|
Name |
Accession |
Description |
Interval |
E-value |
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
985-4276 |
0e+00 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 1083.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 985 TYHNILNVMPEGQACLEkaydCVNGIMSDLEEYLSEWLSYQSLWVLQAEQLFEMLGTSLSKWMKTLMEIRKGRLVFDTQD 1064
Cdd:COG5245 146 LSHELELIFRSGEQWVG----CMRKLYESVCSERDGFYEEKSFWSRFHMEMCHIREFCRSKAFRFACDVLRKSGKYVTVA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1065 TRKVIFPVSVEYGK-AQQKILFKYDYWhkemlvkfGAVVGDEMQKFFNSVskwRNVLETQSVDGGSTSDT-----IGLIS 1138
Cdd:COG5245 222 TLDSLLSSSKYSELgRRLHFYANMDFS--------GIYFPKSFSEFKDSV---ISATQAVSRDIGRQSRMarrliLVQMD 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1139 FVQSLKKQTKSGQDAVDLYRSSQRLLNQQRYQFPAQWLYSENVEGEWSAFTEILSLrDASIQTQMMNLQTKFAQEDELVe 1218
Cdd:COG5245 291 SLARLIVDRICEYVSIEWLGCCEELLTCSMESMSSLVNSFDGEESEAMSLESSLFY-EFRGGEHLAGFYSAFGDIKRIL- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1219 kRTVETLTEWNKSKPVEGAQRPQEALNVITAFEAKLNKLTEERN------KMRKARVALDlsdsahapsegDKLTVATEE 1292
Cdd:COG5245 369 -LFTWSFKKLGTLLPSLPGYSSGGMDYGEEYRSLLWELGSEVGDpdsgpvRKWMRKDLFD-----------AKVRSGVSF 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1293 LAAMKDVWKALQPVYTGIDEAKEKTWLSVQprKIRQSLDELMNQlKQLP--VKCRTYKSYEHVKQMLHTYGKMNMlvaEL 1370
Cdd:COG5245 437 GKQEEFVSDIFNITFERIHGMDPTTLEDDE--EDTPALAILLGQ-EEAGrfVKLCKIMRMFSFFNSLEMFSRRTL---AN 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1371 KSEALKerHWHQMMK--EMRVNWNLSDLTLGQVWDADILRHehTIKKILLVAQGEMA--LEEFLREMREYWQNYEVElvn 1446
Cdd:COG5245 511 RMAIVK--YLSSVVRtgPLFLQRDFFGRMSELLMARDMFME--VDGVLRLFFGGEWSgiVQLSGIRRAKRCVERQID--- 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1447 yqnktRLIKGWddlfnkLKEHQNSLSAMKLSPYYKQFEESAQSWdEKLNKINAMfdvwidvqrRWVYLEGLFSGSAEIST 1526
Cdd:COG5245 584 -----DEIREW------CSSVLSDDFLEERAVRVERGADGARRL-RASSGSPVL---------RRLDEYLMMMSLEDLMP 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1527 LLPFESSRFATITTDVLALMKKVAASPRILDVVNMQGAQRLlERLADMLAKIQKALGEYLERERSSFPRFyfVGDEDLLE 1606
Cdd:COG5245 643 LIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILEDVGDDL-DLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMD 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1607 IMGNSKDITRIQKHLKKMFAGITAIdINEEDRsITAFHSREGEKVDLVKIVstkdvRINDWLQALEAemkhtLARQLAAS 1686
Cdd:COG5245 720 RVRELENRVYSYRFFVKKIAKEEMK-TVFSSR-IQKKEPFSLDSEAYVGFF-----RLYEKSIVIRG-----INRSMGRV 787
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1687 LTHFSKMNIQTMTTDDYVEWLDKFPAQVITLTAEIWwCDEMEKTLAD--GKGAENVEQAVVKTLELLADSVLKeqppirr 1764
Cdd:COG5245 788 LSQYLESVQEALEIEDGSFFVSRHRVRDGGLEKGRG-CDAWENCFDPplSEYFRILEKIFPSEEGYFFDEVLK------- 859
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1765 kKMEALITELVHKRDTCRKLVSMKIRAANDFGWLQCMRFyfdPKQVDPVRCCVVKMANSQffYGFEYLGIQERLVRTPLT 1844
Cdd:COG5245 860 -RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISEL---PQGLYKRFIKVRSSYRSA--EMFAKNTIPFFVFEHSMD 933
