|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1044-4326 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 1199.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1044 EVEQYVKVWLQYQCLWDMQAENIYNRLGEDLSKWQALLVQIRRARGTFDNAETKKEF-GPVVIDYGKVQSKVNLKYDSWh 1122
Cdd:COG5245 170 SVCSERDGFYEEKSFWSRFHMEMCHIREFCRSKAFRFACDVLRKSGKYVTVATLDSLlSSSKYSELGRRLHFYANMDFS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1123 kevlskfGQMLGSNMTEFHSQISKSRQEL--EQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQRF 1200
Cdd:COG5245 249 -------GIYFPKSFSEFKDSVISATQAVsrDIGRQSRMARRLILVQMDSLARLIVDRICEYVSIEWLGCCEELLTCSME 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1201 QFPPSWLYIDNIEgewgafNDIMRRKDSAIQQQvaNLQMKIVQEDRAVESRTTDLLTDWE-----KTKPVTGNLRPEEAL 1275
Cdd:COG5245 322 SMSSLVNSFDGEE------SEAMSLESSLFYEF--RGGEHLAGFYSAFGDIKRILLFTWSfkklgTLLPSLPGYSSGGMD 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1276 QALTIYEGKFGRLKDDREKCAKAKEALELTDTgllsgSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQpr 1355
Cdd:COG5245 394 YGEEYRSLLWELGSEVGDPDSGPVRKWMRKDL-----FDAKVRSGVSFGKQEEFVSDIFNITFERIHGMDPTTLEDDE-- 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1356 KLRQNLDGLLNQlknfpARLRQYASYEFVQRLlkgYMKINML------VIELKSEALKdrHWKQLMKrlhvnwvvseltl 1429
Cdd:COG5245 467 EDTPALAILLGQ-----EEAGRFVKLCKIMRM---FSFFNSLemfsrrTLANRMAIVK--YLSSVVR------------- 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1430 gqIWDVDLQKN-----EAIVKDVLLVAqgEMALEEFLKQIREVWNTYELDLVNYQNKC------RLIRGWddlfnkVKEH 1498
Cdd:COG5245 524 --TGPLFLQRDffgrmSELLMARDMFM--EVDGVLRLFFGGEWSGIVQLSGIRRAKRCverqidDEIREW------CSSV 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1499 INSVSAMKLSPYykvFEEDAlsweDKLNRIMALFDVWIdvqRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMK 1578
Cdd:COG5245 594 LSDDFLEERAVR---VERGA----DGARRLRASSGSPV---LRRLDEYLMMMSLEDLMPLIPHAVHRKMSLVSGVRGIYK 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1579 KVSKSPLVMDVLNIQgVQRSLERLADLLGKIQKALGEYLERERSSFPRFyfVGDEDLLEIIGNSKNVAKLQKHFKKMFAG 1658
Cdd:COG5245 664 RVVSGCEAINTILED-VGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRVRELENRVYSYRFFVKKIAK 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1659 VSSIILNEDSsvVLGISSREGEEVMFKTPVSITEHPKINEWLTlvEKEMRVtLAKLLaesvtevEIFGKATSIDPNTYIt 1738
Cdd:COG5245 741 EEMKTVFSSR--IQKKEPFSLDSEAYVGFFRLYEKSIVIRGIN--RSMGRV-LSQYL-------ESVQEALEIEDGSFF- 807
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1739 wIDKYQAQLVVLSAQIaWSENVENALSNvggggdvgPLQSVLSNVEVT----LNVLADSVLmeqpplrrRKLEHLITELV 1814
Cdd:COG5245 808 -VSRHRVRDGGLEKGR-GCDAWENCFDP--------PLSEYFRILEKIfpseEGYFFDEVL--------KRLDPGHEIKS 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1815 HQRDVTRSLIKSKIDNAKSFEWLSQMRFYFDPKQTDVLQQLSIQMAnakfnYGFEYLGVQDKLVQTPLTDRCYLTMTQAL 1894
Cdd:COG5245 870 RIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKRFIKVRSSYRSA-----EMFAKNTIPFFVFEHSMDTSQHQKLFEAV 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1895 EARLggSPFgpAGTGKTESVKALGHQLGRFVlvfncdETFDFQAmgRIFVGLCQVGAWGcFDEFNRLEERMLsAVSQQVQ 1974
Cdd:COG5245 945 CDEV--CRF--VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR-TILVDEY 1010
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1975 CIQEALREHSNPNydktsapitcELLNKQVKVSPDMAIFITMNPgyagRSNLPDNLKKLFRSLAMTKPDRQLIAQvmlys 2054
Cdd:COG5245 1011 LNSDEFRMLEELN----------SAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGAIKSR----- 1071
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2055 qgfrtAEVLANKIVPFFKLCDEQLSSQSHYDFglRALKSVLvsagnvkreriQKIKREKEERGEAVDEGEIAENLPeqei 2134
Cdd:COG5245 1072 -----RESLDREIGAFNNEVDGIAREEDELMF--YPMFKSL-----------KAKHRMLEEKTEYLNKILSITGLP---- 1129
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2135 liqSVCETMVPklvaedipllfslLSDVFPGvqyhrgEMTALREelKKVCQEMYltygDGEEVGGMWVEKVLQLYQITQI 2214
Cdd:COG5245 1130 ---LISDTLRE-------------RIDTLDA------EWDSFCR--ISESLKKY----ESQQVSGLDVAQFVSFLRSVDT 1181
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2215 NHGLMMVGPSGSGKSMAWRVLLKALerlegvegvAHIIDPKAIsKDHLYGTLdpntrEWTdGLFTHVLRkiiDNVRGELQ 2294
Cdd:COG5245 1182 GAFHAEYFRVFLCKIKHYTDACDYL---------WHVKSPYVK-KKYFDADM-----ELR-QFFLMFNR---EDMEARLA 1242
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2295 -KRQWIVFDgdvdpEWVENLNSVLDDNKLLTLPNGERlslppnvRIMFEVQDlkyATLATVSRCGMVWFSEDVLSTDMIF 2373
Cdd:COG5245 1243 dSKMEYEVE-----RYVEKTKAEVSSLKLELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRLSTKGVF 1307
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2374 NNFLARLRSiPLDEGEDEAQRRRKGKEDEGEeaaspmlqiqrdaatimqpyfTSNGLVTKALEHAFKLEHIMDLTRLRCL 2453
Cdd:COG5245 1308 LDELGDTKR-YLDECLDFFSCFEEVQKEIDE---------------------LSMVFCADALRFSADLYHIVKERRFSGV 1365
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2454 --GSLFSM-LHQACRNVAQyNANHPDfpmqieqLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPN- 2529
Cdd:COG5245 1366 laGSDASEsLGGKSIELAA-ILEHKD-------LIVEMKRGINDVLKLRIFGDKCRESTPRFYLISDGDLIKDLNERSDy 1437
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2530 --IPIIDYEVSISGE-WSPwqakVPQIEVETHKVAAP-DVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFS 2605
Cdd:COG5245 1438 eeMLIMMFNISAVITnNGS----IAGFELRGERVMLRkEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCP 1513
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2606 ALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMV 2685
Cdd:COG5245 1514 SLRSELITEVKYFNFSTCTMTPSKLSVLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLV 1593
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2686 EHGGFYRTSDQTWVKLERIQFVGACNPPTDPGRKPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAE 2765
Cdd:COG5245 1594 ERQGFWSSIAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSE 1673
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2766 PLTAAMVEFYTMSQERFTQDTQPHYIYSPREMTRWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTD 2845
Cdd:COG5245 1674 ETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSR 1753
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2846 ENIDMVALKHFPNIDKEKAMSRPILYSNWLSKDYIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFR 2925
Cdd:COG5245 1754 QDLYDFGLRAIREMIAGHIGEAEITFSMILFFGMACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLL 1833
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2926 QPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQIKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLER 3005
Cdd:COG5245 1834 VVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLED 1913
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3006 MNTLLANGEVPGLFEGDEYATLMTQCKEGAQKEGLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFN 3085
Cdd:COG5245 1914 FNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEKDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGIRSPALKN 1993
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3086 RCVLNWFGDWSTEALYQVGKEFtskMDLEKPNYIVPDYMPVVydKLPQPPTHREAIVNSCVFVHQTLHQANARLAkrggr 3165
Cdd:COG5245 1994 RCFIDFKKLWDTEEMSQYANSV---ETLSRDGGRVFFINGEL--GVGKGALISEVFGDDAVVIEGRGFEISMIEG----- 2063
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3166 TMAITPRHYLDFINHYANLFHEKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQ 3245
Cdd:COG5245 2064 SLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGER 2143
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3246 QEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLL 3325
Cdd:COG5245 2144 LEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDL 2223
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3326 LGESTTDWKQIRSIIMRENFIPTIVNFSAE-EISDAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADML 3404
