|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1009-4316 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 1157.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1009 TYRNLLTKLPEGkilENAYGAIEQKVSEVRNYVDEWLRYQSLWDLQADMLYGRLGEDVNLWIKCLNDIKQSRTTFDTSDT 1088
Cdd:COG5245 146 LSHELELIFRSG---EQWVGCMRKLYESVCSERDGFYEEKSFWSRFHMEMCHIREFCRSKAFRFACDVLRKSGKYVTVAT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1089 RRAY-GPIIIDYAKVQAKVTLKYDSWhkealgkfGTLLGTEMTSFHSKVSKSRTDLEmQSIEAASTSDAVSFITYVQSL- 1166
Cdd:COG5245 223 LDSLlSSSKYSELGRRLHFYANMDFS--------GIYFPKSFSEFKDSVISATQAVS-RDIGRQSRMARRLILVQMDSLa 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1167 --KKDMIAWDKQVEVFREAQRILERQRFQFPNTWLHVDNIEGEWSAFNEIIKRkDTAIQTQVASLqAKIVAEDKAVETRT 1244
Cdd:COG5245 294 rlIVDRICEYVSIEWLGCCEELLTCSMESMSSLVNSFDGEESEAMSLESSLFY-EFRGGEHLAGF-YSAFGDIKRILLFT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1245 VDFLNDWEKtKPTGGKIRPDDALQQLQIFESKYSRLKEERDNVVKAKEALelqesAVPNNSAERMNVALEELQDLRGVWS 1324
Cdd:COG5245 372 WSFKKLGTL-LPSLPGYSSGGMDYGEEYRSLLWELGSEVGDPDSGPVRKW-----MRKDLFDAKVRSGVSFGKQEEFVSD 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1325 ELSKVWTQIDETREKPWLSVQprkLRQQLEAMMAQLKELPaRLRMYESYEYVKKLIQSYIKVNMLIVELKSDALKerHWK 1404
Cdd:COG5245 446 IFNITFERIHGMDPTTLEDDE---EDTPALAILLGQEEAG-RFVKLCKIMRMFSFFNSLEMFSRRTLANRMAIVK--YLS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1405 QLTK----QLRVNWVLS-DLSLGQVWDVNLQKNEgivkdIILVAQGEMA--LEEFLKQVRESWQNYELDlinyqnkcRII 1477
Cdd:COG5245 520 SVVRtgplFLQRDFFGRmSELLMARDMFMEVDGV-----LRLFFGGEWSgiVQLSGIRRAKRCVERQID--------DEI 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1478 RGWddlfnkVKEHINSVAAMKLSPYYkvfeEEALTWEEKLNRINAlfdvwIDVqRRWVYLEGIFSGSADIKTLLPVETSR 1557
Cdd:COG5245 587 REW------CSSVLSDDFLEERAVRV----ERGADGARRLRASSG-----SPV-LRRLDEYLMMMSLEDLMPLIPHAVHR 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1558 FQSISSEFLGLMKKVTKSPKVMDVLNIPaVQRSLERLADLLGKIQKALGEYLERERTSFPRFyfVGDEDLLEIIGNSKNI 1637
Cdd:COG5245 651 KMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRVRELENR 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1638 ARLQKHFKKMFAGVAAILLNEenNVILGISSREGEEVHFMNPVSTVEHPKINEWLSLvekqmrfTLASLLAQAVQDIKQF 1717
Cdd:COG5245 728 VYSYRFFVKKIAKEEMKTVFS--SRIQKKEPFSLDSEAYVGFFRLYEKSIVIRGINR-------SMGRVLSQYLESVQEA 798
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1718 RDGKiDPQAYMEwcdKYQAQIVVLAAQiLWSEDVESALQQASennqSKPMQRVLGNVESTLNVLADSVLqeqpplrrRKL 1797
Cdd:COG5245 799 LEIE-DGSFFVS---RHRVRDGGLEKG-RGCDAWENCFDPPL----SEYFRILEKIFPSEEGYFFDEVL--------KRL 861
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1798 EHLINEFVHKRTVTRRLLNNGVTSPKSFQWLCEMRFYfdprqTEVLQQLTIHMANARFFYGFEYLGVQDRLVQTPLTDRC 1877
Cdd:COG5245 862 DPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-----QGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQ 936
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1878 YLTMTQALESRLggSPFgpAGTGKTESVKALGNQLGRFVlvfncdETFDFQAmgRIFVGLCQVGAWGcFDEFNRLEERML 1957
Cdd:COG5245 937 HQKLFEAVCDEV--CRF--VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR 1003
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1958 sACSQQIQTIQEALKYemdsNKESITveLVGKQVRVSPDMAIFITMNPgyagRSNLPDNLKKLFRSLAMTTPDRQlIAEV 2037
Cdd:COG5245 1004 -TILVDEYLNSDEFRM----LEELNS--AVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGA-IKSR 1071
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2038 MlfsqgfrsaEKLACKIVPFFKLCDEQLSNQSHYDFglRALKSVLisagnvkrdrimKIKEQMKQRGDENIDEASVAENL 2117
Cdd:COG5245 1072 R---------ESLDREIGAFNNEVDGIAREEDELMF--YPMFKSL------------KAKHRMLEEKTEYLNKILSITGL 1128
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2118 PeqeiliqsvcetmvpklvaedipllfsLLSDVFpnvgytRAEMKGLKEEIRKVCQEDYLVCGEGDEQGAAW-MEKVLQL 2196
Cdd:COG5245 1129 P---------------------------LISDTL------RERIDTLDAEWDSFCRISESLKKYESQQVSGLdVAQFVSF 1175
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2197 YQISNLNHGLMMVGPSGSGKSTAWKTLLKalerFEGVEGVAHVIDPkaiskealygVLDPnTREWTdGLFTHILRkiiDN 2276
Cdd:COG5245 1176 LRSVDTGAFHAEYFRVFLCKIKHYTDACD----YLWHVKSPYVKKK----------YFDA-DMELR-QFFLMFNR---ED 1236
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2277 VRGEI-NKRQWIIFDgdvdpEWVENLNSVLDDNKLLTLPNGERlslppnvRVMFEVQDlkfATLATVSRCGMVWFSEDVL 2355
Cdd:COG5245 1237 MEARLaDSKMEYEVE-----RYVEKTKAEVSSLKLELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRL 1301
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2356 STEMIFENYLSRLRsipledgdedfvgviKPAKDKEEEVSPSLQVQRDIALLLLPFFSAdgivvrTLEYAMDQEHIMD-- 2433
Cdd:COG5245 1302 STKGVFLDELGDTK---------------RYLDECLDFFSCFEEVQKEIDELSMVFCAD------ALRFSADLYHIVKer 1360
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2434 -----FTRLRALSSLFSMLNQAARNVltfnaqhpdfpcSADQLEHYIPKALVYSVLWSFAGDAKLKVRIDLGDFVRSVTT 2508
Cdd:COG5245 1361 rfsgvLAGSDASESLGGKSIELAAIL------------EHKDLIVEMKRGINDVLKLRIFGDKCRESTPRFYLISDGDLI 1428
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2509 VPLPGaagapIIDYE------VNMSGDWVPWSnKVPVIEVETHKVASP-DIVVPTLDTVRHESLLYTWLAEHKPLVLCGP 2581
Cdd:COG5245 1429 KDLNE-----RSDYEemlimmFNISAVITNNG-SIAGFELRGERVMLRkEVVIPTSDTGFVDSFSNEALNTLRSYIYCGP 1502
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2582 PGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRKTPNGVVLSPVQIGKWLVLFCDEINLPDMDSYGT 2661
Cdd:COG5245 1503 PGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYP 1582
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2662 QRVISFLRQLVEHKGFYRASDQAWVSLERIQFVGACNPPTDPGRKPLSHRFLRHVPIIYVDYPGETSLKQIYGTFSRAML 2741
Cdd:COG5245 1583 PTVIVFLRPLVERQGFWSSIAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSY 1662
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2742 RLMPALRGYAEPLTNAMVEFYLASQDRFTQDMQPHYVYSPREMTRWVRGICEAIRPLDSLPVEGLVRLWAHEALRLFQDR 2821
Cdd:COG5245 1663 LCFDEFNRLSEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDVSLIIDWYCEAIREKIDR 1742
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2822 LVDDSERRWTNENIDLVGQKHFPGINQEEALQRPILYSNWLSKDYMPVNREELREYVHARLKVFYEEELDVPLVLFDEVL 2901
Cdd:COG5245 1743 LVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFGMACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDAL 1822
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2902 DHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSIFQIKVHNKYTSEDFDEDLRCVLRRSGCKDEKIAFILDE 2981
Cdd:COG5245 1823 LHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFE 1902
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2982 SNVLDSGFLERMNTLLANGEVPGLFEGDEYTTLMTQCKEGAQREGLMLDSSDELYKWFTQQVMRNLHVVFTMNPSTDGLK 3061
Cdd:COG5245 1903 SIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEKDTEATLTRVFLVYMEENLPVVFSACCSQDTSV 1982
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3062 DRAATSPALFNRCVLNWFGDWSDSALFQVGKEFTTrvdLEKPNWHAPDFFPSVCPLVPANpTHRDAVINSCVYvhqtlHQ 3141
Cdd:COG5245 1983 LAGIRSPALKNRCFIDFKKLWDTEEMSQYANSVET---LSRDGGRVFFINGELGVGKGAL-ISEVFGDDAVVI-----EG 2053
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3142 ANARLAKRGGrTMAVTPRHYLDFIHHFVKLYNEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAA 3221
Cdd:COG5245 2054 RGFEISMIEG-SLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNA 2132
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3222 NAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRKYVMADLAQVEPAVIDAQAAVKSIRKQQLVEVRTMANPPSV 3301
Cdd:COG5245 2133 DDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGD 2212
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3302 VKLALESICLLLGENATDWKSIRAVIMRENFINSIVSNFGTENITDDVREKMKSKYLSNPDYNFEKVNRASMACGPMVKW 3381
Cdd:COG5245 2213 LCIEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPDEIEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRW 2292
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3382 AIAQIEYADMLKRVEPLREELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRS 3461