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1845 DRCYLTMTQALHSRLggSPFgpAGTGKTESVKALGHQLGRFVlvfncdETFDFQAmgRILVGLCQVGAWGcFDEFNRLEE 1924
Cdd:COG5245 934 TSQHQKLFEAVCDEV--CRF--VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDE 1000
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1925 RMLsAVSQQIQTIQEAVRAGGDMSVDLVGKRLnVNSNIGIFITMNPgysgRSNLPDNLKQLFRSLAMTQPdrqliaqvml 2004
Cdd:COG5245 1001 ISR-TILVDEYLNSDEFRMLEELNSAVVEHGL-KSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIP---------- 1064
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2005 FSQGFRTAETLANKIVPLFILCKEQLSDQCHYDFglRALKYVLvsagnikrdkldKMGSAALEDVAEQQMLIQSVcetlv 2084
Cdd:COG5245 1065 FGAIKSRRESLDREIGAFNNEVDGIAREEDELMF--YPMFKSL------------KAKHRMLEEKTEYLNKILSI----- 1125
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2085 pklvnediaLLFSLLSDVfpgihytanqMRELRQQL----STVCDEHLLIYSDVQGEMGSMWLDKVLQLYQITNLNHGLM 2160
Cdd:COG5245 1126 ---------TGLPLISDT----------LRERIDTLdaewDSFCRISESLKKYESQQVSGLDVAQFVSFLRSVDTGAFHA 1186
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2161 LVGSSGSGKTMAWKVLLKALERWENVEGVAHVIDAkamskdslygvmdpnTREWTdGLFTSVIRkiiDNVRGE-ADRRQW 2239
Cdd:COG5245 1187 EYFRVFLCKIKHYTDACDYLWHVKSPYVKKKYFDA---------------DMELR-QFFLMFNR---EDMEARlADSKME 1247
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2240 IIFDgdvdpEWVENLNSVLDDNKLLTLPNGERlsippnvRIIFEVADlkyATLATVSRCGMVWFSEEVVTSEMLFERYLS 2319
Cdd:COG5245 1248 YEVE-----RYVEKTKAEVSSLKLELSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRLSTKGVFLDELG 1312
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2320 IIRRvPLDSDSAIsfssssapVNLIGEDAKPTRSIEIqrtAALALQTHFSPDgivpgslKYAVSELEHIMPPTPQRLLSS 2399
Cdd:COG5245 1313 DTKR-YLDECLDF--------FSCFEEVQKEIDELSM---VFCADALRFSAD-------LYHIVKERRFSGVLAGSDASE 1373
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2400 FFSMMSYSIRKIVSHDEGliddsveIDQIQSFVLRSmltnLVWAFSGDGKWKSREMMSDFIRQATTISLPPnqqacLIDY 2479
Cdd:COG5245 1374 SLGGKSIELAAILEHKDL-------IVEMKRGINDV----LKLRIFGDKCRESTPRFYLISDGDLIKDLNE-----RSDY 1437
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2480 E------VQLSGDWQPWlSKVPTMEIESHRVA-AADLVVPTIDTVRHEMLLAAWLAEHKPLVLCGPPGSGKTMTLLAALR 2552
Cdd:COG5245 1438 EemlimmFNISAVITNN-GSIAGFELRGERVMlRKEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLR 1516
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2553 SQQEMEVVNVNFSSSTTPELLLRTFDHYCEYRRTPNGVVLAPVQLSQWLVIFCDEINLPAPDKYGTQRVISFLRQLVELN 2632
Cdd:COG5245 1517 SELITEVKYFNFSTCTMTPSKLSVLERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQ 1596
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2633 GFYRTSDHSWVSLERIQFVGACNPPTDPGRHPMTSRFLRHVPIVYVDYPGQTSLQQIYGTFNRAMLKMTPAVRGLADQLT 2712
Cdd:COG5245 1597 GFWSSIAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETM 1676
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2713 NAMVDVYLASQEHFTQDDQPHYVYSPRELTRWVRGISEAITPLESLSAEQLVRLWAHEAIRLFQDRLVTEEEREWTDKLV 2792
