|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1009-4315 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 1161.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1009 TYRNLLTKLPEGkilENAYGAIEQKVSEVRNYVDEWLRYQSLWDLQADMLYGRLGEDVNLWIKCLNDIKQSRTTFDTSDT 1088
Cdd:COG5245 146 LSHELELIFRSG---EQWVGCMRKLYESVCSERDGFYEEKSFWSRFHMEMCHIREFCRSKAFRFACDVLRKSGKYVTVAT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1089 RRAY-GPIIIDYAKVQAKVTLKYDSWhkealgkfGTLLGTEMTSFHSKVSKSRTDLEmQSIEAASTSDAVSFITYVQSL- 1166
Cdd:COG5245 223 LDSLlSSSKYSELGRRLHFYANMDFS--------GIYFPKSFSEFKDSVISATQAVS-RDIGRQSRMARRLILVQMDSLa 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1167 --KKDMIAWDKQVEVFREAQRILERQRFQFPNTWLHVDNIEGEWSAFNEIIKRkDTAIQTQVASLqAKIVAEDKAVETRT 1244
Cdd:COG5245 294 rlIVDRICEYVSIEWLGCCEELLTCSMESMSSLVNSFDGEESEAMSLESSLFY-EFRGGEHLAGF-YSAFGDIKRILLFT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1245 VDFLNDWEKtKPTGGKIRPDDALQQLQIFESKYSRLKEERDNVVKAKEALelqesAVPNNSAERMNVALEELQDLRGVWS 1324
Cdd:COG5245 372 WSFKKLGTL-LPSLPGYSSGGMDYGEEYRSLLWELGSEVGDPDSGPVRKW-----MRKDLFDAKVRSGVSFGKQEEFVSD 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1325 ELSKVWTQIDETREKPWLSVQprkLRQQLEAMMAQLKELPaRLRMYESYEYVKKLIQSYIKVNMLIVELKSDALKerHWK 1404
Cdd:COG5245 446 IFNITFERIHGMDPTTLEDDE---EDTPALAILLGQEEAG-RFVKLCKIMRMFSFFNSLEMFSRRTLANRMAIVK--YLS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1405 QLTK----QLRVNWVLS-DLSLGQVWDVNLQKNEgivkdIILVAQGEMA--LEEFLKQVRESWQNYELDlinyqnkcRII 1477
Cdd:COG5245 520 SVVRtgplFLQRDFFGRmSELLMARDMFMEVDGV-----LRLFFGGEWSgiVQLSGIRRAKRCVERQID--------DEI 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1478 RGWddlfnkVKEHINSVAAMKLSPYYkvfeEEALTWEEKLNRINAlfdvwIDVqRRWVYLEGIFSGSADIKTLLPVETSR 1557
Cdd:COG5245 587 REW------CSSVLSDDFLEERAVRV----ERGADGARRLRASSG-----SPV-LRRLDEYLMMMSLEDLMPLIPHAVHR 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1558 FQSISSEFLGLMKKVTKSPKVMDVLNIPaVQRSLERLADLLGKIQKALGEYLERERTSFPRFyfVGDEDLLEIIGNSKNI 1637
Cdd:COG5245 651 KMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRVRELENR 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1638 ARLQKHFKKMFAGVAAILLNEenNVILGISSREGEEVHFMNPVSTVEHPKINEWLSLvekqmrfTLASLLAQAVQDIKQF 1717
Cdd:COG5245 728 VYSYRFFVKKIAKEEMKTVFS--SRIQKKEPFSLDSEAYVGFFRLYEKSIVIRGINR-------SMGRVLSQYLESVQEA 798
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1718 RDGKiDPQAYMEwcdKYQAQIVVLAAQiLWSEDVESALQQASennqSKPMQRVLGNVESTLNVLADSVLqeqpplrrRKL 1797
Cdd:COG5245 799 LEIE-DGSFFVS---RHRVRDGGLEKG-RGCDAWENCFDPPL----SEYFRILEKIFPSEEGYFFDEVL--------KRL 861
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1798 EHLINEFVHKRTVTRRLLNNGVTSPKSFQWLCEMRFYfdprqTEVLQQLTIHMANARFFYGFEYLGVQDRLVQTPLTDRC 1877
Cdd:COG5245 862 DPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-----QGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQ 936
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1878 YLTMTQALESRLggSPFgpAGTGKTESVKALGNQLGRFVlvfncdETFDFQAmgRIFVGLCQVGAWGcFDEFNRLEERML 1957
Cdd:COG5245 937 HQKLFEAVCDEV--CRF--VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR 1003
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1958 sACSQQIQTIQEALKYemdsNKESITveLVGKQVRVSPDMAIFITMNPgyagRSNLPDNLKKLFRSLAMTTPDRQlIAEV 2037
Cdd:COG5245 1004 -TILVDEYLNSDEFRM----LEELNS--AVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGA-IKSR 1071
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2038 MlfsqgfrsaEKLACKIVPFFKLCDEQLSNQSHYDFglRALKSVLisagnvkrdrimKIKEQMKQRGDENIDEASVAENL 2117
Cdd:COG5245 1072 R---------ESLDREIGAFNNEVDGIAREEDELMF--YPMFKSL------------KAKHRMLEEKTEYLNKILSITGL 1128
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2118 PeqeiliqsvcetmvpklvaedipllfsLLSDVFpnvgytRAEMKGLKEEIRKVCQEDYLVCGEGDEQGAAW-MEKVLQL 2196
Cdd:COG5245 1129 P---------------------------LISDTL------RERIDTLDAEWDSFCRISESLKKYESQQVSGLdVAQFVSF 1175
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2197 YQISNLNHGLMMVGPSGSGKSTAWKTLLKalerFEGVEGVAHVIDPkaiskealygVLDPnTREWTdGLFTHILRkiiDN 2276
Cdd:COG5245 1176 LRSVDTGAFHAEYFRVFLCKIKHYTDACD----YLWHVKSPYVKKK----------YFDA-DMELR-QFFLMFNR---ED 1236
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2277 VRGEI-NKRQWIIFDgdvdpEWVENLNSVLDDNKLLTLPNGERlslppnvRVMFEVQDlkfATLATVSRCGMVWFSEDVL 2355
Cdd:COG5245 1237 MEARLaDSKMEYEVE-----RYVEKTKAEVSSLKLELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRL 1301
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2356 STEMIFENYLSRLRsipledgdedfvgviKPAKDKEEEVSPSLQVQRDIALLLLPFFSAdgivvrTLEYAMDQEHIMD-- 2433
Cdd:COG5245 1302 STKGVFLDELGDTK---------------RYLDECLDFFSCFEEVQKEIDELSMVFCAD------ALRFSADLYHIVKer 1360
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2434 -----FTRLRALSSLFSMLNQAARNVltfnaqhpdfpcSADQLEHYIPKALVYSVLWSFAGDAKLKVRIDLGDFVRSVTT 2508
Cdd:COG5245 1361 rfsgvLAGSDASESLGGKSIELAAIL------------EHKDLIVEMKRGINDVLKLRIFGDKCRESTPRFYLISDGDLI 1428
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2509 VPLPGaagapIIDYE------VNMSGDWVPWSnKVPVIEVETHKVASP-DIVVPTLDTVRHESLLYTWLAEHKPLVLCGP 2581
Cdd:COG5245 1429 KDLNE-----RSDYEemlimmFNISAVITNNG-SIAGFELRGERVMLRkEVVIPTSDTGFVDSFSNEALNTLRSYIYCGP 1502
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2582 PGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRKTPNGVVLSPVQIGKWLVLFCDEINLPDMDSYGT 2661
Cdd:COG5245 1503 PGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYP 1582
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2662 QRVISFLRQLVEHKGFYRASDQAWVSLERIQFVGACNPPTDPGRKPLSHRFLRHVPIIYVDYPGETSLKQIYGTFSRAML 2741
Cdd:COG5245 1583 PTVIVFLRPLVERQGFWSSIAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSY 1662
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2742 RLMPALRGYAEPLTNAMVEFYLASQDRFTQDMQPHYVYSPREMTRWVRGICEAIRPLDSLPVEGLVRLWAHEALRLFQDR 2821
