|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1022-4337 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 1157.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1022 TYRNLLTKLPEGkilENAYGAIEQKVSEVRNYVDEWLRYQSLWDLQADMLYGRLGEDVNLWIKCLNDIKQSRTTFDTSDT 1101
Cdd:COG5245 146 LSHELELIFRSG---EQWVGCMRKLYESVCSERDGFYEEKSFWSRFHMEMCHIREFCRSKAFRFACDVLRKSGKYVTVAT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1102 RRAY-GPIIIDYAKVQAKVTLKYDSWhkealgkfGTLLGTEMTSFHSKVSKSRTDLEmQSIEAASTSDAVSFITYVQSL- 1179
Cdd:COG5245 223 LDSLlSSSKYSELGRRLHFYANMDFS--------GIYFPKSFSEFKDSVISATQAVS-RDIGRQSRMARRLILVQMDSLa 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1180 --KKDMIAWDKQVEVFREAQRILERQRFQFPNTWLHVDNIEGEWSAFNEIIKRkDTAIQTQVASLqAKIVAEDKAVETRT 1257
Cdd:COG5245 294 rlIVDRICEYVSIEWLGCCEELLTCSMESMSSLVNSFDGEESEAMSLESSLFY-EFRGGEHLAGF-YSAFGDIKRILLFT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1258 VDFLNDWEKtKPTGGKIRPDDALQQLQIFESKYSRLKEERDNVVKAKEALelqesAVPNNSAERMNVALEELQDLRGVWS 1337
Cdd:COG5245 372 WSFKKLGTL-LPSLPGYSSGGMDYGEEYRSLLWELGSEVGDPDSGPVRKW-----MRKDLFDAKVRSGVSFGKQEEFVSD 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1338 ELSKVWTQIDETREKPWLSVQprkLRQQLEAMMAQLKELPaRLRMYESYEYVKKLIQSYIKVNMLIVELKSDALKerHWK 1417
Cdd:COG5245 446 IFNITFERIHGMDPTTLEDDE---EDTPALAILLGQEEAG-RFVKLCKIMRMFSFFNSLEMFSRRTLANRMAIVK--YLS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1418 QLTK----QLRVNWVLS-DLSLGQVWDVNLQKNEgivkdIILVAQGEMA--LEEFLKQVRESWQNYELDlinyqnkcRII 1490
Cdd:COG5245 520 SVVRtgplFLQRDFFGRmSELLMARDMFMEVDGV-----LRLFFGGEWSgiVQLSGIRRAKRCVERQID--------DEI 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1491 RGWddlfnkVKEHINSVAAMKLSPYYkvfeEEALTWEEKLNRINAlfdvwIDVqRRWVYLEGIFSGSADIKTLLPVETSR 1570
Cdd:COG5245 587 REW------CSSVLSDDFLEERAVRV----ERGADGARRLRASSG-----SPV-LRRLDEYLMMMSLEDLMPLIPHAVHR 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1571 FQSISSEFLGLMKKVTKSPKVMDVLNIPaVQRSLERLADLLGKIQKALGEYLERERTSFPRFyfVGDEDLLEIIGNSKNI 1650
Cdd:COG5245 651 KMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRVRELENR 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1651 ARLQKHFKKMFAGVAAILLNEenNVILGISSREGEEVHFMNPVSTVEHPKINEWLSLvekqmrfTLASLLAQAVQDIKQF 1730
Cdd:COG5245 728 VYSYRFFVKKIAKEEMKTVFS--SRIQKKEPFSLDSEAYVGFFRLYEKSIVIRGINR-------SMGRVLSQYLESVQEA 798
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1731 RDGKiDPQAYMEwcdKYQAQIVVLAAQiLWSEDVESALQQASennqSKPMQRVLGNVESTLNVLADSVLqeqpplrrRKL 1810
Cdd:COG5245 799 LEIE-DGSFFVS---RHRVRDGGLEKG-RGCDAWENCFDPPL----SEYFRILEKIFPSEEGYFFDEVL--------KRL 861
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1811 EHLINEFVHKRTVTRRLLNNGVTSPKSFQWLCEMRFYfdprqTEVLQQLTIHMANARFFYGFEYLGVQDRLVQTPLTDRC 1890
Cdd:COG5245 862 DPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-----QGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQ 936
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1891 YLTMTQALESRLggSPFgpAGTGKTESVKALGNQLGRFVlvfncdETFDFQAmgRIFVGLCQVGAWGcFDEFNRLEERML 1970
Cdd:COG5245 937 HQKLFEAVCDEV--CRF--VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR 1003
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1971 sACSQQIQTIQEALKYemdsNKESITveLVGKQVRVSPDMAIFITMNPgyagRSNLPDNLKKLFRSLAMTTPDRQlIAEV 2050
Cdd:COG5245 1004 -TILVDEYLNSDEFRM----LEELNS--AVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGA-IKSR 1071
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2051 MlfsqgfrsaEKLACKIVPFFKLCDEQLSNQSHYDFglRALKSVLisagnvkrdrimKIKEQMKQRGDENIDEASVAENL 2130
Cdd:COG5245 1072 R---------ESLDREIGAFNNEVDGIAREEDELMF--YPMFKSL------------KAKHRMLEEKTEYLNKILSITGL 1128
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2131 PeqeiliqsvcetmvpklvaedipllfsLLSDVFpnvgytRAEMKGLKEEIRKVCQEDYLVCGEGDEQgaawmEKGLGst 2210
Cdd:COG5245 1129 P---------------------------LISDTL------RERIDTLDAEWDSFCRISESLKKYESQQ-----VSGLD-- 1168
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2211 wVDKVLQLYQISNLNHGLMMVGPSGSGKSTAWKTLLKalerFEGVEGVAHVIDPkaiskealygVLDPnTREWTdGLFTH 2290
Cdd:COG5245 1169 -VAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYTDACD----YLWHVKSPYVKKK----------YFDA-DMELR-QFFLM 1231
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2291 ILRkiiDNVRGEI-NKRQWIIFDgdvdpEWVENLNSVLDDNKLLTLPNGERlslppnvRVMFEVQDlkfATLATVSRCGM 2369
Cdd:COG5245 1232 FNR---EDMEARLaDSKMEYEVE-----RYVEKTKAEVSSLKLELSSVGEG-------QVVVSNLG---SIGDKVGRCLV 1293
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2370 VWFSEDVLSTEMIFENYLSRLRsipledgdedfvgviKPAKDKEEEVSPSLQVQRDIALLLLPFFSAdgivvrTLEYAMD 2449
Cdd:COG5245 1294 EYDSISRLSTKGVFLDELGDTK---------------RYLDECLDFFSCFEEVQKEIDELSMVFCAD------ALRFSAD 1352
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2450 QEHIMD-------FTRLRALSSLFSMLNQAARNVltfnaqhpdfpcSADQLEHYIPKALVYSVLWSFAGDAKLKVRIDLG 2522
Cdd:COG5245 1353 LYHIVKerrfsgvLAGSDASESLGGKSIELAAIL------------EHKDLIVEMKRGINDVLKLRIFGDKCRESTPRFY 1420
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2523 DFVRSVTTVPLPGaagapIIDYE------VNMSGDWVPWSnKVPVIEVETHKVASP-DIVVPTLDTVRHESLLYTWLAEH 2595
Cdd:COG5245 1421 LISDGDLIKDLNE-----RSDYEemlimmFNISAVITNNG-SIAGFELRGERVMLRkEVVIPTSDTGFVDSFSNEALNTL 1494
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2596 KPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRKTPNGVVLSPVQIGKWLVLFCDEINL 2675
Cdd:COG5245 1495 RSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINL 1574
