGSKFDREiwSNElSPVLNLWKKLNQnsnlihqKVPPPND----------RQGSPILSFIILEQ 3874
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGGGGGGS--SRE-EIVLELAKDILE-------KLPEPFDieeaeekypvGYEDPLNTVLLQEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3875 FNAIRLVQSVHQSLAALSKVIRGTTLLSSEVQKLASALLNQKCPLAWQSKWEGPEDPL-QYLRGLVARALAIQNWVDKAE 3953
Cdd:pfam18199 74 ERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLgSWIRDLLERLKQLQDWLDDEG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3954 KQAllseTLDLSELFHPDTFLNALRQETARAVGRSVDSLKFVASWKGRLQEAKLQIK------ISGLLLEGCSFDG--NQ 4025
Cdd:pfam18199 154 PPK----VFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSPEEVTEPpedgvyVHGLFLEGARWDRknGC 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034575401 4026 LSEnQLDSPSVSSVLPCFMGWIPQDAcgPYSPDECISLPVYTSAERDR--VVTNIDVPCGGNQDQWIQCGAALFL 4098
Cdd:pfam18199 230 LVE-SEPKELFSPLPVIHLKPVESDK--KKLDENTYECPVYKTSERHStnFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
3658-3796 |
2.70e-49 |
|
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the C-terminal region of dynein heavy chain.
Pssm-ID: 465676 Cd Length: 139 Bit Score: 172.64 E-value: 2.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3658 LFSLAWFHAACQERRNYIPQGWTKFYEFSLSDLRAGYNIIDRLFDGAKD-VQWEFVHGLLENAIYGGRIDNYFDLRVLQS 3736
Cdd:pfam18198 5 LFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYDEkIPWDALRYLIGEINYGGRVTDDWDRRLLNT 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3737 YLKQFFNSSVIDvfnqrNKKSIFPYSVSLPQSCSILDYRAVIEKIPEDDKPSFFGLPANI 3796
Cdd:pfam18198 85 YLEEFFNPEVLE-----EDFKFSPSLYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2419-2605 |
1.08e-44 |
|
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This particular family is the D4 ATP-binding region of the motor.
Pssm-ID: 463701 [Multi-domain] Cd Length: 259 Bit Score: 164.32 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2419 LDILLFHEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTITSLVSHMHGAVLFSPKISRGYELKQFKNDLKHVLQLAGIE 2498
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2499 AQQVVLLLEDYQFVHPTFLEMINSLLSSGEVPGLYTLEELEPLLLPLKDQASQDGFFGP---VFNYFTYRIQQNLHIVLI 2575
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSreaVYNYFVKRCRNNLHIVLC 160
|
170 180 190
....*....|....*....|....*....|
gi 1034575401 2576 MDSANSNFMINCESNPALHKKCQVLWMEGW 2605
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEW 190
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
3524-3623 |
2.01e-39 |
|
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of dynein heavy chain. The chain also contains ATPase activity and microtubule binding ability and acts as a motor for the movement of organelles and vesicles along microtubules. Dynein is also involved in cilia and flagella movement. The dynein subunit consists of at least two heavy chains and a number of intermediate and light chains. The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This C-terminal domain carries the D6 region of the dynein motor where the P-loop has been lost in evolution but the general structure of a potential ATP binding site appears to be retained.
Pssm-ID: 460782 Cd Length: 115 Bit Score: 143.74 E-value: 2.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3524 GADPSQELQELANAERSGECYHQVAMGQGQADLAIQMLKECARNGDWLCLKNLHLVVSWLPVLEKELNTLQPK---DTFR 3600
Cdd:pfam03028 13 GSDPTADLEKLAKKLGFGGKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILEELPEEtlhPDFR 92
|
90 100
....*....|....*....|...