Cdd:COG5245 1663 LCFDEFNRLSEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDVSLIIDWYCEAIREKIDR 1742
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2822 LVDDSERRWTNENIDLVGQKHFPGINQEEALQRPILYSNWLSKDYMPVNREELREYVHARLKVFYEEELDVPLVLFDEVL 2901
Cdd:COG5245 1743 LVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFGMACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDAL 1822
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2902 DHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSIFQIKVHNKYTSEDFDEDLRCVLRRSGCKDEKIAFILDE 2981
Cdd:COG5245 1823 LHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFE 1902
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2982 SNVLDSGFLERMNTLLANGEVPGLFEGDEYTTLMTQCKEGAQREGLMLDSSDELYKWFTQQVMRNLHVVFTMNPSTDGLK 3061
Cdd:COG5245 1903 SIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEKDTEATLTRVFLVYMEENLPVVFSACCSQDTSV 1982
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3062 DRAATSPALFNRCVLNWFGDWSDSALFQVGKEFTTrvdLEKPNWHAPDFFPSVCPLVPANpTHRDAVINSCVYvhqtlHQ 3141
Cdd:COG5245 1983 LAGIRSPALKNRCFIDFKKLWDTEEMSQYANSVET---LSRDGGRVFFINGELGVGKGAL-ISEVFGDDAVVI-----EG 2053
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3142 ANARLAKRGGrTMAVTPRHYLDFIHHFVKLYNEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAA 3221
Cdd:COG5245 2054 RGFEISMIEG-SLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNA 2132
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3222 NAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRKYVMADLAQVEPAVIDAQAAVSSIKKKHLAEVRSMANPPAV 3301
Cdd:COG5245 2133 DDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGD 2212
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3302 VKLALESVCELLNESATDWKAIRGILVKDSFISSIVNLETDKITD-DVREKMKSKYLSNPDYNFEKVNRASMACGPMVKW 3380
Cdd:COG5245 2213 LCIEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPDEIEFDlEARRFREARECSDPSFTGSILNRASKACGPLKRW 2292
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3381 AIAQIEYADMLKRVEPLREELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRS 3460
Cdd:COG5245 2293 LVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRS 2372
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3461 IALLKSLNIERERWESTSETFKSQMSTIIGDVLLSAAFIAYGGYFDQHYRLNLFTTwSQHLQAASIQYRADIART--EYL 3538
Cdd:COG5245 2373 IFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIRRRQfiTEG 2451
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3539 SNPDERLRWQANalpTDDLCTENA-IMLKRFNRYPLIIDPSGQATTFLLNEYAGKKITKTSFLDDSFRKNLESALRFGNP 3617
Cdd:COG5245 2452 VQKIEDFKEEAC---STDYGLENSrIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSD 2528
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3618 LLVQDVENYDPILNPVLNRELRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDICSRVTFVNFTVTRSSLQSQC 3697
Cdd:COG5245 2529 KIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEI 2608
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3698 LNQVLKAERPDIDEKRSDLLKLQGEFRLRLRQLEKSLLQALNDAKGKILDDDSVITTLETLKKEAYDINQKVDETDKVIA 3777
Cdd:COG5245 2609 PDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIED 2688
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3778 EIETVSQQYlPLSVACS-NIYFTMDSLNQVHFLYQYSLKMFLDIFSTVLyNNPKLEGRTdhserLGIVTRDLFQVCYERV 3856
Cdd:COG5245 2689 RIDALKSEY-NASVKRLeSIRVEIAMFDEKALMYNKSICELSSEFEKWR-RMKSKYLCA-----IRYMLMSSEWILDHED 2761
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3857 ARGMIHIDRLTFALLM-----CKIHLKGTSESNLDAEFNFFlrsregllanptpveGLSAEQIESVNRLALRLpifrkll 3931
Cdd:COG5245 2762 RSGFIHRLDVSFLLRTkrfvsTLLEDKNYRQVLSSCSLYGN---------------DVISHSCDRFDRDVYRA------- 2819
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3932 ekvrsipelgawlqqsspeqvvpqlwdeSKALSPIASSVHQLLLIQAFRPDRviaaaHNVVNTVLGEDF-MPNAEQELDF 4010
Cdd:COG5245 2820 ----------------------------LKHQMDNRTHSTILTSNSKTNPYK-----EYTYNDSWAEAFeVEDSGDLYKF 2866
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 4011 TSVVDKQLNCNTPALlcsvpgfdasgrvddLAAEQNKQISSI--AIGSAEGFNQAERAINMACKTGRWVLLKNVHLAPQW 4088
Cdd:COG5245 2867 EEGLLELIVGHAPLI---------------YAHKKSLENERNvdRLGSKENEVYAVLNSLFSRKEKSWFEVYNISLSFGW 2931
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 4089 LVQLEKKM----HSLQPHSGFRLFLT-MEINPKVPVNLLRAGRIFVFEPPPGIRANLLRTFSTVPAarMMK-TPSERARL 4162
Cdd:COG5245 2932 FKRYVEDVvypiKASRVCGKVKNMWTsMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLVEIDRY--PFDyTLVIACDD 3009
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 4163 YFLLAWFHAIVQERLRYVPLGWAKKYEFNESDLRVACDTLDtwiDTTAMGRTNlppeKVPWDALVTLLSQSIYGGKIDND 4242
Cdd:COG5245 3010 AFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLK---NILFLNHLN----ARKWGNNRDLIFTIVYGKKHSLM 3082
|
3290 3300 3310 3320 3330 3340 3350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221330856 4243 FDQRLLTSFLKKLFTArsfEADFALVANVDGASGGLRHITMPDGTRRDHFLKwIENLTDRQTPSWLGLPNNAE 4315
Cdd:COG5245 3083 EDSKVVDKYCRGYGAH---ETSSQILASVPGGDPELVKFHMEEMCRSSAFGV-IGQLPDLALCAWLMGPCDSE 3151
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1857-2217 |
3.13e-168 |
|
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: 522.04 E-value: 3.13e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1857 YGFEYLGVQDRLVQTPLTDRCYLTMTQALESRLGGSPFGPAGTGKTESVKALGNQLGRFVLVFNCDETFDFQAMGRIFVG 1936
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1937 LCQVGAWGCFDEFNRLEERMLSACSQQIQTIQEALKyemdSNKESITVElvGKQVRVSPDMAIFITMNPGYAGRSNLPDN 2016
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALA----ANLKTFVFE--GSEIKLNPSCGIFITMNPGYAGRTELPDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2017 LKKLFRSLAMTTPDRQLIAEVMLFSQGFRSAEKLACKIVPFFKLCDEQLSNQSHYDFGLRALKSVLISAGNVKRDRimki 2096
Cdd:pfam12774 155 LKALFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSN---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2097 keqmkqrgdenideasvaENLPEQEILIQSVCETMVPKLVAEDIPLLFSLLSDVFPNVGYTRAEMKGLKEEIRKVCQEDY 2176