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2676 PDMDSYGTQRVISFLRQLVEHKGFYRASDQAWVSLERIQFVGACNPPTDPGRKPLSHRFLRHVPIIYVDYPGETSLKQIY 2755
Cdd:COG5245 1575 PYGFEYYPPTVIVFLRPLVERQGFWSSIAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIY 1654
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2756 GTFSRAMLRLMPALRGYAEPLTNAMVEFYLASQDRFTQDMQPHYVYSPREMTRWVRGICEAIRPLDSLPVEGLVRLWAHE 2835
Cdd:COG5245 1655 EAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDVSLIIDWYCE 1734
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2836 ALRLFQDRLVDDSERRWTNENIDLVGQKHFPGINQEEALQRPILYSNWLSKDYMPVNREELREYVHARLKVFYEEELDVP 2915
Cdd:COG5245 1735 AIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFGMACLLKKDLAVFVEEVRKIFGSSHLDVE 1814
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2916 LVLFDEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSIFQIKVHNKYTSEDFDEDLRCVLRRSGCKDE 2995
Cdd:COG5245 1815 AVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGG 1894
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2996 KIAFILDESNVLDSGFLERMNTLLANGEVPGLFEGDEYTTLMTQCKEGAQREGLMLDSSDELYKWFTQQVMRNLHVVFTM 3075
Cdd:COG5245 1895 RECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEKDTEATLTRVFLVYMEENLPVVFSA 1974
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3076 NPSTDGLKDRAATSPALFNRCVLNWFGDWSDSALFQVGKEFTTrvdLEKPNWHAPDFFPSVCPLVPANpTHRDAVINSCV 3155
Cdd:COG5245 1975 CCSQDTSVLAGIRSPALKNRCFIDFKKLWDTEEMSQYANSVET---LSRDGGRVFFINGELGVGKGAL-ISEVFGDDAVV 2050
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3156 YvhqtlHQANARLAKRGGrTMAVTPRHYLDFIHHFVKLYNEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQE 3235
Cdd:COG5245 2051 I-----EGRGFEISMIEG-SLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVI 2124
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3236 LQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRKYVMADLAQVEPAVIDAQAAVSSIKKKHLAEVR 3315
Cdd:COG5245 2125 LGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIR 2204
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3316 SMANPPAVVKLALESVCELLNESATDWKAIRGILVKDSFISSIVNLETDKITD-DVREKMKSKYLSNPDYNFEKVNRASM 3394
Cdd:COG5245 2205 SFIRPPGDLCIEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPDEIEFDlEARRFREARECSDPSFTGSILNRASK 2284
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3395 ACGPMVKWAIAQIEYADMLKRVEPLREELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLEN 3474
Cdd:COG5245 2285 ACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDT 2364
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3475 VQAKVDRSIALLKSLNIERERWESTSETFKSQMSTIIGDVLLSAAFIAYGGYFDQHYRLNLFTTwSQHLQAASIQYRADI 3554
Cdd:COG5245 2365 VHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIR 2443
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3555 ART--EYLSNPDERLRWQANalpTDDLCTENA-IMLKRFNRYPLIIDPSGQATTFLLNEYAGKKITKTSFLDDSFRKNLE 3631
Cdd:COG5245 2444 RRQfiTEGVQKIEDFKEEAC---STDYGLENSrIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLS 2520
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3632 SALRFGNPLLVQDVENYDPILNPVLNRELRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDICSRVTFVNFTVT 3711
Cdd:COG5245 2521 QARREGSDKIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSK 2600
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3712 RSSLQSQCLNQVLKAERPDIDEKRSDLLKLQGEFRLRLRQLEKSLLQALNDAKGKILDDDSVITTLETLKKEAYDINQKV 3791
Cdd:COG5245 2601 VLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEE 2680
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3792 DETDKVIAEIETVSQQYlPLSVACS-NIYFTMDSLNQVHFLYQYSLKMFLDIFSTVLyNNPKLEGRTdhserLGIVTRDL 3870
Cdd:COG5245 2681 SESMEIEDRIDALKSEY-NASVKRLeSIRVEIAMFDEKALMYNKSICELSSEFEKWR-RMKSKYLCA-----IRYMLMSS 2753
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3871 FQVCYERVARGMIHIDRLTFALLM-----CKIHLKGTSESNLDAEFNFFlrsregllanptpveGLSAEQIESVNRLALR 3945
Cdd:COG5245 2754 EWILDHEDRSGFIHRLDVSFLLRTkrfvsTLLEDKNYRQVLSSCSLYGN---------------DVISHSCDRFDRDVYR 2818
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3946 LpifrkllekvrsipelgawlqqsspeqvvpqlwdeSKALSPIASSVHQLLLIQAFRPDRviaaaHNVVNTVLGEDF-MP 4024
Cdd:COG5245 2819 A-----------------------------------LKHQMDNRTHSTILTSNSKTNPYK-----EYTYNDSWAEAFeVE 2858
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 4025 NAEQELDFTSVVDKQLNCNTPALlcsvpgfdasgrvddLAAEQNKQISSI--AIGSAEGFNQAERAINMACKTGRWVLLK 4102
Cdd:COG5245 2859 DSGDLYKFEEGLLELIVGHAPLI---------------YAHKKSLENERNvdRLGSKENEVYAVLNSLFSRKEKSWFEVY 2923
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 4103 NVHLAPQWLVQLEKKM----HSLQPHSGFRLFLT-MEINPKVPVNLLRAGRIFVFEPPPGIRANLLRTFSTVPAarMMK- 4176
Cdd:COG5245 2924 NISLSFGWFKRYVEDVvypiKASRVCGKVKNMWTsMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLVEIDRY--PFDy 3001
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 4177 TPSERARLYFLLAWFHAIVQERLRYVPLGWAKKYEFNESDLRVACDTLDtwiDTTAMGRTNlppeKVPWDALVTLLSQSI 4256
Cdd:COG5245 3002 TLVIACDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLK---NILFLNHLN----ARKWGNNRDLIFTIV 3074
|
3290 3300 3310 3320 3330 3340 3350 3360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 4257 YGGKIDNDFDQRLLTSFLKKLFTArsfEADFALVANVDGASGGLRHITMPDGTRRDHFLKwIENLTDRQTPSWLGLPNNA 4336
Cdd:COG5245 3075 YGKKHSLMEDSKVVDKYCRGYGAH---ETSSQILASVPGGDPELVKFHMEEMCRSSAFGV-IGQLPDLALCAWLMGPCDS 3150
|
.