Cdd:COG5245 2224 LGFEAKIWFGEQQSLRRDDFIRIIGKYPDEiEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVL 2303
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3405 KRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAER 3484
Cdd:COG5245 2304 EVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINED 2383
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3485 ERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYFDQQMRQNLFTTwSHHLQQANIQFRTDIART--EYLSNADERLRWQA 3562
Cdd:COG5245 2384 SEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIRRRQfiTEGVQKIEDFKEEA 2462
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3563 SSlpaDDLCTENA-IMLKRFNRYPLIIDPSGQATEFIMNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDP 3641
Cdd:COG5245 2463 CS---TDYGLENSrIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEALDE 2539
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3642 VLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPD 3721
Cdd:COG5245 2540 EIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGP 2619
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3722 VDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRILDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLP 3801
Cdd:COG5245 2620 LFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNA 2699
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3802 LSTACSSIYFTMESLKQVHFLYQYSLQFFLDIYHNVLyenpNLKGATDHTQRLSVITKDLFqvafnrvargMLHQDHITF 3881
Cdd:COG5245 2700 SVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWR----RMKSKYLCAIRYMLMSSEWI----------LDHEDRSGF 2765
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3882 AMLLariklkgtmgeptydaEFQHFLRGKEIVLsagSTPKVQGLTVEQAEAVArlsclpAFKDLIAKvQADEFGiwLESS 3961
Cdd:COG5245 2766 IHRL----------------DVSFLLRTKRFVS---TLLEDKNYRQVLSSCSL------YGNDVISH-SCDRFD--RDVY 2817
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3962 SPEQTVPYLWTEETpatpigqaihRLLLIQAFRPDRLLAMAHMFVSTNLGEsFMSIMEqplDLTHIVGTEVKPNTPVLMC 4041
Cdd:COG5245 2818 RALKHQMDNRTHST----------ILTSNSKTNPYKEYTYNDSWAEAFEVE-DSGDLY---KFEEGLLELIVGHAPLIYA 2883
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4042 svpgydasgHVEDLAAEQNTQitsiAIGSAEGFNQADKAINTAVKSGRWVMLKNVHLAPGWLMQL-----EKKLHSLQPH 4116
Cdd:COG5245 2884 ---------HKKSLENERNVD----RLGSKENEVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYvedvvYPIKASRVCG 2950
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4117 ACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRTFSSIPVsrMCK-SPNERARLYFLLAWFHAVIQERLRYAP 4195
Cdd:COG5245 2951 KVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLVEIDRY--PFDyTLVIACDDAFYLSWEHAAVASVISAGP 3028
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4196 LGWSKKYEFGESDLRSACDTVDTWLddtAKGRQNispdKIPWSALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTtrSF 4275
Cdd:COG5245 3029 KENNEEIYFGDKDFEFKTHLLKNIL---FLNHLN----ARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGA--HE 3099
|
3290 3300 3310 3320 3330
....*....|....*....|....*....|....*....|....*....|...
gi 1958782055 4276 DSEFKLACKVDGHKDIQ--MPDGIRREEFVQWVELLPDAQTPSWLGLPNNAER 4326
Cdd:COG5245 3100 TSSQILASVPGGDPELVkfHMEEMCRSSAFGVIGQLPDLALCAWLMGPCDSEY 3152
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1866-2229 |
5.32e-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: 5.32e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1866 YGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALGHQLGRFVLVFNCDETFDFQAMGRIFVG 1945
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1946 LCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNpnydktsapiTCELLNKQVKVSPDMAIFITMNPGYAGRSN 2025
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLK----------TFVFEGSEIKLNPSCGIFITMNPGYAGRTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2026 LPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQLSSQSHYDFGLRALKSVLVSAGNVKRER 2105
Cdd:pfam12774 151 LPDNLKALFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2106 iqkikrekeergeavdegeiaENLPEQEILIQSVCETMVPKLVAEDIPLLFSLLSDVFPGVQYHRGEMTALREELKKVCQ 2185
Cdd:pfam12774 231 ---------------------PNLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCK 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958782055 2186 EMYLTYGDgeevggMWVEKVLQLYQITQINHGLMMVGPSGSGKS 2229
Cdd:pfam12774 290 ELGLQPHD------AFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
240-830 |
1.24e-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: 1.24e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 240 LNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDTG 319
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKALDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 320 LKQALETVNDYNPLMKDF--PLNDLLSATELDKIRQALVAIFTHLRKI-RNTKY--PIQRALRLVEAISRDLSSQLLKVL 394
Cdd:pfam08385 81 LTDALNEAKDNVKYLKTLerPFEDLEELTDPPEIIEAIPPLMNTIRLIwSISRYynTSERMTVLLEKISNQLIEQCKKYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 395 GTRKLMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKReenlkmvWRINPAHR-----KLQARLDQMRKFRR 469
Cdd:pfam08385 161 SPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERP-------WDFSERYIfgrfdAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 470 QHEQLRAV--IVRVLRPQVTAVaqqnqgeapepqdmkVAEVlfdaadanaIEEVNLAYENVKEV--DGLDVSKEGteaWE 545
Cdd:pfam08385 234 TIEQFSKLekIGGTKGPELEGV---------------IEEI---------LEEFQEAYKVFKSKtyDILDVSNEG---FD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 546 AAMKRYDERIDRVETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQY 625
Cdd:pfam08385 287 DDYEEFKERIKDLERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 626 pqsQACKMSHvRDLPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGweNHVEGQKLKQDGDSFRMKLN--TQEIFDDWARK 703
Cdd:pfam08385 367 ---YNPSPIA-KNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLL--KHAEGKKVIKKYNELAKKLDeyERLIYEAWLKE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 704 VQQRNLGVSGR-IFTIESARVRgrsgnvlKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIES 782
Cdd:pfam08385 441 VEEASEGNLKRpLLVRHPETGK-------LLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELL 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1958782055 783 VRTYERTCEKV--EERNtislLVAGLKKEVQALIAEGI-ALVWESYKLDPY 830
Cdd:pfam08385 514 VRWYNKIRSTLlpVERP----LLAPHLKDIDEKLEPGLtTLTWNSLGIDEY 560
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4330-4641 |
3.36e-61 |
|
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: 213.64 E-value: 3.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4330 TTQGVDMISKMLKMQMLEDEDdlayAETEKKTRTDstsdgrpawmrTLHTTASNWLHLIPQTL---SPLKRTVENIKDPL 4406
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSG----GGGGGSSREE-----------IVLELAKDILEKLPEPFdieEAEEKYPVGYEDPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4407 FRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVSDFSERIKQL 4486
Cdd:pfam18199 66 NTVLLQEIERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLKQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4487 QNISQAaaaggakELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVT--ASQSTTLDACSFG--VTGLKL 4562
Cdd:pfam18199 146 QDWLDD-------EGPPKVFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTkkVSPEEVTEPPEDGvyVHGLFL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4563 QGATCS--NNKL--SLSNAISTVLPLTQLRWGKQTSAEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGVA 4638
Cdd:pfam18199 219 EGARWDrkNGCLveSEPKELFSPLPVIHLKPVESDKKKLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVA 298
|
...