Cdd:pfam12774 231 ------------------PNLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELG 292
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 221330856 2177 LVCGEgdeqgaAWMEKVLQLYQISNLNHGLMMVGPSGSGKS 2217
Cdd:pfam12774 293 LQPHD------AFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1309-1710 |
1.03e-142 |
|
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: 452.10 E-value: 1.03e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1309 MNVALEELQDLRGVWSELSKVWTQIDETREKPWLSVQPRKLRQQLEAMMAQLKELPARLRMYESYEYVKKLIQSYIKVNM 1388
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1389 LIVELKSDALKERHWKQLTKQLRVNW--VLSDLSLGQVWDVNLQKNEGIVKDIILVAQGEMALEEFLKQVRESWQNYELD 1466
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFdpLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1467 LINYQN-KCRIIRGWDDLFNKVKEHINSVAAMKLSPYYKVFEEEALTWEEKLNRINALFDVWIDVQRRWVYLEGIFSGSa 1545
Cdd:pfam08393 161 LVPYKDtGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSSE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1546 DIKTLLPVETSRFQSISSEFLGLMKKVTKSPKVMDVLNIPAVQRSLERLADLLGKIQKALGEYLERERTSFPRFYFVGDE 1625
Cdd:pfam08393 240 DIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSND 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1626 DLLEIIGNSKNIARLQKHFKKMFAGVAAILLNeENNVILGISSREGEEVHFMNPVSTVEhPKINEWLSLVEKQMRFTLAS 1705
Cdd:pfam08393 320 ELLEILSQTKDPTRVQPHLKKCFEGIASLEFD-ENKEITGMISKEGEVVPFSKPPVEAK-GNVEEWLNELEEEMRETLRD 397
|
....*
gi 221330856 1706 LLAQA 1710
Cdd:pfam08393 398 LLKEA 402
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
242-826 |
1.38e-133 |
|
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: 432.39 E-value: 1.38e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 242 LNLLQNGVNRWIAEIKKVTKLNRDPGSGTALQEISFWLNLERALYRIQEKRESPEVALTLDILKHGKRFHATVSFDTDTG 321
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKALDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 322 LKQALATVADYNPLMKDF--PINDLLSATELEKIRPAVQQIFAHLRKV-RNTKY--PIQRCLKLIEAISRDLSQQLLKVL 396
Cdd:pfam08385 81 LTDALNEAKDNVKYLKTLerPFEDLEELTDPPEIIEAIPPLMNTIRLIwSISRYynTSERMTVLLEKISNQLIEQCKKYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 397 GTRRLMHIPFDEFERVMNQCFEIFSCWDDEYDKLQGLLRDIVKKKRdehlkmvWRVSPAHK-----KLQTRMEHMRKFRR 471
Cdd:pfam08385 161 SPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERP-------WDFSERYIfgrfdAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 472 QHEQLRTviLRVLRPTKpavgddGNVVETKQpysldaadANAIEEVNLAYENVKEV--DCLDITKEGseaWEAAVKRYEE 549
Cdd:pfam08385 234 TIEQFSK--LEKIGGTK------GPELEGVI--------EEILEEFQEAYKVFKSKtyDILDVSNEG---FDDDYEEFKE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 550 KIDRVETRITAHLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIEALHEKFKVQypqsKSCRL 629
Cdd:pfam08385 295 RIKDLERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQ----KYNPS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 630 SSVRDLPPVAGSIIWARQIDNQLTMYLKRVEDVLGKGweTHIEGQKLKADGDSFRAKLS--ISDVFHEWARKVQERNFGS 707
Cdd:pfam08385 371 PIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLL--KHAEGKKVIKKYNELAKKLDeyERLIYEAWLKEVEEASEGN 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 708 TGR-IFTIESTRSRigrgnvlRLRVNFLPEIITLAKEVRNIKNLGFRVPLTIVNKAHQANQIYPYAISLIESVRTYERTL 786
Cdd:pfam08385 449 LKRpLLVRHPETGK-------LLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIR 521
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 221330856 787 EKIedRASIVPLVAGLRKDVLNLVSEGIGLI-WESYKLDPY 826
Cdd:pfam08385 522 STL--LPVERPLLAPHLKDIDEKLEPGLTTLtWNSLGIDEY 560
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3545-3765 |
1.16e-99 |
|
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: 320.54 E-value: 1.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3545 LRWQANALPTDDLCTENAIMLKRFNRYPLIIDPSGQATTFLLNEYAGKKITKTSFLDDSFRKNLESALRFGNPLLVQDV- 3623
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3624 ENYDPILNPVLNRELRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDICSRVTFVNFTVTRSSLQSQCLNQVLK 3703
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221330856 3704 AERPDIDEKRSDLLKLQGEFRLRLRQLEKSLLQALNDAKGKILDDDSVITTLETLKKEAYDI 3765
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2893-3171 |
6.22e-68 |
|
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: 231.34 E-value: 6.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2893 PLVLFDEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSIFQIKVHNKYTSEDFDEDLRCVLRRSGCKD 2972
Cdd:pfam12780 2 DLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2973 EKIAFILDESNVLDSGFLERMNTLLANGEVPGLFEGDEYTTLMTQCKEGAQREGLmLDSSDELYKWFTQQVMRNLHVVFT 3052
Cdd:pfam12780 82 KPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNI-EDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3053 MNPSTDGLKDRAATSPALFNRCVLNWFGDWSDSALFQVGKEFTTRVdlekpnwhapdffpsvcpLVPANptHRDAVINSC 3132
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDI------------------EIPEE--LKSNVVKVF 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 221330856 3133 VYVHQTLHQANARLAKRGGRTMAVTPRHYLDFIHHFVKL 3171
Cdd:pfam12780 221 VYVHSSVEDMSKKFYEELKRKNYVTPKSYLELLRLYKNL 259
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4320-4633 |
2.12e-58 |
|
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: 205.55 E-value: 2.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 4320 TTRGTDLVSKLLKMQQLEDddelaysvedqseqsavGRGEDGRPSWMKTLHNSATAWLELLPKNL---QVLKRTVENIKD 4396
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSD-----------------SGGGGGGSSREEIVLELAKDILEKLPEPFdieEAEEKYPVGYED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 4397 PLYRYFEREVTSGSRLLQTVILDLQDVVLICQGEKKQTNHHRSMLSELVRGIIPKGWKRYTVPAGCTVIQWITDFSNRVQ 4476