gi 1034575401 3601 LWLTAEVHPNFTPILLQSSLKIT 3623
Cdd:pfam03028 93 LWLTSEPSPKFPISILQNSIKIT 115
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1768-1904 |
9.54e-30 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 116.62 E-value: 9.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1768 GVVIVGPSGAGKSTLWRMLRAALCKTgkvVKQYTMNPKAMPRYQLLGHIDMDTR--EWSDGVLTNSARqvvrepqdvSSW 1845
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNR---PVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAAR---------EGE 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034575401 1846 IICDGDID---PEWIESLNSVLDDNRLLTMPSGERIQFGP-NVNFVFETHDL----SCASPATISRM 1904
Cdd:pfam07728 69 IAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMNPLdrglNELSPALRSRF 135
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
2691-3023 |
1.94e-26 |
|
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This family is the region between D4 and D5 and is the two predicted alpha-helical coiled coil segments that form the stalk supporting the ATP-sensitive microtubule binding component.
Pssm-ID: 463699 [Multi-domain] Cd Length: 344 Bit Score: 114.02 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2691 LQAGVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQMITVSMQDASEQKTELERLKHRIAEEVVKIEERKNKIDD 2770
Cdd:pfam12777 3 LENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2771 ELKEVQPLVNEAKLAVGNIKPESLSEIRSLRMPPDVIRDILEGVLRLMGIF-----DTSWVSMKSFLAK-RGVREDIATF 2844
Cdd:pfam12777 83 DLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGgkipkDKSWKAAKIMMAKvDGFLDSLIKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2845 DARNISKEIRESVEEllFKNKGSFDPKNAKRASTAAAPLAAWVKANIQYSHVLERIHP----LETEQAGLESNLKKTEDR 2920
Cdd:pfam12777 163 DKEHIHEACLKAFKP--YLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPkrqaLEEANADLAAAQEKLAAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2921 KRKLEELlnsvGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEELATLPKRAQL 3000
Cdd:pfam12777 241 KAKIAEL----NANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILL 316
|
330 340
....*....|....*....|....
gi 1034575401 3001 AAAFITYLSAAPESLRKTCLEE-W 3023
Cdd:pfam12777 317 ISAFISYLGFFTKKYRNELLDKfW 340
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
28-468 |
4.74e-25 |
|
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains to form dimers, and with intermediate chain-light chain complexes to form a basal cargo binding unit. The region featured in this family includes the sequences implicated in mediating these interactions. It is thought to be flexible and not to adopt a rigid conformation.
Pssm-ID: 462457 Cd Length: 560 Bit Score: 113.44 E-value: 4.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 28 VWRQTEHdhYPES-RMLHLLDIIGGSFGRFVQKKLGTLNLWEDPYYLVKESLKAGISICEQWVIVCNHLTGQVWQRYVPH 106
Cdd:pfam08385 128 IWSISRY--YNTSeRMTVLLEKISNQLIEQCKKYLSPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRER 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 107 PWK-NEKYFPETLDKLGKRLEEVLAIRTIHEKFLYFLPASEEKIICLTRVFEP--------FTGLNPVQYNP--YTEPLW 175
Cdd:pfam08385 206 PWDfSERYIFGRFDAFLERLEKILELFETIEQFSKLEKIGGTKGPELEGVIEEileefqeaYKVFKSKTYDIldVSNEGF 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 176 KAAVSQYEKIIAPAEQKIAGKLKNYISEIQdSPQQLLQAFLKYKELVKRPTISKELMLERETLLARLVDSIKDFRLDFEN 255
Cdd:pfam08385 286 DDDYEEFKERIKDLERRLQAFIDQAFDDAR-STESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDK 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 256 rcrgipGDASGPLSGKNLSEVVNSIVWVRQLELKVDDTIKIAEALLSDLpgfrcFHQSAKDLLD-------QLKLYEQEQ 328
Cdd:pfam08385 365 ------QKYNPSPIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLL-----KHAEGKKVIKkynelakKLDEYERLI 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 329 FDDWSRDIqsglsDSRSGLCIEASsrIMELD-SNDGLLKVHYSDRLVILLREVRQLSALGFVIPAKIQQVANIAQKFCKQ 407
Cdd:pfam08385 434 YEAWLKEV-----EEASEGNLKRP--LLVRHpETGKLLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPY 506
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034575401 408 AIILKQVAHFYNSIDQQMIQSQRPMMLQSALAFEQIIKNskagsgGKSQITWDNpKELEGY 468
Cdd:pfam08385 507 AESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEP------GLTTLTWNS-LGIDEY 560
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2078-2217 |
1.90e-20 |
|
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).