Cdd:COG5245 2293 LVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRS 2372
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3462 IALLKSLNIERERWESTSETFKSQMSTIIGDVLLSAAFIAYGGYFDQHYRLNLFTTwSQHLQAASIQYRADIART--EYL 3539
Cdd:COG5245 2373 IFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIRRRQfiTEG 2451
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3540 SNPDERLRWQANalpTDDLCTENA-IMLKRFNRYPLIIDPSGQATTFLLNEYAGKKITKTSFLDDSFRKNLESALRFGNP 3618
Cdd:COG5245 2452 VQKIEDFKEEAC---STDYGLENSrIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSD 2528
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3619 LLVQDVENYDPILNPVLNRELRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDICSRVTFVNFTVTRSSLQSQC 3698
Cdd:COG5245 2529 KIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEI 2608
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3699 LNQVLKAERPDIDEKRSDLLKLQGEFRLRLRQLEKSLLQALNDAKGKILDDDSVITTLETLKKEAYDINQKVDETDKVIA 3778
Cdd:COG5245 2609 PDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIED 2688
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3779 EIETVSQQYlPLSVACS-NIYFTMDSLNQVHFLYQYSLKMFLDIFSTVLyNNPKLEGRTdhserLGIVTRDLFQVCYERV 3857
Cdd:COG5245 2689 RIDALKSEY-NASVKRLeSIRVEIAMFDEKALMYNKSICELSSEFEKWR-RMKSKYLCA-----IRYMLMSSEWILDHED 2761
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3858 ARGMIHIDRLTFALLM-----CKIHLKGTSESNLDAEFNFFlrsregllanptpveGLSAEQIESVNRLALRLpifrkll 3932
Cdd:COG5245 2762 RSGFIHRLDVSFLLRTkrfvsTLLEDKNYRQVLSSCSLYGN---------------DVISHSCDRFDRDVYRA------- 2819
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3933 ekvrsipelgawlqqsspeqvvpqlwdeSKALSPIASSVHQLLLIQAFRPDRviaaaHNVVNTVLGEDF-MPNAEQELDF 4011
Cdd:COG5245 2820 ----------------------------LKHQMDNRTHSTILTSNSKTNPYK-----EYTYNDSWAEAFeVEDSGDLYKF 2866
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4012 TSVVDKQLNCNTPALlcsvpgfdasgrvddLAAEQNKQISSI--AIGSAEGFNQAERAINMACKTGRWVLLKNVHLAPQW 4089
Cdd:COG5245 2867 EEGLLELIVGHAPLI---------------YAHKKSLENERNvdRLGSKENEVYAVLNSLFSRKEKSWFEVYNISLSFGW 2931
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4090 LVQLEKKM----HSLQPHSGFRLFLT-MEINPKVPVNLLRAGRIFVFEPPPGIRANLLRTFSTVPAarMMK-TPSERARL 4163
Cdd:COG5245 2932 FKRYVEDVvypiKASRVCGKVKNMWTsMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLVEIDRY--PFDyTLVIACDD 3009
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4164 YFLLAWFHAIVQERLRYVPLGWAKKYEFNESDLRVACDTLDtwiDTTAMGRTNlppeKVPWDALVTLLSQSIYGGKIDND 4243
Cdd:COG5245 3010 AFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLK---NILFLNHLN----ARKWGNNRDLIFTIVYGKKHSLM 3082
|
3290 3300 3310 3320 3330 3340 3350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24658015 4244 FDQRLLTSFLKKLFTArsfEADFALVANVDGASGGLRHITMPDGTRRDHFLKwIENLTDRQTPSWLGLPNNAE 4316
Cdd:COG5245 3083 EDSKVVDKYCRGYGAH---ETSSQILASVPGGDPELVKFHMEEMCRSSAFGV-IGQLPDLALCAWLMGPCDSE 3151
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1857-2217 |
3.13e-168 |
|
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities: AAA1-AAA6). This is the first site (out of four nucleotide binding sites in the dynein motor) where the movement depends on ATP hydrolysis. When this site is nucleotide free or bound to ADP, the microtubule binding domain (MTBD) binds to the microtubule and the linker adopts the straight post-power-stroke conformation. Upon ATP binding and hydrolysis, the MTBD detaches from the microtubule and the linker is primed into the pre-power-stroke conformation. Dynein's AAA+ domains are each divided into an alpha/beta large subdomain designated with an L and and alpha small subdomains designated with an S. This is the AAA1 large (AAA1L) subdomain with the accompanying small subdomain (AAA1S). AAA1L, AAA1S and AAA2L enclose ADP.vanadate (ADP.Vi, ATP-hydrolysis transition state analogue). The AAA1L sensor-I loop, which varies in position depending on dynein's nucleotide state, swings in to contact AAA2L forming the important AAA1 nucleotide-binding site.
Pssm-ID: 463697 [Multi-domain] Cd Length: 327 Bit Score: 522.04 E-value: 3.13e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1857 YGFEYLGVQDRLVQTPLTDRCYLTMTQALESRLGGSPFGPAGTGKTESVKALGNQLGRFVLVFNCDETFDFQAMGRIFVG 1936
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1937 LCQVGAWGCFDEFNRLEERMLSACSQQIQTIQEALKyemdSNKESITVElvGKQVRVSPDMAIFITMNPGYAGRSNLPDN 2016
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALA----ANLKTFVFE--GSEIKLNPSCGIFITMNPGYAGRTELPDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2017 LKKLFRSLAMTTPDRQLIAEVMLFSQGFRSAEKLACKIVPFFKLCDEQLSNQSHYDFGLRALKSVLISAGNVKRDRimki 2096
Cdd:pfam12774 155 LKALFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSN---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2097 keqmkqrgdenideasvaENLPEQEILIQSVCETMVPKLVAEDIPLLFSLLSDVFPNVGYTRAEMKGLKEEIRKVCQEDY 2176
Cdd:pfam12774 231 ------------------PNLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELG 292
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 24658015 2177 LVCGEgdeqgaAWMEKVLQLYQISNLNHGLMMVGPSGSGKS 2217
Cdd:pfam12774 293 LQPHD------AFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
242-826 |
1.41e-133 |
|
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains to form dimers, and with intermediate chain-light chain complexes to form a basal cargo binding unit. The region featured in this family includes the sequences implicated in mediating these interactions. It is thought to be flexible and not to adopt a rigid conformation.
Pssm-ID: 462457 Cd Length: 560 Bit Score: 432.39 E-value: 1.41e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 242 LNLLQNGVNRWIAEIKKVTKLNRDPGSGTALQEISFWLNLERALYRIQEKRESPEVALTLDILKHGKRFHATVSFDTDTG 321
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKALDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 322 LKQALATVADYNPLMKDF--PINDLLSATELEKIRPAVQQIFAHLRKV-RNTKY--PIQRCLKLIEAISRDLSQQLLKVL 396
Cdd:pfam08385 81 LTDALNEAKDNVKYLKTLerPFEDLEELTDPPEIIEAIPPLMNTIRLIwSISRYynTSERMTVLLEKISNQLIEQCKKYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 397 GTRRLMHIPFDEFERVMNQCFEIFSCWDDEYDKLQGLLRDIVKKKRdehlkmvWRVSPAHK-----KLQTRMEHMRKFRR 471
Cdd:pfam08385 161 SPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERP-------WDFSERYIfgrfdAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 472 QHEQLRTviLRVLRPTKpavgddGNVVETKQpysldaadANAIEEVNLAYENVKEV--DCLDITKEGseaWEAAVKRYEE 549
Cdd:pfam08385 234 TIEQFSK--LEKIGGTK------GPELEGVI--------EEILEEFQEAYKVFKSKtyDILDVSNEG---FDDDYEEFKE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 550 KIDRVETRITAHLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIEALHEKFKVQypqsKSCRL 629
Cdd:pfam08385 295 RIKDLERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQ----KYNPS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 630 SSVRDLPPVAGSIIWARQIDNQLTMYLKRVEDVLGKGweTHIEGQKLKADGDSFRAKLS--ISDVFHEWARKVQERNFGS 707
Cdd:pfam08385 371 PIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLL--KHAEGKKVIKKYNELAKKLDeyERLIYEAWLKEVEEASEGN 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 708 TGR-IFTIESTRSRigrgnvlRLRVNFLPEIITLAKEVRNIKNLGFRVPLTIVNKAHQANQIYPYAISLIESVRTYERTL 786
Cdd:pfam08385 449 LKRpLLVRHPETGK-------LLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIR 521
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 24658015 787 EKIedRASIVPLVAGLRKDVLNLVSEGIGLI-WESYKLDPY 826
Cdd:pfam08385 522 STL--LPVERPLLAPHLKDIDEKLEPGLTTLtWNSLGIDEY 560
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4321-4634 |
2.18e-58 |
|
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein heavy chain. This domain is a complex structure comprising six alpha-helices and an incomplete six-stranded antiparallel beta-barrel. The shape of this domain is distinctively flat, spreading over the AAA1, AAA5 and AAA6 domain.