gi 442630300 4337 E 4337
Cdd:COG5245 3151 E 3151
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1870-2239 |
6.55e-167 |
|
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: 518.19 E-value: 6.55e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1870 YGFEYLGVQDRLVQTPLTDRCYLTMTQALESRLGGSPFGPAGTGKTESVKALGNQLGRFVLVFNCDETFDFQAMGRIFVG 1949
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1950 LCQVGAWGCFDEFNRLEERMLSACSQQIQTIQEALKyemdSNKESITVElvGKQVRVSPDMAIFITMNPGYAGRSNLPDN 2029
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALA----ANLKTFVFE--GSEIKLNPSCGIFITMNPGYAGRTELPDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2030 LKKLFRSLAMTTPDRQLIAEVMLFSQGFRSAEKLACKIVPFFKLCDEQLSNQSHYDFGLRALKSVLISAGNVKRDRimki 2109
Cdd:pfam12774 155 LKALFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSN---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2110 keqmkqrgdenideasvaENLPEQEILIQSVCETMVPKLVAEDIPLLFSLLSDVFPNVGYTRAEMKGLKEEIRKVCQEDY 2189
Cdd:pfam12774 231 ------------------PNLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELG 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 442630300 2190 LVCGEgdeqgaawmekglgsTWVDKVLQLYQISNLNHGLMMVGPSGSGKS 2239
Cdd:pfam12774 293 LQPHD---------------AFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1322-1723 |
9.99e-143 |
|
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: 9.99e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1322 MNVALEELQDLRGVWSELSKVWTQIDETREKPWLSVQPRKLRQQLEAMMAQLKELPARLRMYESYEYVKKLIQSYIKVNM 1401
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1402 LIVELKSDALKERHWKQLTKQLRVNW--VLSDLSLGQVWDVNLQKNEGIVKDIILVAQGEMALEEFLKQVRESWQNYELD 1479
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFdpLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1480 LINYQN-KCRIIRGWDDLFNKVKEHINSVAAMKLSPYYKVFEEEALTWEEKLNRINALFDVWIDVQRRWVYLEGIFSGSa 1558
Cdd:pfam08393 161 LVPYKDtGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSSE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1559 DIKTLLPVETSRFQSISSEFLGLMKKVTKSPKVMDVLNIPAVQRSLERLADLLGKIQKALGEYLERERTSFPRFYFVGDE 1638
Cdd:pfam08393 240 DIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSND 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1639 DLLEIIGNSKNIARLQKHFKKMFAGVAAILLNeENNVILGISSREGEEVHFMNPVSTVEhPKINEWLSLVEKQMRFTLAS 1718
Cdd:pfam08393 320 ELLEILSQTKDPTRVQPHLKKCFEGIASLEFD-ENKEITGMISKEGEVVPFSKPPVEAK-GNVEEWLNELEEEMRETLRD 397
|
....*
gi 442630300 1719 LLAQA 1723
Cdd:pfam08393 398 LLKEA 402
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
242-839 |
4.85e-132 |
|
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: 428.15 E-value: 4.85e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 242 LNLLQNGVNRWIAEIKKVTKLNRDPGSGTALQEISFWLNLERALYRIQEKRESPEVALTLDILKHGKRFHATVSFDTDTG 321
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKALDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 322 LKQALATVADYNPLMKDF--PINDLLSATELEKIRPAVQQIFAHLRKV-RNTKY--PIQRCLKLIEAISRDLSQQLLKVL 396
Cdd:pfam08385 81 LTDALNEAKDNVKYLKTLerPFEDLEELTDPPEIIEAIPPLMNTIRLIwSISRYynTSERMTVLLEKISNQLIEQCKKYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 397 GTRRLMHIPFDEFERVMNQCFEIFSCWDDEYDKLQGLLRDIVKKKRdehlkmvWRVSPAHK-----KLQTRMEHMRKFRR 471
Cdd:pfam08385 161 SPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERP-------WDFSERYIfgrfdAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 472 QHEQLRTviLRVLRPTKpavgddGNVVETKQpysldaadANAIEEVNLAYENVKEV--DCLDITKEGseaWEAAVKRYEE 549
Cdd:pfam08385 234 TIEQFSK--LEKIGGTK------GPELEGVI--------EEILEEFQEAYKVFKSKtyDILDVSNEG---FDDDYEEFKE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 550 KIDRVETRITAHLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIEALHEKFKVQypqsKSCRL 629
Cdd:pfam08385 295 RIKDLERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQ----KYNPS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 630 SSVRDLPPVAGSIIWARQIDNQLTMYLKRVEDVLGKGweTHIEGQKLKADGDSFRAKLS--ISDVFHEWARKVQERNFGS 707
Cdd:pfam08385 371 PIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLL--KHAEGKKVIKKYNELAKKLDeyERLIYEAWLKEVEEASEGN 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 708 TGR-IFTIESTRSRigrgnvlRLRVNFLPEIITLAKEVRNIKNLGFRVPLTIVNKAHQANQIYPYAISLIESVRTYERTL 786
Cdd:pfam08385 449 LKRpLLVRHPETGK-------LLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIR 521
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 442630300 787 EKLNNrslaqnsVFKiedrasivPLVAGLRKDVLNLVSEGIGLI-WESYKLDPY 839
Cdd:pfam08385 522 STLLP-------VER--------PLLAPHLKDIDEKLEPGLTTLtWNSLGIDEY 560
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3567-3787 |
1.17e-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: 1.17e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3567 LRWQANALPTDDLCTENAIMLKRFNRYPLIIDPSGQATTFLLNEYAGKKITKTSFLDDSFRKNLESALRFGNPLLVQDV- 3645
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3646 ENYDPILNPVLNRELRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDICSRVTFVNFTVTRSSLQSQCLNQVLK 3725
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630300 3726 AERPDIDEKRSDLLKLQGEFRLRLRQLEKSLLQALNDAKGKILDDDSVITTLETLKKEAYDI 3787
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 ... |
2915-3193 |
6.07e-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: 6.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2915 PLVLFDEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSIFQIKVHNKYTSEDFDEDLRCVLRRSGCKD 2994
Cdd:pfam12780 2 DLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2995 EKIAFILDESNVLDSGFLERMNTLLANGEVPGLFEGDEYTTLMTQCKEGAQREGLmLDSSDELYKWFTQQVMRNLHVVFT 3074
Cdd:pfam12780 82 KPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNI-EDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3075 MNPSTDGLKDRAATSPALFNRCVLNWFGDWSDSALFQVGKEFTTRVdlekpnwhapdffpsvcpLVPANptHRDAVINSC 3154
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDI------------------EIPEE--LKSNVVKVF 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 442630300 3155 VYVHQTLHQANARLAKRGGRTMAVTPRHYLDFIHHFVKL 3193
