|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1051-4342 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 1235.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1051 LTYSDLLTKIPDDslTNAYEVIEAKVTQVKGYVDIWLQYQSLWDLESQYIFNFLGDDLAKWQQLLLEIKKARTTFDNSET 1130
Cdd:COG5245 145 LLSHELELIFRSG--EQWVGCMRKLYESVCSERDGFYEEKSFWSRFHMEMCHIREFCRSKAFRFACDVLRKSGKYVTVAT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1131 EQSF-GPVVIDYEQVQSKVNAKYDSWQREVLNRFgSMLGTSMKEFHGAVSKARydlelhsvdGNSTGEAVTFITFVQD-- 1207
Cdd:COG5245 223 LDSLlSSSKYSELGRRLHFYANMDFSGIYFPKSF-SEFKDSVISATQAVSRDI---------GRQSRMARRLILVQMDsl 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1208 --LKRKVAKWENDVELFRQGQKTLERQRYQFPSDWLYCDQIDGEWSAFNEILSRKNNaIQDQIAGLQmkivtedKLVEQK 1285
Cdd:COG5245 293 arLIVDRICEYVSIEWLGCCEELLTCSMESMSSLVNSFDGEESEAMSLESSLFYEFR-GGEHLAGFY-------SAFGDI 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1286 ISEILLDWEKNK-----PVQGNIKPDIATNTLNIFEGRVTRVKEEFDMVCRAKEALDLDLSMDDRLEPVLEELRDLKSVW 1360
Cdd:COG5245 365 KRILLFTWSFKKlgtllPSLPGYSSGGMDYGEEYRSLLWELGSEVGDPDSGPVRKWMRKDLFDAKVRSGVSFGKQEEFVS 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1361 SSLAKIWQSIFEIKDTLWATVvprkirtqldtlMNSTKDMPNRMRQYAAFEYVQ--ESLRLYVKVNPL------LTDLKS 1432
Cdd:COG5245 445 DIFNITFERIHGMDPTTLEDD------------EEDTPALAILLGQEEAGRFVKlcKIMRMFSFFNSLemfsrrTLANRM 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1433 EALRerHWRQLFKAlrveGRWTLSEmtvgniwDLDLRRNESLV-RDIIVVAQGEMALEEFLKqvretWTNYVLELVNYQN 1511
Cdd:COG5245 513 AIVK--YLSSVVRT----GPLFLQR-------DFFGRMSELLMaRDMFMEVDGVLRLFFGGE-----WSGIVQLSGIRRA 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1512 KCRLIRGWDDLFAK-CSENLNFLSAMKLSPYykvFEEEAAGWEE--KLNRIHVLFdvwidvqrqWVYLEGIFTGSHDIKH 1588
Cdd:COG5245 575 KRCVERQIDDEIREwCSSVLSDDFLEERAVR---VERGADGARRlrASSGSPVLR---------RLDEYLMMMSLEDLMP 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1589 LLPVETSRFQNINSEFLTVMKKVYKSPFVLDVLNIANIQkSLERLADLLGKIQKALGEYLERERSSFPRFyfVGDEDLLE 1668
Cdd:COG5245 643 LIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILEDVGD-DLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMD 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1669 IIGNSKDVVRIQKHFKKMFAGINSIILNDDVTTvlGMSSKEDENVMFKTPVSIKDNPRINDWLTlveKEMRMSLAQILaE 1748
Cdd:COG5245 720 RVRELENRVYSYRFFVKKIAKEEMKTVFSSRIQ--KKEPFSLDSEAYVGFFRLYEKSIVIRGIN---RSMGRVLSQYL-E 793
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1749 SVQEmnvfyLAETLDPAAFLSwidKVPDQLVVLTSQItWTSTVERALVTMADSGNPSNEQPIQQALDYvlralnvLADTV 1828
Cdd:COG5245 794 SVQE-----ALEIEDGSFFVS---RHRVRDGGLEKGR-GCDAWENCFDPPLSEYFRILEKIFPSEEGY-------FFDEV 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1829 LqdlapiqrKKCEHLITDLVHQRDVIRALIRTKVSSPKDFSWLSQMRFYfnashEDPLQCLTITMANASFLYGYEYFGVT 1908
Cdd:COG5245 858 L--------KRLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-----QGLYKRFIKVRSSYRSAEMFAKNTIP 924
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1909 ERLVQTPLTDRCYLTLTQALESRLggSPFgpAGTGKTESVKALGIQLGRFVlvfccdENFDFQAmgRIFIGLSQVGAWGc 1988
Cdd:COG5245 925 FFVFEHSMDTSQHQKLFEAVCDEV--CRF--VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG- 991
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1989 FDEFNRLEERILsAVSQQVQTIQLGLKEAKTNpnneIELVGKNVRVNTNTGIFITMNPgyagRSNLPDNLKKLFRSIAMT 2068
Cdd:COG5245 992 TEESALLDEISR-TILVDEYLNSDEFRMLEEL----NSAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSN 1062
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2069 KPDKELIAQvmlssqgfrtAESLASKVIPLFNLCNEKLSPQSHYDFglRALKSVLVSAGNMkrdrlqelrssnpenitae 2148
Cdd:COG5245 1063 IPFGAIKSR----------RESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRM------------------- 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2149 ferISESVPEQEILIQSIRETVVPKLVAEDISVLmgllkgvfpGVEYNPVSlqplRKAIKdICDKRRLVIGDLWMEKILQ 2228
Cdd:COG5245 1112 ---LEEKTEYLNKILSITGLPLISDTLRERIDTL---------DAEWDSFC----RISES-LKKYESQQVSGLDVAQFVS 1174
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2229 LYQIQRIHHGLMMVGPSGSGKSNAWQVLLAAMEVVENVesqsYVIDPkamskealygVLDPTTrEWTdGLFTNILRkivD 2308
Cdd:COG5245 1175 FLRSVDTGAFHAEYFRVFLCKIKHYTDACDYLWHVKSP----YVKKK----------YFDADM-ELR-QFFLMFNR---E 1235
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2309 NVRGESA-KRHWIIFDgdvdpEWVENLNSVLDDNKLLTLPNGERlslppnvRIVFEveTLKyATLATVSRCGMVWYSSDV 2387
Cdd:COG5245 1236 DMEARLAdSKMEYEVE-----RYVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISR 1300
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2388 IDNKMVFANYFATlRNVPLDEVDEEVTV---RRVETEEnraaspilLTQQACANILEphfaedglvskaleYASTLDHIM 2464
Cdd:COG5245 1301 LSTKGVFLDELGD-TKRYLDECLDFFSCfeeVQKEIDE--------LSMVFCADALR--------------FSADLYHIV 1357
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2465 DftpMRVLGTLFSLINKSVRNVIQYNN--QHSDFpmgaEQLDSYISKRLVSSTIWSFSGDAKLELRARLGDFVRGVTTID 2542
Cdd:COG5245 1358 K---ERRFSGVLAGSDASESLGGKSIElaAILEH----KDLIVEMKRGINDVLKLRIFGDKCRESTPRFYLISDGDLIKD 1430
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2543 LPQMANSS---IIDFDVNINSGEWIPwqskVPVVEIETHTVAEA-DVVIPTVDTVRHEEVLYSWLSEHKPLILCGPPGSG 2618
Cdd:COG5245 1431 LNERSDYEemlIMMFNISAVITNNGS----IAGFELRGERVMLRkEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSG 1506
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2619 KTMTLFSALRKLPEMEVVGLNFSSATTPELILKTLEQHCEYRKTPNGVLLSPVLLGRWLVVFCDEINLPSMDKYGTQRVI 2698
Cdd:COG5245 1507 KEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVI 1586
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2699 SFMRQLVECGGFWRTTDKSWVKLERIQFVGACNPPTDPGRIPLTHRFLRHVPLVMVDYPGEISLKQIYSTFCRAMLKVVP 2778
Cdd:COG5245 1587 VFLRPLVERQGFWSSIAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFD 1666
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2779 SLRAYSEPLTAAMVELYLCSQSHFVPEMQAHYIYSPRELTRWMRGIFEAIKPMETLSVEGLVRIWAHEALRLFQDRLVTE 2858
Cdd:COG5245 1667 EFNRLSEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQ 1746