Pssm-ID: 463698 [Multi-domain] Cd Length: 179 Bit Score: 91.68 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2078 KQPFILVGPEGCGKGMLLRYAFSQL--RSTQIATVHCSAQTTSrhllqklSQTCMVISTN----TGRVYRPKDCERLVLY 2151
Cdd:pfam12775 31 GKPVLLVGPTGTGKTVIIQNLLRKLdkEKYLPLFINFSAQTTS-------NQTQDIIESKlekrRKGVYGPPGGKKLVVF 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034575401 2152 LKDINLPKLDKWGTSTLVAFLQQVLTYQGFYD-ENLEWVGLENIQIVASMS-AGGrlGRHKLTTRFTS 2217
Cdd:pfam12775 104 IDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDrKKLTFKEIVDVQFVAAMGpPGG--GRNDITPRLLR 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2680-3032 |
1.25e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2680 KKKELLKRQSHLQAGVSKLNEAKALVDELNRkageqsvlLKTKQDEadaalqmitVSMQDASEQKTELERLKHRIAEEVV 2759
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKEELER--------LKKRLTG---------LTPEKLEKELEELEKAKEEIEEEIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2760 KIEERKNKIDDELKEVQPLVNEAKLAVG---------------NIKPESLSEIRSLRMPPDVIRDILEGVLRLMgifdts 2824
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKEL------ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2825 wVSMKSFLAKRgvREDIATfdaRNISKEIRESVEELlfknkGSFDPKNAKrastaaaplaawvKANIQYSHVLERIHPLE 2904
Cdd:PRK03918 483 -RELEKVLKKE--SELIKL---KELAEQLKELEEKL-----KKYNLEELE-------------KKAEEYEKLKEKLIKLK 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2905 TEQAGLESNLKKTEDRKRKLEELLNsvgqKVSELKEkfqsrtsEAAKLEAEVSK-AQETIKAAEVLINQLDREHKRWN-- 2981
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLAELEK----KLDELEE-------ELAELLKELEElGFESVEELEERLKELEPFYNEYLel 607
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034575401 2982 ----AQVVEITEELATLPKRAQLAAAFITYLSAAPESLRKTcLEEWTKSAGLEKF 3032
Cdd:PRK03918 608 kdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE-LEELEKKYSEEEY 661
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2679-2996 |
2.48e-08 |
|
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: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2679 SKKKELLKRQshLQAGVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQmitvsmqDASEQKTELERLKHRIAEEV 2758
Cdd:TIGR02169 680 RERLEGLKRE--LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ-------EEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2759 VKIEERKNKIDDELKEVQPL---VNEAKLAVGNIKPE-SLSEIRSLRmppDVIRDILEGVLRLMGIFDtswvSMKSFLAK 2834
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELeedLHKLEEALNDLEARlSHSRIPEIQ---AELSKLEEEVSRIEARLR----EIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2835 RGVREDIAtfdarniSKEIRESVEELLfknkgsfdpknakrastaaaplaawvKANIQYSHVLERIHPLETEQAGLESNL 2914
Cdd:TIGR02169 824 LTLEKEYL-------EKEIQELQEQRI--------------------------DLKEQIKSIEKEIENLNGKKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2915 KKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIK----AAEVLINQLDrEHKRWNAQVVEITEE 2990
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSelkaKLEALEEELS-EIEDPKGEDEEIPEE 949
|
....*.
gi 1034575401 2991 LATLPK 2996
Cdd:TIGR02169 950 ELSLED 955
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2886-3003 |
2.88e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2886 WVKANIQYSHVLERIHPLETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKA 2965
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110
....*....|....*....|....*....|....*...