gi 1958782055 4639 VLC 4641
Cdd:pfam18199 299 LLL 301
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2568-2731 |
2.24e-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: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2568 PTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRAL--PDMEVVGLNFSSATTPELLLKTFDHYCEYRRTpng 2645
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2646 vvlAPVQLGKWLVLFCDEIN-LPDMDKYGTQRVISFIRQMVEhggfyrtsdqtwvKLERIQFVGACNPPTDPG-RKPLSH 2723
Cdd:cd00009 78 ---ELAEKAKPGVLFIDEIDsLSRGAQNALLRVLETLNDLRI-------------DRENVRVIGATNRPLLGDlDRALYD 141
|
....*...
gi 1958782055 2724 RFLRHVPV 2731
Cdd:cd00009 142 RLDIRIVI 149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3185-3498 |
2.34e-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: 57.37 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3185 FHEKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHK 3264
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3265 QQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQHlVEVRSMANPPAAVKLALESIcllLGESTTDWKQIRSIImren 3344
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-ESLEAELEELEAELEELESR---LEELEEQLETLRSKV---- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3345 fiptivnfsaeeisDAIREKMKKNymsnpsyNYEIVNRASLacgpmvkwaIAQLNyadmlKRVEPLRNELQKLEDDAKDN 3424
Cdd:TIGR02168 389 --------------AQLELQIASL-------NNEIERLEAR---------LERLE-----DRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782055 3425 QQKA-----NEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQM 3498
Cdd:TIGR02168 434 ELKElqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2586-2735 |
2.37e-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: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2586 HKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRRTPNG-------VVLAPVQLGKWLV 2658
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGsgelrlrLALALARKLKPDV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782055 2659 LFCDEINLpdMDKYGTQRVISFIRQMVEHGGFYRTsdqtwvklERIQFVGACNPPTDPGRKPLSHRFLRHVPVVYVD 2735
Cdd:smart00382 82 LILDEITS--LLDAEQEALLLLLEELRLLLLLKSE--------KNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
3187-3559 |
2.53e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3187 EKRSELEEQQMHLNvglrkikETVDQVEELRRDLRIKSQELEvknaAANDKLKKMVKD--QQEAEKKKVMS-QEIQEQLH 3263
Cdd:PRK04863 297 TSRRQLAAEQYRLV-------EMARELAELNEAESDLEQDYQ----AASDHLNLVQTAlrQQEKIERYQADlEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3264 KQQEVIADKQmsvkEDLDKVEPAVIEAQNAVKSIKKQ------HLVEVRSMANPPAAVKLALESICLLLGESTTDWkqir 3337
Cdd:PRK04863 366 EQNEVVEEAD----EQQEENEARAEAAEEEVDELKSQladyqqALDVQQTRAIQYQQAVQALERAKQLCGLPDLTA---- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3338 siimrENFIPTIVNFSAEE---------------ISDAIREKMKKNYMSNPSYNYEIV-NRASlacgpmvKWAIAQLNYA 3401
Cdd:PRK04863 438 -----DNAEDWLEEFQAKEqeateellsleqklsVAQAAHSQFEQAYQLVRKIAGEVSrSEAW-------DVARELLRRL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3402 DMLK----RVEPLRNELQKLEDDAKdNQQKAN------------------EVEQMIRDLEASIARYKEEYAVLISEAQAI 3459
Cdd:PRK04863 506 REQRhlaeQLQQLRMRLSELEQRLR-QQQRAErllaefckrlgknlddedELEQLQEELEARLESLSESVSEARERRMAL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3460 KADLAAVEAKVNRstallksLSAERERWEKTSETFkNQMSTIAGDCLLSAAFIayagyfDQQMRQNLFTTWShhLQQANI 3539
Cdd:PRK04863 585 RQQLEQLQARIQR-------LAARAPAWLAAQDAL-ARLREQSGEEFEDSQDV------TEYMQQLLERERE--LTVERD 648
|
410 420
....*....|....*....|....*...