Cdd:pfam18199 64 PLNTVLLQEIERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 4477 QLQKVSqlvsqagakELQGFP--VWLGGLLNPEAYITATRQCVAQANSWSLEELALDVTITDAGLKNDQ----KDCCFgV 4550
Cdd:pfam18199 144 QLQDWL---------DDEGPPkvFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSPEEVteppEDGVY-V 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 4551 TGLKLQGAQC-KNNELLLAST---IMMDLPVTILKWIKISSEPRISKL-TLPVYLNSTR--TELLFTVDLavAAGQESHS 4623
Cdd:pfam18199 214 HGLFLEGARWdRKNGCLVESEpkeLFSPLPVIHLKPVESDKKKLDENTyECPVYKTSERhsTNFVFSVDL--PTDKPPDH 291
|
330
....*....|
gi 221330856 4624 FYERGVAVLT 4633
Cdd:pfam18199 292 WILRGVALLL 301
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
4159-4314 |
2.11e-56 |
|
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: 193.05 E-value: 2.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 4159 RARLYFLLAWFHAIVQERLRYVPLGWAKKYEFNESDLRVACDTLDTWIDTtamgrtnlPPEKVPWDALVTLLSQSIYGGK 4238
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDE--------YDEKIPWDALRYLIGEINYGGR 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221330856 4239 IDNDFDQRLLTSFLKKLFTARSFEADFALVANVdgasgglrhITMPDGTRRDHFLKWIENLTDRQTPSWLGLPNNA 4314
Cdd:pfam18198 73 VTDDWDRRLLNTYLEEFFNPEVLEEDFKFSPSL---------YYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
3186-3521 |
2.60e-44 |
|
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: 166.40 E-value: 2.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3186 LNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRKYVMA 3265
Cdd:pfam12777 3 LENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3266 DLAQVEPAVIDAQAAVSSIKKKHLAEVRSMANPPAVVKLALESVCELLNESA-----TDWKAIRGILVK-DSFISSIVNL 3339
Cdd:pfam12777 83 DLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGGkipkdKSWKAAKIMMAKvDGFLDSLIKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3340 ETDKITDDVREKMKSkYLSNPDYNFEKVNRASMACGPMVKWAIAQIEYADMLKRVEPLREELrsleEQADVNLASAKETk 3419
Cdd:pfam12777 163 DKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQAL----EEANADLAAAQEK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3420 dlVEQLERSIAAYKEEYAQLISQ-----AQAIKTDLENVQAKVDRSIA--LLKSLNIERERWESTSETFKSQMSTIIGDV 3492
Cdd:pfam12777 237 --LAAIKAKIAELNANLAKLTAAfekatADKIKCQQEADATARTILLAnrLVGGLASENIRWADAVENFKQQERTLCGDI 314
|
330 340 350
....*....|....*....|....*....|
gi 221330856 3493 LLSAAFIAYGGYFDQHYRLNLF-TTWSQHL 3521
Cdd:pfam12777 315 LLISAFISYLGFFTKKYRNELLdKFWIPYI 344
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2551-2724 |
1.61e-42 |
|
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: 155.24 E-value: 1.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2551 DIVVPTLDTVRHESLLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALP--DMEVVGLNFSSATTPELLLKTFDHYCEYRK 2628
Cdd:pfam12775 9 EILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDkeKYLPLFINFSAQTTSNQTQDIIESKLEKRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2629 tpnGVVLSPVqIGKWLVLFCDEINLPDMDSYGTQRVISFLRQLVEHKGFYRASDQAWVSLERIQFVGACNPPTdPGRKPL 2708
Cdd:pfam12775 89 ---KGVYGPP-GGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPG-GGRNDI 163
|
170
....*....|....*.
gi 221330856 2709 SHRFLRHVPIIYVDYP 2724
Cdd:pfam12775 164 TPRLLRHFNVFNITFP 179
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
4019-4129 |
8.14e-37 |
|
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: 136.42 E-value: 8.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 4019 NCNTPALLCSVPGFDASGRVDDLAAEQN--KQISSIAIGSAEGFnQAERAINMACKTGRWVLLKNVHLAPQWLVQLEKKM 4096
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGfgGKLHSISLGQGQGP-IAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKIL 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 221330856 4097 HSLQ---PHSGFRLFLTMEINPKVPVNLLRAGRIFV 4129
Cdd:pfam03028 80 EELPeetLHPDFRLWLTSEPSPKFPISILQNSIKIT 115
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2408-2535 |
2.04e-22 |
|
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA domain 5 in the dynein heavy chain. This domain is composed of 8 alpha helices.
Pssm-ID: 465532 [Multi-domain] Cd Length: 126 Bit Score: 95.43 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2408 LLPFFsaDGIVVRTLEYAMDQ-EHIMDFTRLRALSSLFSMLNQAARNVLTFNAQHPdfpCSADQLEHYIPKALVYSVLWS 2486
Cdd:pfam17852 1 LEPLF--EWLVPPALEFVRKNcKEIVPTSDLNLVQSLCRLLESLLDEVLEYNGVHP---LSPDKLKEYLEKLFLFALVWS 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 221330856 2487 FAGDAKLKVRIDLGDFVRSVTT-VPLPGAAGAPIIDYEVNM-SGDWVPWSN 2535
Cdd:pfam17852 76 IGGTLDEDSRKKFDEFLRELFSgLDLPPPEKGTVYDYFVDLeKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2205-2345 |
6.41e-15 |
|
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: 74.64 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2205 GLMMVGPSGSGKSTAWKTLLKALERFEGVEgvahVIDPKAISKEALYGVLDPNTR--EWTDGLFTHILRKiidnvrgein 2282
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFY----VQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAARE---------- 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221330856 2283 krQWIIFDGDVD---PEWVENLNSVLDDNKLLTLPNGERLSLPP-NVRVMFEV----QDLKFATLATVSRC 2345
Cdd:pfam07728 67 --GEIAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMnpldRGLNELSPALRSRF 135
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2555-2718 |
9.88e-11 |
|
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: 62.93 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2555 PTLDTVRHESLLYTWLAEHKPLVLCGPPGSGKTMTLFSALRAL--PDMEVVGLNFSSATTPELLLKTFDHYCEYRKTpng 2632
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2633 vvlSPVQIGKWLVLFCDEIN-LPDMDSYGTQRVISFLRQLVEhkgfyrasdqawvSLERIQFVGACNPPTDPG-RKPLSH 2710
Cdd:cd00009 78 ---ELAEKAKPGVLFIDEIDsLSRGAQNALLRVLETLNDLRI-------------DRENVRVIGATNRPLLGDlDRALYD 141
|
....*...