gi 1034575401 2966 AEVLINQLDREHKRWNAQVVEITEELATLpkRAQLAAA 3003
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEEL--EEELEEA 349
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2680-3001 |
3.88e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2680 KKKELLKRQSHLQagvSKLNEAKALVDELNRKAGEqsvllKTKQDEADAALQMitvsmQDASEQKTELERLKhriAEEVV 2759
Cdd:PTZ00121 1477 KKAEEAKKADEAK---KKAEEAKKKADEAKKAAEA-----KKKADEAKKAEEA-----KKADEAKKAEEAKK---ADEAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2760 KIEERKNKidDELKEVQPLVN-EAKLAVGNIKPESLSEIRSLRMPpDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVR 2838
Cdd:PTZ00121 1541 KAEEKKKA--DELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2839 EDIATFDARNiSKEIRESVEELlfKNKGSFDPKNA----KRASTAAAPLAAWVKANIQYSHVLERIHPLETEQAGLESNL 2914
Cdd:PTZ00121 1618 AKIKAEELKK-AEEEKKKVEQL--KKKEAEEKKKAeelkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2915 KKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLinQLDREHKRWNAQVVEITEELATL 2994
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEE 1772
|
....*..
gi 1034575401 2995 PKRAQLA 3001
Cdd:PTZ00121 1773 IRKEKEA 1779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2684-2994 |
2.02e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2684 LLKRQSHLQAGVSKLNEAKALVD----ELNRKAGEQSVLLKTKQDEADAALQMITVSMQDASEQKTELERLKHRIAEEVV 2759
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEerleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2760 KIEERKNKIDDELKEVQPLVNEAKLAVGNIkpESLS-EIRSLRMPPDVIRDILEGVLRLMGifdtswvSMKSFLAKRGVR 2838
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDI--ESLAaEIEELEELIEELESELEALLNERA-------SLEEALALLRSE 895
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2839 EDIATFDARNISKEIRESVEELlfknkgsfDPKNAKRASTAAAplaaWVKANIQYSHVLERI--------HPLETEQAGL 2910
Cdd:TIGR02168 896 LEELSEELRELESKRSELRREL--------EELREKLAQLELR----LEGLEVRIDNLQERLseeysltlEEAEALENKI 963
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2911 ESNLKKTEDRKRKLEELLNSVG-------QKVSELKEKFQSRTSEAAKLEAEVSKAQETikaaevlINQLDRE-HKRWNA 2982
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKELGpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEA-------IEEIDREaRERFKD 1036
|
330
....*....|..
gi 1034575401 2983 QVVEITEELATL 2994
Cdd:TIGR02168 1037 TFDQVNENFQRV 1048
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2678-2990 |
2.39e-05 |
|
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: 50.84 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2678 SSKKKELLKRQSHLQAGVSKLNEAKALVDELNRK----AGEQSVLLKTKQDEADAALQMItVSMQDASEQktELERLkhr 2753
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlGEEEQLRVKEKIGELEAEIASL-ERSIAEKER--ELEDA--- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2754 iAEEVVKIEERKNKIDDELKEVqplvnEAKLAVGNIKPESLSEIrslrmppdvirdilegvlrlmgifdtswvsmksFLA 2833
Cdd:TIGR02169 321 -EERLAKLEAEIDKLLAEIEEL-----EREIEEERKRRDKLTEE---------------------------------YAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2834 KRGVREDIATfDARNISKEIRESVEELlfknkgsfdpKNAKRASTAAAPLAAWVKANIqySHVLERIHPLETEQAGLESN 2913
Cdd:TIGR02169 362 LKEELEDLRA-ELEEVDKEFAETRDEL----------KDYREKLEKLKREINELKREL--DRLQEELQRLSEELADLNAA 428
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034575401 2914 LKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEE 2990
Cdd:TIGR02169 429 IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
2903-2990 |
3.03e-05 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 46.24 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2903 LETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSR---TSEAAKLEAEVSKAQETIKAAE-------VLINQ 2972
Cdd:pfam04871 6 LESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELEAEVkklEEALKKLKAELSEEKQKEKEKQselddllLLLGD 85
|
90
....*....|....*...