Cdd:pfam12780 221 VYVHSSVEDMSKKFYEELKRKNYVTPKSYLELLRLYKNL 259
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4342-4655 |
2.13e-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: 2.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 4342 TTRGTDLVSKLLKMQQLEDddelaysvedqseqsavGRGEDGRPSWMKTLHNSATAWLELLPKNL---QVLKRTVENIKD 4418
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSD-----------------SGGGGGGSSREEIVLELAKDILEKLPEPFdieEAEEKYPVGYED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 4419 PLYRYFEREVTSGSRLLQTVILDLQDVVLICQGEKKQTNHHRSMLSELVRGIIPKGWKRYTVPAGCTVIQWITDFSNRVQ 4498
Cdd:pfam18199 64 PLNTVLLQEIERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 4499 QLQKVSqlvsqagakELQGFP--VWLGGLLNPEAYITATRQCVAQANSWSLEELALDVTITDAGLKNDQ----KDCCFgV 4572
Cdd:pfam18199 144 QLQDWL---------DDEGPPkvFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSPEEVteppEDGVY-V 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 4573 TGLKLQGAQC-KNNELLLAST---IMMDLPVTILKWIKISSEPRISKL-TLPVYLNSTR--TELLFTVDLavAAGQESHS 4645
Cdd:pfam18199 214 HGLFLEGARWdRKNGCLVESEpkeLFSPLPVIHLKPVESDKKKLDENTyECPVYKTSERhsTNFVFSVDL--PTDKPPDH 291
|
330
....*....|
gi 442630300 4646 FYERGVAVLT 4655
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 ... |
4181-4336 |
2.12e-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: 2.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 4181 RARLYFLLAWFHAIVQERLRYVPLGWAKKYEFNESDLRVACDTLDTWIDTtamgrtnlPPEKVPWDALVTLLSQSIYGGK 4260
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDE--------YDEKIPWDALRYLIGEINYGGR 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442630300 4261 IDNDFDQRLLTSFLKKLFTARSFEADFALVANVdgasgglrhITMPDGTRRDHFLKWIENLTDRQTPSWLGLPNNA 4336
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 ... |
3208-3543 |
2.62e-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: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3208 LNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRKYVMA 3287
Cdd:pfam12777 3 LENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3288 DLAQVEPAVIDAQAAVSSIKKKHLAEVRSMANPPAVVKLALESVCELLNESA-----TDWKAIRGILVK-DSFISSIVNL 3361
Cdd:pfam12777 83 DLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGGkipkdKSWKAAKIMMAKvDGFLDSLIKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3362 ETDKITDDVREKMKSkYLSNPDYNFEKVNRASMACGPMVKWAIAQIEYADMLKRVEPLREELrsleEQADVNLASAKETk 3441
Cdd:pfam12777 163 DKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQAL----EEANADLAAAQEK- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3442 dlVEQLERSIAAYKEEYAQLISQ-----AQAIKTDLENVQAKVDRSIA--LLKSLNIERERWESTSETFKSQMSTIIGDV 3514
Cdd:pfam12777 237 --LAAIKAKIAELNANLAKLTAAfekatADKIKCQQEADATARTILLAnrLVGGLASENIRWADAVENFKQQERTLCGDI 314
|
330 340 350
....*....|....*....|....*....|
gi 442630300 3515 LLSAAFIAYGGYFDQHYRLNLF-TTWSQHL 3543
Cdd:pfam12777 315 LLISAFISYLGFFTKKYRNELLdKFWIPYI 344
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2573-2746 |
1.62e-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: 1.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2573 DIVVPTLDTVRHESLLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALP--DMEVVGLNFSSATTPELLLKTFDHYCEYRK 2650
Cdd:pfam12775 9 EILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDkeKYLPLFINFSAQTTSNQTQDIIESKLEKRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2651 tpnGVVLSPVqIGKWLVLFCDEINLPDMDSYGTQRVISFLRQLVEHKGFYRASDQAWVSLERIQFVGACNPPTdPGRKPL 2730
Cdd:pfam12775 89 ---KGVYGPP-GGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPG-GGRNDI 163
|
170
....*....|....*.
gi 442630300 2731 SHRFLRHVPIIYVDYP 2746
Cdd:pfam12775 164 TPRLLRHFNVFNITFP 179
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
4041-4151 |
8.34e-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: 8.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 4041 NCNTPALLCSVPGFDASGRVDDLAAEQN--KQISSIAIGSAEGFnQAERAINMACKTGRWVLLKNVHLAPQWLVQLEKKM 4118
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGfgGKLHSISLGQGQGP-IAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKIL 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 442630300 4119 HSLQ---PHSGFRLFLTMEINPKVPVNLLRAGRIFV 4151
Cdd:pfam03028 80 EELPeetLHPDFRLWLTSEPSPKFPISILQNSIKIT 115
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2430-2557 |
2.05e-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: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2430 LLPFFsaDGIVVRTLEYAMDQ-EHIMDFTRLRALSSLFSMLNQAARNVLTFNAQHPdfpCSADQLEHYIPKALVYSVLWS 2508
Cdd:pfam17852 1 LEPLF--EWLVPPALEFVRKNcKEIVPTSDLNLVQSLCRLLESLLDEVLEYNGVHP---LSPDKLKEYLEKLFLFALVWS 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 442630300 2509 FAGDAKLKVRIDLGDFVRSVTT-VPLPGAAGAPIIDYEVNM-SGDWVPWSN 2557
Cdd:pfam17852 76 IGGTLDEDSRKKFDEFLRELFSgLDLPPPEKGTVYDYFVDLeKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2227-2367 |
6.45e-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: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2227 GLMMVGPSGSGKSTAWKTLLKALERFEGVEgvahVIDPKAISKEALYGVLDPNTR--EWTDGLFTHILRKiidnvrgein 2304
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFY----VQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAARE---------- 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442630300 2305 krQWIIFDGDVD---PEWVENLNSVLDDNKLLTLPNGERLSLPP-NVRVMFEV----QDLKFATLATVSRC 2367
Cdd:pfam07728 67 --GEIAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMnpldRGLNELSPALRSRF 135
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2577-2740 |
9.83e-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: 9.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2577 PTLDTVRHESLLYTWLAEHKPLVLCGPPGSGKTMTLFSALRAL--PDMEVVGLNFSSATTPELLLKTFDHYCEYRKTpng 2654
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2655 vvlSPVQIGKWLVLFCDEIN-LPDMDSYGTQRVISFLRQLVEhkgfyrasdqawvSLERIQFVGACNPPTDPG-RKPLSH 2732
Cdd:cd00009 78 ---ELAEKAKPGVLFIDEIDsLSRGAQNALLRVLETLNDLRI-------------DRENVRVIGATNRPLLGDlDRALYD 141
|
....*...