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2859 EERKWTDDEIDRIALKHFPGLDREQALARPILYSNWLSKNYVPVDREELREYAKARLKVFYEEELDVPLALFNDVLDHVL 2938
Cdd:COG5245 1747 KESSTSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFGMACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHIL 1826
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2939 RIDRVFRQMQGHMLLIGVSGSGKTTLSRFVAWMNGLSVFQIKVHNKYSAADFDEDLRTVLRRAGCKGEKVCFILDESNVL 3018
Cdd:COG5245 1827 RSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPV 1906
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3019 DSGFLERMNTLLANAEVPGLFEGDEYSSLMTQCKEGAQRDGLMLDSSEELYKWFTQQVMKNLHVVFTMNPPEGGLASRAA 3098
Cdd:COG5245 1907 ESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEKDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGI 1986
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3099 TSPALFNRCVLDWFGDWSDQAFFQVGQEF-TTSLDLDR-PNYSPPLKFpvvyrnLPETPTHRHAIINAFVYVHQSLYEvn 3176
Cdd:COG5245 1987 RSPALKNRCFIDFKKLWDTEEMSQYANSVeTLSRDGGRvFFINGELGV------GKGALISEVFGDDAVVIEGRGFEI-- 2058
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3177 aklSKRNGKRGYvTPRHYLDFIRHYVRLYNEKREDLEEQQRHLNVGLDKLKDTVVKVEELRKSLAVKKNELEIKNKQAND 3256
Cdd:COG5245 2059 ---SMIEGSLGE-SKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADD 2134
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3257 KLQKMVADQQEAEKKKATSIEIQAALEAQNKEISRRTAAVMADLANAEPAVLEAQKAVTDIKKAQLTEVRSMGNPPEMVK 3336
Cdd:COG5245 2135 ALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLC 2214
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3337 MAMESVCTLLGNKLESWKTVQGIIRREDFISSIVNFDTDRQMTPAMRQKMKAEYLSNPSYNFETVNHASKACGPLVKWVI 3416
Cdd:COG5245 2215 IEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPDEIEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLV 2294
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3417 AQVNYSQILDKIGPLRQEVQELESSAQMTEIKASSIEKMIEELENSIATYKEEYAVLISEVGSIKSEMERVKSKVERSVT 3496
Cdd:COG5245 2295 RECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIF 2374
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3497 LLESLSSERVRWEAGSHSFDTQMATTVGDVLLSSAFLAYGGYFDQQYRELLFHKWADHLTKA-GIQFKADISLAEYLSTA 3575
Cdd:COG5245 2375 VSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGMSFIRISKEfRDKEIRRRQFITEGVQK 2454
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3576 DDRLSWTEHalpADDLCVENAIILQRF-NRYPLIIDPSGQATTFLMNEYKNRKITVTSFLDDSFLKNLESALRFGNPLLI 3654
Cdd:COG5245 2455 IEDFKEEAC---STDYGLENSRIRKDLqDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKII 2531
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3655 KDVEHLDPIMNPVLNKELRRTGGRVLIRLGNQDIDFSPAFTLFLSTRDPSVSFPPDVCSRVSFVNFTVTRGSLQSQCLSK 3734
Cdd:COG5245 2532 GDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDA 2611
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3735 VLKAERPDVDRRRADLIKLQGEFKVKLRHLEKSLLQALNESKGNILDDDKVIATLETLKLEAADVTRKVEETEGVMQEVE 3814
Cdd:COG5245 2612 LEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRID 2691
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3815 QTTAIYSPLAHSCSSIFFVMEQLNRLNHFYQFSLDFFSDIFNFVLH-ENPELNGVKDygqrldiLTRDLFNVSYRRASLS 3893
Cdd:COG5245 2692 ALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWRRmKSKYLCAIRY-------MLMSSEWILDHEDRSG 2764
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3894 LLHDDHITFAM-----LLTQIKIRGTSSQADDAEYDF--LLSPDSNPSGKITAEFTEEQRAARTQEFAKLasfrdmpANI 3966
Cdd:COG5245 2765 FIHRLDVSFLLrtkrfVSTLLEDKNYRQVLSSCSLYGndVISHSCDRFDRDVYRALKHQMDNRTHSTILT-------SNS 2837
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3967 DSNADTwSKFWNDSKAEAhvpvfwepsqaeavndfkkllvikcfrpdrllaattkyiDQVFTPNfvnqAELDFAKLVREE 4046
Cdd:COG5245 2838 KTNPYK-EYTYNDSWAEA---------------------------------------FEVEDSG----DLYKFEEGLLEL 2873
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 4047 VKASTPIslcsIPGHDAAYRVDNLAQEQgvrlssvamGSQEGLTLADQAIASATKTGNWVLLKNVHLALTWLGQ-LDKRL 4125
Cdd:COG5245 2874 IVGHAPL----IYAHKKSLENERNVDRL---------GSKENEVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRyVEDVV 2940
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 4126 HSLKA----HPNFRLFLTMETNPKVPVNLLRLSRVLMFEPQPGIKANLQEsLRGIPSARLSKGPTERARLYFMVAWLHAV 4201
Cdd:COG5245 2941 YPIKAsrvcGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYAD-LVEIDRYPFDYTLVIACDDAFYLSWEHAA 3019
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 4202 VLERLRYVPLGWTKSYEFNDSDQDCALSTIDVWLdtvgqgrANVSPDRIPWDAIRTLLCQSVYGGRVDSEVDQQLLESFV 4281
Cdd:COG5245 3020 VASVISAGPKENNEEIYFGDKDFEFKTHLLKNIL-------FLNHLNARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYC 3092
|
3290 3300 3310 3320 3330 3340
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1940753919 4282 NSFFrpeCYDLSFKLVESGDGDDTGLT---APEGTKMSQFlEWIDELPAREPPTWLRLPATAER 4342
Cdd:COG5245 3093 RGYG---AHETSSQILASVPGGDPELVkfhMEEMCRSSAF-GVIGQLPDLALCAWLMGPCDSEY 3152
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1900-2250 |
4.86e-172 |
|
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: 532.83 E-value: 4.86e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1900 YGYEYFGVTERLVQTPLTDRCYLTLTQALESRLGGSPFGPAGTGKTESVKALGIQLGRFVLVFCCDENFDFQAMGRIFIG 1979
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1980 LSQVGAWGCFDEFNRLEERILSAVSQQVQTIQLGLKEAKTNpnneIELVGKNVRVNTNTGIFITMNPGYAGRSNLPDNLK 2059
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKT----FVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2060 KLFRSIAMTKPDKELIAQVMLSSQGFRTAESLASKVIPLFNLCNEKLSPQSHYDFGLRALKSVLVSAGNMKRdrlqelrs 2139
Cdd:pfam12774 157 ALFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKR-------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2140 SNPEnitaeferisesVPEQEILIQSIRETVVPKLVAEDISVLMGLLKGVFPGVEYNPVSLQPLRKAIKDICDKRRLVIG 2219
Cdd:pfam12774 229 SNPN------------LNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPH 296
|
330 340 350
....*....|....*....|....*....|.