Pssm-ID: 465677 Cd Length: 301 Bit Score: 205.55 E-value: 2.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4321 TTRGTDLVSKLLKMQQLEDddelaysvedqseqsavGRGEDGRPSWMKTLHNSATAWLELLPKNL---QVLKRTVENIKD 4397
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSD-----------------SGGGGGGSSREEIVLELAKDILEKLPEPFdieEAEEKYPVGYED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4398 PLYRYFEREVTSGSRLLQTVILDLQDVVLICQGEKKQTNHHRSMLSELVRGIIPKGWKRYTVPAGCTVIQWITDFSNRVQ 4477
Cdd:pfam18199 64 PLNTVLLQEIERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4478 QLQKVSqlvsqagakELQGFP--VWLGGLLNPEAYITATRQCVAQANSWSLEELALDVTITDAGLKNDQ----KDCCFgV 4551
Cdd:pfam18199 144 QLQDWL---------DDEGPPkvFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSPEEVteppEDGVY-V 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4552 TGLKLQGAQC-KNNELLLAST---IMMDLPVTILKWIKISSEPRISKL-TLPVYLNSTR--TELLFTVDLavAAGQESHS 4624
Cdd:pfam18199 214 HGLFLEGARWdRKNGCLVESEpkeLFSPLPVIHLKPVESDKKKLDENTyECPVYKTSERhsTNFVFSVDL--PTDKPPDH 291
|
330
....*....|
gi 24658015 4625 FYERGVAVLT 4634
Cdd:pfam18199 292 WILRGVALLL 301
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2555-2718 |
9.98e-11 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 62.93 E-value: 9.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2555 PTLDTVRHESLLYTWLAEHKPLVLCGPPGSGKTMTLFSALRAL--PDMEVVGLNFSSATTPELLLKTFDHYCEYRKTpng 2632
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2633 vvlSPVQIGKWLVLFCDEIN-LPDMDSYGTQRVISFLRQLVEhkgfyrasdqawvSLERIQFVGACNPPTDPG-RKPLSH 2710
Cdd:cd00009 78 ---ELAEKAKPGVLFIDEIDsLSRGAQNALLRVLETLNDLRI-------------DRENVRVIGATNRPLLGDlDRALYD 141
|
....*...
gi 24658015 2711 RFLRHVPI 2718
Cdd:cd00009 142 RLDIRIVI 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2573-2718 |
1.80e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2573 HKPLVLCGPPGSGKTMTLFSALRALPDMevvGLNFSSATTPELLLKTFDHYCEYRKTPNGVVLSPVQI----------GK 2642
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPP---GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRlrlalalarkLK 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24658015 2643 WLVLFCDEI-NLPDMDSYGTQRVISFLRQLVEHKgfyrasdqawvSLERIQFVGACNPPTDPGRKPLSHRFLRHVPI 2718
Cdd:smart00382 79 PDVLILDEItSLLDAEQEALLLLLEELRLLLLLK-----------SEKNLTVILTTNDEKDLGPALLRRRFDRRIVL 144
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3172-3469 |
2.60e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3172 YNEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKslavKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLAD 3251
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEE----EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3252 QTVKIEEKRKYVMADLAQVEPAVIDAQAAVKSIRKQQLVEVRTMANppsvvklaLESICLLLGENATDWKSIRAVIMRE- 3330
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE--------LESRLEELEEQLETLRSKVAQLELQi 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3331 NFINSIVSNFGTE-NITDDVREKMKSkylSNPDYNFEKVNrasmacgpmvkwaiAQIEYADMlkRVEPLREELRSLEEQA 3409
Cdd:TIGR02168 396 ASLNNEIERLEARlERLEDRRERLQQ---EIEELLKKLEE--------------AELKELQA--ELEELEEELEELQEEL 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3410 DVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALLKSLN 3469
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
|
| RND_1 |
NF037998 |
protein translocase SecDF, variant type; Members of this family are identified by TCDB as ... |
3175-3369 |
2.40e-03 |
|
protein translocase SecDF, variant type; Members of this family are identified by TCDB as belonging to 2.A.6.4.4, a variant 12-TM type SecDF, as found in Spiroplasma, Mesoplasma, and Acholeplasma.
Pssm-ID: 468306 Cd Length: 1237 Bit Score: 44.38 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3175 KRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSlavKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTV 3254
Cdd:NF037998 642 KEKLSSKLLLKIKKINDKIDLLKKKEENKEAK---KNAKLIEKVKAKIKKLEQKITKLKLNKKKSNKIIKIRWKKKDWIF 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3255 KIEEKRKYVMADLAQVEPAVIDaqaavKSIRKQQLVEVRTMANPPSVVKLALESICLLLG--------------ENATDW 3320
Cdd:NF037998 719 FLKDNTDVILAIESEIEIQVIE-----KIKVKRNENNIFNITKIIIIIGLILSIIGGIVGftfgpnydstfgkgTTYTVY 793
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24658015 3321 KSIRAVIMRENFINSIVSNFGTENITDDVrEKMKSKYLSNPDYNFEKVN 3369
Cdd:NF037998 794 GDNLEELSNNNFVVTDIIDFGSKDKANEI-QELKDKIINEVSDPQAESS 841
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3172-3287 |
3.58e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3172 YNEKRSDLEEQQlhlnvglNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMfqDQQEAEKKKIQSQEIQI--RL 3249
Cdd:PRK12704 77 LRERRNELQKLE-------KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQEL--EKKEEELEELIEEQLQEleRI 147
|
90 100 110
....*....|....*....|....*....|....*...
gi 24658015 3250 ADQTVkiEEKRKYVMADLaqVEPAVIDAQAAVKSIRKQ 3287
Cdd:PRK12704 148 SGLTA--EEAKEILLEKV--EEEARHEAAVLIKEIEEE 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1009-4316 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 1157.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1009 TYRNLLTKLPEGkilENAYGAIEQKVSEVRNYVDEWLRYQSLWDLQADMLYGRLGEDVNLWIKCLNDIKQSRTTFDTSDT 1088
Cdd:COG5245 146 LSHELELIFRSG---EQWVGCMRKLYESVCSERDGFYEEKSFWSRFHMEMCHIREFCRSKAFRFACDVLRKSGKYVTVAT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1089 RRAY-GPIIIDYAKVQAKVTLKYDSWhkealgkfGTLLGTEMTSFHSKVSKSRTDLEmQSIEAASTSDAVSFITYVQSL- 1166
Cdd:COG5245 223 LDSLlSSSKYSELGRRLHFYANMDFS--------GIYFPKSFSEFKDSVISATQAVS-RDIGRQSRMARRLILVQMDSLa 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1167 --KKDMIAWDKQVEVFREAQRILERQRFQFPNTWLHVDNIEGEWSAFNEIIKRkDTAIQTQVASLqAKIVAEDKAVETRT 1244
Cdd:COG5245 294 rlIVDRICEYVSIEWLGCCEELLTCSMESMSSLVNSFDGEESEAMSLESSLFY-EFRGGEHLAGF-YSAFGDIKRILLFT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1245 VDFLNDWEKtKPTGGKIRPDDALQQLQIFESKYSRLKEERDNVVKAKEALelqesAVPNNSAERMNVALEELQDLRGVWS 1324
Cdd:COG5245 372 WSFKKLGTL-LPSLPGYSSGGMDYGEEYRSLLWELGSEVGDPDSGPVRKW-----MRKDLFDAKVRSGVSFGKQEEFVSD 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1325 ELSKVWTQIDETREKPWLSVQprkLRQQLEAMMAQLKELPaRLRMYESYEYVKKLIQSYIKVNMLIVELKSDALKerHWK 1404
Cdd:COG5245 446 IFNITFERIHGMDPTTLEDDE---EDTPALAILLGQEEAG-RFVKLCKIMRMFSFFNSLEMFSRRTLANRMAIVK--YLS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1405 QLTK----QLRVNWVLS-DLSLGQVWDVNLQKNEgivkdIILVAQGEMA--LEEFLKQVRESWQNYELDlinyqnkcRII 1477
Cdd:COG5245 520 SVVRtgplFLQRDFFGRmSELLMARDMFMEVDGV-----LRLFFGGEWSgiVQLSGIRRAKRCVERQID--------DEI 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1478 RGWddlfnkVKEHINSVAAMKLSPYYkvfeEEALTWEEKLNRINAlfdvwIDVqRRWVYLEGIFSGSADIKTLLPVETSR 1557
Cdd:COG5245 587 REW------CSSVLSDDFLEERAVRV----ERGADGARRLRASSG-----SPV-LRRLDEYLMMMSLEDLMPLIPHAVHR 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1558 FQSISSEFLGLMKKVTKSPKVMDVLNIPaVQRSLERLADLLGKIQKALGEYLERERTSFPRFyfVGDEDLLEIIGNSKNI 1637
Cdd:COG5245 651 KMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRVRELENR 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1638 ARLQKHFKKMFAGVAAILLNEenNVILGISSREGEEVHFMNPVSTVEHPKINEWLSLvekqmrfTLASLLAQAVQDIKQF 1717
Cdd:COG5245 728 VYSYRFFVKKIAKEEMKTVFS--SRIQKKEPFSLDSEAYVGFFRLYEKSIVIRGINR-------SMGRVLSQYLESVQEA 798
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1718 RDGKiDPQAYMEwcdKYQAQIVVLAAQiLWSEDVESALQQASennqSKPMQRVLGNVESTLNVLADSVLqeqpplrrRKL 1797
Cdd:COG5245 799 LEIE-DGSFFVS---RHRVRDGGLEKG-RGCDAWENCFDPPL----SEYFRILEKIFPSEEGYFFDEVL--------KRL 861
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1798 EHLINEFVHKRTVTRRLLNNGVTSPKSFQWLCEMRFYfdprqTEVLQQLTIHMANARFFYGFEYLGVQDRLVQTPLTDRC 1877
Cdd:COG5245 862 DPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-----QGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQ 936
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1878 YLTMTQALESRLggSPFgpAGTGKTESVKALGNQLGRFVlvfncdETFDFQAmgRIFVGLCQVGAWGcFDEFNRLEERML 1957
Cdd:COG5245 937 HQKLFEAVCDEV--CRF--VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR 1003
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1958 sACSQQIQTIQEALKYemdsNKESITveLVGKQVRVSPDMAIFITMNPgyagRSNLPDNLKKLFRSLAMTTPDRQlIAEV 2037
Cdd:COG5245 1004 -TILVDEYLNSDEFRM----LEELNS--AVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIPFGA-IKSR 1071
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2038 MlfsqgfrsaEKLACKIVPFFKLCDEQLSNQSHYDFglRALKSVLisagnvkrdrimKIKEQMKQRGDENIDEASVAENL 2117
