|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1046-4329 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 1192.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1046 EVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEF-GPVVIDYGKVQSKVNLKYDSWh 1124
Cdd:COG5245 170 SVCSERDGFYEEKSFWSRFHMEMCHIREFCRSKAFRFACDVLRKSGKYVTVATLDSLlSSSKYSELGRRLHFYANMDFS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1125 kevlskfGQMLGSNMTEFHSQISKSRQEL--EQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQRF 1202
Cdd:COG5245 249 -------GIYFPKSFSEFKDSVISATQAVsrDIGRQSRMARRLILVQMDSLARLIVDRICEYVSIEWLGCCEELLTCSME 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1203 QFPPSWLYIDNIEgewgafNDIMRRKDSAIQQQvaNLQMKIVQEDRAVESRTTDLLTDWE-----KTKPVTGNLRPEEAL 1277
Cdd:COG5245 322 SMSSLVNSFDGEE------SEAMSLESSLFYEF--RGGEHLAGFYSAFGDIKRILLFTWSfkklgTLLPSLPGYSSGGMD 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1278 QALTIYEGKFGRLKDDREKCAKAKEALELTDTgllsgSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQpr 1357
Cdd:COG5245 394 YGEEYRSLLWELGSEVGDPDSGPVRKWMRKDL-----FDAKVRSGVSFGKQEEFVSDIFNITFERIHGMDPTTLEDDE-- 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1358 KLRQNLDALLNQlksfpARLRQYASYEFVQRLlkgYMKINML------VIELKSEALKdrHWKQLMKrlhvnwvvseltl 1431
Cdd:COG5245 467 EDTPALAILLGQ-----EEAGRFVKLCKIMRM---FSFFNSLemfsrrTLANRMAIVK--YLSSVVR------------- 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1432 gqIWDVDLQKN-----EAIVKDVLLVAqgEMALEEFLKQIREVWNTYELDLVNYQNKC------RLIRGWddlfnkVKEH 1500
Cdd:COG5245 524 --TGPLFLQRDffgrmSELLMARDMFM--EVDGVLRLFFGGEWSGIVQLSGIRRAKRCverqidDEIREW------CSSV 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1501 INSVSAMKLSPYykvFEEDAlsweDKLNRIMALFDVWIdvqRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMK 1580
Cdd:COG5245 594 LSDDFLEERAVR---VERGA----DGARRLRASSGSPV---LRRLDEYLMMMSLEDLMPLIPHAVHRKMSLVSGVRGIYK 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1581 KVSKSPLVMDVLNIQgVQRSLERLADLLGKIQKALGEYLERERSSFPRFyfVGDEDLLEIIGNSKNVAKLQKHFKKMFAG 1660
Cdd:COG5245 664 RVVSGCEAINTILED-VGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRVRELENRVYSYRFFVKKIAK 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1661 VSSIILNEDNsvVLGISSREGEEVMFKTPVSITEHPKINEWLTlvEKEMRVtLAKLLaesvtevEIFGKATSIDPNTYIt 1740
Cdd:COG5245 741 EEMKTVFSSR--IQKKEPFSLDSEAYVGFFRLYEKSIVIRGIN--RSMGRV-LSQYL-------ESVQEALEIEDGSFF- 807
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1741 wIDKYQAQLVVLSAQIaWSENVETALSSmggggdaaPLHSVLSNVEVT----LNVLADSVLmeqpplrrRKLEHLITELV 1816
Cdd:COG5245 808 -VSRHRVRDGGLEKGR-GCDAWENCFDP--------PLSEYFRILEKIfpseEGYFFDEVL--------KRLDPGHEIKS 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1817 HQRDVTRSLIKSKIDNAKSFEWLSQMRFYFDPKQTDVLQQLSIQMAnakfnYGFEYLGVQDKLVQTPLTDRCYLTMTQAL 1896
Cdd:COG5245 870 RIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKRFIKVRSSYRSA-----EMFAKNTIPFFVFEHSMDTSQHQKLFEAV 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1897 EARLggSPFgpAGTGKTESVKALGHQLGRFVlvfncdETFDFQAmgRIFVGLCQVGAWGcFDEFNRLEERMLsAVSQQVQ 1976
Cdd:COG5245 945 CDEV--CRF--VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR-TILVDEY 1010
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1977 CIQEALREHSNPNydktsapitcELLNKQVKVSPDMAIFITMNPgyagRSNLPDNLKKLFRSLAMTKPDRQLIAQvmlys 2056
Cdd:COG5245 1011 LNSDEFRMLEELN----------SAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGAIKSR----- 1071
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2057 qgfrtAEVLANKIVPFFKLCDEQLSSQSHYDFglRALKSVLvsagnvkreriQKIKREKEERGEAVDEGEIAENLPeqei 2136
Cdd:COG5245 1072 -----RESLDREIGAFNNEVDGIAREEDELMF--YPMFKSL-----------KAKHRMLEEKTEYLNKILSITGLP---- 1129
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2137 liqSVCETMVPklvaedipllfslLSDVFPGvqyhrgEMTALREelKKVCQEMYltygDGEEVGGMWVEKVLQLYQITQI 2216
Cdd:COG5245 1130 ---LISDTLRE-------------RIDTLDA------EWDSFCR--ISESLKKY----ESQQVSGLDVAQFVSFLRSVDT 1181
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2217 NHGLMMVGPSGSGKSMAWRVLLKALerlegvegvAHIIDPKAIsKDHLYGTLdpntrEWTdGLFTHVLRkiiDSVRGELQ 2296
Cdd:COG5245 1182 GAFHAEYFRVFLCKIKHYTDACDYL---------WHVKSPYVK-KKYFDADM-----ELR-QFFLMFNR---EDMEARLA 1242
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2297 -KRQWIVFDgdvdpEWVENLNSVLDDNKLLTLPNGERlslppnvRIMFEVQDlkyATLATVSRCGMVWFSEDVLSTDMIF 2375
Cdd:COG5245 1243 dSKMEYEVE-----RYVEKTKAEVSSLKLELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRLSTKGVF 1307
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2376 NNFLARLRSiPLDEGEDEAQRRRKGKEDEGEeaaspmlqiqrdaatimqpyfTSNGLVTKALEHAFQLEHIMDLTRLRCL 2455
Cdd:COG5245 1308 LDELGDTKR-YLDECLDFFSCFEEVQKEIDE---------------------LSMVFCADALRFSADLYHIVKERRFSGV 1365
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2456 --GSLFSM-LHQACRNVAQyNANHPDfpmqieqLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPN- 2531
Cdd:COG5245 1366 laGSDASEsLGGKSIELAA-ILEHKD-------LIVEMKRGINDVLKLRIFGDKCRESTPRFYLISDGDLIKDLNERSDy 1437
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2532 --IPIIDYEVSISGE-WSPwqakVPQIEVETHKVAAP-DVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFS 2607
Cdd:COG5245 1438 eeMLIMMFNISAVITnNGS----IAGFELRGERVMLRkEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCP 1513
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2608 ALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMV 2687
Cdd:COG5245 1514 SLRSELITEVKYFNFSTCTMTPSKLSVLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLV 1593
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2688 EHGGFYRTSDQTWVKLERIQFVGACNPPTDPGRKPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAE 2767
Cdd:COG5245 1594 ERQGFWSSIAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSE 1673
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2768 PLTAAMVEFYTMSQERFTQDTQPHYIYSPREMTRWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTD 2847
Cdd:COG5245 1674 ETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSR 1753
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2848 ENIDTVALKHFPNIDREKAMSRPILYSNWLSKDYIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFR 2927
Cdd:COG5245 1754 QDLYDFGLRAIREMIAGHIGEAEITFSMILFFGMACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLL 1833
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2928 QPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQIKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLER 3007
Cdd:COG5245 1834 VVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLED 1913
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3008 MNTLLANGEVPGLFEGDEYATLMTQCKEGAQKEGLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFN 3087
Cdd:COG5245 1914 FNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEKDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGIRSPALKN 1993
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3088 RCVLNWFGDWSTEALYQVGKEFtskMDLEKPNYIVPDYMPVVydKLPQPPSHREAIVNSCVFVHQTLHQANARLAkrggr 3167
Cdd:COG5245 1994 RCFIDFKKLWDTEEMSQYANSV---ETLSRDGGRVFFINGEL--GVGKGALISEVFGDDAVVIEGRGFEISMIEG----- 2063
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3168 TMAITPRHYLDFINHYANLFHEKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQ 3247
Cdd:COG5245 2064 SLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGER 2143
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3248 QEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLL 3327
Cdd:COG5245 2144 LEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDL 2223
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3328 LGESTTDWKQIRSIIMRENFIPTIVNFSAE-EISDAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADML 3406