Cdd:COG5245 1677 SASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDL 1756
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2793 DTTAERYFGNAcRLDEALKRPLLYSCWLSRNYVPVTREELQDYVSARLKGFYEEELDVKLVLFDQMLDHVLRIDRIYRQS 2872
Cdd:COG5245 1757 YDFGLRAIREM-IAGHIGEAEITFSMILFFGMACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVV 1835
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2873 QGHLLLIGTAGAGKTTLSRFVAWLNGLSVFQLKVHSKYTAADFDEDMRTVLRRAGCRNEKLCFIMDESNMLDTGFLERLN 2952
Cdd:COG5245 1836 GGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFN 1915
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2953 TLLANGEVPGLFEGDEHTTLMTQIKEGAQRQGLILDSHDELYKWFTQQVMRNLHVVFTMNPSGSGLRERASTSPALFNRC 3032
Cdd:COG5245 1916 PLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEKDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGIRSPALKNRC 1995
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3033 VLNWFGDWSENALYQVGSE-LTRTMDLDRTDYEGSvrltpscELVPSQP--TYRDAVVNTlcLVHKTvqkfNEMETKKGH 3109
Cdd:COG5245 1996 FIDFKKLWDTEEMSQYANSvETLSRDGGRVFFING-------ELGVGKGalISEVFGDDA--VVIEG----RGFEISMIE 2062
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3110 RVMACTPRHFLDFIKQFMSLFHEKRSDLEEEKIHLNIGLNKISETEEQVKELQKSLKLKSNELQEKKEAANLKLKEMLGD 3189
Cdd:COG5245 2063 GSLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGE 2142
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3190 QQKAEEEKKFSEQLQKELAEQLKQMAEKKTFVENDLAQVEPAVAEAQTAVQGIKKSQLVEVKSMSSPPVTVKLTLEAICI 3269
Cdd:COG5245 2143 RLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCD 2222
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3270 LLGENVgTDWKAIRQVMMKDDFMTRILQFDTEL-LTPEILKQME-KYIQNPDWEFDKVNRASVACGPMVKWARAQLLYST 3347
Cdd:COG5245 2223 LLGFEA-KIWFGEQQSLRRDDFIRIIGKYPDEIeFDLEARRFREaRECSDPSFTGSILNRASKACGPLKRWLVRECNRSK 2301
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3348 MLHKVEPLRNELKRLEQEaAKKTQEGKVVDVRIT-ELEESIGKYKEEYAQLIGQAENIKQDLLSVQEKVNRSTELLSSLR 3426
Cdd:COG5245 2302 VLEVKIPLREEEKRIDGE-AFLVEDRLTLGKGLSsDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILI 2380
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3427 SERDRWSSGSAGFSQQMDSLVGDALLSSAFLAYAGYYDQMLRDEIFHKWFnHVVNAGLHFRHDLAR--IEYLSTVDDRLQ 3504
Cdd:COG5245 2381 NEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGMSF-IRISKEFRDKEIRRRqfITEGVQKIEDFK 2459
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3505 WQLNSlpvDDLCTENA-IMLHRFNRYPLIIDPSGQAVEYIMKQFAGKNIQKTSFLDESFRKNLESALRFGNSLLVQDVEA 3583
Cdd:COG5245 2460 EEACS---TDYGLENSrIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIGDAEA 2536
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3584 YDPILNPVLNREVKRAGGRVLITIGDQDIDLSPSFQIFMITRDSTVEFSPDICSRVTFVNFTVTSSSLASQCLNQVLRSE 3663
Cdd:COG5245 2537 LDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLV 2616
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3664 RPDVDKKRNDLLKLQGEFAVRLRHLEKALLAALNESKGKILDDNSVIETLEKLKNEAAEVAQKSAETDKVMAEVDAVSAQ 3743