gi 221330856 2711 RFLRHVPI 2718
Cdd:cd00009 142 RLDIRIVI 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2573-2718 |
1.81e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2573 HKPLVLCGPPGSGKTMTLFSALRALPDMevvGLNFSSATTPELLLKTFDHYCEYRKTPNGVVLSPVQI----------GK 2642
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPP---GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRlrlalalarkLK 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221330856 2643 WLVLFCDEI-NLPDMDSYGTQRVISFLRQLVEHKgfyrasdqawvSLERIQFVGACNPPTDPGRKPLSHRFLRHVPI 2718
Cdd:smart00382 79 PDVLILDEItSLLDAEQEALLLLLEELRLLLLLK-----------SEKNLTVILTTNDEKDLGPALLRRRFDRRIVL 144
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3133-3490 |
6.30e-06 |
|
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: 52.75 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3133 VYVHQTLHQANARLAKRGGRTMAVTPRHYLDFIHHFVklyNEKRSDLEEQQLHLNvglNKIAETVEQVEEMQKSLAVKKQ 3212
Cdd:TIGR02168 625 VLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVI---TGGSAKTNSSILERR---REIEELEEKIEELEEKIAELEK 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3213 ELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLAdqtvKIEEKRKYVMADLAQVEPAVIDAQAavssiKKKHLAEV 3292
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLA----RLEAEVEQLEERIAQLSKELTELEA-----EIEELEER 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3293 RSMANPPAVVKLA-LESVCELLNESATDWKAIRGILVKdsfISSIVNLETDKITdDVREKMkskylsnpdynfEKVNRAS 3371
Cdd:TIGR02168 770 LEEAEEELAEAEAeIEELEAQIEQLKEELKALREALDE---LRAELTLLNEEAA-NLRERL------------ESLERRI 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3372 MACGPMVKWAIAQIEyaDMLKRVEPLREELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYAQLIsqaqaikTDLE 3451
Cdd:TIGR02168 834 AATERRLEDLEEQIE--ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS-------EELR 904
|
330 340 350
....*....|....*....|....*....|....*....
gi 221330856 3452 NVQAKVDRSIALLKSLNIERERWESTSETFKSQMSTIIG 3490
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3170-3464 |
3.22e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3170 KLYNEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRL 3249
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3250 ADQTVKIEEKRKYVMADLAQVEPAVIDAQAAVSSIKKKhLAEVRSmanppavvklALESVCELLNESATDWKAIRgilvk 3329
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAE-LAEAEE----------ALLEAEAELAEAEEELEELA----- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3330 dsfiSSIVNLETDKItddvrekmkskylsnpdynfEKVNRAsmacgpmvkwAIAQIEYADMLKRVEPLREELRSLEEQAD 3409
Cdd:COG1196 386 ----EELLEALRAAA--------------------ELAAQL----------EELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 221330856 3410 VNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALL 3464
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3169-3489 |
3.41e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3169 VKLYNEKRSDLEEQQLHLNVGLNKIAETVEQ----VEEMQKSLAVKKQEL-QAKNEAANAKlKQMFQDQQEAEK--KKI- 3240
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKkqqeINEKTTEISNTQTQLnQLKDEQNKIK-KQLSEKQKELEQnnKKIk 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3241 ----QSQEIQIRLAD-QTVKIEEKRKYVMADLAQVEPAVIDAQAAVSSIKKKhLAEVRSMANPPAVVKLALESV-CELLN 3314
Cdd:TIGR04523 285 elekQLNQLKSEISDlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKI-ISQLNEQISQLKKELTNSESEnSEKQR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3315 ESATDWKAIRGILV-KDSFISSIVNLETDKitddvrEKMKSKYLSNPDYNFEKVNRASmacgpmvkwaIAQIEYADMLKR 3393
Cdd:TIGR04523 364 ELEEKQNEIEKLKKeNQSYKQEIKNLESQI------NDLESKIQNQEKLNQQKDEQIK----------KLQQEKELLEKE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3394 VEPLRE-------ELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYaqlisqaQAIKTDLENVQAKVDRSIALLKS 3466
Cdd:TIGR04523 428 IERLKEtiiknnsEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI-------NKIKQNLEQKQKELKSKEKELKK 500
|
330 340
....*....|....*....|...
gi 221330856 3467 LNIERERWESTSETFKSQMSTII 3489
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLK 523
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2907-2997 |
4.24e-05 |
|
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: 46.76 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2907 IDRIFRQPQGHLLLIGVSGAGKTTLSRFVAW---MNGLSIFQIKVHNKYTSEDFDEDLRCVLRRS----GCKDEKIAFIL 2979
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASDLLEGLVVAELFGHFLVRLlfelAEKAKPGVLFI 90
|
90
....*....|....*...