Cdd:COG5245 1072 R---------ESLDREIGAFNNEVDGIAREEDELMF--YPMFKSL------------KAKHRMLEEKTEYLNKILSITGL 1128
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2118 PeqeiliqsvcetmvpklvaedipllfsLLSDVFpnvgytRAEMKGLKEEIRKVCQEDYLVCGEGDEQGAAW-MEKVLQL 2196
Cdd:COG5245 1129 P---------------------------LISDTL------RERIDTLDAEWDSFCRISESLKKYESQQVSGLdVAQFVSF 1175
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2197 YQISNLNHGLMMVGPSGSGKSTAWKTLLKalerFEGVEGVAHVIDPkaiskealygVLDPnTREWTdGLFTHILRkiiDN 2276
Cdd:COG5245 1176 LRSVDTGAFHAEYFRVFLCKIKHYTDACD----YLWHVKSPYVKKK----------YFDA-DMELR-QFFLMFNR---ED 1236
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2277 VRGEI-NKRQWIIFDgdvdpEWVENLNSVLDDNKLLTLPNGERlslppnvRVMFEVQDlkfATLATVSRCGMVWFSEDVL 2355
Cdd:COG5245 1237 MEARLaDSKMEYEVE-----RYVEKTKAEVSSLKLELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRL 1301
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2356 STEMIFENYLSRLRsipledgdedfvgviKPAKDKEEEVSPSLQVQRDIALLLLPFFSAdgivvrTLEYAMDQEHIMD-- 2433
Cdd:COG5245 1302 STKGVFLDELGDTK---------------RYLDECLDFFSCFEEVQKEIDELSMVFCAD------ALRFSADLYHIVKer 1360
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2434 -----FTRLRALSSLFSMLNQAARNVltfnaqhpdfpcSADQLEHYIPKALVYSVLWSFAGDAKLKVRIDLGDFVRSVTT 2508
Cdd:COG5245 1361 rfsgvLAGSDASESLGGKSIELAAIL------------EHKDLIVEMKRGINDVLKLRIFGDKCRESTPRFYLISDGDLI 1428
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2509 VPLPGaagapIIDYE------VNMSGDWVPWSnKVPVIEVETHKVASP-DIVVPTLDTVRHESLLYTWLAEHKPLVLCGP 2581
Cdd:COG5245 1429 KDLNE-----RSDYEemlimmFNISAVITNNG-SIAGFELRGERVMLRkEVVIPTSDTGFVDSFSNEALNTLRSYIYCGP 1502
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2582 PGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRKTPNGVVLSPVQIGKWLVLFCDEINLPDMDSYGT 2661
Cdd:COG5245 1503 PGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYP 1582
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2662 QRVISFLRQLVEHKGFYRASDQAWVSLERIQFVGACNPPTDPGRKPLSHRFLRHVPIIYVDYPGETSLKQIYGTFSRAML 2741
Cdd:COG5245 1583 PTVIVFLRPLVERQGFWSSIAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSY 1662
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2742 RLMPALRGYAEPLTNAMVEFYLASQDRFTQDMQPHYVYSPREMTRWVRGICEAIRPLDSLPVEGLVRLWAHEALRLFQDR 2821
Cdd:COG5245 1663 LCFDEFNRLSEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDVSLIIDWYCEAIREKIDR 1742
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2822 LVDDSERRWTNENIDLVGQKHFPGINQEEALQRPILYSNWLSKDYMPVNREELREYVHARLKVFYEEELDVPLVLFDEVL 2901
Cdd:COG5245 1743 LVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFGMACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDAL 1822
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2902 DHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSIFQIKVHNKYTSEDFDEDLRCVLRRSGCKDEKIAFILDE 2981
Cdd:COG5245 1823 LHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFE 1902
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2982 SNVLDSGFLERMNTLLANGEVPGLFEGDEYTTLMTQCKEGAQREGLMLDSSDELYKWFTQQVMRNLHVVFTMNPSTDGLK 3061
Cdd:COG5245 1903 SIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEKDTEATLTRVFLVYMEENLPVVFSACCSQDTSV 1982
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3062 DRAATSPALFNRCVLNWFGDWSDSALFQVGKEFTTrvdLEKPNWHAPDFFPSVCPLVPANpTHRDAVINSCVYvhqtlHQ 3141
Cdd:COG5245 1983 LAGIRSPALKNRCFIDFKKLWDTEEMSQYANSVET---LSRDGGRVFFINGELGVGKGAL-ISEVFGDDAVVI-----EG 2053
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3142 ANARLAKRGGrTMAVTPRHYLDFIHHFVKLYNEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAA 3221
Cdd:COG5245 2054 RGFEISMIEG-SLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNA 2132
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3222 NAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRKYVMADLAQVEPAVIDAQAAVKSIRKQQLVEVRTMANPPSV 3301
Cdd:COG5245 2133 DDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGD 2212
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3302 VKLALESICLLLGENATDWKSIRAVIMRENFINSIVSNFGTENITDDVREKMKSKYLSNPDYNFEKVNRASMACGPMVKW 3381
Cdd:COG5245 2213 LCIEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPDEIEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRW 2292
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3382 AIAQIEYADMLKRVEPLREELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRS 3461
Cdd:COG5245 2293 LVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRS 2372
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3462 IALLKSLNIERERWESTSETFKSQMSTIIGDVLLSAAFIAYGGYFDQHYRLNLFTTwSQHLQAASIQYRADIART--EYL 3539
Cdd:COG5245 2373 IFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIRRRQfiTEG 2451
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3540 SNPDERLRWQANalpTDDLCTENA-IMLKRFNRYPLIIDPSGQATTFLLNEYAGKKITKTSFLDDSFRKNLESALRFGNP 3618
Cdd:COG5245 2452 VQKIEDFKEEAC---STDYGLENSrIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSD 2528
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3619 LLVQDVENYDPILNPVLNRELRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDICSRVTFVNFTVTRSSLQSQC 3698
Cdd:COG5245 2529 KIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEI 2608
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3699 LNQVLKAERPDIDEKRSDLLKLQGEFRLRLRQLEKSLLQALNDAKGKILDDDSVITTLETLKKEAYDINQKVDETDKVIA 3778
Cdd:COG5245 2609 PDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIED 2688
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3779 EIETVSQQYlPLSVACS-NIYFTMDSLNQVHFLYQYSLKMFLDIFSTVLyNNPKLEGRTdhserLGIVTRDLFQVCYERV 3857
Cdd:COG5245 2689 RIDALKSEY-NASVKRLeSIRVEIAMFDEKALMYNKSICELSSEFEKWR-RMKSKYLCA-----IRYMLMSSEWILDHED 2761
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3858 ARGMIHIDRLTFALLM-----CKIHLKGTSESNLDAEFNFFlrsregllanptpveGLSAEQIESVNRLALRLpifrkll 3932
Cdd:COG5245 2762 RSGFIHRLDVSFLLRTkrfvsTLLEDKNYRQVLSSCSLYGN---------------DVISHSCDRFDRDVYRA------- 2819
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3933 ekvrsipelgawlqqsspeqvvpqlwdeSKALSPIASSVHQLLLIQAFRPDRviaaaHNVVNTVLGEDF-MPNAEQELDF 4011
Cdd:COG5245 2820 ----------------------------LKHQMDNRTHSTILTSNSKTNPYK-----EYTYNDSWAEAFeVEDSGDLYKF 2866
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4012 TSVVDKQLNCNTPALlcsvpgfdasgrvddLAAEQNKQISSI--AIGSAEGFNQAERAINMACKTGRWVLLKNVHLAPQW 4089
Cdd:COG5245 2867 EEGLLELIVGHAPLI---------------YAHKKSLENERNvdRLGSKENEVYAVLNSLFSRKEKSWFEVYNISLSFGW 2931
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4090 LVQLEKKM----HSLQPHSGFRLFLT-MEINPKVPVNLLRAGRIFVFEPPPGIRANLLRTFSTVPAarMMK-TPSERARL 4163
Cdd:COG5245 2932 FKRYVEDVvypiKASRVCGKVKNMWTsMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLVEIDRY--PFDyTLVIACDD 3009
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4164 YFLLAWFHAIVQERLRYVPLGWAKKYEFNESDLRVACDTLDtwiDTTAMGRTNlppeKVPWDALVTLLSQSIYGGKIDND 4243
Cdd:COG5245 3010 AFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLK---NILFLNHLN----ARKWGNNRDLIFTIVYGKKHSLM 3082
|
3290 3300 3310 3320 3330 3340 3350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24658015 4244 FDQRLLTSFLKKLFTArsfEADFALVANVDGASGGLRHITMPDGTRRDHFLKwIENLTDRQTPSWLGLPNNAE 4316
Cdd:COG5245 3083 EDSKVVDKYCRGYGAH---ETSSQILASVPGGDPELVKFHMEEMCRSSAFGV-IGQLPDLALCAWLMGPCDSE 3151
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1857-2217 |
3.13e-168 |
|
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities: AAA1-AAA6). This is the first site (out of four nucleotide binding sites in the dynein motor) where the movement depends on ATP hydrolysis. When this site is nucleotide free or bound to ADP, the microtubule binding domain (MTBD) binds to the microtubule and the linker adopts the straight post-power-stroke conformation. Upon ATP binding and hydrolysis, the MTBD detaches from the microtubule and the linker is primed into the pre-power-stroke conformation. Dynein's AAA+ domains are each divided into an alpha/beta large subdomain designated with an L and and alpha small subdomains designated with an S. This is the AAA1 large (AAA1L) subdomain with the accompanying small subdomain (AAA1S). AAA1L, AAA1S and AAA2L enclose ADP.vanadate (ADP.Vi, ATP-hydrolysis transition state analogue). The AAA1L sensor-I loop, which varies in position depending on dynein's nucleotide state, swings in to contact AAA2L forming the important AAA1 nucleotide-binding site.