gi 442630300 2733 RFLRHVPI 2740
Cdd:cd00009 142 RLDIRIVI 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2595-2740 |
1.75e-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: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2595 HKPLVLCGPPGSGKTMTLFSALRALPDMevvGLNFSSATTPELLLKTFDHYCEYRKTPNGVVLSPVQI----------GK 2664
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPP---GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRlrlalalarkLK 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442630300 2665 WLVLFCDEI-NLPDMDSYGTQRVISFLRQLVEHKgfyrasdqawvSLERIQFVGACNPPTDPGRKPLSHRFLRHVPI 2740
Cdd:smart00382 79 PDVLILDEItSLLDAEQEALLLLLEELRLLLLLK-----------SEKNLTVILTTNDEKDLGPALLRRRFDRRIVL 144
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3155-3512 |
6.12e-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: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3155 VYVHQTLHQANARLAKRGGRTMAVTPRHYLDFIHHFVklyNEKRSDLEEQQLHLNvglNKIAETVEQVEEMQKSLAVKKQ 3234
Cdd:TIGR02168 625 VLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVI---TGGSAKTNSSILERR---REIEELEEKIEELEEKIAELEK 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3235 ELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLAdqtvKIEEKRKYVMADLAQVEPAVIDAQAavssiKKKHLAEV 3314
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLA----RLEAEVEQLEERIAQLSKELTELEA-----EIEELEER 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3315 RSMANPPAVVKLA-LESVCELLNESATDWKAIRGILVKdsfISSIVNLETDKITdDVREKMkskylsnpdynfEKVNRAS 3393
Cdd:TIGR02168 770 LEEAEEELAEAEAeIEELEAQIEQLKEELKALREALDE---LRAELTLLNEEAA-NLRERL------------ESLERRI 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3394 MACGPMVKWAIAQIEyaDMLKRVEPLREELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYAQLIsqaqaikTDLE 3473
Cdd:TIGR02168 834 AATERRLEDLEEQIE--ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS-------EELR 904
|
330 340 350
....*....|....*....|....*....|....*....
gi 442630300 3474 NVQAKVDRSIALLKSLNIERERWESTSETFKSQMSTIIG 3512
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3192-3486 |
3.13e-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: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3192 KLYNEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRL 3271
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3272 ADQTVKIEEKRKYVMADLAQVEPAVIDAQAAVSSIKKKhLAEVRSmanppavvklALESVCELLNESATDWKAIRgilvk 3351
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAE-LAEAEE----------ALLEAEAELAEAEEELEELA----- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3352 dsfiSSIVNLETDKItddvrekmkskylsnpdynfEKVNRAsmacgpmvkwAIAQIEYADMLKRVEPLREELRSLEEQAD 3431
Cdd:COG1196 386 ----EELLEALRAAA--------------------ELAAQL----------EELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 442630300 3432 VNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALL 3486
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3191-3511 |
3.34e-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: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3191 VKLYNEKRSDLEEQQLHLNVGLNKIAETVEQ----VEEMQKSLAVKKQEL-QAKNEAANAKlKQMFQDQQEAEK--KKI- 3262
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKkqqeINEKTTEISNTQTQLnQLKDEQNKIK-KQLSEKQKELEQnnKKIk 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3263 ----QSQEIQIRLAD-QTVKIEEKRKYVMADLAQVEPAVIDAQAAVSSIKKKhLAEVRSMANPPAVVKLALESV-CELLN 3336
Cdd:TIGR04523 285 elekQLNQLKSEISDlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKI-ISQLNEQISQLKKELTNSESEnSEKQR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3337 ESATDWKAIRGILV-KDSFISSIVNLETDKitddvrEKMKSKYLSNPDYNFEKVNRASmacgpmvkwaIAQIEYADMLKR 3415
Cdd:TIGR04523 364 ELEEKQNEIEKLKKeNQSYKQEIKNLESQI------NDLESKIQNQEKLNQQKDEQIK----------KLQQEKELLEKE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3416 VEPLRE-------ELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYaqlisqaQAIKTDLENVQAKVDRSIALLKS 3488
Cdd:TIGR04523 428 IERLKEtiiknnsEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI-------NKIKQNLEQKQKELKSKEKELKK 500
|
330 340
....*....|....*....|...