Cdd:COG5245 2224 LGFEAKIWFGEQQSLRRDDFIRIIGKYPDEiEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVL 2303
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3407 KRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAER 3486
Cdd:COG5245 2304 EVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINED 2383
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3487 ERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYFDQQMRQNLFTTwSHHLQQANIQFRTDIART--EYLSNADERLRWQA 3564
Cdd:COG5245 2384 SEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIRRRQfiTEGVQKIEDFKEEA 2462
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3565 SSlpaDDLCTENA-IMLKRFNRYPLIIDPSGQATEFIMNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDP 3643
Cdd:COG5245 2463 CS---TDYGLENSrIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEALDE 2539
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3644 VLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPD 3723
Cdd:COG5245 2540 EIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGP 2619
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3724 VDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRILDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLP 3803
Cdd:COG5245 2620 LFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNA 2699
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3804 LSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVLyenpNLKGVTDHTQRLSIITKDLFqvafnrvargMLHQDHITF 3883
Cdd:COG5245 2700 SVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWR----RMKSKYLCAIRYMLMSSEWI----------LDHEDRSGF 2765
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3884 AMLLariklkgtvgeptydaEFQHFLRGNEIVLSagstpriqgLTVEQAEAVVRLSCLPAFKDLIakVQADEQFGiwLDS 3963
Cdd:COG5245 2766 IHRL----------------DVSFLLRTKRFVST---------LLEDKNYRQVLSSCSLYGNDVI--SHSCDRFD--RDV 2816
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3964 SSPEQTVPYLWSEETpatpigqaihRLLLIQAFRPDRLLAMAHMFVSTNLGEsFMSIMEqplDLTHIVGTEVKPNTPVLM 4043
Cdd:COG5245 2817 YRALKHQMDNRTHST----------ILTSNSKTNPYKEYTYNDSWAEAFEVE-DSGDLY---KFEEGLLELIVGHAPLIY 2882
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4044 CsvpgydasgHVEDLAAEQNTQitsiAIGSAEGFNQADKAINTAVKSGRWVMLKNVHLAPGWLMQL-----EKKLHSLQP 4118
Cdd:COG5245 2883 A---------HKKSLENERNVD----RLGSKENEVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYvedvvYPIKASRVC 2949
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4119 HACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRTFSSIPVSrICKSPNERARLYFLLAWFHAIIQERLRYAP 4198
Cdd:COG5245 2950 GKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLVEIDRYP-FDYTLVIACDDAFYLSWEHAAVASVISAGP 3028
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4199 LGWSKKYEFGESDLRSACDTVDTWLddtAKGRQNispdKIPWSALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTtrSF 4278
Cdd:COG5245 3029 KENNEEIYFGDKDFEFKTHLLKNIL---FLNHLN----ARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGA--HE 3099
|
3290 3300 3310 3320 3330
....*....|....*....|....*....|....*....|....*....|...
gi 33350932 4279 DSEFKLACKVDGHKDIQ--MPDGIRREEFVQWVELLPDTQTPSWLGLPNNAER 4329
Cdd:COG5245 3100 TSSQILASVPGGDPELVkfHMEEMCRSSAFGVIGQLPDLALCAWLMGPCDSEY 3152
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1868-2231 |
5.33e-171 |
|
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: 529.75 E-value: 5.33e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1868 YGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALGHQLGRFVLVFNCDETFDFQAMGRIFVG 1947
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1948 LCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNpnydktsapiTCELLNKQVKVSPDMAIFITMNPGYAGRSN 2027
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLK----------TFVFEGSEIKLNPSCGIFITMNPGYAGRTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2028 LPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQLSSQSHYDFGLRALKSVLVSAGNVKRER 2107
Cdd:pfam12774 151 LPDNLKALFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2108 iqkikrekeergeavdegeiaENLPEQEILIQSVCETMVPKLVAEDIPLLFSLLSDVFPGVQYHRGEMTALREELKKVCQ 2187
Cdd:pfam12774 231 ---------------------PNLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCK 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 33350932 2188 EMYLTYGDgeevggMWVEKVLQLYQITQINHGLMMVGPSGSGKS 2231
Cdd:pfam12774 290 ELGLQPHD------AFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
242-832 |
1.17e-142 |
|
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: 458.58 E-value: 1.17e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 242 LNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDTG 321
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKALDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 322 LKQALETVNDYNPLMKDF--PLNDLLSATELDKIRQALVAIFTHLRKI-RNTKY--PIQRALRLVEAISRDLSSQLLKVL 396
Cdd:pfam08385 81 LTDALNEAKDNVKYLKTLerPFEDLEELTDPPEIIEAIPPLMNTIRLIwSISRYynTSERMTVLLEKISNQLIEQCKKYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 397 GTRKLMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKReenlkmvWRINPAHR-----KLQARLDQMRKFRR 471
Cdd:pfam08385 161 SPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERP-------WDFSERYIfgrfdAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 472 QHEQLRAV--IVRVLRPQVTAVaqqnqgevpepqdmkVAEVlfdaadanaIEEVNLAYENVKEV--DGLDVSKEGteaWE 547
Cdd:pfam08385 234 TIEQFSKLekIGGTKGPELEGV---------------IEEI---------LEEFQEAYKVFKSKtyDILDVSNEG---FD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 548 AAMKRYDERIDRVETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQY 627
Cdd:pfam08385 287 DDYEEFKERIKDLERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 628 pqsQACKMSHvRDLPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGweNHVEGQKLKQDGDSFRMKLN--TQEIFDDWARK 705
Cdd:pfam08385 367 ---YNPSPIA-KNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLL--KHAEGKKVIKKYNELAKKLDeyERLIYEAWLKE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 706 VQQRNLGVSGR-IFTIESTRVRgrtgnvlKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIES 784
Cdd:pfam08385 441 VEEASEGNLKRpLLVRHPETGK-------LLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELL 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 33350932 785 VRTYERTCEKV--EERNtislLVAGLKKEVQALIAEGI-ALVWESYKLDPY 832
Cdd:pfam08385 514 VRWYNKIRSTLlpVERP----LLAPHLKDIDEKLEPGLtTLTWNSLGIDEY 560
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4333-4644 |
6.24e-62 |
|
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: 215.56 E-value: 6.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4333 TTQGVDMISKMLKMQMLEDEDdlayAETEKKTRTDstsdgrpawmrTLHTTASNWLHLIPQTLSH---LKRTVENIKDPL 4409
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSG----GGGGGSSREE-----------IVLELAKDILEKLPEPFDIeeaEEKYPVGYEDPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4410 FRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVSDFSERIKQL 4489
Cdd:pfam18199 66 NTVLLQEIERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLKQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4490 QNISLAaasggakELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVT--TSQGATLDACSFG--VTGLKL 4565
Cdd:pfam18199 146 QDWLDD-------EGPPKVFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTkkVSPEEVTEPPEDGvyVHGLFL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4566 QGATCN--NNKL--SLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGVA 4641
Cdd:pfam18199 219 EGARWDrkNGCLveSEPKELFSPLPVIHLKPVESDKKKLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVA 298
|
...