Pssm-ID: 463697 [Multi-domain] Cd Length: 327 Bit Score: 522.04 E-value: 3.13e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1857 YGFEYLGVQDRLVQTPLTDRCYLTMTQALESRLGGSPFGPAGTGKTESVKALGNQLGRFVLVFNCDETFDFQAMGRIFVG 1936
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1937 LCQVGAWGCFDEFNRLEERMLSACSQQIQTIQEALKyemdSNKESITVElvGKQVRVSPDMAIFITMNPGYAGRSNLPDN 2016
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALA----ANLKTFVFE--GSEIKLNPSCGIFITMNPGYAGRTELPDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2017 LKKLFRSLAMTTPDRQLIAEVMLFSQGFRSAEKLACKIVPFFKLCDEQLSNQSHYDFGLRALKSVLISAGNVKRDRimki 2096
Cdd:pfam12774 155 LKALFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSN---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2097 keqmkqrgdenideasvaENLPEQEILIQSVCETMVPKLVAEDIPLLFSLLSDVFPNVGYTRAEMKGLKEEIRKVCQEDY 2176
Cdd:pfam12774 231 ------------------PNLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELG 292
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 24658015 2177 LVCGEgdeqgaAWMEKVLQLYQISNLNHGLMMVGPSGSGKS 2217
Cdd:pfam12774 293 LQPHD------AFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1309-1710 |
9.94e-143 |
|
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic cells, as they can convert energy derived from the hydrolysis of ATP to force and movement along cytoskeletal polymers, such as microtubules. This region is found C-terminal to the dynein heavy chain N-terminal region 1 (pfam08385) in many members of this family. No functions seem to have been attributed specifically to this region.
Pssm-ID: 462462 [Multi-domain] Cd Length: 402 Bit Score: 452.10 E-value: 9.94e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1309 MNVALEELQDLRGVWSELSKVWTQIDETREKPWLSVQPRKLRQQLEAMMAQLKELPARLRMYESYEYVKKLIQSYIKVNM 1388
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1389 LIVELKSDALKERHWKQLTKQLRVNW--VLSDLSLGQVWDVNLQKNEGIVKDIILVAQGEMALEEFLKQVRESWQNYELD 1466
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFdpLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1467 LINYQN-KCRIIRGWDDLFNKVKEHINSVAAMKLSPYYKVFEEEALTWEEKLNRINALFDVWIDVQRRWVYLEGIFSGSa 1545
Cdd:pfam08393 161 LVPYKDtGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSSE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1546 DIKTLLPVETSRFQSISSEFLGLMKKVTKSPKVMDVLNIPAVQRSLERLADLLGKIQKALGEYLERERTSFPRFYFVGDE 1625
Cdd:pfam08393 240 DIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSND 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1626 DLLEIIGNSKNIARLQKHFKKMFAGVAAILLNeENNVILGISSREGEEVHFMNPVSTVEhPKINEWLSLVEKQMRFTLAS 1705
Cdd:pfam08393 320 ELLEILSQTKDPTRVQPHLKKCFEGIASLEFD-ENKEITGMISKEGEVVPFSKPPVEAK-GNVEEWLNELEEEMRETLRD 397
|
....*
gi 24658015 1706 LLAQA 1710
Cdd:pfam08393 398 LLKEA 402
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
242-826 |
1.41e-133 |
|
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains to form dimers, and with intermediate chain-light chain complexes to form a basal cargo binding unit. The region featured in this family includes the sequences implicated in mediating these interactions. It is thought to be flexible and not to adopt a rigid conformation.
Pssm-ID: 462457 Cd Length: 560 Bit Score: 432.39 E-value: 1.41e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 242 LNLLQNGVNRWIAEIKKVTKLNRDPGSGTALQEISFWLNLERALYRIQEKRESPEVALTLDILKHGKRFHATVSFDTDTG 321
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKALDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 322 LKQALATVADYNPLMKDF--PINDLLSATELEKIRPAVQQIFAHLRKV-RNTKY--PIQRCLKLIEAISRDLSQQLLKVL 396
Cdd:pfam08385 81 LTDALNEAKDNVKYLKTLerPFEDLEELTDPPEIIEAIPPLMNTIRLIwSISRYynTSERMTVLLEKISNQLIEQCKKYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 397 GTRRLMHIPFDEFERVMNQCFEIFSCWDDEYDKLQGLLRDIVKKKRdehlkmvWRVSPAHK-----KLQTRMEHMRKFRR 471
Cdd:pfam08385 161 SPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERP-------WDFSERYIfgrfdAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 472 QHEQLRTviLRVLRPTKpavgddGNVVETKQpysldaadANAIEEVNLAYENVKEV--DCLDITKEGseaWEAAVKRYEE 549
Cdd:pfam08385 234 TIEQFSK--LEKIGGTK------GPELEGVI--------EEILEEFQEAYKVFKSKtyDILDVSNEG---FDDDYEEFKE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 550 KIDRVETRITAHLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIEALHEKFKVQypqsKSCRL 629
Cdd:pfam08385 295 RIKDLERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQ----KYNPS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 630 SSVRDLPPVAGSIIWARQIDNQLTMYLKRVEDVLGKGweTHIEGQKLKADGDSFRAKLS--ISDVFHEWARKVQERNFGS 707
Cdd:pfam08385 371 PIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLL--KHAEGKKVIKKYNELAKKLDeyERLIYEAWLKEVEEASEGN 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 708 TGR-IFTIESTRSRigrgnvlRLRVNFLPEIITLAKEVRNIKNLGFRVPLTIVNKAHQANQIYPYAISLIESVRTYERTL 786
Cdd:pfam08385 449 LKRpLLVRHPETGK-------LLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIR 521
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 24658015 787 EKIedRASIVPLVAGLRKDVLNLVSEGIGLI-WESYKLDPY 826
Cdd:pfam08385 522 STL--LPVERPLLAPHLKDIDEKLEPGLTTLtWNSLGIDEY 560
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3546-3766 |
1.21e-99 |
|
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the fifth AAA+ domain subdomain AAA5S. Structural analysis reveal that it is the coiled-coil buttress interface. The relative movement of AAA5S together with the stalk (AAA4S), is coupled to rearrangements in the AAA+ ring. Closure of the AAA1 site and the rigid body movement of AAA2-AAA4 force the AAA4/AAA5 interface to close and the AAA6L subdomain to rotate towards the ring centre. The AAA5S subdomain rotates as a unit together with AAA6L, and this movement pulls the buttress relative to the stalk.
Pssm-ID: 463702 [Multi-domain] Cd Length: 222 Bit Score: 320.54 E-value: 1.21e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3546 LRWQANALPTDDLCTENAIMLKRFNRYPLIIDPSGQATTFLLNEYAGKKITKTSFLDDSFRKNLESALRFGNPLLVQDV- 3624
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3625 ENYDPILNPVLNRELRRTGGRVLITLGDQDIDLSPSFVIFLSTRDPTVEFPPDICSRVTFVNFTVTRSSLQSQCLNQVLK 3704
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24658015 3705 AERPDIDEKRSDLLKLQGEFRLRLRQLEKSLLQALNDAKGKILDDDSVITTLETLKKEAYDI 3766
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2893-3171 |
6.53e-68 |
|
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This particular family is the D4 ATP-binding region of the motor.