gi 442630300 3489 LNIERERWESTSETFKSQMSTII 3511
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLK 523
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3211-3803 |
4.09e-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: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3211 GLNKIAETVEQVEEMQKSLAVKKQELQAKN---EAANAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRkyvMA 3287
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEqllEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE---LE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3288 DLAQVEpavidaQAAVSSIKKKhLAEVRSMANPPAVVKLALESVCELLNESATDWKAIRGILVKDSFISSIVNLETDKIT 3367
Cdd:TIGR02169 319 DAEERL------AKLEAEIDKL-LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3368 ---DDVREKMKSkYLSNPDYNFEKVNRASMACGPMvKWAIAQIE--YADMLKRVEPLREELRSLEEQadvnlasAKETKD 3442
Cdd:TIGR02169 392 eklEKLKREINE-LKRELDRLQEELQRLSEELADL-NAAIAGIEakINELEEEKEDKALEIKKQEWK-------LEQLAA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3443 LVEQLERSIAAYKEEYAQlisqaqaIKTDLENVQAKVDRSIALLKSLNIERERWESTSETFKSQMSTIIGDVllsAAFIA 3522
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDR-------VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTV---AQLGS 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3523 YggyfDQHYRLNLFTTWSQHLQAASIQYRADIART-EYLSnpdERLRWQANALPTDDlctenaimLKRFNRYPLIIDPSG 3601
Cdd:TIGR02169 533 V----GERYATAIEVAAGNRLNNVVVEDDAVAKEAiELLK---RRKAGRATFLPLNK--------MRDERRDLSILSEDG 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3602 qATTFLLNeyagkkitktsFLDdsFRKNLESALR--FGNPLLVQDVEnydpilnpvlnrELRRTGGRV-LITLgDQDIdL 3678
Cdd:TIGR02169 598 -VIGFAVD-----------LVE--FDPKYEPAFKyvFGDTLVVEDIE------------AARRLMGKYrMVTL-EGEL-F 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3679 SPSFVIflstrdptvefppdicsrvtfvnftvTRSSLQSQCLNQVLKAERPDIDEKRSDLLKLQGEF------RLRLRQL 3752
Cdd:TIGR02169 650 EKSGAM--------------------------TGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELsslqseLRRIENR 703
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 442630300 3753 EKSLLQALNDAKGKILDDDSVITTL----ETLKKEAYDINQKVDETDKVIAEIET 3803
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIENVKS 758
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2929-3019 |
4.22e-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: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2929 IDRIFRQPQGHLLLIGVSGAGKTTLSRFVAW---MNGLSIFQIKVHNKYTSEDFDEDLRCVLRRS----GCKDEKIAFIL 3001
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASDLLEGLVVAELFGHFLVRLlfelAEKAKPGVLFI 90
|
90
....*....|....*...
gi 442630300 3002 DESNVLDSGFLERMNTLL 3019
Cdd:cd00009 91 DEIDSLSRGAQNALLRVL 108
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3212-3327 |
5.23e-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: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3212 LNKIAE----TVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRKYVMA 3287
Cdd:COG3883 124 LSKIADadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 442630300 3288 DLAQVEPAVIDAQAAVSSIKKKHLAEVRSMANPPAVVKLA 3327
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3194-3490 |
5.89e-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: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3194 YNEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKslavKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLAD 3273
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEE----EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3274 QTVKIEEKRKYVMADLAQVEPAVIDAQAAVSSIKKKHLAEVRSMANppavVKLALESVCELLNESATDWKAIRgiLVKDS 3353
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE----LESRLEELEEQLETLRSKVAQLE--LQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3354 FISSIVNLETDK-ITDDVREKMKSkylSNPDYNFEKVNrasmacgpmvkwaiAQIEYADMlkRVEPLREELRSLEEQADV 3432
Cdd:TIGR02168 398 LNNEIERLEARLeRLEDRRERLQQ---EIEELLKKLEE--------------AELKELQA--ELEELEEELEELQEELER 458
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 442630300 3433 NLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALLKSLN 3490
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3194-3808 |
1.13e-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: 48.90 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3194 YNEKRSDLEEQQLHLNVG-----LNKIAETVEQVEEMQ---KSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQ 3265
Cdd:TIGR02168 215 YKELKAELRELELALLVLrleelREELEELQEELKEAEeelEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3266 EIQIRLADQTVKIEEKRKYVMADLAQVEpAVIDAQAAVSSIKKKHLAEVRSMANPPAVVKLALEsvcELLNESATDWKAI 3345
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELE-AQLEELESKLDELAEELAELEEKLEELKEELESLE---AELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3346 RGILVKDsfissivnletdkitDDVREKMKSKYLSNpdYNFEKVNRasmacgpmvkwaiAQIEYADMLK-----RVEPLR 3420
Cdd:TIGR02168 371 ESRLEEL---------------EEQLETLRSKVAQL--ELQIASLN-------------NEIERLEARLerledRRERLQ 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3421 EELRSLEEQADVNLASA---------KETKDLVEQLERSIAAYKEEYAQLisqaQAIKTDLENVQAKVDRSIALLKSLNI 3491
Cdd:TIGR02168 421 QEIEELLKKLEEAELKElqaeleeleEELEELQEELERLEEALEELREEL----EEAEQALDAAERELAQLQARLDSLER 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3492 ERERWESTSETFK------SQMSTIIGDV--LLSaafiayggyFDQHYRLNLFTTWSQHLQAasiqyradiarteYLSNP 3563
Cdd:TIGR02168 497 LQENLEGFSEGVKallknqSGLSGILGVLseLIS---------VDEGYEAAIEAALGGRLQA-------------VVVEN 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3564 DERLRWQANALptddlcTENAimlkrfnrypliidpSGQATTFLLNEYAGKKITKTsflDDSFRKNLESALRFGNpllvq 3643
Cdd:TIGR02168 555 LNAAKKAIAFL------KQNE---------------LGRVTFLPLDSIKGTEIQGN---DREILKNIEGFLGVAK----- 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3644 DVENYDPILNPVLNRELrrtgGRVLITlgdQDID--------LSPSFVIFlsTRDPTVEFPpdicsrvtfvNFTVTRSSL 3715
Cdd:TIGR02168 606 DLVKFDPKLRKALSYLL----GGVLVV---DDLDnalelakkLRPGYRIV--TLDGDLVRP----------GGVITGGSA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3716 QSqclNQVLKAERPDIDEKRSDLLKLQGEFRlrlrqlekSLLQALNDAKGKILDDDSVittLETLKKEAYDINQKVDETD 3795
Cdd:TIGR02168 667 KT---NSSILERRREIEELEEKIEELEEKIA--------ELEKALAELRKELEELEEE---LEQLRKELEELSRQISALR 732
|
650
....*....|...