gi 33350932 4642 VLC 4644
Cdd:pfam18199 299 LLL 301
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2570-2733 |
2.38e-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: 64.86 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2570 PTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRAL--PDMEVVGLNFSSATTPELLLKTFDHYCEYRRTpng 2647
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2648 vvlAPVQLGKWLVLFCDEIN-LPDMDKYGTQRVISFIRQMVEhggfyrtsdqtwvKLERIQFVGACNPPTDPG-RKPLSH 2725
Cdd:cd00009 78 ---ELAEKAKPGVLFIDEIDsLSRGAQNALLRVLETLNDLRI-------------DRENVRVIGATNRPLLGDlDRALYD 141
|
....*...
gi 33350932 2726 RFLRHVPV 2733
Cdd:cd00009 142 RLDIRIVI 149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3187-3500 |
2.23e-07 |
|
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: 57.76 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3187 FHEKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHK 3266
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3267 QQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQHlVEVRSMANPPAAVKLALESIcllLGESTTDWKQIRSIImren 3346
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-ESLEAELEELEAELEELESR---LEELEEQLETLRSKV---- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3347 fiptivnfsaeeisDAIREKMKKNymsnpsyNYEIVNRASLacgpmvkwaIAQLNyadmlKRVEPLRNELQKLEDDAKDN 3426
Cdd:TIGR02168 389 --------------AQLELQIASL-------NNEIERLEAR---------LERLE-----DRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33350932 3427 QQKA-----NEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQM 3500
Cdd:TIGR02168 434 ELKElqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2588-2737 |
2.42e-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: 50.45 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2588 HKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRRTPNG-------VVLAPVQLGKWLV 2660
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGsgelrlrLALALARKLKPDV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33350932 2661 LFCDEINLpdMDKYGTQRVISFIRQMVEHGGFYRTsdqtwvklERIQFVGACNPPTDPGRKPLSHRFLRHVPVVYVD 2737
Cdd:smart00382 82 LILDEITS--LLDAEQEALLLLLEELRLLLLLKSE--------KNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
3189-3561 |
2.54e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3189 EKRSELEEQQMHLNvglrkikETVDQVEELRRDLRIKSQELEvknaAANDKLKKMVKD--QQEAEKKKVMS-QEIQEQLH 3265
Cdd:PRK04863 297 TSRRQLAAEQYRLV-------EMARELAELNEAESDLEQDYQ----AASDHLNLVQTAlrQQEKIERYQADlEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3266 KQQEVIADKQmsvkEDLDKVEPAVIEAQNAVKSIKKQ------HLVEVRSMANPPAAVKLALESICLLLGESTTDWkqir 3339
Cdd:PRK04863 366 EQNEVVEEAD----EQQEENEARAEAAEEEVDELKSQladyqqALDVQQTRAIQYQQAVQALERAKQLCGLPDLTA---- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3340 siimrENFIPTIVNFSAEE---------------ISDAIREKMKKNYMSNPSYNYEIV-NRASlacgpmvKWAIAQLNYA 3403
Cdd:PRK04863 438 -----DNAEDWLEEFQAKEqeateellsleqklsVAQAAHSQFEQAYQLVRKIAGEVSrSEAW-------DVARELLRRL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3404 DMLK----RVEPLRNELQKLEDDAKdNQQKAN------------------EVEQMIRDLEASIARYKEEYAVLISEAQAI 3461
Cdd:PRK04863 506 REQRhlaeQLQQLRMRLSELEQRLR-QQQRAErllaefckrlgknlddedELEQLQEELEARLESLSESVSEARERRMAL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3462 KADLAAVEAKVNRstallksLSAERERWEKTSETFkNQMSTIAGDCLLSAAFIayagyfDQQMRQNLFTTWShhLQQANI 3541
Cdd:PRK04863 585 RQQLEQLQARIQR-------LAARAPAWLAAQDAL-ARLREQSGEEFEDSQDV------TEYMQQLLERERE--LTVERD 648
|
410 420
....*....|....*....|....*...