Cdd:COG5245 2617 SGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSE 2696
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3744 YQRLSTACSHIYHTLQQLNEIHFLYHYSLDFLVEIFTHVLKTPELssttdYAKRLRIITTSLFQTVFRRVSRGMLHTDKV 3823
Cdd:COG5245 2697 YNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWRRMKSK-----YLCAIRYMLMSSEWILDHEDRSGFIHRLDV 2771
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3824 LLALL-------LMRIHIRSNPSAPAYEQHFDLLLGRSDfvakndeadstipgGLDFLTVENKKsiakarkvvgfenvfa 3896
Cdd:COG5245 2772 SFLLRtkrfvstLLEDKNYRQVLSSCSLYGNDVISHSCD--------------RFDRDVYRALK---------------- 2821
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3897 HLQHNSAAVTSWLTND--NPESNVPVV--WDDAD-----GKLSPLCIAMNSLIVVHALRPDRLMASahrvvstafddhfm 3967
Cdd:COG5245 2822 HQMDNRTHSTILTSNSktNPYKEYTYNdsWAEAFevedsGDLYKFEEGLLELIVGHAPLIYAHKKS-------------- 2887
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3968 qqdkvVDILSIVDNevspsepvllcsatgydasgkiedlavetnrqltsiaIGSAEGFNQADSALGTATKSGRWVLLKNV 4047
Cdd:COG5245 2888 -----LENERNVDR-------------------------------------LGSKENEVYAVLNSLFSRKEKSWFEVYNI 2925
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 4048 HLAPSWLAQ-LEKRLHSMKP---HAQFRLFLTA-EIHPKLPSSILRASRVVVFEPATGLKANLLrSLSSIPPQRLTKAPT 4122
Cdd:COG5245 2926 SLSFGWFKRyVEDVVYPIKAsrvCGKVKNMWTSmVDADMLPIQLLIAIDSFVSSTYPETGCGYA-DLVEIDRYPFDYTLV 3004
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 4123 ERSRLYLLVCWLHALVQERLRYTPLGWSTAYEFSDADLRVACDTLDaavDAVAQGRPNvepeRLPWTTLRTLLSQCIYGG 4202
Cdd:COG5245 3005 IACDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLK---NILFLNHLN----ARKWGNNRDLIFTIVYGK 3077
|
3290 3300 3310 3320 3330 3340 3350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17506419 4203 KIDNQFDQVLLDCVLENLFTAKSFEQDHVLIPKYDGDDSLFTPNMSKKDQMIGWVEELKNEQLPAWLGLPNNAE 4276
Cdd:COG5245 3078 KHSLMEDSKVVDKYCRGYGAHETSSQILASVPGGDPELVKFHMEEMCRSSAFGVIGQLPDLALCAWLMGPCDSE 3151
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1827-2170 |
9.10e-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: 520.50 E-value: 9.10e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1827 YGFEYLGIQERLVRTPLTDRCYLTMTQALHSRLGGSPFGPAGTGKTESVKALGHQLGRFVLVFNCDETFDFQAMGRILVG 1906
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1907 LCQVGAWGCFDEFNRLEERMLSAVSQQIQTIQEAVRAGGDmSVDLVGKRLNVNSNIGIFITMNPGYSGRSNLPDNLKQLF 1986
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLK-TFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1987 RSLAMTQPDRQLIAQVMLFSQGFRTAETLANKIVPLFILCKEQLSDQCHYDFGLRALKYVLVSAGNIKRDKLDKMgsaal 2066
Cdd:pfam12774 160 RPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLN----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2067 edvaEQQMLIQSVCETLVPKLVNEDIALLFSLLSDVFPGIHYTANQMRELRQQLSTVCDEHLLIYSDVqgemgsmWLDKV 2146
Cdd:pfam12774 235 ----EDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDA-------FILKV 303
|
330 340
....*....|....*....|....