gi 442630300 3796 KVIAEIETVSQQY 3808
Cdd:TIGR02168 733 KDLARLEAEVEQL 745
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2597-2736 |
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 442630300 2597 PLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRKTPNGVVLSPVQIGKwlVLFCDEINLP 2676
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAAREGE--IAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630300 2677 DMDsygtqrVISFLRQLVEHKGFYRASD--QAWVSLERIQFVGACNPPtDPGRKPLSHRFLR 2736
Cdd:pfam07728 79 NPD------VLNSLLSLLDERRLLLPDGgeLVKAAPDGFRLIATMNPL-DRGLNELSPALRS 133
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3181-3519 |
1.59e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3181 RHYLDFIHHFVKLYN--EKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAE 3258
Cdd:COG4717 115 REELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3259 K---KKIQSQEIQIRLADQTVK-IEEKRKYVMADLAQVEPAVIDAQ---------------AAVSSIKKKHLAEVRSMAN 3319
Cdd:COG4717 195 QdlaEELEELQQRLAELEEELEeAQEELEELEEELEQLENELEAAAleerlkearlllliaAALLALLGLGGSLLSLILT 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3320 PPAVVKLALESVCELLNESATDWKAIRGILVKDSFISSIVNLETDKITDDVREKMKSKYLSnPDYNFEKVNRASMACGPM 3399
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3400 VKWAIAQIEYadmlkRVEPLREELRSLEEQADVN----LASAKETKDLVEQLERSIAAYKEEYAQLIS--QAQAIKTDLE 3473
Cdd:COG4717 354 REAEELEEEL-----QLEELEQEIAALLAEAGVEdeeeLRAALEQAEEYQELKEELEELEEQLEELLGelEELLEALDEE 428
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 442630300 3474 NVQAKVDRSIALLKSLNIERERWESTSETFKSQMSTIIGDVLLSAA 3519
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEL 474
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
3196-3348 |
2.68e-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: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3196 EKRSDLEEQQLH--LNVGLNKIAETveqveemQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQsQEIQIRLAD 3273
Cdd:COG2268 218 QANREAEEAELEqeREIETARIAEA-------EAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQ-RQLEIAERE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3274 QTVKIEEKRKYV---MADLAQVEPAVIDAQAAV-------SSIK---------KKHLAEVRSMANPPAVVKLALESVCEL 3334
Cdd:COG2268 290 REIELQEKEAEReeaELEADVRKPAEAEKQAAEaeaeaeaEAIRakglaeaegKRALAEAWNKLGDAAILLMLIEKLPEI 369
|
170
....*....|....
gi 442630300 3335 LNESAtdwKAIRGI 3348
Cdd:COG2268 370 AEAAA---KPLEKI 380
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
3185-3510 |
5.76e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3185 DFIHHFVKLYNEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQElqakneaanaklkqmfqdQQEAEKKKIQS 3264
Cdd:PRK01156 465 EKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEIN------------------KSINEYNKIES 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3265 QEIQIrladqtvkieekrKYVMADLAQVEPAVIDAQAAVSSIKKKHLaevrsmanppavvklalesvcELLNESATDWka 3344
Cdd:PRK01156 527 ARADL-------------EDIKIKINELKDKHDKYEEIKNRYKSLKL---------------------EDLDSKRTSW-- 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3345 irgiLVKDSFISSIVNLETDKITDDVREKMKS--KYLSNPDYNFEKVNrasmacgpmvkwaiaqiEYAD-MLKRVEplrE 3421
Cdd:PRK01156 571 ----LNALAVISLIDIETNRSRSNEIKKQLNDleSRLQEIEIGFPDDK-----------------SYIDkSIREIE---N 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3422 ELRSLEEQadVNLASAKetKDLVEQLERSIAAYKEEYA----------QLISQAQAIKTDLENVQAKVDRSiallkslNI 3491
Cdd:PRK01156 627 EANNLNNK--YNEIQEN--KILIEKLRGKIDNYKKQIAeidsiipdlkEITSRINDIEDNLKKSRKALDDA-------KA 695
|
330
....*....|....*....
gi 442630300 3492 ERERWESTSETFKSQMSTI 3510
Cdd:PRK01156 696 NRARLESTIEILRTRINEL 714
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3195-3494 |
7.08e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3195 NEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQE-----AEKKKIQSQ--EI 3267
Cdd:COG4372 62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKErqdleQQRKQLEAQiaEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3268 QIRLADQTVKIEEKRKYVMADLAQVEPAVIDAQAAVSSIKKKHLAEVRSMANPPAVVKLALESVCELLNESATDWKAIRG 3347
Cdd:COG4372 142 QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3348 ILVKDSFISSIVNLEtdKITDDVREKMKSKYLSNPDYNFEKVNRASMACGPMVKWAIAQIEYADMLKRVEPLREELRslE 3427
Cdd:COG4372 222 EAKDSLEAKLGLALS--ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELK--L 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442630300 3428 EQADVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALLKSLNIERE 3494
Cdd:COG4372 298 LALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAE 364
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1907-2019 |
7.64e-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: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 1907 FGPAGTGKTESVKALGNQLGR---FVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSACSQQ---IQTI 1980
Cdd:smart00382 8 VGPPGSGKTTLARALARELGPpggGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDvliLDEI 87
|
90 100 110
....*....|....*....|....*....|....*....
gi 442630300 1981 QEALKYEMDSNKESITVELVGKQVRVSPDMAIFITMNPG 2019
Cdd:smart00382 88 TSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDE 126
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
3190-3494 |
1.08e-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: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3190 FVKLYNEKRSDLEEQQLHLNVGLNKIAETVEQVEEM-QKSLAVKKQELQAKNEAANAKLKQMFQDQQE-AEKKK------ 3261
Cdd:COG5185 230 NIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLrLEKLGENAESSKRLNENANNLIKQFENTKEKiAEYTKsidikk 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3262 -IQSQEIQIRLADQTVKIEEKRKYVMADLAQVEPAVIDAQAAVSSIKKKHLAEVRSMANPPAV---------VKLALESV 3331
Cdd:COG5185 310 aTESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELsksseeldsFKDTIEST 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3332 CELLNESATDWKAiRGILVKDSFISSIVNLETDkitddvREKMKSKYLSNPDYNFE--KVNRASMACGPMVKWAIAQIEY 3409
Cdd:COG5185 390 KESLDEIPQNQRG-YAQEILATLEDTLKAADRQ------IEELQRQIEQATSSNEEvsKLLNELISELNKVMREADEESQ 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3410 ADMLKRVEPLREELRSleeqadvnlaSAKETKDLVEQLERSIAAYKEEYAQLISqaqAIKTDLENVQAKVDRSIALLKSL 3489
Cdd:COG5185 463 SRLEEAYDEINRSVRS----------KKEDLNEELTQIESRVSTLKATLEKLRA---KLERQLEGVRSKLDQVAESLKDF 529
|
....*
gi 442630300 3490 NIERE 3494
Cdd:COG5185 530 MRARG 534
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3195-3449 |
1.15e-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: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3195 NEKRSDLEEQQLHLNVGLNKIAETVEQVEEmqkslavKKQELQAKNEAANAKlKQMFQDQQEAEKKKIQS-----QEIQI 3269
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLEK-------EIQELQEQRIDLKEQ-IKSIEKEIENLNGKKEEleeelEELEA 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3270 RLAD---QTVKIEEKRKYVMADLAQVEPAVIDAQAAVSsIKKKHLAEVrsmanppavvKLALESVCELLnesatdwKAIR 3346
Cdd:TIGR02169 876 ALRDlesRLGDLKKERDELEAQLRELERKIEELEAQIE-KKRKRLSEL----------KAKLEALEEEL-------SEIE 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3347 GILVKDSFISsivnlETDKITDDVREKMkskylsnpdynfEKVNRASMACGPMVKWAIAqiEYADMLKRVEPLREELRSL 3426
Cdd:TIGR02169 938 DPKGEDEEIP-----EEELSLEDVQAEL------------QRVEEEIRALEPVNMLAIQ--EYEEVLKRLDELKEKRAKL 998
|
250 260
....*....|....*....|...