Pssm-ID: 463701 [Multi-domain] Cd Length: 259 Bit Score: 231.34 E-value: 6.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2893 PLVLFDEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSIFQIKVHNKYTSEDFDEDLRCVLRRSGCKD 2972
Cdd:pfam12780 2 DLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2973 EKIAFILDESNVLDSGFLERMNTLLANGEVPGLFEGDEYTTLMTQCKEGAQREGLmLDSSDELYKWFTQQVMRNLHVVFT 3052
Cdd:pfam12780 82 KPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNI-EDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3053 MNPSTDGLKDRAATSPALFNRCVLNWFGDWSDSALFQVGKEFTTRVdlekpnwhapdffpsvcpLVPANptHRDAVINSC 3132
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDI------------------EIPEE--LKSNVVKVF 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 24658015 3133 VYVHQTLHQANARLAKRGGRTMAVTPRHYLDFIHHFVKL 3171
Cdd:pfam12780 221 VYVHSSVEDMSKKFYEELKRKNYVTPKSYLELLRLYKNL 259
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4321-4634 |
2.18e-58 |
|
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein heavy chain. This domain is a complex structure comprising six alpha-helices and an incomplete six-stranded antiparallel beta-barrel. The shape of this domain is distinctively flat, spreading over the AAA1, AAA5 and AAA6 domain.
Pssm-ID: 465677 Cd Length: 301 Bit Score: 205.55 E-value: 2.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4321 TTRGTDLVSKLLKMQQLEDddelaysvedqseqsavGRGEDGRPSWMKTLHNSATAWLELLPKNL---QVLKRTVENIKD 4397
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSD-----------------SGGGGGGSSREEIVLELAKDILEKLPEPFdieEAEEKYPVGYED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4398 PLYRYFEREVTSGSRLLQTVILDLQDVVLICQGEKKQTNHHRSMLSELVRGIIPKGWKRYTVPAGCTVIQWITDFSNRVQ 4477
Cdd:pfam18199 64 PLNTVLLQEIERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4478 QLQKVSqlvsqagakELQGFP--VWLGGLLNPEAYITATRQCVAQANSWSLEELALDVTITDAGLKNDQ----KDCCFgV 4551
Cdd:pfam18199 144 QLQDWL---------DDEGPPkvFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSPEEVteppEDGVY-V 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4552 TGLKLQGAQC-KNNELLLAST---IMMDLPVTILKWIKISSEPRISKL-TLPVYLNSTR--TELLFTVDLavAAGQESHS 4624
Cdd:pfam18199 214 HGLFLEGARWdRKNGCLVESEpkeLFSPLPVIHLKPVESDKKKLDENTyECPVYKTSERhsTNFVFSVDL--PTDKPPDH 291
|
330
....*....|
gi 24658015 4625 FYERGVAVLT 4634
Cdd:pfam18199 292 WILRGVALLL 301
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
4160-4315 |
2.11e-56 |
|
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the C-terminal region of dynein heavy chain.
Pssm-ID: 465676 Cd Length: 139 Bit Score: 193.05 E-value: 2.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4160 RARLYFLLAWFHAIVQERLRYVPLGWAKKYEFNESDLRVACDTLDTWIDTtamgrtnlPPEKVPWDALVTLLSQSIYGGK 4239
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDE--------YDEKIPWDALRYLIGEINYGGR 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24658015 4240 IDNDFDQRLLTSFLKKLFTARSFEADFALVANVdgasgglrhITMPDGTRRDHFLKWIENLTDRQTPSWLGLPNNA 4315
Cdd:pfam18198 73 VTDDWDRRLLNTYLEEFFNPEVLEEDFKFSPSL---------YYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
3186-3522 |
1.72e-43 |
|
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: 164.09 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3186 LNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRKYVMA 3265
Cdd:pfam12777 3 LENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3266 DLAQVEPAVIDAQAAVKSIRKQQLVEVRTMANPPSVVKLALESICLLL---GENATD--WKSIRAVIMR-ENFINSIVsN 3339
Cdd:pfam12777 83 DLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMapgGKIPKDksWKAAKIMMAKvDGFLDSLI-K 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3340 FGTENITDDVREKMKSkYLSNPDYNFEKVNRASMACGPMVKWAIAQIEYADMLKRVEPLREELrsleEQADVNLASAKET 3419
Cdd:pfam12777 162 FDKEHIHEACLKAFKP-YLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQAL----EEANADLAAAQEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3420 kdlVEQLERSIAAYKEEYAQLISQ-----AQAIKTDLENVQAKVDRSIA--LLKSLNIERERWESTSETFKSQMSTIIGD 3492
Cdd:pfam12777 237 ---LAAIKAKIAELNANLAKLTAAfekatADKIKCQQEADATARTILLAnrLVGGLASENIRWADAVENFKQQERTLCGD 313
|
330 340 350
....*....|....*....|....*....|.
gi 24658015 3493 VLLSAAFIAYGGYFDQHYRLNLF-TTWSQHL 3522
Cdd:pfam12777 314 ILLISAFISYLGFFTKKYRNELLdKFWIPYI 344
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2551-2724 |
1.61e-42 |
|
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).
Pssm-ID: 463698 [Multi-domain] Cd Length: 179 Bit Score: 155.24 E-value: 1.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2551 DIVVPTLDTVRHESLLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALP--DMEVVGLNFSSATTPELLLKTFDHYCEYRK 2628
Cdd:pfam12775 9 EILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDkeKYLPLFINFSAQTTSNQTQDIIESKLEKRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2629 tpnGVVLSPVqIGKWLVLFCDEINLPDMDSYGTQRVISFLRQLVEHKGFYRASDQAWVSLERIQFVGACNPPTdPGRKPL 2708
Cdd:pfam12775 89 ---KGVYGPP-GGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPG-GGRNDI 163
|
170
....*....|....*.
gi 24658015 2709 SHRFLRHVPIIYVDYP 2724
Cdd:pfam12775 164 TPRLLRHFNVFNITFP 179
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
4020-4130 |
8.31e-37 |
|
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of dynein heavy chain. The chain also contains ATPase activity and microtubule binding ability and acts as a motor for the movement of organelles and vesicles along microtubules. Dynein is also involved in cilia and flagella movement. The dynein subunit consists of at least two heavy chains and a number of intermediate and light chains. The 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This C-terminal domain carries the D6 region of the dynein motor where the P-loop has been lost in evolution but the general structure of a potential ATP binding site appears to be retained.
Pssm-ID: 460782 Cd Length: 115 Bit Score: 136.42 E-value: 8.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 4020 NCNTPALLCSVPGFDASGRVDDLAAEQN--KQISSIAIGSAEGFnQAERAINMACKTGRWVLLKNVHLAPQWLVQLEKKM 4097
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGfgGKLHSISLGQGQGP-IAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKIL 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 24658015 4098 HSLQ---PHSGFRLFLTMEINPKVPVNLLRAGRIFV 4130
Cdd:pfam03028 80 EELPeetLHPDFRLWLTSEPSPKFPISILQNSIKIT 115
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2408-2535 |
2.02e-22 |
|
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA domain 5 in the dynein heavy chain. This domain is composed of 8 alpha helices.
Pssm-ID: 465532 [Multi-domain] Cd Length: 126 Bit Score: 95.43 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2408 LLPFFsaDGIVVRTLEYAMDQ-EHIMDFTRLRALSSLFSMLNQAARNVLTFNAQHPdfpCSADQLEHYIPKALVYSVLWS 2486
Cdd:pfam17852 1 LEPLF--EWLVPPALEFVRKNcKEIVPTSDLNLVQSLCRLLESLLDEVLEYNGVHP---LSPDKLKEYLEKLFLFALVWS 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 24658015 2487 FAGDAKLKVRIDLGDFVRSVTT-VPLPGAAGAPIIDYEVNM-SGDWVPWSN 2535
Cdd:pfam17852 76 IGGTLDEDSRKKFDEFLRELFSgLDLPPPEKGTVYDYFVDLeKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2205-2345 |
6.42e-15 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 74.64 E-value: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2205 GLMMVGPSGSGKSTAWKTLLKALERFEGVEgvahVIDPKAISKEALYGVLDPNTR--EWTDGLFTHILRKiidnvrgein 2282
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFY----VQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAARE---------- 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24658015 2283 krQWIIFDGDVD---PEWVENLNSVLDDNKLLTLPNGERLSLPP-NVRVMFEV----QDLKFATLATVSRC 2345
Cdd:pfam07728 67 --GEIAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMnpldRGLNELSPALRSRF 135
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2555-2718 |
9.98e-11 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 62.93 E-value: 9.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2555 PTLDTVRHESLLYTWLAEHKPLVLCGPPGSGKTMTLFSALRAL--PDMEVVGLNFSSATTPELLLKTFDHYCEYRKTpng 2632
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrPGAPFLYLNASDLLEGLVVAELFGHFLVRLLF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2633 vvlSPVQIGKWLVLFCDEIN-LPDMDSYGTQRVISFLRQLVEhkgfyrasdqawvSLERIQFVGACNPPTDPG-RKPLSH 2710
Cdd:cd00009 78 ---ELAEKAKPGVLFIDEIDsLSRGAQNALLRVLETLNDLRI-------------DRENVRVIGATNRPLLGDlDRALYD 141
|
....*...
gi 24658015 2711 RFLRHVPI 2718
Cdd:cd00009 142 RLDIRIVI 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2573-2718 |
1.80e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2573 HKPLVLCGPPGSGKTMTLFSALRALPDMevvGLNFSSATTPELLLKTFDHYCEYRKTPNGVVLSPVQI----------GK 2642
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPP---GGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRlrlalalarkLK 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24658015 2643 WLVLFCDEI-NLPDMDSYGTQRVISFLRQLVEHKgfyrasdqawvSLERIQFVGACNPPTDPGRKPLSHRFLRHVPI 2718
Cdd:smart00382 79 PDVLILDEItSLLDAEQEALLLLLEELRLLLLLK-----------SEKNLTVILTTNDEKDLGPALLRRRFDRRIVL 144
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3190-3288 |
3.91e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3190 LNKIAE----TVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRKYVMA 3265
Cdd:COG3883 124 LSKIADadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
90 100
....*....|....*....|...