gi 1958782055 3540 QFRTDI----ARTEYLSNA----DERLR 3559
Cdd:PRK04863 649 ELAARKqaldEEIERLSQPggseDPRLN 676
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1044-4326 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 1199.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1044 EVEQYVKVWLQYQCLWDMQAENIYNRLGEDLSKWQALLVQIRRARGTFDNAETKKEF-GPVVIDYGKVQSKVNLKYDSWh 1122
Cdd:COG5245 170 SVCSERDGFYEEKSFWSRFHMEMCHIREFCRSKAFRFACDVLRKSGKYVTVATLDSLlSSSKYSELGRRLHFYANMDFS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1123 kevlskfGQMLGSNMTEFHSQISKSRQEL--EQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQRF 1200
Cdd:COG5245 249 -------GIYFPKSFSEFKDSVISATQAVsrDIGRQSRMARRLILVQMDSLARLIVDRICEYVSIEWLGCCEELLTCSME 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1201 QFPPSWLYIDNIEgewgafNDIMRRKDSAIQQQvaNLQMKIVQEDRAVESRTTDLLTDWE-----KTKPVTGNLRPEEAL 1275
Cdd:COG5245 322 SMSSLVNSFDGEE------SEAMSLESSLFYEF--RGGEHLAGFYSAFGDIKRILLFTWSfkklgTLLPSLPGYSSGGMD 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1276 QALTIYEGKFGRLKDDREKCAKAKEALELTDTgllsgSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQpr 1355
Cdd:COG5245 394 YGEEYRSLLWELGSEVGDPDSGPVRKWMRKDL-----FDAKVRSGVSFGKQEEFVSDIFNITFERIHGMDPTTLEDDE-- 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1356 KLRQNLDGLLNQlknfpARLRQYASYEFVQRLlkgYMKINML------VIELKSEALKdrHWKQLMKrlhvnwvvseltl 1429
Cdd:COG5245 467 EDTPALAILLGQ-----EEAGRFVKLCKIMRM---FSFFNSLemfsrrTLANRMAIVK--YLSSVVR------------- 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1430 gqIWDVDLQKN-----EAIVKDVLLVAqgEMALEEFLKQIREVWNTYELDLVNYQNKC------RLIRGWddlfnkVKEH 1498
Cdd:COG5245 524 --TGPLFLQRDffgrmSELLMARDMFM--EVDGVLRLFFGGEWSGIVQLSGIRRAKRCverqidDEIREW------CSSV 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1499 INSVSAMKLSPYykvFEEDAlsweDKLNRIMALFDVWIdvqRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMK 1578
Cdd:COG5245 594 LSDDFLEERAVR---VERGA----DGARRLRASSGSPV---LRRLDEYLMMMSLEDLMPLIPHAVHRKMSLVSGVRGIYK 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1579 KVSKSPLVMDVLNIQgVQRSLERLADLLGKIQKALGEYLERERSSFPRFyfVGDEDLLEIIGNSKNVAKLQKHFKKMFAG 1658
Cdd:COG5245 664 RVVSGCEAINTILED-VGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRVRELENRVYSYRFFVKKIAK 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1659 VSSIILNEDSsvVLGISSREGEEVMFKTPVSITEHPKINEWLTlvEKEMRVtLAKLLaesvtevEIFGKATSIDPNTYIt 1738
Cdd:COG5245 741 EEMKTVFSSR--IQKKEPFSLDSEAYVGFFRLYEKSIVIRGIN--RSMGRV-LSQYL-------ESVQEALEIEDGSFF- 807
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1739 wIDKYQAQLVVLSAQIaWSENVENALSNvggggdvgPLQSVLSNVEVT----LNVLADSVLmeqpplrrRKLEHLITELV 1814
Cdd:COG5245 808 -VSRHRVRDGGLEKGR-GCDAWENCFDP--------PLSEYFRILEKIfpseEGYFFDEVL--------KRLDPGHEIKS 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1815 HQRDVTRSLIKSKIDNAKSFEWLSQMRFYFDPKQTDVLQQLSIQMAnakfnYGFEYLGVQDKLVQTPLTDRCYLTMTQAL 1894
Cdd:COG5245 870 RIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKRFIKVRSSYRSA-----EMFAKNTIPFFVFEHSMDTSQHQKLFEAV 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1895 EARLggSPFgpAGTGKTESVKALGHQLGRFVlvfncdETFDFQAmgRIFVGLCQVGAWGcFDEFNRLEERMLsAVSQQVQ 1974
Cdd:COG5245 945 CDEV--CRF--VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR-TILVDEY 1010
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1975 CIQEALREHSNPNydktsapitcELLNKQVKVSPDMAIFITMNPgyagRSNLPDNLKKLFRSLAMTKPDRQLIAQvmlys 2054
Cdd:COG5245 1011 LNSDEFRMLEELN----------SAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGAIKSR----- 1071
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2055 qgfrtAEVLANKIVPFFKLCDEQLSSQSHYDFglRALKSVLvsagnvkreriQKIKREKEERGEAVDEGEIAENLPeqei 2134
Cdd:COG5245 1072 -----RESLDREIGAFNNEVDGIAREEDELMF--YPMFKSL-----------KAKHRMLEEKTEYLNKILSITGLP---- 1129
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2135 liqSVCETMVPklvaedipllfslLSDVFPGvqyhrgEMTALREelKKVCQEMYltygDGEEVGGMWVEKVLQLYQITQI 2214
Cdd:COG5245 1130 ---LISDTLRE-------------RIDTLDA------EWDSFCR--ISESLKKY----ESQQVSGLDVAQFVSFLRSVDT 1181
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2215 NHGLMMVGPSGSGKSMAWRVLLKALerlegvegvAHIIDPKAIsKDHLYGTLdpntrEWTdGLFTHVLRkiiDNVRGELQ 2294
Cdd:COG5245 1182 GAFHAEYFRVFLCKIKHYTDACDYL---------WHVKSPYVK-KKYFDADM-----ELR-QFFLMFNR---EDMEARLA 1242
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2295 -KRQWIVFDgdvdpEWVENLNSVLDDNKLLTLPNGERlslppnvRIMFEVQDlkyATLATVSRCGMVWFSEDVLSTDMIF 2373
Cdd:COG5245 1243 dSKMEYEVE-----RYVEKTKAEVSSLKLELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRLSTKGVF 1307
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2374 NNFLARLRSiPLDEGEDEAQRRRKGKEDEGEeaaspmlqiqrdaatimqpyfTSNGLVTKALEHAFKLEHIMDLTRLRCL 2453
Cdd:COG5245 1308 LDELGDTKR-YLDECLDFFSCFEEVQKEIDE---------------------LSMVFCADALRFSADLYHIVKERRFSGV 1365
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2454 --GSLFSM-LHQACRNVAQyNANHPDfpmqieqLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPN- 2529
Cdd:COG5245 1366 laGSDASEsLGGKSIELAA-ILEHKD-------LIVEMKRGINDVLKLRIFGDKCRESTPRFYLISDGDLIKDLNERSDy 1437
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2530 --IPIIDYEVSISGE-WSPwqakVPQIEVETHKVAAP-DVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFS 2605
Cdd:COG5245 1438 eeMLIMMFNISAVITnNGS----IAGFELRGERVMLRkEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCP 1513
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2606 ALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMV 2685
Cdd:COG5245 1514 SLRSELITEVKYFNFSTCTMTPSKLSVLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLV 1593
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2686 EHGGFYRTSDQTWVKLERIQFVGACNPPTDPGRKPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAE 2765
Cdd:COG5245 1594 ERQGFWSSIAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSE 1673
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2766 PLTAAMVEFYTMSQERFTQDTQPHYIYSPREMTRWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTD 2845
Cdd:COG5245 1674 ETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSR 1753
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2846 ENIDMVALKHFPNIDKEKAMSRPILYSNWLSKDYIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFR 2925
Cdd:COG5245 1754 QDLYDFGLRAIREMIAGHIGEAEITFSMILFFGMACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLL 1833
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2926 QPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQIKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLER 3005
Cdd:COG5245 1834 VVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLED 1913
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3006 MNTLLANGEVPGLFEGDEYATLMTQCKEGAQKEGLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFN 3085
Cdd:COG5245 1914 FNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEKDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGIRSPALKN 1993
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3086 RCVLNWFGDWSTEALYQVGKEFtskMDLEKPNYIVPDYMPVVydKLPQPPTHREAIVNSCVFVHQTLHQANARLAkrggr 3165
Cdd:COG5245 1994 RCFIDFKKLWDTEEMSQYANSV---ETLSRDGGRVFFINGEL--GVGKGALISEVFGDDAVVIEGRGFEISMIEG----- 2063
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3166 TMAITPRHYLDFINHYANLFHEKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQ 3245
Cdd:COG5245 2064 SLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGER 2143
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3246 QEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLL 3325
Cdd:COG5245 2144 LEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDL 2223
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3326 LGESTTDWKQIRSIIMRENFIPTIVNFSAE-EISDAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADML 3404
Cdd:COG5245 2224 LGFEAKIWFGEQQSLRRDDFIRIIGKYPDEiEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVL 2303
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3405 KRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAER 3484
Cdd:COG5245 2304 EVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINED 2383