gi 221330856 2980 DESNVLDSGFLERMNTLL 2997
Cdd:cd00009 91 DEIDSLSRGAQNALLRVL 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3189-3781 |
4.62e-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: 50.07 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3189 GLNKIAETVEQVEEMQKSLAVKKQELQAKN---EAANAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRkyvMA 3265
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEqllEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE---LE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3266 DLAQVEpavidaQAAVSSIKKKhLAEVRSMANPPAVVKLALESVCELLNESATDWKAIRGILVKDSFISSIVNLETDKIT 3345
Cdd:TIGR02169 319 DAEERL------AKLEAEIDKL-LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3346 ---DDVREKMKSkYLSNPDYNFEKVNRASMACGPMvKWAIAQIE--YADMLKRVEPLREELRSLEEQadvnlasAKETKD 3420
Cdd:TIGR02169 392 eklEKLKREINE-LKRELDRLQEELQRLSEELADL-NAAIAGIEakINELEEEKEDKALEIKKQEWK-------LEQLAA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3421 LVEQLERSIAAYKEEYAQlisqaqaIKTDLENVQAKVDRSIALLKSLNIERERWESTSETFKSQMSTIIGDVllsAAFIA 3500
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDR-------VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTV---AQLGS 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3501 YggyfDQHYRLNLFTTWSQHLQAASIQYRADIART-EYLSnpdERLRWQANALPTDDlctenaimLKRFNRYPLIIDPSG 3579
Cdd:TIGR02169 533 V----GERYATAIEVAAGNRLNNVVVEDDAVAKEAiELLK---RRKAGRATFLPLNK--------MRDERRDLSILSEDG 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3580 qATTFLLNeyagkkitktsFLDdsFRKNLESALR--FGNPLLVQDVEnydpilnpvlnrELRRTGGRV-LITLgDQDIdL 3656
Cdd:TIGR02169 598 -VIGFAVD-----------LVE--FDPKYEPAFKyvFGDTLVVEDIE------------AARRLMGKYrMVTL-EGEL-F 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3657 SPSFVIflstrdptvefppdicsrvtfvnftvTRSSLQSQCLNQVLKAERPDIDEKRSDLLKLQGEF------RLRLRQL 3730
Cdd:TIGR02169 650 EKSGAM--------------------------TGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELsslqseLRRIENR 703
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 221330856 3731 EKSLLQALNDAKGKILDDDSVITTL----ETLKKEAYDINQKVDETDKVIAEIET 3781
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIENVKS 758
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3190-3305 |
5.21e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3190 LNKIAE----TVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRKYVMA 3265
Cdd:COG3883 124 LSKIADadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 221330856 3266 DLAQVEPAVIDAQAAVSSIKKKHLAEVRSMANPPAVVKLA 3305
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3172-3468 |
6.16e-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: 49.67 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3172 YNEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKslavKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLAD 3251
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEE----EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3252 QTVKIEEKRKYVMADLAQVEPAVIDAQAAVSSIKKKHLAEVRSMANppavVKLALESVCELLNESATDWKAIRgiLVKDS 3331
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE----LESRLEELEEQLETLRSKVAQLE--LQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3332 FISSIVNLETDK-ITDDVREKMKSkylSNPDYNFEKVNrasmacgpmvkwaiAQIEYADMlkRVEPLREELRSLEEQADV 3410
Cdd:TIGR02168 398 LNNEIERLEARLeRLEDRRERLQQ---EIEELLKKLEE--------------AELKELQA--ELEELEEELEELQEELER 458
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 221330856 3411 NLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALLKSLN 3468
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2575-2714 |
1.17e-04 |
|
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: 44.98 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2575 PLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRKTPNGVVLSPVQIGKwlVLFCDEINLP 2654
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAAREGE--IAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221330856 2655 DMDsygtqrVISFLRQLVEHKGFYRASD--QAWVSLERIQFVGACNPPtDPGRKPLSHRFLR 2714
Cdd:pfam07728 79 NPD------VLNSLLSLLDERRLLLPDGgeLVKAAPDGFRLIATMNPL-DRGLNELSPALRS 133
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3172-3786 |
1.21e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3172 YNEKRSDLEEQQLHLNVG-----LNKIAETVEQVEEMQ---KSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQ 3243
Cdd:TIGR02168 215 YKELKAELRELELALLVLrleelREELEELQEELKEAEeelEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3244 EIQIRLADQTVKIEEKRKYVMADLAQVEpAVIDAQAAVSSIKKKHLAEVRSMANPPAVVKLALEsvcELLNESATDWKAI 3323
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELE-AQLEELESKLDELAEELAELEEKLEELKEELESLE---AELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3324 RGILVKDsfissivnletdkitDDVREKMKSKYLSNpdYNFEKVNRasmacgpmvkwaiAQIEYADMLK-----RVEPLR 3398
Cdd:TIGR02168 371 ESRLEEL---------------EEQLETLRSKVAQL--ELQIASLN-------------NEIERLEARLerledRRERLQ 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3399 EELRSLEEQADVNLASA---------KETKDLVEQLERSIAAYKEEYAQLisqaQAIKTDLENVQAKVDRSIALLKSLNI 3469
Cdd:TIGR02168 421 QEIEELLKKLEEAELKElqaeleeleEELEELQEELERLEEALEELREEL----EEAEQALDAAERELAQLQARLDSLER 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3470 ERERWESTSETFK------SQMSTIIGDV--LLSaafiayggyFDQHYRLNLFTTWSQHLQAasiqyradiarteYLSNP 3541
Cdd:TIGR02168 497 LQENLEGFSEGVKallknqSGLSGILGVLseLIS---------VDEGYEAAIEAALGGRLQA-------------VVVEN 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3542 DERLRWQANALptddlcTENAimlkrfnrypliidpSGQATTFLLNEYAGKKITKTsflDDSFRKNLESALRFGNpllvq 3621
Cdd:TIGR02168 555 LNAAKKAIAFL------KQNE---------------LGRVTFLPLDSIKGTEIQGN---DREILKNIEGFLGVAK----- 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3622 DVENYDPILNPVLNRELrrtgGRVLITlgdQDID--------LSPSFVIFlsTRDPTVEFPpdicsrvtfvNFTVTRSSL 3693
Cdd:TIGR02168 606 DLVKFDPKLRKALSYLL----GGVLVV---DDLDnalelakkLRPGYRIV--TLDGDLVRP----------GGVITGGSA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3694 QSqclNQVLKAERPDIDEKRSDLLKLQGEFRlrlrqlekSLLQALNDAKGKILDDDSVittLETLKKEAYDINQKVDETD 3773
Cdd:TIGR02168 667 KT---NSSILERRREIEELEEKIEELEEKIA--------ELEKALAELRKELEELEEE---LEQLRKELEELSRQISALR 732
|
650
....*....|...