gi 24658015 3266 DLAQVEPAVIDAQAAVKSIRKQQ 3288
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2907-2997 |
4.24e-05 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 46.76 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2907 IDRIFRQPQGHLLLIGVSGAGKTTLSRFVAW---MNGLSIFQIKVHNKYTSEDFDEDLRCVLRRS----GCKDEKIAFIL 2979
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASDLLEGLVVAELFGHFLVRLlfelAEKAKPGVLFI 90
|
90
....*....|....*...
gi 24658015 2980 DESNVLDSGFLERMNTLL 2997
Cdd:cd00009 91 DEIDSLSRGAQNALLRVL 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3170-3465 |
7.42e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3170 KLYNEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRL 3249
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3250 ADQTVKIEEKRKYVMADLAQVEPAVIDAQAAVKSIRKQQlvevrtmanppSVVKLALESICLLLGENATDWKSIRAVIMR 3329
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL-----------AEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3330 EnfinsivsnfgtenitddVREKMkskylsnpdynfEKVNRAsmacgpmvkwAIAQIEYADMLKRVEPLREELRSLEEQA 3409
Cdd:COG1196 391 A------------------LRAAA------------ELAAQL----------EELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 24658015 3410 DVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALL 3465
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2575-2714 |
1.17e-04 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 44.98 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2575 PLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCEYRKTPNGVVLSPVQIGKwlVLFCDEINLP 2654
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAAREGE--IAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24658015 2655 DMDsygtqrVISFLRQLVEHKGFYRASD--QAWVSLERIQFVGACNPPtDPGRKPLSHRFLR 2714
Cdd:pfam07728 79 NPD------VLNSLLSLLDERRLLLPDGgeLVKAAPDGFRLIATMNPL-DRGLNELSPALRS 133
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3169-3283 |
1.69e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3169 VKLYNEKRSDLEEQQlhlnvglNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIR 3248
Cdd:COG3883 135 LEELKADKAELEAKK-------AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
90 100 110
....*....|....*....|....*....|....*
gi 24658015 3249 LADQTVKIEEKRKYVMADLAQVEPAVIDAQAAVKS 3283
Cdd:COG3883 208 AEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3172-3469 |
2.60e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3172 YNEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKslavKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLAD 3251
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEE----EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3252 QTVKIEEKRKYVMADLAQVEPAVIDAQAAVKSIRKQQLVEVRTMANppsvvklaLESICLLLGENATDWKSIRAVIMRE- 3330
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE--------LESRLEELEEQLETLRSKVAQLELQi 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3331 NFINSIVSNFGTE-NITDDVREKMKSkylSNPDYNFEKVNrasmacgpmvkwaiAQIEYADMlkRVEPLREELRSLEEQA 3409
Cdd:TIGR02168 396 ASLNNEIERLEARlERLEDRRERLQQ---EIEELLKKLEE--------------AELKELQA--ELEELEEELEELQEEL 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3410 DVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALLKSLN 3469
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3173-3428 |
4.80e-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: 46.60 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3173 NEKRSDLEEQQLHLNVGLNKIAETVEQVEEmqkslavKKQELQAKNEAANAKlKQMFQDQQEAEKKKIQS-----QEIQI 3247
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLEK-------EIQELQEQRIDLKEQ-IKSIEKEIENLNGKKEEleeelEELEA 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3248 RLAD---QTVKIEEKRKYVMADLAQVEPAVIDAQAAVKSIRKQQlvevrtmanppSVVKLALESiclLLGENATdwksir 3324
Cdd:TIGR02169 876 ALRDlesRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL-----------SELKAKLEA---LEEELSE------ 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3325 avimRENFINSIVSNFGTENITDDVREKMkskylsnpdynfEKVNRASMACGPMVKWAIAqiEYADMLKRVEPLREELRS 3404
Cdd:TIGR02169 936 ----IEDPKGEDEEIPEEELSLEDVQAEL------------QRVEEEIRALEPVNMLAIQ--EYEEVLKRLDELKEKRAK 997
|
250 260
....*....|....*....|....
gi 24658015 3405 LEEQadvnlasAKETKDLVEQLER 3428
Cdd:TIGR02169 998 LEEE-------RKAILERIEEYEK 1014
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3159-3498 |
5.34e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3159 RHYLDFIHHFVKLYN--EKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAE 3236
Cdd:COG4717 115 REELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3237 K---KKIQSQEIQIRLADQTVK-IEEKRKYVMADLAQVEPAVIDAQAavksirKQQLVEVRTMANPPSVVkLALESICLL 3312
Cdd:COG4717 195 QdlaEELEELQQRLAELEEELEeAQEELEELEEELEQLENELEAAAL------EERLKEARLLLLIAAAL-LALLGLGGS 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3313 LGENATDWKSIRAVIM------------RENFINSIVSNFGTENITDDVREKMKSKYLS--------NPDYNFEKVNRAS 3372
Cdd:COG4717 268 LLSLILTIAGVLFLVLgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAalglppdlSPEELLELLDRIE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3373 MACGPMVKWAIAQIEYadmlkRVEPLREELRSLEEQADVN----LASAKETKDLVEQLERSIAAYKEEYAQLIS--QAQA 3446
Cdd:COG4717 348 ELQELLREAEELEEEL-----QLEELEQEIAALLAEAGVEdeeeLRAALEQAEEYQELKEELEELEEQLEELLGelEELL 422
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24658015 3447 IKTDLENVQAKVDRSIALLKSLNIERERWESTSETFKSQMSTIIGDVLLSAA 3498
Cdd:COG4717 423 EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEL 474
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3173-3474 |
7.36e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3173 NEKRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLADQ 3252
Cdd:COG4372 62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3253 TVKIEEKRKyvmaDLAQVEPAVIDAQAAVKSIRKQQLVEVRTMANpPSVVKLALESICLLLGENATDWKSIRAVIMRENF 3332
Cdd:COG4372 142 QSEIAEREE----ELKELEEQLESLQEELAALEQELQALSEAEAE-QALDELLKEANRNAEKEEELAEAEKLIESLPREL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3333 INSIVSNFGTENITDDVREKMKSKYLSNPDYNFEKVNRASMACGPMVKWAIAQIEYADMLKRVEPLREELRSLEEQADVN 3412
Cdd:COG4372 217 AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELK 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24658015 3413 LASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALLKSLNIERER 3474
Cdd:COG4372 297 LLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1894-2006 |
7.53e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 1894 FGPAGTGKTESVKALGNQLGR---FVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSACSQQ---IQTI 1967
Cdd:smart00382 8 VGPPGSGKTTLARALARELGPpggGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDvliLDEI 87
|
90 100 110
....*....|....*....|....*....|....*....
gi 24658015 1968 QEALKYEMDSNKESITVELVGKQVRVSPDMAIFITMNPG 2006
Cdd:smart00382 88 TSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDE 126
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
3174-3282 |
9.11e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.25 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3174 EKRSDLEEQQLH--LNVGLNKIAETveqveemQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQsQEIQIRLAD 3251
Cdd:COG2268 218 QANREAEEAELEqeREIETARIAEA-------EAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQ-RQLEIAERE 289
|
90 100 110
....*....|....*....|....*....|....
gi 24658015 3252 QTVKIEEKRKYV---MADLAQVEPAVIDAQAAVK 3282
Cdd:COG2268 290 REIELQEKEAEReeaELEADVRKPAEAEKQAAEA 323
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3169-3490 |
1.30e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3169 VKLYNEKRSDLEEQQLHLNvglnkiaetvEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIR 3248
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELK----------KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3249 LADQTVKIEEKRKYV------MADLAQVEPAVIDAQaaVKSIRKQQLVEVRTMANPPSvvklalesiclllgenatdwKS 3322
Cdd:TIGR04523 276 LEQNNKKIKELEKQLnqlkseISDLNNQKEQDWNKE--LKSELKNQEKKLEEIQNQIS--------------------QN 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3323 IRAVIMRENFINSI---VSNFGTEN--ITDDVREKM---------KSKYL----------SNPDYNFEKVNRASMACGPM 3378
Cdd:TIGR04523 334 NKIISQLNEQISQLkkeLTNSESENseKQRELEEKQneieklkkeNQSYKqeiknlesqiNDLESKIQNQEKLNQQKDEQ 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3379 VKwaIAQIEYADMLKRVEPLRE-------ELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYaqlisqaQAIKTDL 3451
Cdd:TIGR04523 414 IK--KLQQEKELLEKEIERLKEtiiknnsEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI-------NKIKQNL 484
|
330 340 350
....*....|....*....|....*....|....*....
gi 24658015 3452 ENVQAKVDRSIALLKSLNIERERWESTSETFKSQMSTII 3490
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK 523
|
|
| Muted |
pfam14942 |
Organelle biogenesis, Muted-like protein; The protein is a coiled-coil protein and belongs to ... |
3165-3261 |
2.36e-03 |
|
Organelle biogenesis, Muted-like protein; The protein is a coiled-coil protein and belongs to a family found in eukaryotes. It undergoes alternative splicing forming two isoforms. The larger isoform is 187 amino acids long in protein sequence length and 21 kDa in mass. The smaller isoform is 110 amino acids long in protein sequence length and 12 kDa in mass. This protein associates with other proteins in order to form biogenesis of lysosome-related organelles complex-1 BLOC1 complex. BLOC-1 is required for the normal biogenesis of specialized organelles of the endosomal-lysosomal system.