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3485 ERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYFDQQMRQNLFTTwSHHLQQANIQFRTDIART--EYLSNADERLRWQA 3562
Cdd:COG5245 2384 SEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIRRRQfiTEGVQKIEDFKEEA 2462
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3563 SSlpaDDLCTENA-IMLKRFNRYPLIIDPSGQATEFIMNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDP 3641
Cdd:COG5245 2463 CS---TDYGLENSrIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEALDE 2539
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3642 VLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPD 3721
Cdd:COG5245 2540 EIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGP 2619
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3722 VDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRILDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLP 3801
Cdd:COG5245 2620 LFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNA 2699
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3802 LSTACSSIYFTMESLKQVHFLYQYSLQFFLDIYHNVLyenpNLKGATDHTQRLSVITKDLFqvafnrvargMLHQDHITF 3881
Cdd:COG5245 2700 SVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWR----RMKSKYLCAIRYMLMSSEWI----------LDHEDRSGF 2765
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3882 AMLLariklkgtmgeptydaEFQHFLRGKEIVLsagSTPKVQGLTVEQAEAVArlsclpAFKDLIAKvQADEFGiwLESS 3961
Cdd:COG5245 2766 IHRL----------------DVSFLLRTKRFVS---TLLEDKNYRQVLSSCSL------YGNDVISH-SCDRFD--RDVY 2817
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3962 SPEQTVPYLWTEETpatpigqaihRLLLIQAFRPDRLLAMAHMFVSTNLGEsFMSIMEqplDLTHIVGTEVKPNTPVLMC 4041
Cdd:COG5245 2818 RALKHQMDNRTHST----------ILTSNSKTNPYKEYTYNDSWAEAFEVE-DSGDLY---KFEEGLLELIVGHAPLIYA 2883
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4042 svpgydasgHVEDLAAEQNTQitsiAIGSAEGFNQADKAINTAVKSGRWVMLKNVHLAPGWLMQL-----EKKLHSLQPH 4116
Cdd:COG5245 2884 ---------HKKSLENERNVD----RLGSKENEVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYvedvvYPIKASRVCG 2950
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4117 ACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRTFSSIPVsrMCK-SPNERARLYFLLAWFHAVIQERLRYAP 4195
Cdd:COG5245 2951 KVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLVEIDRY--PFDyTLVIACDDAFYLSWEHAAVASVISAGP 3028
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4196 LGWSKKYEFGESDLRSACDTVDTWLddtAKGRQNispdKIPWSALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTtrSF 4275
Cdd:COG5245 3029 KENNEEIYFGDKDFEFKTHLLKNIL---FLNHLN----ARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGA--HE 3099
|
3290 3300 3310 3320 3330
....*....|....*....|....*....|....*....|....*....|...
gi 1958782055 4276 DSEFKLACKVDGHKDIQ--MPDGIRREEFVQWVELLPDAQTPSWLGLPNNAER 4326
Cdd:COG5245 3100 TSSQILASVPGGDPELVkfHMEEMCRSSAFGVIGQLPDLALCAWLMGPCDSEY 3152
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1866-2229 |
5.32e-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: 5.32e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1866 YGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALGHQLGRFVLVFNCDETFDFQAMGRIFVG 1945
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1946 LCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNpnydktsapiTCELLNKQVKVSPDMAIFITMNPGYAGRSN 2025
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLK----------TFVFEGSEIKLNPSCGIFITMNPGYAGRTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2026 LPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQLSSQSHYDFGLRALKSVLVSAGNVKRER 2105
Cdd:pfam12774 151 LPDNLKALFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2106 iqkikrekeergeavdegeiaENLPEQEILIQSVCETMVPKLVAEDIPLLFSLLSDVFPGVQYHRGEMTALREELKKVCQ 2185
Cdd:pfam12774 231 ---------------------PNLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCK 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958782055 2186 EMYLTYGDgeevggMWVEKVLQLYQITQINHGLMMVGPSGSGKS 2229
Cdd:pfam12774 290 ELGLQPHD------AFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
240-830 |
1.24e-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: 1.24e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 240 LNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDTG 319
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKALDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 320 LKQALETVNDYNPLMKDF--PLNDLLSATELDKIRQALVAIFTHLRKI-RNTKY--PIQRALRLVEAISRDLSSQLLKVL 394
Cdd:pfam08385 81 LTDALNEAKDNVKYLKTLerPFEDLEELTDPPEIIEAIPPLMNTIRLIwSISRYynTSERMTVLLEKISNQLIEQCKKYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 395 GTRKLMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKReenlkmvWRINPAHR-----KLQARLDQMRKFRR 469
Cdd:pfam08385 161 SPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERP-------WDFSERYIfgrfdAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 470 QHEQLRAV--IVRVLRPQVTAVaqqnqgeapepqdmkVAEVlfdaadanaIEEVNLAYENVKEV--DGLDVSKEGteaWE 545
Cdd:pfam08385 234 TIEQFSKLekIGGTKGPELEGV---------------IEEI---------LEEFQEAYKVFKSKtyDILDVSNEG---FD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 546 AAMKRYDERIDRVETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQY 625
Cdd:pfam08385 287 DDYEEFKERIKDLERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 626 pqsQACKMSHvRDLPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGweNHVEGQKLKQDGDSFRMKLN--TQEIFDDWARK 703
Cdd:pfam08385 367 ---YNPSPIA-KNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLL--KHAEGKKVIKKYNELAKKLDeyERLIYEAWLKE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 704 VQQRNLGVSGR-IFTIESARVRgrsgnvlKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIES 782
Cdd:pfam08385 441 VEEASEGNLKRpLLVRHPETGK-------LLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELL 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1958782055 783 VRTYERTCEKV--EERNtislLVAGLKKEVQALIAEGI-ALVWESYKLDPY 830
Cdd:pfam08385 514 VRWYNKIRSTLlpVERP----LLAPHLKDIDEKLEPGLtTLTWNSLGIDEY 560
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1317-1718 |
2.09e-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: 451.33 E-value: 2.09e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1317 VQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLRQNLDGLLNQLKNFPARLRQYASYEFVQRLLKGYMKINM 1396
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1397 LVIELKSEALKDRHWKQLMKRLHVNW--VVSELTLGQIWDVDLQKNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELD 1474
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFdpLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1475 LVNYQN-KCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDALSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSa 1553
Cdd:pfam08393 161 LVPYKDtGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSSE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1554 DIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRSLERLADLLGKIQKALGEYLERERSSFPRFYFVGDE 1633
Cdd:pfam08393 240 DIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSND 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1634 DLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDSSVVlGISSREGEEVMFKTPVSITEhPKINEWLTLVEKEMRVTLAK 1713
Cdd:pfam08393 320 ELLEILSQTKDPTRVQPHLKKCFEGIASLEFDENKEIT-GMISKEGEVVPFSKPPVEAK-GNVEEWLNELEEEMRETLRD 397
|
....*
gi 1958782055 1714 LLAES 1718
Cdd:pfam08393 398 LLKEA 402
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3558-3778 |
2.16e-99 |
|
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the fifth AAA+ domain subdomain AAA5S. Structural analysis reveal that it is the coiled-coil buttress interface. The relative movement of AAA5S together with the stalk (AAA4S), is coupled to rearrangements in the AAA+ ring. Closure of the AAA1 site and the rigid body movement of AAA2-AAA4 force the AAA4/AAA5 interface to close and the AAA6L subdomain to rotate towards the ring centre. The AAA5S subdomain rotates as a unit together with AAA6L, and this movement pulls the buttress relative to the stalk.