gi 17506419 2147 LQLYQITNLNHGLMLVGSSGSGKT 2170
Cdd:pfam12774 304 IQLYETMLVRHGVMLVGPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1286-1686 |
1.95e-137 |
|
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: 437.08 E-value: 1.95e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1286 LTVATEELAAMKDVWKALQPVYTGIDEAKEKTWLSVQPRKIRQSLDELMNQLKQLPVKCRTYKSYEHVKQMLHTYGKMNM 1365
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1366 LVAELKSEALKERHWHQMMKEMRVNW--NLSDLTLGQVWDADILRHEHTIKKILLVAQGEMALEEFLREMREYWQNYEVE 1443
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFdpLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1444 LVNYQN-KTRLIKGWDDLFNKLKEHQNSLSAMKLSPYYKQFEESAQSWDEKLNKINAMFDVWIDVQRRWVYLEGLFSGSa 1522
Cdd:pfam08393 161 LVPYKDtGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSSE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1523 EISTLLPFESSRFATITTDVLALMKKVAASPRILDVVNMQGAQRLLERLADMLAKIQKALGEYLERERSSFPRFYFVGDE 1602
Cdd:pfam08393 240 DIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSND 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1603 DLLEIMGNSKDITRIQKHLKKMFAGITAIDINEEDRsITAFHSREGEKVDLVKIVSTKDVRINDWLQALEAEMKHTLARQ 1682
Cdd:pfam08393 320 ELLEILSQTKDPTRVQPHLKKCFEGIASLEFDENKE-ITGMISKEGEVVPFSKPPVEAKGNVEEWLNELEEEMRETLRDL 398
|
....
gi 17506419 1683 LAAS 1686
Cdd:pfam08393 399 LKEA 402
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
238-811 |
9.37e-105 |
|
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: 349.18 E-value: 9.37e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 238 LNALQSGCNRWVKEIRKVTQLERDPSSGTSLQEMTFWLNLERALLKISQKRDGEEVTLTLEALKCGKR-----FHATvgf 312
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSsylpaFKAL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 313 dsDNGLKQKLAVVQDYNTLMKEF--PLSELVSATDVPKLMHAVVGIFLHLRKLR--STKYP-LQRALRLVEAISRDLNSQ 387
Cdd:pfam08385 78 --DTELTDALNEAKDNVKYLKTLerPFEDLEELTDPPEIIEAIPPLMNTIRLIWsiSRYYNtSERMTVLLEKISNQLIEQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 388 LLKVLSSYNLMRTPIAEFNEIMSQCQALFSKWDDEYDKFIALLRDINKKKRDDPSKlswkvTAVHKRLET---RLMQILQ 464
Cdd:pfam08385 156 CKKYLSPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWDFSE-----RYIFGRFDAfleRLEKILE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 465 FRKQHEQFrTVIERVLRPVGNG-SREREQLMidssegekspdEQVDIAYEFLKNV--DFLDVDSPAWENAFKRYEDQIGV 541
Cdd:pfam08385 231 LFETIEQF-SKLEKIGGTKGPElEGVIEEIL-----------EEFQEAYKVFKSKtyDILDVSNEGFDDDYEEFKERIKD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 542 VETAITTRLKSQLESSRNSNEMFSIFSRYNALFIRPRIRGAIYEYQTRLINRVKEDINELQARFTKargEQGVKIMQTVG 621
Cdd:pfam08385 299 LERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDK---QKYNPSPIAKN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 622 LPPFSAKIMWIRNYERQLQRYMKRVEDVLGKQweNHVDGRQLKADGDNFKVKLN--TQPMFDEWVESV-QSQNWTLPNKI 698
Cdd:pfam08385 376 MPPVAGAIIWARQLFRRIQEPMKRFKEELGLL--KHAEGKKVIKKYNELAKKLDeyERLIYEAWLKEVeEASEGNLKRPL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 699 LTvdRVQVDGRMqlqLKINYHSDSSVLYKEVSHLKSMGFRVPLKIVNWAHQANQMRPSATSLIEAARTFASVNAALASVQ 778
Cdd:pfam08385 454 LV--RHPETGKL---LSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVE 528
|
570 580 590
....*....|....*....|....*....|....