gi 33350932 3542 QFRTDI----ARTEYLSNA----DERLR 3561
Cdd:PRK04863 649 ELAARKqaldEEIERLSQPggseDPRLN 676
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1046-4329 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 1192.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1046 EVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEF-GPVVIDYGKVQSKVNLKYDSWh 1124
Cdd:COG5245 170 SVCSERDGFYEEKSFWSRFHMEMCHIREFCRSKAFRFACDVLRKSGKYVTVATLDSLlSSSKYSELGRRLHFYANMDFS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1125 kevlskfGQMLGSNMTEFHSQISKSRQEL--EQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQRF 1202
Cdd:COG5245 249 -------GIYFPKSFSEFKDSVISATQAVsrDIGRQSRMARRLILVQMDSLARLIVDRICEYVSIEWLGCCEELLTCSME 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1203 QFPPSWLYIDNIEgewgafNDIMRRKDSAIQQQvaNLQMKIVQEDRAVESRTTDLLTDWE-----KTKPVTGNLRPEEAL 1277
Cdd:COG5245 322 SMSSLVNSFDGEE------SEAMSLESSLFYEF--RGGEHLAGFYSAFGDIKRILLFTWSfkklgTLLPSLPGYSSGGMD 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1278 QALTIYEGKFGRLKDDREKCAKAKEALELTDTgllsgSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQpr 1357
Cdd:COG5245 394 YGEEYRSLLWELGSEVGDPDSGPVRKWMRKDL-----FDAKVRSGVSFGKQEEFVSDIFNITFERIHGMDPTTLEDDE-- 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1358 KLRQNLDALLNQlksfpARLRQYASYEFVQRLlkgYMKINML------VIELKSEALKdrHWKQLMKrlhvnwvvseltl 1431
Cdd:COG5245 467 EDTPALAILLGQ-----EEAGRFVKLCKIMRM---FSFFNSLemfsrrTLANRMAIVK--YLSSVVR------------- 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1432 gqIWDVDLQKN-----EAIVKDVLLVAqgEMALEEFLKQIREVWNTYELDLVNYQNKC------RLIRGWddlfnkVKEH 1500
Cdd:COG5245 524 --TGPLFLQRDffgrmSELLMARDMFM--EVDGVLRLFFGGEWSGIVQLSGIRRAKRCverqidDEIREW------CSSV 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1501 INSVSAMKLSPYykvFEEDAlsweDKLNRIMALFDVWIdvqRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMK 1580
Cdd:COG5245 594 LSDDFLEERAVR---VERGA----DGARRLRASSGSPV---LRRLDEYLMMMSLEDLMPLIPHAVHRKMSLVSGVRGIYK 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1581 KVSKSPLVMDVLNIQgVQRSLERLADLLGKIQKALGEYLERERSSFPRFyfVGDEDLLEIIGNSKNVAKLQKHFKKMFAG 1660
Cdd:COG5245 664 RVVSGCEAINTILED-VGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRVRELENRVYSYRFFVKKIAK 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1661 VSSIILNEDNsvVLGISSREGEEVMFKTPVSITEHPKINEWLTlvEKEMRVtLAKLLaesvtevEIFGKATSIDPNTYIt 1740
Cdd:COG5245 741 EEMKTVFSSR--IQKKEPFSLDSEAYVGFFRLYEKSIVIRGIN--RSMGRV-LSQYL-------ESVQEALEIEDGSFF- 807
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1741 wIDKYQAQLVVLSAQIaWSENVETALSSmggggdaaPLHSVLSNVEVT----LNVLADSVLmeqpplrrRKLEHLITELV 1816
Cdd:COG5245 808 -VSRHRVRDGGLEKGR-GCDAWENCFDP--------PLSEYFRILEKIfpseEGYFFDEVL--------KRLDPGHEIKS 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1817 HQRDVTRSLIKSKIDNAKSFEWLSQMRFYFDPKQTDVLQQLSIQMAnakfnYGFEYLGVQDKLVQTPLTDRCYLTMTQAL 1896
Cdd:COG5245 870 RIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKRFIKVRSSYRSA-----EMFAKNTIPFFVFEHSMDTSQHQKLFEAV 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1897 EARLggSPFgpAGTGKTESVKALGHQLGRFVlvfncdETFDFQAmgRIFVGLCQVGAWGcFDEFNRLEERMLsAVSQQVQ 1976
Cdd:COG5245 945 CDEV--CRF--VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR-TILVDEY 1010
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1977 CIQEALREHSNPNydktsapitcELLNKQVKVSPDMAIFITMNPgyagRSNLPDNLKKLFRSLAMTKPDRQLIAQvmlys 2056
Cdd:COG5245 1011 LNSDEFRMLEELN----------SAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGAIKSR----- 1071
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2057 qgfrtAEVLANKIVPFFKLCDEQLSSQSHYDFglRALKSVLvsagnvkreriQKIKREKEERGEAVDEGEIAENLPeqei 2136
Cdd:COG5245 1072 -----RESLDREIGAFNNEVDGIAREEDELMF--YPMFKSL-----------KAKHRMLEEKTEYLNKILSITGLP---- 1129
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2137 liqSVCETMVPklvaedipllfslLSDVFPGvqyhrgEMTALREelKKVCQEMYltygDGEEVGGMWVEKVLQLYQITQI 2216
Cdd:COG5245 1130 ---LISDTLRE-------------RIDTLDA------EWDSFCR--ISESLKKY----ESQQVSGLDVAQFVSFLRSVDT 1181
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2217 NHGLMMVGPSGSGKSMAWRVLLKALerlegvegvAHIIDPKAIsKDHLYGTLdpntrEWTdGLFTHVLRkiiDSVRGELQ 2296
Cdd:COG5245 1182 GAFHAEYFRVFLCKIKHYTDACDYL---------WHVKSPYVK-KKYFDADM-----ELR-QFFLMFNR---EDMEARLA 1242
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2297 -KRQWIVFDgdvdpEWVENLNSVLDDNKLLTLPNGERlslppnvRIMFEVQDlkyATLATVSRCGMVWFSEDVLSTDMIF 2375
Cdd:COG5245 1243 dSKMEYEVE-----RYVEKTKAEVSSLKLELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRLSTKGVF 1307
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2376 NNFLARLRSiPLDEGEDEAQRRRKGKEDEGEeaaspmlqiqrdaatimqpyfTSNGLVTKALEHAFQLEHIMDLTRLRCL 2455
Cdd:COG5245 1308 LDELGDTKR-YLDECLDFFSCFEEVQKEIDE---------------------LSMVFCADALRFSADLYHIVKERRFSGV 1365
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2456 --GSLFSM-LHQACRNVAQyNANHPDfpmqieqLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPN- 2531
Cdd:COG5245 1366 laGSDASEsLGGKSIELAA-ILEHKD-------LIVEMKRGINDVLKLRIFGDKCRESTPRFYLISDGDLIKDLNERSDy 1437
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2532 --IPIIDYEVSISGE-WSPwqakVPQIEVETHKVAAP-DVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFS 2607
Cdd:COG5245 1438 eeMLIMMFNISAVITnNGS----IAGFELRGERVMLRkEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCP 1513
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2608 ALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMV 2687
Cdd:COG5245 1514 SLRSELITEVKYFNFSTCTMTPSKLSVLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLV 1593
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2688 EHGGFYRTSDQTWVKLERIQFVGACNPPTDPGRKPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAE 2767
Cdd:COG5245 1594 ERQGFWSSIAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSE 1673
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2768 PLTAAMVEFYTMSQERFTQDTQPHYIYSPREMTRWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTD 2847
Cdd:COG5245 1674 ETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSR 1753
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2848 ENIDTVALKHFPNIDREKAMSRPILYSNWLSKDYIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFR 2927
Cdd:COG5245 1754 QDLYDFGLRAIREMIAGHIGEAEITFSMILFFGMACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLL 1833
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2928 QPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQIKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLER 3007
Cdd:COG5245 1834 VVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLED 1913
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3008 MNTLLANGEVPGLFEGDEYATLMTQCKEGAQKEGLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFN 3087
Cdd:COG5245 1914 FNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEKDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGIRSPALKN 1993
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3088 RCVLNWFGDWSTEALYQVGKEFtskMDLEKPNYIVPDYMPVVydKLPQPPSHREAIVNSCVFVHQTLHQANARLAkrggr 3167
Cdd:COG5245 1994 RCFIDFKKLWDTEEMSQYANSV---ETLSRDGGRVFFINGEL--GVGKGALISEVFGDDAVVIEGRGFEISMIEG----- 2063
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3168 TMAITPRHYLDFINHYANLFHEKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQ 3247
Cdd:COG5245 2064 SLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGER 2143
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3248 QEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLL 3327
Cdd:COG5245 2144 LEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDL 2223
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3328 LGESTTDWKQIRSIIMRENFIPTIVNFSAE-EISDAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADML 3406
Cdd:COG5245 2224 LGFEAKIWFGEQQSLRRDDFIRIIGKYPDEiEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVL 2303
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3407 KRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAER 3486
Cdd:COG5245 2304 EVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINED 2383
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3487 ERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYFDQQMRQNLFTTwSHHLQQANIQFRTDIART--EYLSNADERLRWQA 3564
Cdd:COG5245 2384 SEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIRRRQfiTEGVQKIEDFKEEA 2462
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3565 SSlpaDDLCTENA-IMLKRFNRYPLIIDPSGQATEFIMNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDP 3643
Cdd:COG5245 2463 CS---TDYGLENSrIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEALDE 2539
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3644 VLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPD 3723
Cdd:COG5245 2540 EIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGP 2619
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3724 VDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRILDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLP 3803
Cdd:COG5245 2620 LFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNA 2699
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3804 LSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVLyenpNLKGVTDHTQRLSIITKDLFqvafnrvargMLHQDHITF 3883