gi 1940753919 2220 DLWMEKILQLYQIQRIHHGLMMVGPSGSGKS 2250
Cdd:pfam12774 297 DAFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
249-822 |
2.21e-130 |
|
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: 423.14 E-value: 2.21e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 249 LNKLQGDVNGWIKEIQKVTKLSRDPASGTAIQEINFWLSMERALEKIDEQLKSDQIVLTLDILKHAKRYHATVSFIADTG 328
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKALDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 329 LKEGTEKVHKYNQLMKDF--PLNELLSATDAIKIRDSLQQIFGHINKKLKLSPY--PIRRALPLVEAISRDLNDQLLRVL 404
Cdd:pfam08385 81 LTDALNEAKDNVKYLKTLerPFEDLEELTDPPEIIEAIPPLMNTIRLIWSISRYynTSERMTVLLEKISNQLIEQCKKYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 405 GSRRLMYMDYDDFEKATAGAVEVFETWDDVIKEFTHVAREVTRRR----SEKFLPIKINpahaKLQERILFVRNFRKQHE 480
Cdd:pfam08385 161 SPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERpwdfSERYIFGRFD----AFLERLEKILELFETIE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 481 QlhqtiLKVMTKPSGFITKA-SLEIEEVEsvslgdvdavEEVRLAYESVKNV--DVLDVSVEGtdmWVTAEVSYSERVSR 557
Cdd:pfam08385 237 Q-----FSKLEKIGGTKGPElEGVIEEIL----------EEFQEAYKVFKSKtyDILDVSNEG---FDDDYEEFKERIKD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 558 VENQIIAQLRDRLGIAKNANEMFRVFSKFNALFVRPKIRGAIQEYQTQLIEKVKDDIKKLHDKFKMQYrhsDAYHMSQlR 637
Cdd:pfam08385 299 LERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQK---YNPSPIA-K 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 638 DLPPISGHIIWARQIERQLSAYMKRVEDVLGKGweLYAEGQKLQSESSSFRKKLD--TKPIYDQWFSEITRRELAVSG-P 714
Cdd:pfam08385 375 NMPPVAGAIIWARQLFRRIQEPMKRFKEELGLL--KHAEGKKVIKKYNELAKKLDeyERLIYEAWLKEVEEASEGNLKrP 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 715 LFeiTRNRAQGNvlQLGVNFDSQIITLFKEVRNLLWLKYQVPHNVSIIAKDAKRVYPIAVSLMETIRTYSQMVNKVqrHG 794
Cdd:pfam08385 453 LL--VRHPETGK--LLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTL--LP 526
|
570 580
....*....|....*....|....*....
gi 1940753919 795 EIATLVAGYRNDAQKMVSRGVN-LRWEHF 822
Cdd:pfam08385 527 VERPLLAPHLKDIDEKLEPGLTtLTWNSL 555
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2588-2751 |
2.84e-10 |
|
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: 61.78 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2588 PTVDTVRHEEVLYSWLSEHKPLILCGPPGSGKTMTLFSALRKLPEMevvGLNFSSATTPELILKTLEQHCEyRKTPNGVL 2667
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRP---GAPFLYLNASDLLEGLVVAELF-GHFLVRLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2668 LSPVLLGRWLVVFCDEINLPSMDKygTQRVISFMRQLVEcggfwrttdkSWVKLERIQFVGACNPPTDPG-RIPLTHRFL 2746
Cdd:cd00009 77 FELAEKAKPGVLFIDEIDSLSRGA--QNALLRVLETLND----------LRIDRENVRVIGATNRPLLGDlDRALYDRLD 144
|
....*
gi 1940753919 2747 RHVPL 2751
Cdd:cd00009 145 IRIVI 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2606-2751 |
3.22e-07 |
|
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: 52.76 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2606 HKPLILCGPPGSGKTMTLFSALRKLPEMEVVGLNFSSATTPELILKTLEQHCEYRKTPNG-------VLLSPVLLGRWLV 2678
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGsgelrlrLALALARKLKPDV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1940753919 2679 VFCDEINlpSMDKYGTQRVISFMRQLvecggfwrTTDKSWVKLERIQFVGACNPPTDPGRIPLTHRFLRHVPL 2751
Cdd:smart00382 82 LILDEIT--SLLDAEQEALLLLLEEL--------RLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVL 144
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3205-3502 |
1.42e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3205 YNEKREDLEEQQRHLNV--------GLDKLKDTVVKVEELRKSLAVKKNELEIKNKQANDKLQKMVADQQEAEKK-KATS 3275
Cdd:TIGR02168 215 YKELKAELRELELALLVlrleelreELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3276 IEIqAALEAQNKEISRR-------TAAVMADLANAEPAVLEAQKAVTDIK------KAQLTEVRSMGNPPEMVKMAMESV 3342
Cdd:TIGR02168 295 NEI-SRLEQQKQILRERlanlerqLEELEAQLEELESKLDELAEELAELEekleelKEELESLEAELEELEAELEELESR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3343 CTLLGNKLESWKT-VQGIIRREDFISS-IVNFDTDRQMTPAMRQKMKAEylsNPSYNFETVNHASKACGplvkwviaqvn 3420
Cdd:TIGR02168 374 LEELEEQLETLRSkVAQLELQIASLNNeIERLEARLERLEDRRERLQQE---IEELLKKLEEAELKELQ----------- 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3421 ysqilDKIGPLRQEVQELESSAQMTEIKASSIEKMIEELENSIATYKEEYAVLISEVGSIKSEMERVKSKVERSVTLLES 3500
Cdd:TIGR02168 440 -----AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
..
gi 1940753919 3501 LS 3502
Cdd:TIGR02168 515 QS 516
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
3201-3495 |
1.45e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3201 YVRLYNEKREDLEEQQRHLNVGLDKLKDTVvkveelrkslavkkNELEIKNKQANDKLQKMVADQ-QEAEKKKATSIEIQ 3279
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNI--------------EEQRKKNGENIARKQNKYDELvEEAKTIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3280 AALEAQNKEISRRTAAvMADLANAepavleaqKAVTDIKKAQLTEVRSM----GNPPemvkmamesVCTllgnkleswkt 3355
Cdd:PHA02562 241 DELLNLVMDIEDPSAA-LNKLNTA--------AAKIKSKIEQFQKVIKMyekgGVCP---------TCT----------- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3356 vQGIIRREDFISSIvnfdtdrqmtpamRQKMKAeylsnpsynfetvnhaskACGPLVKWVIAQVNYSQILDKIGPLRQEV 3435
Cdd:PHA02562 292 -QQISEGPDRITKI-------------KDKLKE------------------LQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940753919 3436 QELES-------SAQMTEIKASSIEKMIEELENSIATYKEEYAVLISEVGSIKSEM-ERVKSKVERSV 3495
Cdd:PHA02562 340 LELKNkistnkqSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKsELVKEKYHRGI 407
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1051-4342 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 1235.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1051 LTYSDLLTKIPDDslTNAYEVIEAKVTQVKGYVDIWLQYQSLWDLESQYIFNFLGDDLAKWQQLLLEIKKARTTFDNSET 1130
Cdd:COG5245 145 LLSHELELIFRSG--EQWVGCMRKLYESVCSERDGFYEEKSFWSRFHMEMCHIREFCRSKAFRFACDVLRKSGKYVTVAT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1131 EQSF-GPVVIDYEQVQSKVNAKYDSWQREVLNRFgSMLGTSMKEFHGAVSKARydlelhsvdGNSTGEAVTFITFVQD-- 1207
Cdd:COG5245 223 LDSLlSSSKYSELGRRLHFYANMDFSGIYFPKSF-SEFKDSVISATQAVSRDI---------GRQSRMARRLILVQMDsl 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1208 --LKRKVAKWENDVELFRQGQKTLERQRYQFPSDWLYCDQIDGEWSAFNEILSRKNNaIQDQIAGLQmkivtedKLVEQK 1285
Cdd:COG5245 293 arLIVDRICEYVSIEWLGCCEELLTCSMESMSSLVNSFDGEESEAMSLESSLFYEFR-GGEHLAGFY-------SAFGDI 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1286 ISEILLDWEKNK-----PVQGNIKPDIATNTLNIFEGRVTRVKEEFDMVCRAKEALDLDLSMDDRLEPVLEELRDLKSVW 1360
Cdd:COG5245 365 KRILLFTWSFKKlgtllPSLPGYSSGGMDYGEEYRSLLWELGSEVGDPDSGPVRKWMRKDLFDAKVRSGVSFGKQEEFVS 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1361 SSLAKIWQSIFEIKDTLWATVvprkirtqldtlMNSTKDMPNRMRQYAAFEYVQ--ESLRLYVKVNPL------LTDLKS 1432