gi 1034575401 2973 LDREHKRWNAQVVEITEE 2990
Cdd:pfam04871 86 LEEKVEKYKARLKELGEE 103
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2674-3017 |
5.50e-05 |
|
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: 49.68 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2674 SAISSSKKKELLKRQSHLQAGVSKLNEAKALVDELnRKAgEQSVLLKTKQDeADAALQMITVSMQDASEQKTELERLKHR 2753
Cdd:TIGR02169 186 IERLDLIIDEKRQQLERLRREREKAERYQALLKEK-REY-EGYELLKEKEA-LERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2754 IAEEVVKIEerknkidDELKE----VQPLVNEAKLAVGNIKPESLSEIRSLRmppDVIRDILEGVLRLMGIFDTSWVSMK 2829
Cdd:TIGR02169 263 LEKRLEEIE-------QLLEElnkkIKDLGEEEQLRVKEKIGELEAEIASLE---RSIAEKERELEDAEERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2830 SFLAK-RGVREDIATFDAR--NISKEI--RESVEELLFKNKGSFDPKNAkrastaaaplaAWVKANIQYSHVLE----RI 2900
Cdd:TIGR02169 333 KLLAEiEELEREIEEERKRrdKLTEEYaeLKEELEDLRAELEEVDKEFA-----------ETRDELKDYREKLEklkrEI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2901 HPLETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRW 2980
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350
....*....|....*....|....*....|....*..
gi 1034575401 2981 NAQVVEITEELATLPKRAQLAAAFITYLSAAPESLRK 3017
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2903-3122 |
7.67e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2903 LETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNA 2982
Cdd:COG4372 78 LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2983 QVVEITEELATLPK------RAQLAAAFITYLSAAPESLRKTCLEEWTKSAGLEKFDLRRF-----LCTESEQLIWKSEG 3051
Cdd:COG4372 158 QLESLQEELAALEQelqalsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEelleaKDSLEAKLGLALSA 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034575401 3052 LpSDDLSIENALVILQSRVCPFLIDPSSQATEWLKTHLKDSRLEVINQQDSNFITALELAVRFGKTLIIQE 3122
Cdd:COG4372 238 L-LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1722-1793 |
9.75e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.88 E-value: 9.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034575401 1722 GIELKEVEydelsaalKQVFEEANYEIIPNQIkkalelyeqlcqrmgVVIVGPSGAGKSTLWRMLRAALCKT 1793
Cdd:COG2401 35 GVELRVVE--------RYVLRDLNLEIEPGEI---------------VLIVGASGSGKSTLLRLLAGALKGT 83
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2679-3050 |
1.16e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2679 SKKKELLKRQSHLQAGVSKLNEAKA-LVDELNRKAGEQSVLLKtKQDEADAALQMITVSMQDASEQKTELERLKHRIAEE 2757
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDdLLAEAGLDDADAEAVEA-RREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2758 VVKIEERKNKIDDELKEVQPLVNEAKLAVGNIKpESLSEIRslrmppDVIRDILEGVlrlmGIFDTSWVSMKSFLA---- 2833
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRR-EEIEELE------EEIEELRERF----GDAPVDLGNAEDFLEelre 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2834 -KRGVREDIATFDA--RNISKEIRESvEELLFKNK---------GS-----FDPKNAKRASTAAAPLaawvKANIQYSHV 2896
Cdd:PRK02224 420 eRDELREREAELEAtlRTARERVEEA-EALLEAGKcpecgqpveGSphvetIEEDRERVEELEAELE----DLEEEVEEV 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2897 LERIHPLEtEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDRE 2976
Cdd:PRK02224 495 EERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034575401 2977 HKRWNAQVVEITEELATLPKRAQLAAAfITYLSAAPESLRKTcLEEWTksaglEKFDLRRflctesEQLIWKSE 3050
Cdd:PRK02224 574 VAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLREK-REALA-----ELNDERR------ERLAEKRE 634
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2682-3003 |
1.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2682 KELLKRQSHLQAGVSKLNEAKALVDELNRKAGEQSVL---LKTKQDEADAALQMITVS----MQDASEQKTELERLKHRI 2754
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELeaeLAELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2755 AEEVVKIEERKNKIDDELKEVQPLV----NEAKLAVGNIKPESLSEIRSLRMPPDVIRDILEGVLRLMGIFD--TSWVSM 2828
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELeaaaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLglLALLFL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2829 KSFLAKRGVREDIATFDARNISKEIRESVEELLFKNKGSFDPKNAKRASTAAAPLAAWVKANIQYSHVLER--IHPLETE 2906
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElqLEELEQE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2907 QAGL--------ESNLKKTEDRKRKLEELLnsvgQKVSELKEKFQSRTSEAAKLEAEVSKAQ--ETIKAAEVLINQLDRE 2976
Cdd:COG4717 372 IAALlaeagvedEEELRAALEQAEEYQELK----EELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEE 447
|
330 340
....*....|....*....|....*..