Cdd:COG5245 2700 SVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWR----RMKSKYLCAIRYMLMSSEWI----------LDHEDRSGF 2765
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3884 AMLLariklkgtvgeptydaEFQHFLRGNEIVLSagstpriqgLTVEQAEAVVRLSCLPAFKDLIakVQADEQFGiwLDS 3963
Cdd:COG5245 2766 IHRL----------------DVSFLLRTKRFVST---------LLEDKNYRQVLSSCSLYGNDVI--SHSCDRFD--RDV 2816
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3964 SSPEQTVPYLWSEETpatpigqaihRLLLIQAFRPDRLLAMAHMFVSTNLGEsFMSIMEqplDLTHIVGTEVKPNTPVLM 4043
Cdd:COG5245 2817 YRALKHQMDNRTHST----------ILTSNSKTNPYKEYTYNDSWAEAFEVE-DSGDLY---KFEEGLLELIVGHAPLIY 2882
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4044 CsvpgydasgHVEDLAAEQNTQitsiAIGSAEGFNQADKAINTAVKSGRWVMLKNVHLAPGWLMQL-----EKKLHSLQP 4118
Cdd:COG5245 2883 A---------HKKSLENERNVD----RLGSKENEVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYvedvvYPIKASRVC 2949
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4119 HACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRTFSSIPVSrICKSPNERARLYFLLAWFHAIIQERLRYAP 4198
Cdd:COG5245 2950 GKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLVEIDRYP-FDYTLVIACDDAFYLSWEHAAVASVISAGP 3028
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4199 LGWSKKYEFGESDLRSACDTVDTWLddtAKGRQNispdKIPWSALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTtrSF 4278
Cdd:COG5245 3029 KENNEEIYFGDKDFEFKTHLLKNIL---FLNHLN----ARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGA--HE 3099
|
3290 3300 3310 3320 3330
....*....|....*....|....*....|....*....|....*....|...
gi 33350932 4279 DSEFKLACKVDGHKDIQ--MPDGIRREEFVQWVELLPDTQTPSWLGLPNNAER 4329
Cdd:COG5245 3100 TSSQILASVPGGDPELVkfHMEEMCRSSAFGVIGQLPDLALCAWLMGPCDSEY 3152
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1868-2231 |
5.33e-171 |
|
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: 529.75 E-value: 5.33e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1868 YGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALGHQLGRFVLVFNCDETFDFQAMGRIFVG 1947
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1948 LCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNpnydktsapiTCELLNKQVKVSPDMAIFITMNPGYAGRSN 2027
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLK----------TFVFEGSEIKLNPSCGIFITMNPGYAGRTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2028 LPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQLSSQSHYDFGLRALKSVLVSAGNVKRER 2107
Cdd:pfam12774 151 LPDNLKALFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2108 iqkikrekeergeavdegeiaENLPEQEILIQSVCETMVPKLVAEDIPLLFSLLSDVFPGVQYHRGEMTALREELKKVCQ 2187
Cdd:pfam12774 231 ---------------------PNLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCK 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 33350932 2188 EMYLTYGDgeevggMWVEKVLQLYQITQINHGLMMVGPSGSGKS 2231
Cdd:pfam12774 290 ELGLQPHD------AFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
242-832 |
1.17e-142 |
|
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: 458.58 E-value: 1.17e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 242 LNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDTG 321
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKALDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 322 LKQALETVNDYNPLMKDF--PLNDLLSATELDKIRQALVAIFTHLRKI-RNTKY--PIQRALRLVEAISRDLSSQLLKVL 396
Cdd:pfam08385 81 LTDALNEAKDNVKYLKTLerPFEDLEELTDPPEIIEAIPPLMNTIRLIwSISRYynTSERMTVLLEKISNQLIEQCKKYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 397 GTRKLMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKReenlkmvWRINPAHR-----KLQARLDQMRKFRR 471
Cdd:pfam08385 161 SPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERP-------WDFSERYIfgrfdAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 472 QHEQLRAV--IVRVLRPQVTAVaqqnqgevpepqdmkVAEVlfdaadanaIEEVNLAYENVKEV--DGLDVSKEGteaWE 547
Cdd:pfam08385 234 TIEQFSKLekIGGTKGPELEGV---------------IEEI---------LEEFQEAYKVFKSKtyDILDVSNEG---FD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 548 AAMKRYDERIDRVETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQY 627
Cdd:pfam08385 287 DDYEEFKERIKDLERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 628 pqsQACKMSHvRDLPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGweNHVEGQKLKQDGDSFRMKLN--TQEIFDDWARK 705
Cdd:pfam08385 367 ---YNPSPIA-KNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLL--KHAEGKKVIKKYNELAKKLDeyERLIYEAWLKE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 706 VQQRNLGVSGR-IFTIESTRVRgrtgnvlKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIES 784
Cdd:pfam08385 441 VEEASEGNLKRpLLVRHPETGK-------LLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELL 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 33350932 785 VRTYERTCEKV--EERNtislLVAGLKKEVQALIAEGI-ALVWESYKLDPY 832
Cdd:pfam08385 514 VRWYNKIRSTLlpVERP----LLAPHLKDIDEKLEPGLtTLTWNSLGIDEY 560
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1319-1720 |
1.34e-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: 451.71 E-value: 1.34e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1319 VQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLRQNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINM 1398
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1399 LVIELKSEALKDRHWKQLMKRLHVNW--VVSELTLGQIWDVDLQKNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELD 1476
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFdpLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1477 LVNYQN-KCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDALSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSa 1555
Cdd:pfam08393 161 LVPYKDtGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSSE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1556 DIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRSLERLADLLGKIQKALGEYLERERSSFPRFYFVGDE 1635
Cdd:pfam08393 240 DIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSND 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1636 DLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVlGISSREGEEVMFKTPVSITEhPKINEWLTLVEKEMRVTLAK 1715
Cdd:pfam08393 320 ELLEILSQTKDPTRVQPHLKKCFEGIASLEFDENKEIT-GMISKEGEVVPFSKPPVEAK-GNVEEWLNELEEEMRETLRD 397
|
....*
gi 33350932 1716 LLAES 1720
Cdd:pfam08393 398 LLKEA 402
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3560-3780 |
3.31e-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: 319.39 E-value: 3.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3560 LRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFIMNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDV- 3638
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3639 ESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLK 3718
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33350932 3719 AERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRILDDDTIITTLENLKREAAEV 3780
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 ... |
2908-3186 |
7.28e-70 |
|
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: 236.74 E-value: 7.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2908 PLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQIKVHRKYTGEDFDEDLRTVLRRSGCKN 2987
Cdd:pfam12780 2 DLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2988 EKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKEGLmLDSHEELYKWFTSQVIRNLHVVFT 3067
Cdd:pfam12780 82 KPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNI-EDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3068 MNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKpnyivpdympvvydklpqppSHREAIVNSC 3147
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDIEIPE--------------------ELKSNVVKVF 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 33350932 3148 VFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANL 3186
Cdd:pfam12780 221 VYVHSSVEDMSKKFYEELKRKNYVTPKSYLELLRLYKNL 259
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4333-4644 |
6.24e-62 |
|
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: 215.56 E-value: 6.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4333 TTQGVDMISKMLKMQMLEDEDdlayAETEKKTRTDstsdgrpawmrTLHTTASNWLHLIPQTLSH---LKRTVENIKDPL 4409
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSG----GGGGGSSREE-----------IVLELAKDILEKLPEPFDIeeaEEKYPVGYEDPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4410 FRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVSDFSERIKQL 4489
Cdd:pfam18199 66 NTVLLQEIERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLKQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4490 QNISLAaasggakELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVT--TSQGATLDACSFG--VTGLKL 4565
Cdd:pfam18199 146 QDWLDD-------EGPPKVFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTkkVSPEEVTEPPEDGvyVHGLFL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4566 QGATCN--NNKL--SLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGVA 4641
Cdd:pfam18199 219 EGARWDrkNGCLveSEPKELFSPLPVIHLKPVESDKKKLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVA 298
|
...