Cdd:COG5245 445 DIFNITFERIHGMDPTTLEDD------------EEDTPALAILLGQEEAGRFVKlcKIMRMFSFFNSLemfsrrTLANRM 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1433 EALRerHWRQLFKAlrveGRWTLSEmtvgniwDLDLRRNESLV-RDIIVVAQGEMALEEFLKqvretWTNYVLELVNYQN 1511
Cdd:COG5245 513 AIVK--YLSSVVRT----GPLFLQR-------DFFGRMSELLMaRDMFMEVDGVLRLFFGGE-----WSGIVQLSGIRRA 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1512 KCRLIRGWDDLFAK-CSENLNFLSAMKLSPYykvFEEEAAGWEE--KLNRIHVLFdvwidvqrqWVYLEGIFTGSHDIKH 1588
Cdd:COG5245 575 KRCVERQIDDEIREwCSSVLSDDFLEERAVR---VERGADGARRlrASSGSPVLR---------RLDEYLMMMSLEDLMP 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1589 LLPVETSRFQNINSEFLTVMKKVYKSPFVLDVLNIANIQkSLERLADLLGKIQKALGEYLERERSSFPRFyfVGDEDLLE 1668
Cdd:COG5245 643 LIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILEDVGD-DLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMD 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1669 IIGNSKDVVRIQKHFKKMFAGINSIILNDDVTTvlGMSSKEDENVMFKTPVSIKDNPRINDWLTlveKEMRMSLAQILaE 1748
Cdd:COG5245 720 RVRELENRVYSYRFFVKKIAKEEMKTVFSSRIQ--KKEPFSLDSEAYVGFFRLYEKSIVIRGIN---RSMGRVLSQYL-E 793
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1749 SVQEmnvfyLAETLDPAAFLSwidKVPDQLVVLTSQItWTSTVERALVTMADSGNPSNEQPIQQALDYvlralnvLADTV 1828
Cdd:COG5245 794 SVQE-----ALEIEDGSFFVS---RHRVRDGGLEKGR-GCDAWENCFDPPLSEYFRILEKIFPSEEGY-------FFDEV 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1829 LqdlapiqrKKCEHLITDLVHQRDVIRALIRTKVSSPKDFSWLSQMRFYfnashEDPLQCLTITMANASFLYGYEYFGVT 1908
Cdd:COG5245 858 L--------KRLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-----QGLYKRFIKVRSSYRSAEMFAKNTIP 924
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1909 ERLVQTPLTDRCYLTLTQALESRLggSPFgpAGTGKTESVKALGIQLGRFVlvfccdENFDFQAmgRIFIGLSQVGAWGc 1988
Cdd:COG5245 925 FFVFEHSMDTSQHQKLFEAVCDEV--CRF--VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG- 991
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1989 FDEFNRLEERILsAVSQQVQTIQLGLKEAKTNpnneIELVGKNVRVNTNTGIFITMNPgyagRSNLPDNLKKLFRSIAMT 2068
Cdd:COG5245 992 TEESALLDEISR-TILVDEYLNSDEFRMLEEL----NSAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSN 1062
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2069 KPDKELIAQvmlssqgfrtAESLASKVIPLFNLCNEKLSPQSHYDFglRALKSVLVSAGNMkrdrlqelrssnpenitae 2148
Cdd:COG5245 1063 IPFGAIKSR----------RESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRM------------------- 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2149 ferISESVPEQEILIQSIRETVVPKLVAEDISVLmgllkgvfpGVEYNPVSlqplRKAIKdICDKRRLVIGDLWMEKILQ 2228
Cdd:COG5245 1112 ---LEEKTEYLNKILSITGLPLISDTLRERIDTL---------DAEWDSFC----RISES-LKKYESQQVSGLDVAQFVS 1174
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2229 LYQIQRIHHGLMMVGPSGSGKSNAWQVLLAAMEVVENVesqsYVIDPkamskealygVLDPTTrEWTdGLFTNILRkivD 2308
Cdd:COG5245 1175 FLRSVDTGAFHAEYFRVFLCKIKHYTDACDYLWHVKSP----YVKKK----------YFDADM-ELR-QFFLMFNR---E 1235
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2309 NVRGESA-KRHWIIFDgdvdpEWVENLNSVLDDNKLLTLPNGERlslppnvRIVFEveTLKyATLATVSRCGMVWYSSDV 2387
Cdd:COG5245 1236 DMEARLAdSKMEYEVE-----RYVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISR 1300
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2388 IDNKMVFANYFATlRNVPLDEVDEEVTV---RRVETEEnraaspilLTQQACANILEphfaedglvskaleYASTLDHIM 2464
Cdd:COG5245 1301 LSTKGVFLDELGD-TKRYLDECLDFFSCfeeVQKEIDE--------LSMVFCADALR--------------FSADLYHIV 1357
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2465 DftpMRVLGTLFSLINKSVRNVIQYNN--QHSDFpmgaEQLDSYISKRLVSSTIWSFSGDAKLELRARLGDFVRGVTTID 2542
Cdd:COG5245 1358 K---ERRFSGVLAGSDASESLGGKSIElaAILEH----KDLIVEMKRGINDVLKLRIFGDKCRESTPRFYLISDGDLIKD 1430
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2543 LPQMANSS---IIDFDVNINSGEWIPwqskVPVVEIETHTVAEA-DVVIPTVDTVRHEEVLYSWLSEHKPLILCGPPGSG 2618
Cdd:COG5245 1431 LNERSDYEemlIMMFNISAVITNNGS----IAGFELRGERVMLRkEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSG 1506
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2619 KTMTLFSALRKLPEMEVVGLNFSSATTPELILKTLEQHCEYRKTPNGVLLSPVLLGRWLVVFCDEINLPSMDKYGTQRVI 2698
Cdd:COG5245 1507 KEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVI 1586
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2699 SFMRQLVECGGFWRTTDKSWVKLERIQFVGACNPPTDPGRIPLTHRFLRHVPLVMVDYPGEISLKQIYSTFCRAMLKVVP 2778
Cdd:COG5245 1587 VFLRPLVERQGFWSSIAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFD 1666
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2779 SLRAYSEPLTAAMVELYLCSQSHFVPEMQAHYIYSPRELTRWMRGIFEAIKPMETLSVEGLVRIWAHEALRLFQDRLVTE 2858
Cdd:COG5245 1667 EFNRLSEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQ 1746
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2859 EERKWTDDEIDRIALKHFPGLDREQALARPILYSNWLSKNYVPVDREELREYAKARLKVFYEEELDVPLALFNDVLDHVL 2938
Cdd:COG5245 1747 KESSTSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFGMACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHIL 1826
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2939 RIDRVFRQMQGHMLLIGVSGSGKTTLSRFVAWMNGLSVFQIKVHNKYSAADFDEDLRTVLRRAGCKGEKVCFILDESNVL 3018
Cdd:COG5245 1827 RSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPV 1906
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3019 DSGFLERMNTLLANAEVPGLFEGDEYSSLMTQCKEGAQRDGLMLDSSEELYKWFTQQVMKNLHVVFTMNPPEGGLASRAA 3098
Cdd:COG5245 1907 ESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEKDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGI 1986
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3099 TSPALFNRCVLDWFGDWSDQAFFQVGQEF-TTSLDLDR-PNYSPPLKFpvvyrnLPETPTHRHAIINAFVYVHQSLYEvn 3176
Cdd:COG5245 1987 RSPALKNRCFIDFKKLWDTEEMSQYANSVeTLSRDGGRvFFINGELGV------GKGALISEVFGDDAVVIEGRGFEI-- 2058
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3177 aklSKRNGKRGYvTPRHYLDFIRHYVRLYNEKREDLEEQQRHLNVGLDKLKDTVVKVEELRKSLAVKKNELEIKNKQAND 3256
Cdd:COG5245 2059 ---SMIEGSLGE-SKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADD 2134
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3257 KLQKMVADQQEAEKKKATSIEIQAALEAQNKEISRRTAAVMADLANAEPAVLEAQKAVTDIKKAQLTEVRSMGNPPEMVK 3336
Cdd:COG5245 2135 ALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLC 2214
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3337 MAMESVCTLLGNKLESWKTVQGIIRREDFISSIVNFDTDRQMTPAMRQKMKAEYLSNPSYNFETVNHASKACGPLVKWVI 3416
Cdd:COG5245 2215 IEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPDEIEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLV 2294
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3417 AQVNYSQILDKIGPLRQEVQELESSAQMTEIKASSIEKMIEELENSIATYKEEYAVLISEVGSIKSEMERVKSKVERSVT 3496
Cdd:COG5245 2295 RECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIF 2374
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3497 LLESLSSERVRWEAGSHSFDTQMATTVGDVLLSSAFLAYGGYFDQQYRELLFHKWADHLTKA-GIQFKADISLAEYLSTA 3575
Cdd:COG5245 2375 VSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGMSFIRISKEfRDKEIRRRQFITEGVQK 2454