Pssm-ID: 464390 [Multi-domain] Cd Length: 146 Bit Score: 41.49 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3165 IHHFVKLYNEKRSDLEEQQLHlNVgLNKIAETVEQV-EEMQKSLAVKKQELQAKNEAANAKLKQMFQdqqeaekkkiQSQ 3243
Cdd:pfam14942 22 IKYFLKEFEEKRGDREVRRLE-NI-TEMINETNENIlPKCKQSMEDNLSELLSKLDAALNMCERLLQ----------REL 89
|
90
....*....|....*...
gi 24658015 3244 EIQIRLADQTVKIEEKRK 3261
Cdd:pfam14942 90 EEEQRKNDRLQENEEQRK 107
|
|
| RND_1 |
NF037998 |
protein translocase SecDF, variant type; Members of this family are identified by TCDB as ... |
3175-3369 |
2.40e-03 |
|
protein translocase SecDF, variant type; Members of this family are identified by TCDB as belonging to 2.A.6.4.4, a variant 12-TM type SecDF, as found in Spiroplasma, Mesoplasma, and Acholeplasma.
Pssm-ID: 468306 Cd Length: 1237 Bit Score: 44.38 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3175 KRSDLEEQQLHLNVGLNKIAETVEQVEEMQKSlavKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTV 3254
Cdd:NF037998 642 KEKLSSKLLLKIKKINDKIDLLKKKEENKEAK---KNAKLIEKVKAKIKKLEQKITKLKLNKKKSNKIIKIRWKKKDWIF 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3255 KIEEKRKYVMADLAQVEPAVIDaqaavKSIRKQQLVEVRTMANPPSVVKLALESICLLLG--------------ENATDW 3320
Cdd:NF037998 719 FLKDNTDVILAIESEIEIQVIE-----KIKVKRNENNIFNITKIIIIIGLILSIIGGIVGftfgpnydstfgkgTTYTVY 793
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24658015 3321 KSIRAVIMRENFINSIVSNFGTENITDDVrEKMKSKYLSNPDYNFEKVN 3369
Cdd:NF037998 794 GDNLEELSNNNFVVTDIIDFGSKDKANEI-QELKDKIINEVSDPQAESS 841
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3190-3288 |
3.07e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3190 LNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMFQDQQEAEKKKIQSQEIQIRLADQTVKIEEKRKYVMADLAQ 3269
Cdd:COG3883 135 LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
90
....*....|....*....
gi 24658015 3270 VEPAVIDAQAAVKSIRKQQ 3288
Cdd:COG3883 215 AAAAAAAAAAAAAAAAAAA 233
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
3168-3481 |
3.51e-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: 43.41 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3168 FVKLYNEKRSDLEEQQLHLNVGLNKIAETVEQVEEM-QKSLAVKKQELQAKNEAANAKLKQMFQDQQE-AEKKK------ 3239
Cdd:COG5185 230 NIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLrLEKLGENAESSKRLNENANNLIKQFENTKEKiAEYTKsidikk 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3240 -IQSQEIQIRLADQTVKIEEKRKYVMADL----AQVEPAVIDAQAAVKSIRKQqlvevrtmanppsVVKLALESICLLLG 3314
Cdd:COG5185 310 aTESLEEQLAAAEAEQELEESKRETETGIqnltAEIEQGQESLTENLEAIKEE-------------IENIVGEVELSKSS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3315 ENATDWKSIRAVImRENFINsIVSNfgTENITDDVREKMkSKYLSNPDYNFEKVNRasmacgpmvkwAIAQI--EYADML 3392
Cdd:COG5185 377 EELDSFKDTIEST-KESLDE-IPQN--QRGYAQEILATL-EDTLKAADRQIEELQR-----------QIEQAtsSNEEVS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3393 KRVEPLREEL--RSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALLKSLNI 3470
Cdd:COG5185 441 KLLNELISELnkVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLD 520
|
330
....*....|.
gi 24658015 3471 ERERWESTSET 3481
Cdd:COG5185 521 QVAESLKDFMR 531
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3172-3287 |
3.58e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3172 YNEKRSDLEEQQlhlnvglNKIAETVEQVEEMQKSLAVKKQELQAKNEAANAKLKQMfqDQQEAEKKKIQSQEIQI--RL 3249
Cdd:PRK12704 77 LRERRNELQKLE-------KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQEL--EKKEEELEELIEEQLQEleRI 147
|
90 100 110
....*....|....*....|....*....|....*...
gi 24658015 3250 ADQTVkiEEKRKYVMADLaqVEPAVIDAQAAVKSIRKQ 3287
Cdd:PRK12704 148 SGLTA--EEAKEILLEKV--EEEARHEAAVLIKEIEEE 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2914-3076 |
4.13e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2914 PQGHLLLIGVSGAGKTTLSRFVAWMNGLSIFQIKVHNkytsedfDEDLRCVLRrsgckdEKIAFILDESNVLDSGFLERM 2993
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------GEDILEEVL------DQLLLIIVGGKKASGSGELRL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 2994 NTL--LANGEVPG-LFEgDEYTTLMTqckegaQREGLMLDSSDELYKWFTQQVMRNLHVVFTMNPSTDglKDRAATSPAL 3070
Cdd:smart00382 68 RLAlaLARKLKPDvLIL-DEITSLLD------AEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKD--LGPALLRRRF 138
|
....*.
gi 24658015 3071 FNRCVL 3076
Cdd:smart00382 139 DRRIVL 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3384-3485 |
4.94e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3384 AQIEYADMLKRVEPLREELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIA 3463
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
90 100
....*....|....*....|..
gi 24658015 3464 LLKSLNIERERWESTSETFKSQ 3485
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEE 387
|
|
| ZapB |
COG3074 |
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ... |
3191-3258 |
6.26e-03 |
|
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 38.41 E-value: 6.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24658015 3191 NKIAETVEQVEEMQ---KSLAVKKQELQAKNEAANAKLKQMfqdQQEAEKKKIQSQEIQIRLADQTVKIEE 3258
Cdd:COG3074 11 AKVQQAVDTIELLQmevEELKEKNEELEQENEELQSENEEL---QSENEQLKTENAEWQERIRSLLGKIDE 78
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
3174-3503 |
6.90e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.33 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3174 EKRSDLEEQQLHLNVGLNKIAETVEQ-VEEMQKSLAVKKQELQAKNEAA--------NAKLKQMFQDQQEAEK------- 3237
Cdd:COG3064 59 EAKAEAEQRAAELAAEAAKKLAEAEKaAAEAEKKAAAEKAKAAKEAEAAaaaekaaaAAEKEKAEEAKRKAEEeakrkae 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3238 -KKIQSQEIQIRLADQTVKIEEKRKYVMADLAQVEPAVIDAQAAVKSIRKQQLVEVRTMANPPSVVKLALESICLLLGEN 3316
Cdd:COG3064 139 eERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3317 ATDWKSIRAVIMRENFINSIVSNFGTENITDDVREKMKSKYLSNPDYNFEKVNRASMACGPMVKWAIAQIEYADMLKRVE 3396
Cdd:COG3064 219 LAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3397 PLREELRSLEEQADVNLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDRSIALLKSLNIERERWE 3476
Cdd:COG3064 299 DSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLG 378
|
330 340
....*....|....*....|....*..
gi 24658015 3477 STSETFKSQMSTIIGDVLLSAAFIAYG 3503
Cdd:COG3064 379 KLADVEEAAGAGILAAAGGGGLLGLRL 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3382-3481 |
8.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3382 AIAQI-EYADMLKRVEPLREELRSLEEQadvnLASAKETKDLVEQLERSIAAYKEEYAQLISQAQAIKTDLENVQAKVDR 3460
Cdd:COG4913 649 ALQRLaEYSWDEIDVASAEREIAELEAE----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
90 100
....*....|....*....|.
gi 24658015 3461 SIALLKSLNIERERWESTSET 3481
Cdd:COG4913 725 AEEELDELQDRLEAAEDLARL 745
|
|
| PulE |
COG2804 |
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell ... |
2573-2602 |
8.50e-03 |
|
Type II secretory pathway ATPase GspE/PulE or T4P pilus assembly pathway ATPase PilB [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442055 [Multi-domain] Cd Length: 561 Bit Score: 42.10 E-value: 8.50e-03
10 20 30
....*....|....*....|....*....|...
gi 24658015 2573 HKP--LVL-CGPPGSGKTMTLFSALRALPDMEV 2602
Cdd:COG2804 310 RRPhgIILvTGPTGSGKTTTLYAALNELNTPER 342
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3141-3238 |
9.80e-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: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658015 3141 QANARLAKRGGRTMAV-TPRHYLDFIHHFVKLyNEKRSDLEEQQLHLNVGL----NKIAETVEQVEEMQKSLAVKKQELQ 3215
Cdd:COG1579 70 EVEARIKKYEEQLGNVrNNKEYEALQKEIESL-KRRISDLEDEILELMERIeeleEELAELEAELAELEAELEEKKAELD 148
|
90 100
....*....|....*....|...
gi 24658015 3216 AKNEAANAKLKQMFQDQQEAEKK 3238
Cdd:COG1579 149 EELAELEAELEELEAEREELAAK 171
|
|
| |