gi 33350932 4642 VLC 4644
Cdd:pfam18199 299 LLL 301
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
4176-4327 |
4.29e-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: 192.28 E-value: 4.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4176 RARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDtakgrqniSPDKIPWSALKTLMAQSIYGGR 4255
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDE--------YDEKIPWDALRYLIGEINYGGR 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33350932 4256 VDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVdghkdIQMPDGIRREEFVQWVELLPDTQTPSWLGLPNNA 4327
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 ... |
3201-3536 |
5.20e-45 |
|
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: 168.33 E-value: 5.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3201 LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAAnDKLKKMVK-DQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVK 3279
Cdd:pfam12777 3 LENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDA-DKLIQVVGiEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3280 EDLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLL---GESTTD--WKQIRSIIMR-ENFIPTIVN 3353
Cdd:pfam12777 82 EDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMapgGKIPKDksWKAAKIMMAKvDGFLDSLIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3354 FSAEEISDAIREKMKKnYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEV 3433
Cdd:pfam12777 162 FDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3434 EQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAF 3513
Cdd:pfam12777 241 KAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISAF 320
|
330 340
....*....|....*....|....
gi 33350932 3514 IAYAGYFDQQMRQNLF-TTWSHHL 3536
Cdd:pfam12777 321 ISYLGFFTKKYRNELLdKFWIPYI 344
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2566-2730 |
6.76e-45 |
|
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: 161.79 E-value: 6.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2566 DVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALP--DMEVVGLNFSSATTPELLLKTFDHYCEYRR 2643
Cdd:pfam12775 9 EILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDkeKYLPLFINFSAQTTSNQTQDIIESKLEKRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2644 tpnGVVLAPVqLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTdPGRKPL 2723
Cdd:pfam12775 89 ---KGVYGPP-GGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPG-GGRNDI 163
|
....*..
gi 33350932 2724 SHRFLRH 2730
Cdd:pfam12775 164 TPRLLRH 170
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
4036-4146 |
9.72e-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: 136.04 E-value: 9.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 4036 KPNTPVLMCSVPGYDASGHVEDLAAEQN--TQITSIAIGSAEGFnQADKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKL 4113
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGfgGKLHSISLGQGQGP-IAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKIL 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 33350932 4114 HSLQ---PHACFRLFLTMEINPKVPVNLLRAGRIFV 4146
Cdd:pfam03028 80 EELPeetLHPDFRLWLTSEPSPKFPISILQNSIKIT 115
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2423-2549 |
2.91e-23 |
|
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: 98.12 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2423 MQPYFtsNGLVTKALEHAFQ-LEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPdfpMQIEQLERYIQRYLVYAILWS 2501
Cdd:pfam17852 1 LEPLF--EWLVPPALEFVRKnCKEIVPTSDLNLVQSLCRLLESLLDEVLEYNGVHP---LSPDKLKEYLEKLFLFALVWS 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 33350932 2502 LSGDSRLKMRAELGEYIRRITT-VPLPTAPNIPIIDYEVSI-SGEWSPWQ 2549
Cdd:pfam17852 76 IGGTLDEDSRKKFDEFLRELFSgLDLPPPEKGTVYDYFVDLeKGEWVPWS 125
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2219-2359 |
8.68e-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: 74.25 E-value: 8.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2219 GLMMVGPSGSGKSMAWRVLLKALERLEGVEGVAHiidpKAISKDHLYGTLDPNTR--EWTDGLFTHVLRKiidsvrgelq 2296
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLT----RDTTEEDLFGRRNIDPGgaSWVDGPLVRAARE---------- 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33350932 2297 krQWIVFDGDVD---PEWVENLNSVLDDNKLLTLPNGERLSLPP-NVRIMFEV----QDLKYATLATVSRC 2359
Cdd:pfam07728 67 --GEIAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMnpldRGLNELSPALRSRF 135
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2570-2733 |
2.38e-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: 64.86 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2570 PTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRAL--PDMEVVGLNFSSATTPELLLKTFDHYCEYRRTpng 2647
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2648 vvlAPVQLGKWLVLFCDEIN-LPDMDKYGTQRVISFIRQMVEhggfyrtsdqtwvKLERIQFVGACNPPTDPG-RKPLSH 2725
Cdd:cd00009 78 ---ELAEKAKPGVLFIDEIDsLSRGAQNALLRVLETLNDLRI-------------DRENVRVIGATNRPLLGDlDRALYD 141
|
....*...
gi 33350932 2726 RFLRHVPV 2733
Cdd:cd00009 142 RLDIRIVI 149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3187-3500 |
2.23e-07 |
|
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: 57.76 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3187 FHEKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHK 3266
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3267 QQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQHlVEVRSMANPPAAVKLALESIcllLGESTTDWKQIRSIImren 3346
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-ESLEAELEELEAELEELESR---LEELEEQLETLRSKV---- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3347 fiptivnfsaeeisDAIREKMKKNymsnpsyNYEIVNRASLacgpmvkwaIAQLNyadmlKRVEPLRNELQKLEDDAKDN 3426
Cdd:TIGR02168 389 --------------AQLELQIASL-------NNEIERLEAR---------LERLE-----DRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33350932 3427 QQKA-----NEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQM 3500
Cdd:TIGR02168 434 ELKElqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3174-3517 |
6.63e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3174 RHYLDFINHYANLF--HEKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKK----MVKDQ 3247
Cdd:COG4717 115 REELEKLEKLLQLLplYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEEL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3248 QEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKEDLDKVEPAViEAQNAVKSIKKQHLV----------------EVRSMA 3311
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-EAAALEERLKEARLLlliaaallallglggsLLSLIL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3312 NPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIvnfsaEEISDAIREKMKKNYMSNPSYNYEIVNRASLAcgp 3391
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL-----EELEEEELEELLAALGLPPDLSPEELLELLDR--- 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3392 MVKWAIAQLNYADMLKR--VEPLRNELQKLEDDAK-----------DNQQKANEVEQMIRDLEASIARYKEEyavliSEA 3458
Cdd:COG4717 346 IEELQELLREAEELEEElqLEELEQEIAALLAEAGvedeeelraalEQAEEYQELKEELEELEEQLEELLGE-----LEE 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 33350932 3459 QAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYA 3517
Cdd:COG4717 421 LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELE 479
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2588-2737 |
2.42e-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: 50.45 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2588 HKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRRTPNG-------VVLAPVQLGKWLV 2660
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGsgelrlrLALALARKLKPDV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33350932 2661 LFCDEINLpdMDKYGTQRVISFIRQMVEHGGFYRTsdqtwvklERIQFVGACNPPTDPGRKPLSHRFLRHVPVVYVD 2737
Cdd:smart00382 82 LILDEITS--LLDAEQEALLLLLEELRLLLLLKSE--------KNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2922-3012 |
1.96e-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: 47.53 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2922 IDRIFRQPQGHLLLIGVSGAGKTTLSRFVAW---MNGLSVYQIKVHRKYTGEDFDEDLRTVLRRS----GCKNEKIAFIM 2994
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASDLLEGLVVAELFGHFLVRLlfelAEKAKPGVLFI 90
|
90
....*....|....*...