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3576 DDRLSWTEHalpADDLCVENAIILQRF-NRYPLIIDPSGQATTFLMNEYKNRKITVTSFLDDSFLKNLESALRFGNPLLI 3654
Cdd:COG5245 2455 IEDFKEEAC---STDYGLENSRIRKDLqDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKII 2531
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3655 KDVEHLDPIMNPVLNKELRRTGGRVLIRLGNQDIDFSPAFTLFLSTRDPSVSFPPDVCSRVSFVNFTVTRGSLQSQCLSK 3734
Cdd:COG5245 2532 GDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDA 2611
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3735 VLKAERPDVDRRRADLIKLQGEFKVKLRHLEKSLLQALNESKGNILDDDKVIATLETLKLEAADVTRKVEETEGVMQEVE 3814
Cdd:COG5245 2612 LEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRID 2691
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3815 QTTAIYSPLAHSCSSIFFVMEQLNRLNHFYQFSLDFFSDIFNFVLH-ENPELNGVKDygqrldiLTRDLFNVSYRRASLS 3893
Cdd:COG5245 2692 ALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWRRmKSKYLCAIRY-------MLMSSEWILDHEDRSG 2764
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3894 LLHDDHITFAM-----LLTQIKIRGTSSQADDAEYDF--LLSPDSNPSGKITAEFTEEQRAARTQEFAKLasfrdmpANI 3966
Cdd:COG5245 2765 FIHRLDVSFLLrtkrfVSTLLEDKNYRQVLSSCSLYGndVISHSCDRFDRDVYRALKHQMDNRTHSTILT-------SNS 2837
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3967 DSNADTwSKFWNDSKAEAhvpvfwepsqaeavndfkkllvikcfrpdrllaattkyiDQVFTPNfvnqAELDFAKLVREE 4046
Cdd:COG5245 2838 KTNPYK-EYTYNDSWAEA---------------------------------------FEVEDSG----DLYKFEEGLLEL 2873
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 4047 VKASTPIslcsIPGHDAAYRVDNLAQEQgvrlssvamGSQEGLTLADQAIASATKTGNWVLLKNVHLALTWLGQ-LDKRL 4125
Cdd:COG5245 2874 IVGHAPL----IYAHKKSLENERNVDRL---------GSKENEVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRyVEDVV 2940
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 4126 HSLKA----HPNFRLFLTMETNPKVPVNLLRLSRVLMFEPQPGIKANLQEsLRGIPSARLSKGPTERARLYFMVAWLHAV 4201
Cdd:COG5245 2941 YPIKAsrvcGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYAD-LVEIDRYPFDYTLVIACDDAFYLSWEHAA 3019
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 4202 VLERLRYVPLGWTKSYEFNDSDQDCALSTIDVWLdtvgqgrANVSPDRIPWDAIRTLLCQSVYGGRVDSEVDQQLLESFV 4281
Cdd:COG5245 3020 VASVISAGPKENNEEIYFGDKDFEFKTHLLKNIL-------FLNHLNARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYC 3092
|
3290 3300 3310 3320 3330 3340
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1940753919 4282 NSFFrpeCYDLSFKLVESGDGDDTGLT---APEGTKMSQFlEWIDELPAREPPTWLRLPATAER 4342
Cdd:COG5245 3093 RGYG---AHETSSQILASVPGGDPELVkfhMEEMCRSSAF-GVIGQLPDLALCAWLMGPCDSEY 3152
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1900-2250 |
4.86e-172 |
|
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: 532.83 E-value: 4.86e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1900 YGYEYFGVTERLVQTPLTDRCYLTLTQALESRLGGSPFGPAGTGKTESVKALGIQLGRFVLVFCCDENFDFQAMGRIFIG 1979
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1980 LSQVGAWGCFDEFNRLEERILSAVSQQVQTIQLGLKEAKTNpnneIELVGKNVRVNTNTGIFITMNPGYAGRSNLPDNLK 2059
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKT----FVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2060 KLFRSIAMTKPDKELIAQVMLSSQGFRTAESLASKVIPLFNLCNEKLSPQSHYDFGLRALKSVLVSAGNMKRdrlqelrs 2139
Cdd:pfam12774 157 ALFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKR-------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2140 SNPEnitaeferisesVPEQEILIQSIRETVVPKLVAEDISVLMGLLKGVFPGVEYNPVSLQPLRKAIKDICDKRRLVIG 2219
Cdd:pfam12774 229 SNPN------------LNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPH 296
|
330 340 350
....*....|....*....|....*....|.
gi 1940753919 2220 DLWMEKILQLYQIQRIHHGLMMVGPSGSGKS 2250
Cdd:pfam12774 297 DAFILKVIQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1346-1749 |
2.16e-150 |
|
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: 474.05 E-value: 2.16e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1346 LEPVLEELRDLKSVWSSLAKIWQSIFEIKDTLWATVVPRKIRTQLDTLMNSTKDMPNRMRQYAAFEYVQESLRLYVKVNP 1425
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1426 LLTDLKSEALRERHWRQLFKALRVEGRWTLSEMTVGNIWDLDLRRNESLVRDIIVVAQGEMALEEFLKQVRETWTNYVLE 1505
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1506 LVNYQN-KCRLIRGWDDLFAKCSENLNFLSAMKLSPYYKVFEEEAAGWEEKLNRIHVLFDVWIDVQRQWVYLEGIFTGSh 1584
Cdd:pfam08393 161 LVPYKDtGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSSE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1585 DIKHLLPVETSRFQNINSEFLTVMKKVYKSPFVLDVLNIANIQKSLERLADLLGKIQKALGEYLERERSSFPRFYFVGDE 1664
Cdd:pfam08393 240 DIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSND 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 1665 DLLEIIGNSKDVVRIQKHFKKMFAGINSIILNDDvTTVLGMSSKEDENVMFKTPVSIKDNPrINDWLTLVEKEMRMSLAQ 1744
Cdd:pfam08393 320 ELLEILSQTKDPTRVQPHLKKCFEGIASLEFDEN-KEITGMISKEGEVVPFSKPPVEAKGN-VEEWLNELEEEMRETLRD 397
|
....*
gi 1940753919 1745 ILAES 1749
Cdd:pfam08393 398 LLKEA 402
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
249-822 |
2.21e-130 |
|
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: 423.14 E-value: 2.21e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 249 LNKLQGDVNGWIKEIQKVTKLSRDPASGTAIQEINFWLSMERALEKIDEQLKSDQIVLTLDILKHAKRYHATVSFIADTG 328
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKALDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 329 LKEGTEKVHKYNQLMKDF--PLNELLSATDAIKIRDSLQQIFGHINKKLKLSPY--PIRRALPLVEAISRDLNDQLLRVL 404
Cdd:pfam08385 81 LTDALNEAKDNVKYLKTLerPFEDLEELTDPPEIIEAIPPLMNTIRLIWSISRYynTSERMTVLLEKISNQLIEQCKKYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 405 GSRRLMYMDYDDFEKATAGAVEVFETWDDVIKEFTHVAREVTRRR----SEKFLPIKINpahaKLQERILFVRNFRKQHE 480
Cdd:pfam08385 161 SPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERpwdfSERYIFGRFD----AFLERLEKILELFETIE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 481 QlhqtiLKVMTKPSGFITKA-SLEIEEVEsvslgdvdavEEVRLAYESVKNV--DVLDVSVEGtdmWVTAEVSYSERVSR 557
Cdd:pfam08385 237 Q-----FSKLEKIGGTKGPElEGVIEEIL----------EEFQEAYKVFKSKtyDILDVSNEG---FDDDYEEFKERIKD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 558 VENQIIAQLRDRLGIAKNANEMFRVFSKFNALFVRPKIRGAIQEYQTQLIEKVKDDIKKLHDKFKMQYrhsDAYHMSQlR 637
Cdd:pfam08385 299 LERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQK---YNPSPIA-K 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 638 DLPPISGHIIWARQIERQLSAYMKRVEDVLGKGweLYAEGQKLQSESSSFRKKLD--TKPIYDQWFSEITRRELAVSG-P 714
Cdd:pfam08385 375 NMPPVAGAIIWARQLFRRIQEPMKRFKEELGLL--KHAEGKKVIKKYNELAKKLDeyERLIYEAWLKEVEEASEGNLKrP 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 715 LFeiTRNRAQGNvlQLGVNFDSQIITLFKEVRNLLWLKYQVPHNVSIIAKDAKRVYPIAVSLMETIRTYSQMVNKVqrHG 794
Cdd:pfam08385 453 LL--VRHPETGK--LLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTL--LP 526
|
570 580
....*....|....*....|....*....