gi 221330856 3774 KVIAEIETVSQQY 3786
Cdd:TIGR02168 733 KDLARLEAEVEQL 745
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3159-3497 |
1.64e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3159 RHYLDFIHHFVKLYN--EKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAE 3236
Cdd:COG4717 115 REELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3237 K---KKIQSQEIQIRLADQTVK-IEEKRKYVMADLAQVEPAVIDAQ---------------AAVSSIKKKHLAEVRSMAN 3297
Cdd:COG4717 195 QdlaEELEELQQRLAELEEELEeAQEELEELEEELEQLENELEAAAleerlkearlllliaAALLALLGLGGSLLSLILT 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3298 PPAVVKLALESVCELLNESATDWKAIRGILVKDSFISSIVNLETDKITDDVREKMKSKYLSnPDYNFEKVNRASMACGPM 3377
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3378 VKWAIAQIEYadmlkRVEPLREELRSLEEQADVN----LASAKETKDLVEQLERSIAAYKEEYAQLIS--QAQAIKTDLE 3451
Cdd:COG4717 354 REAEELEEEL-----QLEELEQEIAALLAEAGVEdeeeLRAALEQAEEYQELKEELEELEEQLEELLGelEELLEALDEE 428
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 221330856 3452 NVQAKVDRSIALLKSLNIERERWESTSETFKSQMSTIIGDVLLSAA 3497
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEL 474
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
3174-3326 |
2.69e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.79 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3174 EKRSDLEEQQLH--LNVGLNKIAETveqveemQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQsQEIQIRLAD 3251
Cdd:COG2268 218 QANREAEEAELEqeREIETARIAEA-------EAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQ-RQLEIAERE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3252 QTVKIEEKRKYV---MADLAQVEPAVIDAQAAV-------SSIK---------KKHLAEVRSMANPPAVVKLALESVCEL 3312
Cdd:COG2268 290 REIELQEKEAEReeaELEADVRKPAEAEKQAAEaeaeaeaEAIRakglaeaegKRALAEAWNKLGDAAILLMLIEKLPEI 369
|
170
....*....|....
gi 221330856 3313 LNESAtdwKAIRGI 3326
Cdd:COG2268 370 AEAAA---KPLEKI 380
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
3163-3488 |
5.69e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3163 DFIHHFVKLYNEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQElqakneaanaklkqmfqdQQEAEKKKIQS 3242
Cdd:PRK01156 465 EKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEIN------------------KSINEYNKIES 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3243 QEIQIrladqtvkieekrKYVMADLAQVEPAVIDAQAAVSSIKKKHLaevrsmanppavvklalesvcELLNESATDWka 3322
Cdd:PRK01156 527 ARADL-------------EDIKIKINELKDKHDKYEEIKNRYKSLKL---------------------EDLDSKRTSW-- 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3323 irgiLVKDSFISSIVNLETDKITDDVREKMKS--KYLSNPDYNFEKVNrasmacgpmvkwaiaqiEYAD-MLKRVEplrE 3399
Cdd:PRK01156 571 ----LNALAVISLIDIETNRSRSNEIKKQLNDleSRLQEIEIGFPDDK-----------------SYIDkSIREIE---N 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3400 ELRSLEEQadVNLASAKetKDLVEQLERSIAAYKEEYA----------QLISQAQAIKTDLENVQAKVDRSiallkslNI 3469
Cdd:PRK01156 627 EANNLNNK--YNEIQEN--KILIEKLRGKIDNYKKQIAeidsiipdlkEITSRINDIEDNLKKSRKALDDA-------KA 695
|
330
....*....|....*....
gi 221330856 3470 ERERWESTSETFKSQMSTI 3488
Cdd:PRK01156 696 NRARLESTIEILRTRINEL 714
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1894-2006 |
7.68e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 1894 FGPAGTGKTESVKALGNQLGR---FVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSACSQQ---IQTI 1967
Cdd:smart00382 8 VGPPGSGKTTLARALARELGPpggGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDvliLDEI 87
|
90 100 110
....*....|....*....|....*....|....*....
gi 221330856 1968 QEALKYEMDSNKESITVELVGKQVRVSPDMAIFITMNPG 2006
Cdd:smart00382 88 TSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDE 126
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3173-3472 |
7.75e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3173 NEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQE-----AEKKKIQSQ--EI 3245
Cdd:COG4372 62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKErqdleQQRKQLEAQiaEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3246 QIRLADQTVKIEEKRKYVMADLAQVEPAVIDAQAAVSSIKKKHLAEVRSMANPPAVVKLALESVCELLNESATDWKAIRG 3325
Cdd:COG4372 142 QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3326 ILVKDSFISSIVNLEtdKITDDVREKMKSKYLSNPDYNFEKVNRASMACGPMVKWAIAQIEYADMLKRVEPLREELRslE 3405
Cdd:COG4372 222 EAKDSLEAKLGLALS--ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELK--L 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221330856 3406 EQADVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALLKSLNIERE 3472
Cdd:COG4372 298 LALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAE 364
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
3168-3472 |
1.12e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3168 FVKLYNEKRSDLEEQQLHLNVGLNKIAETVEQVEEM-QKSLAVKKQELQAKNEAANAKLKQMFQDQQE-AEKKK------ 3239
Cdd:COG5185 230 NIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLrLEKLGENAESSKRLNENANNLIKQFENTKEKiAEYTKsidikk 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3240 -IQSQEIQIRLADQTVKIEEKRKYVMADLAQVEPAVIDAQAAVSSIKKKHLAEVRSMANPPAV---------VKLALESV 3309
Cdd:COG5185 310 aTESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELsksseeldsFKDTIEST 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3310 CELLNESATDWKAiRGILVKDSFISSIVNLETDkitddvREKMKSKYLSNPDYNFE--KVNRASMACGPMVKWAIAQIEY 3387
Cdd:COG5185 390 KESLDEIPQNQRG-YAQEILATLEDTLKAADRQ------IEELQRQIEQATSSNEEvsKLLNELISELNKVMREADEESQ 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3388 ADMLKRVEPLREELRSleeqadvnlaSAKETKDLVEQLERSIAAYKEEYAQLISqaqAIKTDLENVQAKVDRSIALLKSL 3467
Cdd:COG5185 463 SRLEEAYDEINRSVRS----------KKEDLNEELTQIESRVSTLKATLEKLRA---KLERQLEGVRSKLDQVAESLKDF 529
|
....*
gi 221330856 3468 NIERE 3472
Cdd:COG5185 530 MRARG 534
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3173-3427 |
1.20e-03 |
|
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: 45.44 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3173 NEKRSDLEEQQLHLNVGLNKIAETVEQVEEmqkslavKKQELQAKNEAANAKlKQMFQDQQEAEKKKIQS-----QEIQI 3247
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLEK-------EIQELQEQRIDLKEQ-IKSIEKEIENLNGKKEEleeelEELEA 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3248 RLAD---QTVKIEEKRKYVMADLAQVEPAVIDAQAAVSsIKKKHLAEVrsmanppavvKLALESVCELLnesatdwKAIR 3324
Cdd:TIGR02169 876 ALRDlesRLGDLKKERDELEAQLRELERKIEELEAQIE-KKRKRLSEL----------KAKLEALEEEL-------SEIE 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3325 GILVKDSFISsivnlETDKITDDVREKMkskylsnpdynfEKVNRASMACGPMVKWAIAqiEYADMLKRVEPLREELRSL 3404
Cdd:TIGR02169 938 DPKGEDEEIP-----EEELSLEDVQAEL------------QRVEEEIRALEPVNMLAIQ--EYEEVLKRLDELKEKRAKL 998
|
250 260
....*....|....*....|...
gi 221330856 3405 EEQadvnlasAKETKDLVEQLER 3427
Cdd:TIGR02169 999 EEE-------RKAILERIEEYEK 1014
|
|
| Muted |
pfam14942 |
Organelle biogenesis, Muted-like protein; The protein is a coiled-coil protein and belongs to ... |
3165-3261 |
2.36e-03 |
|
Organelle biogenesis, Muted-like protein; The protein is a coiled-coil protein and belongs to a family found in eukaryotes. It undergoes alternative splicing forming two isoforms. The larger isoform is 187 amino acids long in protein sequence length and 21 kDa in mass. The smaller isoform is 110 amino acids long in protein sequence length and 12 kDa in mass. This protein associates with other proteins in order to form biogenesis of lysosome-related organelles complex-1 BLOC1 complex. BLOC-1 is required for the normal biogenesis of specialized organelles of the endosomal-lysosomal system.