gi 1034575401 2977 HKRWNAQVVEITEELATLPKRAQLAAA 3003
Cdd:COG4717 448 LEELREELAELEAELEQLEEDGELAEL 474
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2668-2967 |
1.56e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2668 TFLHVYSAISSSKKKELLKRQshLQAGVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQMITVSMQDASEQKTEL 2747
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAE--LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2748 ERLKHRIAEEVVKIEERKNKIDDELKEVQPLVNEAKLAVGnIKPESLSE-IRSLRMppdvirdilegvlrlmgifdtswv 2826
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALL-LSPEDFLDaVRRLQY------------------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2827 sMKSFLAKRgvrediatfdaRNISKEIRESVEELlfknkgsfdpkNAKRAStaaaplaawvkaniqyshvlerihpLETE 2906
Cdd:COG4942 141 -LKYLAPAR-----------REQAEELRADLAEL-----------AALRAE-------------------------LEAE 172
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034575401 2907 QAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAE 2967
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2904-2984 |
1.77e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2904 ETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQ 2983
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
.
gi 1034575401 2984 V 2984
Cdd:COG3883 95 L 95
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
2903-2967 |
2.62e-04 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 44.96 E-value: 2.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034575401 2903 LETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSEL-------KEKFQSRTSEAAKLEAEVSKAQETIKAAE 2967
Cdd:pfam05266 107 LLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELerqlalaKEKKEAADKEIARLKSEAEKLEQEIQDVE 178
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2892-3002 |
2.73e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2892 QYSHVLERIHPLETEQAGLESNLKKTEDRKRKLEELLNSVG---------QKVSELKEKFQSRTSEAAKLEAEVSKAQET 2962
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealqKEIESLKRRISDLEDEILELMERIEELEEE 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1034575401 2963 IKAAEVLIN----QLDREHKRWNAQVVEITEELATLP-KRAQLAA 3002
Cdd:COG1579 126 LAELEAELAeleaELEEKKAELDEELAELEAELEELEaEREELAA 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2738-2995 |
2.97e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2738 QDASEQKTELERLKHRIAEEVVKIEERKNKIDDELKEVQPLvnEAKLAvgnikpESLSEIRSLRMPPDVIRDILEGVLRL 2817
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--ERRIA------ALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2818 MGIFDTSWVSMKSFLAKRgvrediatfdARNISKEIRESVEELLFKNKgsfDPKNAKRASTaaaplaaWVKANIQYshVL 2897
Cdd:COG4942 92 IAELRAELEAQKEELAEL----------LRALYRLGRQPPLALLLSPE---DFLDAVRRLQ-------YLKYLAPA--RR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2898 ERIHPLETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREH 2977
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|....*...