gi 33350932 2995 DESNVLDSGFLERMNTLL 3012
Cdd:cd00009 91 DEIDSLSRGAQNALLRVL 108
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
3189-3561 |
2.54e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3189 EKRSELEEQQMHLNvglrkikETVDQVEELRRDLRIKSQELEvknaAANDKLKKMVKD--QQEAEKKKVMS-QEIQEQLH 3265
Cdd:PRK04863 297 TSRRQLAAEQYRLV-------EMARELAELNEAESDLEQDYQ----AASDHLNLVQTAlrQQEKIERYQADlEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3266 KQQEVIADKQmsvkEDLDKVEPAVIEAQNAVKSIKKQ------HLVEVRSMANPPAAVKLALESICLLLGESTTDWkqir 3339
Cdd:PRK04863 366 EQNEVVEEAD----EQQEENEARAEAAEEEVDELKSQladyqqALDVQQTRAIQYQQAVQALERAKQLCGLPDLTA---- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3340 siimrENFIPTIVNFSAEE---------------ISDAIREKMKKNYMSNPSYNYEIV-NRASlacgpmvKWAIAQLNYA 3403
Cdd:PRK04863 438 -----DNAEDWLEEFQAKEqeateellsleqklsVAQAAHSQFEQAYQLVRKIAGEVSrSEAW-------DVARELLRRL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3404 DMLK----RVEPLRNELQKLEDDAKdNQQKAN------------------EVEQMIRDLEASIARYKEEYAVLISEAQAI 3461
Cdd:PRK04863 506 REQRhlaeQLQQLRMRLSELEQRLR-QQQRAErllaefckrlgknlddedELEQLQEELEARLESLSESVSEARERRMAL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3462 KADLAAVEAKVNRstallksLSAERERWEKTSETFkNQMSTIAGDCLLSAAFIayagyfDQQMRQNLFTTWShhLQQANI 3541
Cdd:PRK04863 585 RQQLEQLQARIQR-------LAARAPAWLAAQDAL-ARLREQSGEEFEDSQDV------TEYMQQLLERERE--LTVERD 648
|
410 420
....*....|....*....|....*...
gi 33350932 3542 QFRTDI----ARTEYLSNA----DERLR 3561
Cdd:PRK04863 649 ELAARKqaldEEIERLSQPggseDPRLN 676
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3234-3488 |
7.51e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3234 AAANDKLKKMVKDQQEAEKKKvmsQEIQEQLHKQQEVIADKQmsvkEDLDKVEPAVIEAQNAVKSIKKQhLVEVRsmanp 3313
Cdd:COG3883 12 AFADPQIQAKQKELSELQAEL---EAAQAELDALQAELEELN----EEYNELQAELEALQAEIDKLQAE-IAEAE----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3314 pAAVKLALEsiclLLGesttdwKQIRSIIMRENFIPTI-VNFSAEEISDAIrekmkknymsnpsynyeivNRASlacgpm 3392
Cdd:COG3883 79 -AEIEERRE----ELG------ERARALYRSGGSVSYLdVLLGSESFSDFL-------------------DRLS------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3393 vkwAIAQLNYADmLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASiaryKEEYAVLISEAQAIKADLAAVEAKV 3472
Cdd:COG3883 123 ---ALSKIADAD-ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA----KAELEAQQAEQEALLAQLSAEEAAA 194
|
250
....*....|....*.
gi 33350932 3473 NRSTALLKSLSAERER 3488
Cdd:COG3883 195 EAQLAELEAELAAAEA 210
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2590-2729 |
9.64e-05 |
|
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: 45.36 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2590 PLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRRTPNGVVLAPVQLGKwlVLFCDEINLP 2669
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAAREGE--IAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33350932 2670 DMDKYGTQ-RVISFIRQMVEHGGFYRTsdqtwVKLERIQFVGACNPPtDPGRKPLSHRFLR 2729
Cdd:pfam07728 79 NPDVLNSLlSLLDERRLLLPDGGELVK-----AAPDGFRLIATMNPL-DRGLNELSPALRS 133
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3189-3490 |
2.68e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3189 EKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAA---ANDKLKKMVKDQQEAEKKKVMSQEIQEQLH 3265
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLLAELARLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3266 KQQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQHlvevrsmanppAAVKLALESICLLLGESTTDWKQIRSIIMRE 3345
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAEL-----------AEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3346 nfIPTIVNFSAEEISDAIREkmkknymsnpsynyeivnraslacgpmvkwAIAQLNYADMLKRVEPLRNELQKLEDDAKD 3425
Cdd:COG1196 392 --LRAAAELAAQLEELEEAE------------------------------EALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33350932 3426 NQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWE 3490
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3189-3485 |
3.38e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3189 EKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEvknaaandklkkmvKDQQEAEKKKVMSQEIQEQLHKQQ 3268
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE--------------KEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3269 EVIADKQMSVKEDLDKVEpAVIEAQNAVKsikkqhlvevrsmanppAAVKLALESICLLLGESttDWKQIRSIImreNFI 3348
Cdd:TIGR02169 747 SSLEQEIENVKSELKELE-ARIEELEEDL-----------------HKLEEALNDLEARLSHS--RIPEIQAEL---SKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3349 PTIVNfSAEEISDAI-----REKMKKNYMSNPSYNYEIVNRAslacgpmvkwaiAQLNYADMLKRVEPLRNELQKLEDDA 3423
Cdd:TIGR02169 804 EEEVS-RIEARLREIeqklnRLTLEKEYLEKEIQELQEQRID------------LKEQIKSIEKEIENLNGKKEELEEEL 870
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33350932 3424 KDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAE 3485
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3402-3485 |
3.72e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3402 YADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVN-RSTALLK 3480
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEaEREELAA 170
|
....*
gi 33350932 3481 SLSAE 3485
Cdd:COG1579 171 KIPPE 175
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2932-3089 |
4.98e-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: 43.05 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2932 HLLLIGVSGAGKTTLS-RFVAWMNGLSVYQIKVHRKYTGEDF----------DEDLRTVLRRSGcKNEKIAFImDESNVL 3000
Cdd:pfam07728 1 GVLLVGPPGTGKTELAeRLAAALSNRPVFYVQLTRDTTEEDLfgrrnidpggASWVDGPLVRAA-REGEIAVL-DEINRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3001 DSGFLERMNTLLANGEVPgLFEGDEYAtlmtqckegaqkeglmldsHEELYkwftsqvirNLHVVFTMNPSSEGLKDraa 3080
Cdd:pfam07728 79 NPDVLNSLLSLLDERRLL-LPDGGELV-------------------KAAPD---------GFRLIATMNPLDRGLNE--- 126
|
....*....