Pssm-ID: 464390 [Multi-domain] Cd Length: 146 Bit Score: 41.49 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3165 IHHFVKLYNEKRSDLEEQQLHlNVgLNKIAETVEQV-EEMQKSLAVKKQELQAKNEAANAKLKQMFQdqqeaekkkiQSQ 3243
Cdd:pfam14942 22 IKYFLKEFEEKRGDREVRRLE-NI-TEMINETNENIlPKCKQSMEDNLSELLSKLDAALNMCERLLQ----------REL 89
|
90
....*....|....*...
gi 221330856 3244 EIQIRLADQTVKIEEKRK 3261
Cdd:pfam14942 90 EEEQRKNDRLQENEEQRK 107
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3192-3487 |
3.30e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3192 KIAETVEQVEEMQKSLAVKKQEL-QAKNEaanakLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRKYVMADLAQV 3270
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELrRIENR-----LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3271 EpaviDAQAAVSSIKKKHLAEVRSMANPPAVVKLALESVCELLNESAtdWKAIRGILvkdSFISSIVNlETDKITDDVRE 3350
Cdd:TIGR02169 750 E----QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAEL---SKLEEEVS-RIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3351 KMKSKYLsnpdynfekvnrasmacgpmvkwaiaQIEYADmlKRVEPLREELRSLEEQADVNLASAKETKDLVEQLERSIA 3430
Cdd:TIGR02169 820 KLNRLTL--------------------------EKEYLE--KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 221330856 3431 AYKEEYAQLISQaqaiktdLENVQAKVDRSIALLKSLNIERERWESTSETFKSQMST 3487
Cdd:TIGR02169 872 ELEAALRDLESR-------LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2914-3076 |
4.09e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2914 PQGHLLLIGVSGAGKTTLSRFVAWMNGLSIFQIKVHNkytsedfDEDLRCVLRrsgckdEKIAFILDESNVLDSGFLERM 2993
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------GEDILEEVL------DQLLLIIVGGKKASGSGELRL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 2994 NTL--LANGEVPG-LFEgDEYTTLMTqckegaQREGLMLDSSDELYKWFTQQVMRNLHVVFTMNPSTDglKDRAATSPAL 3070
Cdd:smart00382 68 RLAlaLARKLKPDvLIL-DEITSLLD------AEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKD--LGPALLRRRF 138
|
....*.
gi 221330856 3071 FNRCVL 3076
Cdd:smart00382 139 DRRIVL 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3383-3484 |
4.94e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3383 AQIEYADMLKRVEPLREELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIA 3462
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
90 100
....*....|....*....|..
gi 221330856 3463 LLKSLNIERERWESTSETFKSQ 3484
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEE 387
|
|
| ZapB |
COG3074 |
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
3191-3258 |
6.14e-03 |
|
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 38.41 E-value: 6.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221330856 3191 NKIAETVEQVEEMQ---KSLAVKKQELQAKNEAANAKLKQMfqdQQEAEKKKIQSQEIQIRLADQTVKIEE 3258
Cdd:COG3074 11 AKVQQAVDTIELLQmevEELKEKNEELEQENEELQSENEEL---QSENEQLKTENAEWQERIRSLLGKIDE 78
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
3174-3502 |
8.04e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.33 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3174 EKRSDLEEQQLHLNVGLNKIAETVEQ-VEEMQKSLAVKKQELQAKNEAA--------NAKLKQMFQDQQEAEKKKIQSQE 3244
Cdd:COG3064 59 EAKAEAEQRAAELAAEAAKKLAEAEKaAAEAEKKAAAEKAKAAKEAEAAaaaekaaaAAEKEKAEEAKRKAEEEAKRKAE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3245 IQIRLAD---------QTVKIEEKRKYVMADLAQVEPAVIDAQAAVSSIKKKHLAEVRSMANPPAVVKLALESVCELLNE 3315
Cdd:COG3064 139 EERKAAEaeaaakaeaEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3316 SATDWKAIRGILVKDSFISSIVNLETDKITDDVREKMKSKYLSNPDYNFEKVNRASMACGPMVKWAIAQIEYADMLKRVE 3395
Cdd:COG3064 219 LAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3396 PLREELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALLKSLNIERERWE 3475
Cdd:COG3064 299 DSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLG 378
|
330 340
....*....|....*....|....*..
gi 221330856 3476 STSETFKSQMSTIIGDVLLSAAFIAYG 3502
Cdd:COG3064 379 KLADVEEAAGAGILAAAGGGGLLGLRL 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3381-3480 |
8.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3381 AIAQI-EYADMLKRVEPLREELRSLEEQadvnLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDR 3459
Cdd:COG4913 649 ALQRLaEYSWDEIDVASAEREIAELEAE----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
90 100
....*....|....*....|.
gi 221330856 3460 SIALLKSLNIERERWESTSET 3480
Cdd:COG4913 725 AEEELDELQDRLEAAEDLARL 745
|
|
| PulE |
COG2804 |
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ... |
2573-2602 |
8.50e-03 |
|
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442055 [Multi-domain] Cd Length: 561 Bit Score: 42.10 E-value: 8.50e-03
10 20 30
....*....|....*....|....*....|...
gi 221330856 2573 HKP--LVL-CGPPGSGKTMTLFSALRALPDMEV 2602
Cdd:COG2804 310 RRPhgIILvTGPTGSGKTTTLYAALNELNTPER 342
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3172-3287 |
9.54e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330856 3172 YNEKRSDLEEQQlhlnvglNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMfqDQQEAEKKKIQSQEIQI--RL 3249
Cdd:PRK12704 77 LRERRNELQKLE-------KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQEL--EKKEEELEELIEEQLQEleRI 147
|
90 100 110
....*....|....*....|....*....|....*...
gi 221330856 3250 ADQTVkiEEKRKYVMADLaqVEPAVIDAQAAVSSIKKK 3287
Cdd:PRK12704 148 SGLTA--EEAKEILLEKV--EEEARHEAAVLIKEIEEE 181
|
|
|