gi 1940753919 795 EIATLVAGYRNDAQKMVSRGVN-LRWEHF 822
Cdd:pfam08385 527 VERPLLAPHLKDIDEKLEPGLTtLTWNSL 555
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3579-3799 |
1.90e-101 |
|
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: 325.55 E-value: 1.90e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3579 LSWTEHALPADDLCVENAIILQRFNRYPLIIDPSGQATTFLMNEYKNRKITVTSFLDDSFLKNLESALRFGNPLLIKDV- 3657
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3658 EHLDPIMNPVLNKELRRTGGRVLIRLGNQDIDFSPAFTLFLSTRDPSVSFPPDVCSRVSFVNFTVTRGSLQSQCLSKVLK 3737
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1940753919 3738 AERPDVDRRRADLIKLQGEFKVKLRHLEKSLLQALNESKGNILDDDKVIATLETLKLEAADV 3799
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 ... |
2926-3204 |
5.49e-67 |
|
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: 228.65 E-value: 5.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2926 PLALFNDVLDHVLRIDRVFRQMQGHMLLIGVSGSGKTTLSRFVAWMNGLSVFQIKVHNKYSAADFDEDLRTVLRRAGCKG 3005
Cdd:pfam12780 2 DLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3006 EKVCFILDESNVLDSGFLERMNTLLANAEVPGLFEGDEYSSLMTQCKEGAQRDGLmLDSSEELYKWFTQQVMKNLHVVFT 3085
Cdd:pfam12780 82 KPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNI-EDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3086 MNPPEGGLASRAATSPALFNRCVLDWFGDWSDQAFFQVGQEFTTSLDLDRpnyspplkfpvvyrnlpetpTHRHAIINAF 3165
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDIEIPE--------------------ELKSNVVKVF 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 1940753919 3166 VYVHQSLYEVNAKLSKRNGKRGYVTPRHYLDFIRHYVRL 3204
Cdd:pfam12780 221 VYVHSSVEDMSKKFYEELKRKNYVTPKSYLELLRLYKNL 259
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
3219-3555 |
3.23e-49 |
|
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: 180.65 E-value: 3.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3219 LNVGLDKLKDTVVKVEELRKSLAVKKNELEIKNKQANDKLQKMVADQQEAEKKKATSIEIQAALEAQNKEISRRTAAVMA 3298
Cdd:pfam12777 3 LENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3299 DLANAEPAVLEAQKAVTDIKKAQLTEVRSMGNPPEMVKMAMESVCTLLGN-----KLESWKTVQGIIRRED-FISSIVNF 3372
Cdd:pfam12777 83 DLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPggkipKDKSWKAAKIMMAKVDgFLDSLIKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3373 DtdRQMTPAMRQKMKAEYLSNPSYNFETVNHASKACGPLVKWVIAQVNYSQILDKIGPLRQEVQELESSAQMTEIKASSI 3452
Cdd:pfam12777 163 D--KEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3453 EKMIEELENSIATYKEEYAVLISEVGSIKSEMERVKSKVERSVTLLESLSSERVRWEAGSHSFDTQMATTVGDVLLSSAF 3532
Cdd:pfam12777 241 KAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISAF 320
|
330 340
....*....|....*....|....
gi 1940753919 3533 LAYGGYFDQQYRELLFHK-WADHL 3555
Cdd:pfam12777 321 ISYLGFFTKKYRNELLDKfWIPYI 344
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
4188-4340 |
3.59e-45 |
|
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: 161.08 E-value: 3.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 4188 RARLYFMVAWLHAVVLERLRYVPLGWTKSYEFNDSDQDCALSTIDVWLDTVgqgranvsPDRIPWDAIRTLLCQSVYGGR 4267
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEY--------DEKIPWDALRYLIGEINYGGR 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1940753919 4268 VDSEVDQQLLESFVNSFFRPECYDLSFKLVESgdgddtGLTAPEGTKMSQFLEWIDELPAREPPTWLRLPATA 4340
Cdd:pfam18198 73 VTDDWDRRLLNTYLEEFFNPEVLEEDFKFSPS------LYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2584-2748 |
5.37e-41 |
|
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: 150.62 E-value: 5.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2584 DVVIPTVDTVRHEEVLYSWLSEHKPLILCGPPGSGKTMTLFSALRKLP--EMEVVGLNFSSATTPELILKTLEQHCEYRK 2661
Cdd:pfam12775 9 EILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDkeKYLPLFINFSAQTTSNQTQDIIESKLEKRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2662 TpnGVLLSPVllGRWLVVFCDEINLPSMDKYGTQRVISFMRQLVECGGFWRTTDKSWVKLERIQFVGACNPPTdPGRIPL 2741
Cdd:pfam12775 89 K--GVYGPPG--GKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPG-GGRNDI 163
|
....*..
gi 1940753919 2742 THRFLRH 2748
Cdd:pfam12775 164 TPRLLRH 170
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
4048-4152 |
1.94e-32 |
|
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: 123.71 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 4048 KASTPISLCSIPGHDAAYRVDNLAQEQG--VRLSSVAMGSQEGlTLADQAIASATKTGNWVLLKNVHLALTWLGQLDKRL 4125
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGfgGKLHSISLGQGQG-PIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKIL 79
|
90 100 110
....*....|....*....|....*....|
gi 1940753919 4126 HSL---KAHPNFRLFLTMETNPKVPVNLLR 4152
Cdd:pfam03028 80 EELpeeTLHPDFRLWLTSEPSPKFPISILQ 109
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2440-2568 |
2.99e-26 |
|
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: 106.60 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2440 LEPHFaeDGLVSKALEYA-STLDHIMDFTPMRVLGTLFSLINKSVRNVIQYNNQHsdfPMGAEQLDSYISKRLVSSTIWS 2518
Cdd:pfam17852 1 LEPLF--EWLVPPALEFVrKNCKEIVPTSDLNLVQSLCRLLESLLDEVLEYNGVH---PLSPDKLKEYLEKLFLFALVWS 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1940753919 2519 FSGDAKLELRARLGDFVRGVTT-IDLPQMANSSIIDFDVNINSGEWIPWQS 2568
Cdd:pfam17852 76 IGGTLDEDSRKKFDEFLRELFSgLDLPPPEKGTVYDYFVDLEKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2238-2378 |
1.32e-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: 76.18 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2238 GLMMVGPSGSGKSNAWQVLLAAMEvveNVESQsYVIDPKAMSKEALYGVLDPTTR--EWTDGLFTnilrkivdnvrgESA 2315
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALS---NRPVF-YVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLV------------RAA 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1940753919 2316 KRHWIIFDGDVD---PEWVENLNSVLDDNKLLTLPNGERLSLPP-NVRIVFEVETL----KYATLATVSRC 2378
Cdd:pfam07728 65 REGEIAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMNPLdrglNELSPALRSRF 135
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2588-2751 |
2.84e-10 |
|
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: 61.78 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2588 PTVDTVRHEEVLYSWLSEHKPLILCGPPGSGKTMTLFSALRKLPEMevvGLNFSSATTPELILKTLEQHCEyRKTPNGVL 2667
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRP---GAPFLYLNASDLLEGLVVAELF-GHFLVRLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2668 LSPVLLGRWLVVFCDEINLPSMDKygTQRVISFMRQLVEcggfwrttdkSWVKLERIQFVGACNPPTDPG-RIPLTHRFL 2746
Cdd:cd00009 77 FELAEKAKPGVLFIDEIDSLSRGA--QNALLRVLETLND----------LRIDRENVRVIGATNRPLLGDlDRALYDRLD 144
|
....*
gi 1940753919 2747 RHVPL 2751
Cdd:cd00009 145 IRIVI 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2606-2751 |
3.22e-07 |
|
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: 52.76 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2606 HKPLILCGPPGSGKTMTLFSALRKLPEMEVVGLNFSSATTPELILKTLEQHCEYRKTPNG-------VLLSPVLLGRWLV 2678
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGsgelrlrLALALARKLKPDV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1940753919 2679 VFCDEINlpSMDKYGTQRVISFMRQLvecggfwrTTDKSWVKLERIQFVGACNPPTDPGRIPLTHRFLRHVPL 2751
Cdd:smart00382 82 LILDEIT--SLLDAEQEALLLLLEEL--------RLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVL 144
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2940-3030 |
1.48e-06 |
|
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: 50.99 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2940 IDRVFRQMQGHMLLIGVSGSGKTTLSRFVAW---MNGLSVFQIKVHNKYS----AADFDEDLRTVLRRAGCKGEKVCFIL 3012
Cdd:cd00009 11 REALELPPPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASDLLEglvvAELFGHFLVRLLFELAEKAKPGVLFI 90
|
90
....*....|....*...