Pssm-ID: 463702 [Multi-domain] Cd Length: 222 Bit Score: 319.77 E-value: 2.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3558 LRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFIMNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDV- 3636
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3637 ESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLK 3716
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782055 3717 AERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRILDDDTIITTLENLKREAAEV 3778
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 ... |
2906-3184 |
3.77e-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: 237.51 E-value: 3.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2906 PLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQIKVHRKYTGEDFDEDLRTVLRRSGCKN 2985
Cdd:pfam12780 2 DLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2986 EKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKEGLmLDSHEELYKWFTSQVIRNLHVVFT 3065
Cdd:pfam12780 82 KPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNI-EDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3066 MNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKpnyivpdympvvydklpqppTHREAIVNSC 3145
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDIEIPE--------------------ELKSNVVKVF 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958782055 3146 VFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANL 3184
Cdd:pfam12780 221 VYVHSSVEDMSKKFYEELKRKNYVTPKSYLELLRLYKNL 259
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4330-4641 |
3.36e-61 |
|
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: 213.64 E-value: 3.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4330 TTQGVDMISKMLKMQMLEDEDdlayAETEKKTRTDstsdgrpawmrTLHTTASNWLHLIPQTL---SPLKRTVENIKDPL 4406
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSG----GGGGGSSREE-----------IVLELAKDILEKLPEPFdieEAEEKYPVGYEDPL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4407 FRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVSDFSERIKQL 4486
Cdd:pfam18199 66 NTVLLQEIERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLKQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4487 QNISQAaaaggakELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVT--ASQSTTLDACSFG--VTGLKL 4562
Cdd:pfam18199 146 QDWLDD-------EGPPKVFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTkkVSPEEVTEPPEDGvyVHGLFL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4563 QGATCS--NNKL--SLSNAISTVLPLTQLRWGKQTSAEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGVA 4638
Cdd:pfam18199 219 EGARWDrkNGCLveSEPKELFSPLPVIHLKPVESDKKKLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVA 298
|
...
gi 1958782055 4639 VLC 4641
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 ... |
4173-4324 |
6.50e-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: 191.90 E-value: 6.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4173 RARLYFLLAWFHAVIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDtakgrqniSPDKIPWSALKTLMAQSIYGGR 4252
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDE--------YDEKIPWDALRYLIGEINYGGR 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782055 4253 VDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVdghkdIQMPDGIRREEFVQWVELLPDAQTPSWLGLPNNA 4324
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 ... |
3199-3534 |
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 1958782055 3199 LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAAnDKLKKMVK-DQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVK 3277
Cdd:pfam12777 3 LENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDA-DKLIQVVGiEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3278 EDLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLL---GESTTD--WKQIRSIIMR-ENFIPTIVN 3351
Cdd:pfam12777 82 EDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMapgGKIPKDksWKAAKIMMAKvDGFLDSLIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3352 FSAEEISDAIREKMKKnYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEV 3431
Cdd:pfam12777 162 FDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3432 EQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAF 3511
Cdd:pfam12777 241 KAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISAF 320
|
330 340
....*....|....*....|....
gi 1958782055 3512 IAYAGYFDQQMRQNLF-TTWSHHL 3534
Cdd:pfam12777 321 ISYLGFFTKKYRNELLdKFWIPYI 344
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2564-2728 |
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 1958782055 2564 DVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALP--DMEVVGLNFSSATTPELLLKTFDHYCEYRR 2641
Cdd:pfam12775 9 EILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDkeKYLPLFINFSAQTTSNQTQDIIESKLEKRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2642 tpnGVVLAPVqLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTdPGRKPL 2721
Cdd:pfam12775 89 ---KGVYGPP-GGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPG-GGRNDI 163
|
....*..
gi 1958782055 2722 SHRFLRH 2728
Cdd:pfam12775 164 TPRLLRH 170
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
4033-4143 |
9.34e-37 |
|
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of dynein heavy chain. The chain also contains ATPase activity and microtubule binding ability and acts as a motor for the movement of organelles and vesicles along microtubules. Dynein is also involved in cilia and flagella movement. The dynein subunit consists of at least two heavy chains and a number of intermediate and light chains. The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This C-terminal domain carries the D6 region of the dynein motor where the P-loop has been lost in evolution but the general structure of a potential ATP binding site appears to be retained.
Pssm-ID: 460782 Cd Length: 115 Bit Score: 136.04 E-value: 9.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 4033 KPNTPVLMCSVPGYDASGHVEDLAAEQN--TQITSIAIGSAEGFnQADKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKL 4110
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGfgGKLHSISLGQGQGP-IAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKIL 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 1958782055 4111 HSLQ---PHACFRLFLTMEINPKVPVNLLRAGRIFV 4143
Cdd:pfam03028 80 EELPeetLHPDFRLWLTSEPSPKFPISILQNSIKIT 115
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2421-2547 |
1.15e-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: 99.28 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2421 MQPYFtsNGLVTKALEHAFK-LEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPdfpMQIEQLERYIQRYLVYAILWS 2499
Cdd:pfam17852 1 LEPLF--EWLVPPALEFVRKnCKEIVPTSDLNLVQSLCRLLESLLDEVLEYNGVHP---LSPDKLKEYLEKLFLFALVWS 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2500 LSGDSRLKMRAELGEYIRRITT-VPLPTAPNIPIIDYEVSI-SGEWSPWQ 2547
Cdd:pfam17852 76 IGGTLDEDSRKKFDEFLRELFSgLDLPPPEKGTVYDYFVDLeKGEWVPWS 125
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2217-2357 |
8.67e-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: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2217 GLMMVGPSGSGKSMAWRVLLKALERLEGVEGVAHiidpKAISKDHLYGTLDPNTR--EWTDGLFTHVLRKiidnvrgelq 2294
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLT----RDTTEEDLFGRRNIDPGgaSWVDGPLVRAARE---------- 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782055 2295 krQWIVFDGDVD---PEWVENLNSVLDDNKLLTLPNGERLSLPP-NVRIMFEV----QDLKYATLATVSRC 2357
Cdd:pfam07728 67 --GEIAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMnpldRGLNELSPALRSRF 135
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2568-2731 |
2.24e-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: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2568 PTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRAL--PDMEVVGLNFSSATTPELLLKTFDHYCEYRRTpng 2645
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2646 vvlAPVQLGKWLVLFCDEIN-LPDMDKYGTQRVISFIRQMVEhggfyrtsdqtwvKLERIQFVGACNPPTDPG-RKPLSH 2723
Cdd:cd00009 78 ---ELAEKAKPGVLFIDEIDsLSRGAQNALLRVLETLNDLRI-------------DRENVRVIGATNRPLLGDlDRALYD 141
|
....*...