gi 17506419 779 gvDSLLASYKKDIQNQLIEGAT-LGWDSYKVDQY 811
Cdd:pfam08385 529 --RPLLAPHLKDIDEKLEPGLTtLTWNSLGIDEY 560
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3503-3723 |
2.14e-96 |
|
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: 311.30 E-value: 2.14e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3503 LQWQLNSLPVDDLCTENAIMLHRFNRYPLIIDPSGQAVEYIMKQFAGKNIQKTSFLDESFRKNLESALRFGNSLLVQDV- 3581
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3582 EAYDPILNPVLNREVKRAGGRVLITIGDQDIDLSPSFQIFMITRDSTVEFSPDICSRVTFVNFTVTSSSLASQCLNQVLR 3661
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17506419 3662 SERPDVDKKRNDLLKLQGEFAVRLRHLEKALLAALNESKGKILDDNSVIETLEKLKNEAAEV 3723
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 ... |
2852-3129 |
3.89e-59 |
|
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: 205.92 E-value: 3.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2852 LVLFDQMLDHVLRIDRIYRQSQGHLLLIGTAGAGKTTLSRFVAWLNGLSVFQLKVHSKYTAADFDEDMRTVLRRAGCRNE 2931
Cdd:pfam12780 3 LVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2932 KLCFIMDESNMLDTGFLERLNTLLANGEVPGLFEGDEHTTLMTQIKEGAQRQGlILDSHDELYKWFTQQVMRNLHVVFTM 3011
Cdd:pfam12780 83 PTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQN-IEDSREAVYNYFVKRCRNNLHIVLCM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3012 NPSGSGLRERASTSPALFNRCVLNWFGDWSENALYQVgseltrtmdldrtdyeGSVRLTPscELVPSqpTYRDAVVNTLC 3091
Cdd:pfam12780 162 SPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAV----------------AEKFLED--IEIPE--ELKSNVVKVFV 221
|
250 260 270
....*....|....*....|....*....|....*...
gi 17506419 3092 LVHKTVQKFNEMETKKGHRVMACTPRHFLDFIKQFMSL 3129
Cdd:pfam12780 222 YVHSSVEDMSKKFYEELKRKNYVTPKSYLELLRLYKNL 259
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4281-4563 |
2.10e-46 |
|
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: 170.88 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 4281 TKRGESMLRNMLKV---TDEELAFNEDGKEEVkpqwmaqLGELAKQWLQLLPKEI---VKMRRTVENIKDPLFRFFEREV 4354
Cdd:pfam18199 1 TNETNELLSTLLSLqprSDSGGGGGGSSREEI-------VLELAKDILEKLPEPFdieEAEEKYPVGYEDPLNTVLLQEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 4355 NLGSQLLKDIRRDLNEISAVCRAEKKQNNETRALAASLQKGEVPTGWKRYTVPREVTVMDWMTDLNERLKQLIRIgGADN 4434
Cdd:pfam18199 74 ERFNKLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLKQLQDW-LDDE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 4435 LKRETFWLGGTFSPEAYITATRQQVAQANTWSLEQLNLHIHIGRTDSTDVFR--------ISGIDIRGAK-SVGGNKL-- 4503
Cdd:pfam18199 153 GPPKVFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSPEEVTeppedgvyVHGLFLEGARwDRKNGCLve 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17506419 4504 -ELCELVkSECDIVEFSWKQDVADGT-----RLPLYLYGDRRQLISPLAFHL---SSATVFYQRGVALV 4563
Cdd:pfam18199 233 sEPKELF-SPLPVIHLKPVESDKKKLdentyECPVYKTSERHSTNFVFSVDLptdKPPDHWILRGVALL 300
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
3144-3476 |
1.53e-44 |
|
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This family is the region between D4 and D5 and is the two predicted alpha-helical coiled coil segments that form the stalk supporting the ATP-sensitive microtubule binding component.