gi 442630300 3427 EEQadvnlasAKETKDLVEQLER 3449
Cdd:TIGR02169 999 EEE-------RKAILERIEEYEK 1014
|
|
| Muted |
pfam14942 |
Organelle biogenesis, Muted-like protein; The protein is a coiled-coil protein and belongs to ... |
3187-3283 |
2.30e-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: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3187 IHHFVKLYNEKRSDLEEQQLHlNVgLNKIAETVEQV-EEMQKSLAVKKQELQAKNEAANAKLKQMFQdqqeaekkkiQSQ 3265
Cdd:pfam14942 22 IKYFLKEFEEKRGDREVRRLE-NI-TEMINETNENIlPKCKQSMEDNLSELLSKLDAALNMCERLLQ----------REL 89
|
90
....*....|....*...
gi 442630300 3266 EIQIRLADQTVKIEEKRK 3283
Cdd:pfam14942 90 EEEQRKNDRLQENEEQRK 107
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3214-3509 |
3.18e-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: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3214 KIAETVEQVEEMQKSLAVKKQEL-QAKNEaanakLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRKYVMADLAQV 3292
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELrRIENR-----LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3293 EpaviDAQAAVSSIKKKHLAEVRSMANPPAVVKLALESVCELLNESAtdWKAIRGILvkdSFISSIVNlETDKITDDVRE 3372
Cdd:TIGR02169 750 E----QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAEL---SKLEEEVS-RIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3373 KMKSKYLsnpdynfekvnrasmacgpmvkwaiaQIEYADmlKRVEPLREELRSLEEQADVNLASAKETKDLVEQLERSIA 3452
Cdd:TIGR02169 820 KLNRLTL--------------------------EKEYLE--KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 442630300 3453 AYKEEYAQLISQaqaiktdLENVQAKVDRSIALLKSLNIERERWESTSETFKSQMST 3509
Cdd:TIGR02169 872 ELEAALRDLESR-------LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2936-3098 |
4.04e-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: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 2936 PQGHLLLIGVSGAGKTTLSRFVAWMNGLSIFQIKVHNkytsedfDEDLRCVLRrsgckdEKIAFILDESNVLDSGFLERM 3015
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------GEDILEEVL------DQLLLIIVGGKKASGSGELRL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3016 NTL--LANGEVPG-LFEgDEYTTLMTqckegaQREGLMLDSSDELYKWFTQQVMRNLHVVFTMNPSTDglKDRAATSPAL 3092
Cdd:smart00382 68 RLAlaLARKLKPDvLIL-DEITSLLD------AEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKD--LGPALLRRRF 138
|
....*.
gi 442630300 3093 FNRCVL 3098
Cdd:smart00382 139 DRRIVL 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3405-3506 |
4.88e-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: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3405 AQIEYADMLKRVEPLREELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIA 3484
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
90 100
....*....|....*....|..
gi 442630300 3485 LLKSLNIERERWESTSETFKSQ 3506
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEE 387
|
|
| ZapB |
COG3074 |
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
3213-3280 |
6.11e-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: 6.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442630300 3213 NKIAETVEQVEEMQ---KSLAVKKQELQAKNEAANAKLKQMfqdQQEAEKKKIQSQEIQIRLADQTVKIEE 3280
Cdd:COG3074 11 AKVQQAVDTIELLQmevEELKEKNEELEQENEELQSENEEL---QSENEQLKTENAEWQERIRSLLGKIDE 78
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
3196-3524 |
7.61e-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: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3196 EKRSDLEEQQLHLNVGLNKIAETVEQ-VEEMQKSLAVKKQELQAKNEAA--------NAKLKQMFQDQQEAEKKKIQSQE 3266
Cdd:COG3064 59 EAKAEAEQRAAELAAEAAKKLAEAEKaAAEAEKKAAAEKAKAAKEAEAAaaaekaaaAAEKEKAEEAKRKAEEEAKRKAE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3267 IQIRLADQ---------TVKIEEKRKYVMADLAQVEPAVIDAQAAVSSIKKKHLAEVRSMANPPAVVKLALESVCELLNE 3337
Cdd:COG3064 139 EERKAAEAeaaakaeaeAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3338 SATDWKAIRGILVKDSFISSIVNLETDKITDDVREKMKSKYLSNPDYNFEKVNRASMACGPMVKWAIAQIEYADMLKRVE 3417
Cdd:COG3064 219 LAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3418 PLREELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALLKSLNIERERWE 3497
Cdd:COG3064 299 DSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLG 378
|
330 340
....*....|....*....|....*..
gi 442630300 3498 STSETFKSQMSTIIGDVLLSAAFIAYG 3524
Cdd:COG3064 379 KLADVEEAAGAGILAAAGGGGLLGLRL 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3403-3502 |
8.03e-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: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3403 AIAQI-EYADMLKRVEPLREELRSLEEQadvnLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDR 3481
Cdd:COG4913 649 ALQRLaEYSWDEIDVASAEREIAELEAE----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
90 100
....*....|....*....|.
gi 442630300 3482 SIALLKSLNIERERWESTSET 3502
Cdd:COG4913 725 AEEELDELQDRLEAAEDLARL 745
|
|
| PulE |
COG2804 |
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ... |
2595-2624 |
8.32e-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: 42.49 E-value: 8.32e-03
10 20 30
....*....|....*....|....*....|...
gi 442630300 2595 HKP--LVL-CGPPGSGKTMTLFSALRALPDMEV 2624
Cdd:COG2804 310 RRPhgIILvTGPTGSGKTTTLYAALNELNTPER 342
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3194-3309 |
9.58e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630300 3194 YNEKRSDLEEQQlhlnvglNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMfqDQQEAEKKKIQSQEIQI--RL 3271
Cdd:PRK12704 77 LRERRNELQKLE-------KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQEL--EKKEEELEELIEEQLQEleRI 147
|
90 100 110
....*....|....*....|....*....|....*...
gi 442630300 3272 ADQTVkiEEKRKYVMADLaqVEPAVIDAQAAVSSIKKK 3309
Cdd:PRK12704 148 SGLTA--EEAKEILLEKV--EEEARHEAAVLIKEIEEE 181
|
|
| |