gi 1940753919 3013 DESNVLDSGFLERMNTLL 3030
Cdd:cd00009 91 DEIDSLSRGAQNALLRVL 108
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2950-3107 |
3.34e-06 |
|
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: 49.21 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2950 HMLLIGVSGSGKTTLS-RFVAWMNGLSVFQIKVHNKYSAADF----------DEDLRTVLRRAGCKGEkVCFiLDESNVL 3018
Cdd:pfam07728 1 GVLLVGPPGTGKTELAeRLAAALSNRPVFYVQLTRDTTEEDLfgrrnidpggASWVDGPLVRAAREGE-IAV-LDEINRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3019 DSGFLERMNTLLANAEVPgLFEGDEYsslmtqckEGAQRDGLMldsseelykwftqqvmknlhVVFTMNPPEGGLASraa 3098
Cdd:pfam07728 79 NPDVLNSLLSLLDERRLL-LPDGGEL--------VKAAPDGFR--------------------LIATMNPLDRGLNE--- 126
|
....*....
gi 1940753919 3099 TSPALFNRC 3107
Cdd:pfam07728 127 LSPALRSRF 135
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3205-3502 |
1.42e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3205 YNEKREDLEEQQRHLNV--------GLDKLKDTVVKVEELRKSLAVKKNELEIKNKQANDKLQKMVADQQEAEKK-KATS 3275
Cdd:TIGR02168 215 YKELKAELRELELALLVlrleelreELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3276 IEIqAALEAQNKEISRR-------TAAVMADLANAEPAVLEAQKAVTDIK------KAQLTEVRSMGNPPEMVKMAMESV 3342
Cdd:TIGR02168 295 NEI-SRLEQQKQILRERlanlerqLEELEAQLEELESKLDELAEELAELEekleelKEELESLEAELEELEAELEELESR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3343 CTLLGNKLESWKT-VQGIIRREDFISS-IVNFDTDRQMTPAMRQKMKAEylsNPSYNFETVNHASKACGplvkwviaqvn 3420
Cdd:TIGR02168 374 LEELEEQLETLRSkVAQLELQIASLNNeIERLEARLERLEDRRERLQQE---IEELLKKLEEAELKELQ----------- 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3421 ysqilDKIGPLRQEVQELESSAQMTEIKASSIEKMIEELENSIATYKEEYAVLISEVGSIKSEMERVKSKVERSVTLLES 3500
Cdd:TIGR02168 440 -----AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
..
gi 1940753919 3501 LS 3502
Cdd:TIGR02168 515 QS 516
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3196-3327 |
3.34e-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: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3196 DFIRHYVRLynekrEDLEEQQRHLnvgLDKLKDTVVKVEELRKSLAVKKNELEIKNKQANDKLQKMVADQQEAEKKKATS 3275
Cdd:COG3883 116 DFLDRLSAL-----SKIADADADL---LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1940753919 3276 IEIQAALEAQNKEISRRTAAVMADLANAEPAVLEAQKAVTDIKKAQLTEVRS 3327
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| Phage_GP20 |
pfam06810 |
Phage minor structural protein GP20; This family consists of several phage minor structural ... |
3205-3304 |
4.58e-04 |
|
Phage minor structural protein GP20; This family consists of several phage minor structural protein GP20 sequences of around 180 residues in length. The function of this family is unknown.
Pssm-ID: 429131 [Multi-domain] Cd Length: 149 Bit Score: 43.50 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3205 YNEKREDLEEQQRHLNVGLDKLKDTVVKVEELRKSLAvkknELEIKNKQANDKLQKMVADQQeaekkkaTSIEIQAALEA 3284
Cdd:pfam06810 23 VNTERDTLKEQLATRDKQLKDLKKVAKDNEELQKQID----ELQAKNKDAEADYEAKIADLK-------FDNAIKLALKG 91
|
90 100
....*....|....*....|
gi 1940753919 3285 QNkeiSRRTAAVMADLANAE 3304
Cdd:pfam06810 92 AK---AKNEKAVKALLDKDK 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3193-3328 |
7.52e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3193 HYLDFIRHYVRLYNEKREDLEEQQRHLNVGLDKLKdtvVKVEELRKSLAVKKNELEIKNKQANDKLQKM----------V 3262
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELE---AELEELRLELEELELELEEAQAEEYELLAELarleqdiarlE 308
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1940753919 3263 ADQQEAEKKKATSIEIQAALEAQNKEISRRTAAVMADLANAEPAVLEAQKAVTDIKKAQLTEVRSM 3328
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
2112-2361 |
1.19e-03 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 44.76 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2112 YDFGLRALKSVLVSAGNMKRDRLQELRSSNPENITAEFERISESVPEQEILIQSIRETVVPKLVAEDISVLMGLLKGVFP 2191
Cdd:COG1401 105 YELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2192 GVEYnPVSLQPLRKAIKDICDKRRLvigdlwmEKILQLYQIQRIHHGLMMVGPSGSGKSnaWQVLLAAMEVVENVESQSY 2271
Cdd:COG1401 185 EELY-SEDLESEDDYLKDLLREKFE-------ETLEAFLAALKTKKNVILAGPPGTGKT--YLARRLAEALGGEDNGRIE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2272 VI-------DPKAMskEALYGVLDPTTREWTDGLFTNILRKIVDNvrgeSAKRHWIIFD----GDVD------------P 2328
Cdd:COG1401 255 FVqfhpswsYEDFL--LGYRPSLDEGKYEPTPGIFLRFCLKAEKN----PDKPYVLIIDeinrANVEkyfgellsllesD 328
|
250 260 270
....*....|....*....|....*....|....*.