Pssm-ID: 463699 [Multi-domain] Cd Length: 344 Bit Score: 167.17 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3144 LNIGLNKISETEEQVKELQKSLKLKSNELQEKKEAANlKLKEMLG-DQQKAEEEKKFSEQLQKELAEQLKQMAEKKTFVE 3222
Cdd:pfam12777 3 LENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDAD-KLIQVVGiEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3223 NDLAQVEPAVAEAQTAVQGIKKSQLVEVKSMSSPPVTVKLTLEAICILL--GENVGTD--WKAIRQVMMK-DDFMTRILQ 3297
Cdd:pfam12777 82 EDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMapGGKIPKDksWKAAKIMMAKvDGFLDSLIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3298 FDTELLTPEILKQMEKYIQNPDWEFDKVNRASVACGPMVKWARAQLLYSTMLHKVEPLRNELKRLEQEAAKKTQEGKVVD 3377
Cdd:pfam12777 162 FDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAAIK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3378 VRITELEESIGKYKEEYAQLIGQAENIKQDLLSVQEKVNRSTELLSSLRSERDRWSSGSAGFSQQMDSLVGDALLSSAFL 3457
Cdd:pfam12777 242 AKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISAFI 321
|
330
....*....|....*....
gi 17506419 3458 AYAGYYDQMLRDEIFHKWF 3476
Cdd:pfam12777 322 SYLGFFTKKYRNELLDKFW 340
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2508-2672 |
1.08e-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: 155.63 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2508 DLVVPTIDTVRHEMLLAAWLAEHKPLVLCGPPGSGKTMTLLAALRS--QQEMEVVNVNFSSSTTPELLLRTFDHYCEYRR 2585
Cdd:pfam12775 9 EILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKldKEKYLPLFINFSAQTTSNQTQDIIESKLEKRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2586 tpnGVVLAPVqLSQWLVIFCDEINLPAPDKYGTQRVISFLRQLVELNGFYRTSDHSWVSLERIQFVGACNPPTdPGRHPM 2665
Cdd:pfam12775 89 ---KGVYGPP-GGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPG-GGRNDI 163
|
....*..