gi 1034575401 2978 KRWNAQVVEITEELATLP 2995
Cdd:COG4942 230 ARLEAEAAAAAERTPAAG 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2680-3295 |
3.03e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2680 KKKELLKRQSHLQAGVSKLNEAKALVDELNRKAGEQSVLLKTKQDEADAALQMITVSMQDASEQKTELERLKHRIAEEVV 2759
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2760 KIEERKNKIDDELKEVQPLVNEAKlavgnikpESLSEIRSLRmppdvirdilegvlrlmgifdtswvsmksflakrgvre 2839
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAE--------AELAEAEEAL-------------------------------------- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2840 diatfdaRNISKEIRESVEEllfknkgsfdpknakrastaaaplaaWVKANIQYSHVLERIHPLETEQAGLESNLKKTED 2919
Cdd:COG1196 368 -------LEAEAELAEAEEE--------------------------LEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2920 RKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEELATLPKRAQ 2999
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3000 LAAAFITYLSAAPESLRKtcleewtksagLEKFDLRRFLCTESEQLIWkseglpsDDLSIENALVILQSRVCPFLIDPSS 3079
Cdd:COG1196 495 LLLEAEADYEGFLEGVKA-----------ALLLAGLRGLAGAVAVLIG-------VEAAYEAALEAALAAALQNIVVEDD 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3080 QATEWLKTHLKDSRLEVINQQDSNFITALELAVRfgKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEE 3159
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA--ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3160 FRLFLSTRNPNPFIppdAASIVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLAKLEESLLETLA 3239
Cdd:COG1196 635 ALRRAVTLAGRLRE---VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034575401 3240 TSQGNILENKDLIESLNQTKASSALIQESLKESYKLQISLDQERDAYLPLAESASK 3295
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2837-3096 |
6.82e-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: 45.83 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2837 VREDIATFDArnISKEIRESVEELLF-KNKGS--FDPKNAKRASTAAAPLAAWVKANIQYSHVLERIHPLETEQAGLESN 2913
Cdd:TIGR02169 182 VEENIERLDL--IIDEKRQQLERLRReREKAEryQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2914 LKKTEDRKRKLEELLNSVGQKVSEL--------KEKFQSRTSEAAK--------------LEAEVSKAQETIKAAEVLIN 2971
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASlersiaekereledAEERLAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2972 QLDREHKRWNAQVVEITEELATLPKRAQLAAAFITYLSAAPESLRKTCLEEWTKSAGL--EKFDLRRflctESEQLIWKS 3049
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLkrEINELKR----ELDRLQEEL 415
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034575401 3050 EGLPSDDLSIENALVILQSRVcpflidpssqaTEwLKTHLKDSRLEV 3096
Cdd:TIGR02169 416 QRLSEELADLNAAIAGIEAKI-----------NE-LEEEKEDKALEI 450
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1483-1606 |
1.18e-03 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 41.89 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1483 GPAGTGKTESVKALGGLL-GRQVLVFNCDE---------GIDVKSMGRIFVGLV-----KCGAWGCFDEFNRLEESVLSA 1547
Cdd:pfam07728 6 GPPGTGKTELAERLAAALsNRPVFYVQLTRdtteedlfgRRNIDPGGASWVDGPlvraaREGEIAVLDEINRANPDVLNS 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1548 VSMQIQTiqdalkNHRTVCElLGKEVEVNSNSGIFI-TMNPAGKgygGRQKLPDNLKQLF 1606
Cdd:pfam07728 86 LLSLLDE------RRLLLPD-GGELVKAAPDGFRLIaTMNPLDR---GLNELSPALRSRF 135
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2903-3148 |
1.58e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2903 LETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNA 2982
Cdd:COG4372 57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2983 QVVEITEELATLPKRAQLAAAFITYLSAAPESLRKTCLEEWTKSAGLEKFDLRRFLCTESEQLIWKSEGLPSDDLSIENA 3062
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 3063 LVILQSRVCPFLIDPSSQATEWLKTHLKDSRLEVINQQDSNFITALELAVRFGKTLIIQEMDGVEPVLYPLLRRDLVAQG 3142
Cdd:COG4372 217 AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELK 296
|
....*.
gi 1034575401 3143 PRYVVQ 3148
Cdd:COG4372 297 LLALLL 302
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2914-3017 |
1.91e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2914 LKKTEDRKRKLEELLNSVGQKVSELKEKfqsrtseAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEELAT 2993
Cdd:COG3883 135 LEELKADKAELEAKKAELEAKLAELEAL-------KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
90 100
....*....|....*....|....