gi 1940753919 2329 EWVENLNsvlddnklLTLP---NGERLSLPPNVRIV 2361
Cdd:COG1401 329 KRGEELS--------IELPysgEGEEFSIPPNLYII 356
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3192-3499 |
1.28e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3192 RHYLDFIRHYVRLYN--EKREDLEEQQRHLNVGLDKLKDTVVKVEELRKSLAVKKNELEIKNKQANDKLQKMVADQQEAE 3269
Cdd:COG4717 115 REELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3270 KKKATSIE-IQAALEAQNKEISRRTAAVMAdlANAEPAVLEAQKAVTDIKKaQLTEVRSMGnppemvkMAMESVCTLLGN 3348
Cdd:COG4717 195 QDLAEELEeLQQRLAELEEELEEAQEELEE--LEEELEQLENELEAAALEE-RLKEARLLL-------LIAAALLALLGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3349 K---LESWKTVQGIIRREDFISSIVNFDTDRQMTPAMRQKMKAEYLS-----------------------NPSYNFETVN 3402
Cdd:COG4717 265 GgslLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPaleeleeeeleellaalglppdlSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3403 HASKACGPLVKW--VIAQVNYSQILDKIGPL-------------------------RQEVQELE---------SSAQMTE 3446
Cdd:COG4717 345 RIEELQELLREAeeLEEELQLEELEQEIAALlaeagvedeeelraaleqaeeyqelKEELEELEeqleellgeLEELLEA 424
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1940753919 3447 IKASSIEKMIEELENSIATYKEEYAVLISEVGSIKSEMERVKSKVERSVTLLE 3499
Cdd:COG4717 425 LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQE 477
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
3201-3495 |
1.45e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3201 YVRLYNEKREDLEEQQRHLNVGLDKLKDTVvkveelrkslavkkNELEIKNKQANDKLQKMVADQ-QEAEKKKATSIEIQ 3279
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNI--------------EEQRKKNGENIARKQNKYDELvEEAKTIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3280 AALEAQNKEISRRTAAvMADLANAepavleaqKAVTDIKKAQLTEVRSM----GNPPemvkmamesVCTllgnkleswkt 3355
Cdd:PHA02562 241 DELLNLVMDIEDPSAA-LNKLNTA--------AAKIKSKIEQFQKVIKMyekgGVCP---------TCT----------- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3356 vQGIIRREDFISSIvnfdtdrqmtpamRQKMKAeylsnpsynfetvnhaskACGPLVKWVIAQVNYSQILDKIGPLRQEV 3435
Cdd:PHA02562 292 -QQISEGPDRITKI-------------KDKLKE------------------LQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940753919 3436 QELES-------SAQMTEIKASSIEKMIEELENSIATYKEEYAVLISEVGSIKSEM-ERVKSKVERSV 3495
Cdd:PHA02562 340 LELKNkistnkqSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKsELVKEKYHRGI 407
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
3234-3323 |
1.97e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 43.95 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3234 EELRKSLAVKKNELEIK---NKQANDKLQKMVADQQEAEKKKATSI-EIQAALEAQNKEISRRTAAVMADLANAEPAVLE 3309
Cdd:TIGR04320 257 AALQAKLATAQADLAAAqtaLNTAQAALTSAQTAYAAAQAALATAQkELANAQAQALQTAQNNLATAQAALANAEARLAK 336
|
90 100
....*....|....*....|
gi 1940753919 3310 AQKAVT------DIKKAQLT 3323
Cdd:TIGR04320 337 AKEALAnlnadlAKKQAALD 356
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3197-3326 |
2.13e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3197 FIRHYVRLYNEKREDLEEQQRhlnvgLDKLKDTVvkvEELRKSLAVKKNELEIKNKQANDKLQKMVADQQEAEKKKATSI 3276
Cdd:PRK03918 600 FYNEYLELKDAEKELEREEKE-----LKKLEEEL---DKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLEL 671
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1940753919 3277 EIQ-AALEAQNKEISRRTAAVMADLANAE---PAVLEAQKAVTDIKKA--QLTEVR 3326
Cdd:PRK03918 672 SRElAGLRAELEELEKRREEIKKTLEKLKeelEEREKAKKELEKLEKAleRVEELR 727
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2949-3090 |
2.49e-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: 41.59 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2949 GHMLLIGVSGSGKTTLSRFVAWMNGLSVFQIKVHNkysaadfDEDLRTVLRragckgEKVCFILDESNVLDSGFLERMNT 3028
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------GEDILEEVL------DQLLLIIVGGKKASGSGELRLRL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1940753919 3029 LLANAEVPG---LFEgDEYSSLMTqckegaQRDGLMLDSSEELYKWFTQQVMKNLHVVFTMNPPE 3090
Cdd:smart00382 70 ALALARKLKpdvLIL-DEITSLLD------AEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEK 127
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3192-3299 |
2.73e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3192 RHYLDFIRHYVRLYNEKREDLEEQQRHLNVGLDKLKDTVVKVEELRKSLAVKKNELEIKNKQANDKLQkmvADQQEAEKK 3271
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA---ELAAELAEL 218
|
90 100
....*....|....*....|....*...
gi 1940753919 3272 KATSIEIQAALEAQNKEISRRTAAVMAD 3299
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2608-2733 |
3.40e-03 |
|
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: 40.74 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2608 PLILCGPPGSGKTMTLFSALRKLPEMEVVGLNFSSATTPElilkTLEQHCEYR----KTPNGVLLSPVLLGRwlVVFCDE 2683
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTEE----DLFGRRNIDpggaSWVDGPLVRAAREGE--IAVLDE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2684 INLPSMDKYGTQRVISFMRQLVECGGFWRTTdkswVKLERIQFVGACNPP 2733
Cdd:pfam07728 75 INRANPDVLNSLLSLLDERRLLLPDGGELVK----AAPDGFRLIATMNPL 120
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
2951-3025 |
4.46e-03 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 40.27 E-value: 4.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940753919 2951 MLLIGVSGSGKTTLSRFVAWMNGLSVFQIKVH---NKYsAADFDEDLRTVLRRAGCKGEKVCFIlDEsnvLDSGFLER 3025
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSelvSKY-VGESEKRLRELFEAAKKLAPCVIFI-DE---IDALAGSR 73
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3172-3291 |
5.19e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3172 LYEVNAKLSKRNGKRgyvtpRHYLDFIRHYVRLYNEKREDLEEQQRHLNVGLDKLKDTVVKVEELRKSLAVKKNELEIKN 3251
Cdd:TIGR02168 290 LYALANEISRLEQQK-----QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1940753919 3252 KQANDKLQKMVADQQEAEKKKATSIEIQAALEAQNKEISR 3291
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3208-3327 |
5.27e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 3208 KREDLEEQQRHLNVGLDKLKDTVVKVEELRKSLAVKKNELEIKNKQANDKLQKMVADQQEAEKKKAtsiEIQAALEAQNK 3287
Cdd:TIGR02169 785 EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK---SIEKEIENLNG 861
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1940753919 3288 EIsrrtAAVMADLANAEPAVLEAQKAVTDIKK------AQLTEVRS 3327
Cdd:TIGR02169 862 KK----EELEEELEELEAALRDLESRLGDLKKerdeleAQLRELER 903
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
2815-3025 |
8.42e-03 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 41.82 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2815 RELTRWMRGIFEAIKPMETLSVEGLVRIWAHEALRLFQDRLVTEEERKWTDDEIDRIALKHFPgLDREQALARPILYSNW 2894
Cdd:COG0464 42 LLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLL-LLLLLLLLDLERALLE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2895 LSKNYVPVDREELREYAKARLKVFYEEELDVPLALFNDV--LDHV-----------LRIDRVFRQMQ----GHMLLIGVS 2957
Cdd:COG0464 121 LLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLggLEEVkeelrelvalpLKRPELREEYGlpppRGLLLYGPP 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1940753919 2958 GSGKTTLSRFVAWMNGLSVFQIKVHN---KY---SAADFDEDLRTVLRRAGCkgekVCFIlDEsnvLDSGFLER 3025
Cdd:COG0464 201 GTGKTLLARALAGELGLPLIEVDLSDlvsKYvgeTEKNLREVFDKARGLAPC----VLFI-DE---ADALAGKR 266
|
|
| AAA_lid_1 |
pfam17857 |
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3. |
2787-2876 |
8.88e-03 |
|
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3.
Pssm-ID: 465535 [Multi-domain] Cd Length: 100 Bit Score: 38.76 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940753919 2787 LTAAMVELYLCSQSHFVPE-MQAHYIYSPRELTRWMRGI-FEAIKPMETlsVEGLVRIWAHEALRLFQDRLVTEEERKwT 2864
Cdd:pfam17857 1 LIAAALAFHQKIAATFLPTaIKFHYIFNLRDFANIFQGIlFSSAECLKS--PLDLIRLWLHESERVYGDKMVDEKDFD-L 77
|
90
....*....|..
gi 1940753919 2865 DDEIDRIALKHF 2876
Cdd:pfam17857 78 FDKIQMASLKKF 89
|
|
| |