gi 1958782055 2724 RFLRHVPV 2731
Cdd:cd00009 142 RLDIRIVI 149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3185-3498 |
2.34e-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: 57.37 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3185 FHEKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHK 3264
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3265 QQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQHlVEVRSMANPPAAVKLALESIcllLGESTTDWKQIRSIImren 3344
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-ESLEAELEELEAELEELESR---LEELEEQLETLRSKV---- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3345 fiptivnfsaeeisDAIREKMKKNymsnpsyNYEIVNRASLacgpmvkwaIAQLNyadmlKRVEPLRNELQKLEDDAKDN 3424
Cdd:TIGR02168 389 --------------AQLELQIASL-------NNEIERLEAR---------LERLE-----DRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782055 3425 QQKA-----NEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQM 3498
Cdd:TIGR02168 434 ELKElqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3172-3515 |
6.35e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3172 RHYLDFINHYANLF--HEKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKK----MVKDQ 3245
Cdd:COG4717 115 REELEKLEKLLQLLplYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEEL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3246 QEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKEDLDKVEPAViEAQNAVKSIKKQHLV----------------EVRSMA 3309
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-EAAALEERLKEARLLlliaaallallglggsLLSLIL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3310 NPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIvnfsaEEISDAIREKMKKNYMSNPSYNYEIVNRASLAcgp 3389
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL-----EELEEEELEELLAALGLPPDLSPEELLELLDR--- 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3390 MVKWAIAQLNYADMLKR--VEPLRNELQKLEDDAK-----------DNQQKANEVEQMIRDLEASIARYKEEyavliSEA 3456
Cdd:COG4717 346 IEELQELLREAEELEEElqLEELEQEIAALLAEAGvedeeelraalEQAEEYQELKEELEELEEQLEELLGE-----LEE 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782055 3457 QAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYA 3515
Cdd:COG4717 421 LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELE 479
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2586-2735 |
2.37e-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: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2586 HKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRRTPNG-------VVLAPVQLGKWLV 2658
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGsgelrlrLALALARKLKPDV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782055 2659 LFCDEINLpdMDKYGTQRVISFIRQMVEHGGFYRTsdqtwvklERIQFVGACNPPTDPGRKPLSHRFLRHVPVVYVD 2735
Cdd:smart00382 82 LILDEITS--LLDAEQEALLLLLEELRLLLLLKSE--------KNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2920-3010 |
1.83e-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: 47.91 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2920 IDRIFRQPQGHLLLIGVSGAGKTTLSRFVAW---MNGLSVYQIKVHRKYTGEDFDEDLRTVLRRS----GCKNEKIAFIM 2992
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASDLLEGLVVAELFGHFLVRLlfelAEKAKPGVLFI 90
|
90
....*....|....*...
gi 1958782055 2993 DESNVLDSGFLERMNTLL 3010
Cdd:cd00009 91 DEIDSLSRGAQNALLRVL 108
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
3187-3559 |
2.53e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3187 EKRSELEEQQMHLNvglrkikETVDQVEELRRDLRIKSQELEvknaAANDKLKKMVKD--QQEAEKKKVMS-QEIQEQLH 3263
Cdd:PRK04863 297 TSRRQLAAEQYRLV-------EMARELAELNEAESDLEQDYQ----AASDHLNLVQTAlrQQEKIERYQADlEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3264 KQQEVIADKQmsvkEDLDKVEPAVIEAQNAVKSIKKQ------HLVEVRSMANPPAAVKLALESICLLLGESTTDWkqir 3337
Cdd:PRK04863 366 EQNEVVEEAD----EQQEENEARAEAAEEEVDELKSQladyqqALDVQQTRAIQYQQAVQALERAKQLCGLPDLTA---- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3338 siimrENFIPTIVNFSAEE---------------ISDAIREKMKKNYMSNPSYNYEIV-NRASlacgpmvKWAIAQLNYA 3401
Cdd:PRK04863 438 -----DNAEDWLEEFQAKEqeateellsleqklsVAQAAHSQFEQAYQLVRKIAGEVSrSEAW-------DVARELLRRL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3402 DMLK----RVEPLRNELQKLEDDAKdNQQKAN------------------EVEQMIRDLEASIARYKEEYAVLISEAQAI 3459
Cdd:PRK04863 506 REQRhlaeQLQQLRMRLSELEQRLR-QQQRAErllaefckrlgknlddedELEQLQEELEARLESLSESVSEARERRMAL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3460 KADLAAVEAKVNRstallksLSAERERWEKTSETFkNQMSTIAGDCLLSAAFIayagyfDQQMRQNLFTTWShhLQQANI 3539
Cdd:PRK04863 585 RQQLEQLQARIQR-------LAARAPAWLAAQDAL-ARLREQSGEEFEDSQDV------TEYMQQLLERERE--LTVERD 648
|
410 420
....*....|....*....|....*...
gi 1958782055 3540 QFRTDI----ARTEYLSNA----DERLR 3559
Cdd:PRK04863 649 ELAARKqaldEEIERLSQPggseDPRLN 676
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2588-2727 |
9.63e-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: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2588 PLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRRTPNGVVLAPVQLGKwlVLFCDEINLP 2667
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAAREGE--IAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782055 2668 DMDKYGTQ-RVISFIRQMVEHGGFYRTsdqtwVKLERIQFVGACNPPtDPGRKPLSHRFLR 2727
Cdd:pfam07728 79 NPDVLNSLlSLLDERRLLLPDGGELVK-----AAPDGFRLIATMNPL-DRGLNELSPALRS 133
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3232-3486 |
9.90e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3232 AAANDKLKKMVKDQQEAEKKKvmsQEIQEQLHKQQEVIADKQmsvkEDLDKVEPAVIEAQNAVKSIKKQhLVEVRsmanp 3311
Cdd:COG3883 12 AFADPQIQAKQKELSELQAEL---EAAQAELDALQAELEELN----EEYNELQAELEALQAEIDKLQAE-IAEAE----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3312 pAAVKLALEsiclLLGesttdwKQIRSIIMRENFIPTI-VNFSAEEISDAIrekmkknymsnpsynyeivNRASlacgpm 3390
Cdd:COG3883 79 -AEIEERRE----ELG------ERARALYRSGGSVSYLdVLLGSESFSDFL-------------------DRLS------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3391 vkwAIAQLNYADmLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASiaryKEEYAVLISEAQAIKADLAAVEAKV 3470
Cdd:COG3883 123 ---ALSKIADAD-ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA----KAELEAQQAEQEALLAQLSAEEAAA 194
|
250
....*....|....*.