gi 33350932 3081 TSPALFNRC 3089
Cdd:pfam07728 127 LSPALRSRF 135
|
|
| AIP3 |
smart00806 |
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ... |
3191-3323 |
1.50e-03 |
|
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in Saccharomyces cerevisiae that was previously identified as an actin-interacting protein. Actin-interacting protein 3 (Aip3p) localizes at the cell cortex where cytoskeleton assembly must be achieved to execute polarized cell growth, and deletion of AIP3 causes gross defects in cell and cytoskeletal polarity. Aip3p localization is mediated by the secretory pathway, mutations in early- or late-acting components of the secretory apparatus lead to Aip3p mislocalization.
Pssm-ID: 214826 [Multi-domain] Cd Length: 426 Bit Score: 44.66 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3191 RSELEEQQMHLnvgLRKIKETVDQVEELRRDL-----RIKSQELEVKN---AAANDKLKKMV----------KDQQEAEK 3252
Cdd:smart00806 212 KKKLSEDSDSL---LTKVDDLQDIIEALRKDVaqrgvRPSKKQLETVQkelETARKELKKMEeyidiekpiwKKIWEAEL 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33350932 3253 KKVMsqEIQEQLHKQQEVIADkqmsVKEDLDKVEpaviEAQNAVKSIKKQHLVEVRSMANPPAAVKLALES 3323
Cdd:smart00806 289 DKVC--EEQQFLTLQEDLIAD----LKEDLEKAE----ETFDLVEQCCEEQEKGPSKNRNKPVSLPVPTPG 349
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3189-3302 |
1.63e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3189 EKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKkMVKDQQEAEkkkVMSQEIqEQLHKQQ 3268
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG-NVRNNKEYE---ALQKEI-ESLKRRI 105
|
90 100 110
....*....|....*....|....*....|....
gi 33350932 3269 EVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQ 3302
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
3207-3495 |
1.78e-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: 44.56 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3207 KIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQ----EAEKKKVMSQEIQEqlhkqqeviADKQMSVKEDL 3282
Cdd:COG5185 254 KLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKekiaEYTKSIDIKKATES---------LEEQLAAAEAE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3283 DKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWK------QIRSIIMRENFIPTIVNFSA 3356
Cdd:COG5185 325 QELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEldsfkdTIESTKESLDEIPQNQRGYA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3357 EEISDAIREKMKknymsNPSYNYEIVNRaslacgpmvkwAIAQL--NYADMLKRVEPLRNELQKLEDDAKDNQQK--ANE 3432
Cdd:COG5185 405 QEILATLEDTLK-----AADRQIEELQR-----------QIEQAtsSNEEVSKLLNELISELNKVMREADEESQSrlEEA 468
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33350932 3433 VEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSET 3495
Cdd:COG5185 469 YDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMR 531
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3402-3561 |
2.27e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3402 YADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKS 3481
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3482 LSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYFDQQMRQNLfttwSHHLQQANIQFRTDIARTEYLSNADERLR 3561
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EALLNERASLEEALALLRSELEELSEELR 904
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3245-3488 |
4.04e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3245 KDQQEAEKKKVmSQEIQEQLHKQQEVIADKQmSVKEDLDKVEPAVIEAQNAVKSIKKQHLV---EVRSMANPPAAVKLAL 3321
Cdd:COG4942 22 AAEAEAELEQL-QQEIAELEKELAALKKEEK-ALLKQLAALERRIAALARRIRALEQELAAleaELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3322 ESICLLLGEsttdwkQIRSIIMRENFIPTIVNFSAEEISDAIREKMKKNYMSNpsYNYEIVN--RASLACGPMVKWAIAQ 3399
Cdd:COG4942 100 EAQKEELAE------LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP--ARREQAEelRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3400 L--NYADMLKRVEPLRNELQKLEddakdnqqkaNEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTA 3477
Cdd:COG4942 172 EraELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
250
....*....|.
gi 33350932 3478 LLKSLSAERER 3488
Cdd:COG4942 242 RTPAAGFAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3396-3494 |
4.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3396 AIAQLNYADmLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKV-NR 3474
Cdd:COG4913 328 LEAQIRGNG-GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALeEA 406
|
90 100
....*....|....*....|.
gi 33350932 3475 STALLKSLS-AERERWEKTSE 3494
Cdd:COG4913 407 LAEAEAALRdLRRELRELEAE 427
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
2803-2970 |
5.08e-03 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 42.59 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2803 VRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKDYI 2882
Cdd:COG0464 54 VELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 2883 PVDQEELRDYVKARLKVFYEEELDvPLVL-------FNEVLDHVLRIDRIFRQ----PQGHLLLIGVSGAGKTTLSRFVA 2951
Cdd:COG0464 134 PLVTYEDIGGLEEELLELREAILD-DLGGleevkeeLRELVALPLKRPELREEyglpPPRGLLLYGPPGTGKTLLARALA 212
|
170 180
....*....|....*....|..
gi 33350932 2952 WMNGLSVYQIKVHR---KYTGE 2970
Cdd:COG0464 213 GELGLPLIEVDLSDlvsKYVGE 234
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3189-3309 |
7.35e-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: 42.75 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3189 EKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKK-------VMSQEIQ 3261
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREInelkrelDRLQEEL 415
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 33350932 3262 EQLHKQQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSI--KKQHLVEVRS 3309
Cdd:TIGR02169 416 QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQewKLEQLAADLS 465
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| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1905-2021 |
8.76e-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: 40.05 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 1905 FGPAGTGKTESVKALGHQLGR---FVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEA 1981
Cdd:smart00382 8 VGPPGSGKTTLARALARELGPpggGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEI 87
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 33350932 1982 LReHSNPNYDKTSAPITCELLNKQVKVSPDMAIFITMNPG 2021
Cdd:smart00382 88 TS-LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDE 126
|
|
| PulE |
COG2804 |
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ... |
2588-2617 |
8.81e-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: 8.81e-03
10 20 30
....*....|....*....|....*....|...
gi 33350932 2588 HKP--LVL-CGPPGSGKTMTLFSALRALPDMEV 2617
Cdd:COG2804 310 RRPhgIILvTGPTGSGKTTTLYAALNELNTPER 342
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3403-3487 |
9.82e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33350932 3403 ADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKE---------EYAVLISE---------------- 3457
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEieslkrrisdledeil 113
|
90 100 110
....*....|....*....|....*....|....*
gi 33350932 3458 -----AQAIKADLAAVEAKVNRSTALLKSLSAERE 3487
Cdd:COG1579 114 elmerIEELEEELAELEAELAELEAELEEKKAELD 148
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