gi 1034575401 2994 LPKRAQLAAAFITYLSAAPESLRK 3017
Cdd:COG3883 208 AEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1482-1522 |
2.71e-03 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 41.50 E-value: 2.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1034575401 1482 YGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDV------KSMGRIF 1522
Cdd:cd19481 32 YGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKyvgeseKNLRKIF 78
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2915-3002 |
2.99e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2915 KKTEDRKRKLEEL---LNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVVEITEEL 2991
Cdd:COG4942 20 DAAAEAEAELEQLqqeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90
....*....|.
gi 1034575401 2992 ATLpkRAQLAA 3002
Cdd:COG4942 100 EAQ--KEELAE 108
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1482-1565 |
3.01e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 41.36 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 1482 YGPAGTGKTESVKALGGLLGRQ---VLVFNC--------DEGIDVKSMGRIFVGLVKCGAWGC--FDEFNRLEESVLSAV 1548
Cdd:cd00009 25 YGPPGTGKTTLARAIANELFRPgapFLYLNAsdlleglvVAELFGHFLVRLLFELAEKAKPGVlfIDEIDSLSRGAQNAL 104
|
90
....*....|....*..
gi 1034575401 1549 SMQIQTIQDALKNHRTV 1565
Cdd:cd00009 105 LRVLETLNDLRIDRENV 121
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2740-2997 |
3.15e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2740 ASEQKTELERLKHRIAEEVvkieERKNKIDDELKEvqplvNEAKLAvgnikpESLSEIRSLRMPPDVIRDILEGVLRLMG 2819
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFI----KRTENIEELIKE-----KEKELE------EVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2820 IFDTSWVSMKSF-LAKRGVREDIATFDARniSKEIRESVEELlfKNKGSFDPKNAKRastaaaplaawvkaniqyshvLE 2898
Cdd:PRK03918 232 ELEELKEEIEELeKELESLEGSKRKLEEK--IRELEERIEEL--KKEIEELEEKVKE---------------------LK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2899 RIHPLETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFqsrtSEAAKLEAEVSKAQETIKAAEVLINQLDREHK 2978
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHE 362
|
250
....*....|....*....
gi 1034575401 2979 RWNaQVVEITEELATLPKR 2997
Cdd:PRK03918 363 LYE-EAKAKKEELERLKKR 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2899-2999 |
3.32e-03 |
|
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: 43.89 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2899 RIHPLETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHK 2978
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
90 100
....*....|....*....|.
gi 1034575401 2979 RWNAQVVEITEELATLPKRAQ 2999
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAA 820
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2898-3022 |
3.75e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2898 ERIHPLETEQAGLESNLKKTEDRKRKLEELLnsvgQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREH 2977
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETR----DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEV 281
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034575401 2978 KRWNAQVVEITEELATLPKRAQLAAAFITYLSAAPESL--RKTCLEE 3022
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELedRDEELRD 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2906-3004 |
3.84e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2906 EQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLINQLDREHKRWNAQVV 2985
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90
....*....|....*....
gi 1034575401 2986 EITEELAtlpkrAQLAAAF 3004
Cdd:COG4942 101 AQKEELA-----ELLRALY 114
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1769-1785 |
4.60e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.52 E-value: 4.60e-03
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2898-2997 |
4.81e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034575401 2898 ERIHPLETEQAGLESNLKKTEDRKRKLEELLNSVGQKVSELKEKFQSRTSEAA----KLEAEVSKAQETIKAAEVLINQL 2973
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAalleALEEELEALEEALAEAEAALRDL 417
|
90 100
....*....|....*....|....
gi 1034575401 2974 DREHKrwnaqvvEITEELATLPKR 2997
Cdd:COG4913 418 RRELR-------ELEAEIASLERR 434
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1769-1786 |
4.95e-03 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 42.37 E-value: 4.95e-03
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1769-1797 |
9.23e-03 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 40.88 E-value: 9.23e-03
10 20 30
....*....|....*....|....*....|
gi 1034575401 1769 VVIVGPSGAGKSTLWRML-RAALCKTGKVV 1797
Cdd:COG4778 40 VALTGPSGAGKSTLLKCIyGNYLPDSGSIL 69
|
|
| |