gi 1958782055 3471 NRSTALLKSLSAERER 3486
Cdd:COG3883 195 EAQLAELEAELAAAEA 210
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3187-3488 |
2.86e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3187 EKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAA---ANDKLKKMVKDQQEAEKKKVMSQEIQEQLH 3263
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLLAELARLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3264 KQQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQHlvevrsmanppAAVKLALESICLLLGESTTDWKQIRSIIMRE 3343
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAEL-----------AEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3344 nfIPTIVNFSAEEISDAIREkmkknymsnpsynyeivnraslacgpmvkwAIAQLNYADMLKRVEPLRNELQKLEDDAKD 3423
Cdd:COG1196 392 --LRAAAELAAQLEELEEAE------------------------------EALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958782055 3424 NQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWE 3488
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3187-3483 |
3.58e-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: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3187 EKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEvknaaandklkkmvKDQQEAEKKKVMSQEIQEQLHKQQ 3266
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE--------------KEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3267 EVIADKQMSVKEDLDKVEpAVIEAQNAVKsikkqhlvevrsmanppAAVKLALESICLLLGESttDWKQIRSIImreNFI 3346
Cdd:TIGR02169 747 SSLEQEIENVKSELKELE-ARIEELEEDL-----------------HKLEEALNDLEARLSHS--RIPEIQAEL---SKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3347 PTIVNfSAEEISDAI-----REKMKKNYMSNPSYNYEIVNRAslacgpmvkwaiAQLNYADMLKRVEPLRNELQKLEDDA 3421
Cdd:TIGR02169 804 EEEVS-RIEARLREIeqklnRLTLEKEYLEKEIQELQEQRID------------LKEQIKSIEKEIENLNGKKEELEEEL 870
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782055 3422 KDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAE 3483
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3400-3483 |
3.71e-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: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3400 YADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVN-RSTALLK 3478
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEaEREELAA 170
|
....*
gi 1958782055 3479 SLSAE 3483
Cdd:COG1579 171 KIPPE 175
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2930-3087 |
4.97e-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: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2930 HLLLIGVSGAGKTTLS-RFVAWMNGLSVYQIKVHRKYTGEDF----------DEDLRTVLRRSGcKNEKIAFImDESNVL 2998
Cdd:pfam07728 1 GVLLVGPPGTGKTELAeRLAAALSNRPVFYVQLTRDTTEEDLfgrrnidpggASWVDGPLVRAA-REGEIAVL-DEINRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 2999 DSGFLERMNTLLANGEVPgLFEGDEYAtlmtqckegaqkeglmldsHEELYkwftsqvirNLHVVFTMNPSSEGLKDraa 3078
Cdd:pfam07728 79 NPDVLNSLLSLLDERRLL-LPDGGELV-------------------KAAPD---------GFRLIATMNPLDRGLNE--- 126
|
....*....
gi 1958782055 3079 TSPALFNRC 3087
Cdd:pfam07728 127 LSPALRSRF 135
|
|
| AIP3 |
smart00806 |
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ... |
3189-3321 |
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 1958782055 3189 RSELEEQQMHLnvgLRKIKETVDQVEELRRDL-----RIKSQELEVKN---AAANDKLKKMV----------KDQQEAEK 3250
Cdd:smart00806 212 KKKLSEDSDSL---LTKVDDLQDIIEALRKDVaqrgvRPSKKQLETVQkelETARKELKKMEeyidiekpiwKKIWEAEL 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782055 3251 KKVMsqEIQEQLHKQQEVIADkqmsVKEDLDKVEpaviEAQNAVKSIKKQHLVEVRSMANPPAAVKLALES 3321
Cdd:smart00806 289 DKVC--EEQQFLTLQEDLIAD----LKEDLEKAE----ETFDLVEQCCEEQEKGPSKNRNKPVSLPVPTPG 349
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3187-3300 |
1.66e-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: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3187 EKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKkMVKDQQEAEkkkVMSQEIqEQLHKQQ 3266
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG-NVRNNKEYE---ALQKEI-ESLKRRI 105
|
90 100 110
....*....|....*....|....*....|....
gi 1958782055 3267 EVIADKQMSVKEDLDKVEPAVIEAQNAVKSIKKQ 3300
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
3205-3493 |
1.77e-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: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3205 KIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMV---KDQ-QEAEKKKVMSQEIQEqlhkqqeviADKQMSVKEDL 3280
Cdd:COG5185 254 KLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFentKEKiAEYTKSIDIKKATES---------LEEQLAAAEAE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3281 DKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWK------QIRSIIMRENFIPTIVNFSA 3354
Cdd:COG5185 325 QELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEldsfkdTIESTKESLDEIPQNQRGYA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3355 EEISDAIREKMKknymsNPSYNYEIVNRaslacgpmvkwAIAQL--NYADMLKRVEPLRNELQKLEDDAKDNQQK--ANE 3430
Cdd:COG5185 405 QEILATLEDTLK-----AADRQIEELQR-----------QIEQAtsSNEEVSKLLNELISELNKVMREADEESQSrlEEA 468
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958782055 3431 VEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSET 3493
Cdd:COG5185 469 YDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMR 531
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3400-3504 |
2.30e-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: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3400 YADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKS 3479
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
90 100
....*....|....*....|....*
gi 1958782055 3480 LSAERERWEKTSETFKNQMSTIAGD 3504
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSED 853
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3394-3492 |
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 1958782055 3394 AIAQLNYADmLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKV-NR 3472
Cdd:COG4913 328 LEAQIRGNG-GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALeEA 406
|
90 100
....*....|....*....|.
gi 1958782055 3473 STALLKSLS-AERERWEKTSE 3492
Cdd:COG4913 407 LAEAEAALRdLRRELRELEAE 427
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3243-3486 |
4.11e-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: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3243 KDQQEAEKKKVmSQEIQEQLHKQQEVIADKQmSVKEDLDKVEPAVIEAQNAVKSIKKQHLV---EVRSMANPPAAVKLAL 3319
Cdd:COG4942 22 AAEAEAELEQL-QQEIAELEKELAALKKEEK-ALLKQLAALERRIAALARRIRALEQELAAleaELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3320 ESICLLLGEsttdwkQIRSIIMRENFIPTIVNFSAEEISDAIREKMKKNYMSNpsYNYEIVN--RASLACGPMVKWAIAQ 3397
Cdd:COG4942 100 EAQKEELAE------LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP--ARREQAEelRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3398 L--NYADMLKRVEPLRNELQKLEddakdnqqkaNEVEQMIRDLEASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTA 3475
Cdd:COG4942 172 EraELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
250
....*....|.
gi 1958782055 3476 LLKSLSAERER 3486
Cdd:COG4942 242 RTPAAGFAALK 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3187-3307 |
7.40e-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: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3187 EKRSELEEQQMHLNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKK-------VMSQEIQ 3259
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREInelkrelDRLQEEL 415
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3260 EQLHKQQEVIADKQMSVKEDLDKVEPAVIEAQNAVKSI--KKQHLVEVRS 3307
Cdd:TIGR02169 416 QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQewKLEQLAADLS 465
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
2911-2968 |
7.61e-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: 42.21 E-value: 7.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958782055 2911 NEVLDHVLRIDRIFRQ----PQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQIKVHR---KYTGE 2968
Cdd:COG0464 170 RELVALPLKRPELREEyglpPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDlvsKYVGE 234
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1903-2019 |
8.43e-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: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 1903 FGPAGTGKTESVKALGHQLGR---FVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEA 1979
Cdd:smart00382 8 VGPPGSGKTTLARALARELGPpggGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEI 87
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958782055 1980 LReHSNPNYDKTSAPITCELLNKQVKVSPDMAIFITMNPG 2019
Cdd:smart00382 88 TS-LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDE 126
|
|
| PulE |
COG2804 |
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ... |
2586-2615 |
8.65e-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: 8.65e-03
10 20 30
....*....|....*....|....*....|...
gi 1958782055 2586 HKP--LVL-CGPPGSGKTMTLFSALRALPDMEV 2615
Cdd:COG2804 310 RRPhgIILvTGPTGSGKTTTLYAALNELNTPER 342
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3401-3485 |
9.90e-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: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782055 3401 ADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDLEASIARYKE---------EYAVLISE---------------- 3455
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEieslkrrisdledeil 113
|
90 100 110
....*....|....*....|....*....|....*
gi 1958782055 3456 -----AQAIKADLAAVEAKVNRSTALLKSLSAERE 3485
Cdd:COG1579 114 elmerIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| |