gi 17506419 2666 TSRFLRH 2672
Cdd:pfam12775 164 TPRLLRH 170
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
4124-4275 |
1.43e-42 |
|
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: 153.76 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 4124 RSRLYLLVCWLHALVQERLRYTPLGWSTAYEFSDADLRVACDTLDAAVDAVaqgrpnvePERLPWTTLRTLLSQCIYGGK 4203
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEY--------DEKIPWDALRYLIGEINYGGR 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17506419 4204 IDNQFDQVLLDCVLENLFTAKSFEQDHVLIPkydgdDSLFTPNMSKKDQMIGWVEELKNEQLPAWLGLPNNA 4275
Cdd:pfam18198 73 VTDDWDRRLLNTYLEEFFNPEVLEEDFKFSP-----SLYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
3984-4094 |
9.37e-34 |
|
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: 127.56 E-value: 9.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3984 SPSEPVLLCSATGYDASGKIEDLAVETN--RQLTSIAIGSAEGFnQADSALGTATKSGRWVLLKNVHLAPSWLAQLEKRL 4061
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGfgGKLHSISLGQGQGP-IAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKIL 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 17506419 4062 HSM---KPHAQFRLFLTAEIHPKLPSSILRASRVVV 4094
Cdd:pfam03028 80 EELpeeTLHPDFRLWLTSEPSPKFPISILQNSIKIT 115
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2158-2298 |
1.72e-16 |
|
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: 78.87 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2158 GLMLVGSSGSGKTMAWKVLLKALERWENVEGVAHvidaKAMSKDSLYG--VMDPNTREWTDGLFTsvirkiidnvrgEAD 2235
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLT----RDTTEEDLFGrrNIDPGGASWVDGPLV------------RAA 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17506419 2236 RRQWIIFDGDVD---PEWVENLNSVLDDNKLLTLPNGERLSIPP-NVRIIFEV----ADLKYATLATVSRC 2298
Cdd:pfam07728 65 REGEIAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMnpldRGLNELSPALRSRF 135
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2364-2492 |
5.64e-13 |
|
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: 68.46 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2364 LQTHFspDGIVPGSLKYAVSELEHIMPPTPQRLLSSFFSMMSYSIRKIVSHDEgliDDSVEIDQIQSFVLRSMLTNLVWA 2443
Cdd:pfam17852 1 LEPLF--EWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDEVLEYNG---VHPLSPDKLKEYLEKLFLFALVWS 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 17506419 2444 FSGDGKWKSREMMSDFIRQ-ATTISLPPNQQACLIDYEVQL-SGDWQPWLS 2492
Cdd:pfam17852 76 IGGTLDEDSRKKFDEFLRElFSGLDLPPPEKGTVYDYFVDLeKGEWVPWSD 126
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2512-2675 |
5.89e-12 |
|
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: 66.40 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2512 PTIDTVRHEMLLAAWLAEHKPLVLCGPPGSGKTMTLLAALRSQQEME--VVNVNFSSSTTPELLLRTFDHYCEYRRTpng 2589
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGapFLYLNASDLLEGLVVAELFGHFLVRLLF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2590 vvlAPVQLSQWLVIFCDEIN-LPAPDKYGTQRVISFLRQLVELNgfyrtsdhswvslERIQFVGACNPPTDPGRHPM-TS 2667
Cdd:cd00009 78 ---ELAEKAKPGVLFIDEIDsLSRGAQNALLRVLETLNDLRIDR-------------ENVRVIGATNRPLLGDLDRAlYD 141
|
....*...
gi 17506419 2668 RFLRHVPI 2675
Cdd:cd00009 142 RLDIRIVI 149
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2530-2679 |
1.18e-08 |
|
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: 57.00 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2530 HKPLVLCGPPGSGKTMTLLAALRSQQEMEVVNVNFSSSTTPELLLRTFDHYCEYRRTPNG-------VVLAPVQLSQWLV 2602
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGsgelrlrLALALARKLKPDV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17506419 2603 IFCDEINLPAPDKygtqrvisflRQLVELNGFYRTSDHSWVSLERIQFVGACNPPTDPGRHPMTSRFLRHVPIVYVD 2679
Cdd:smart00382 82 LILDEITSLLDAE----------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2855-3032 |
8.62e-08 |
|
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: 54.46 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2855 FDQMLDHVLRIDRIYRQSQGHLLLIGTAGAGKTTLSRFVAW---LNGLSVFQLKVHSKYTAADFDEDMRTVLRRagcrne 2931
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASDLLEGLVVAELFGHFLVR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2932 klcfimdesnmldtgflerlntllangevpglfegdehttLMTQIKEGAQRQGLILDSHDELYKWFTQQVMRNLHVVFTM 3011
Cdd:cd00009 75 ----------------------------------------LLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL 114
|
170 180
....*....|....*....|....*....
gi 17506419 3012 NPSGSGLR--------ERASTSPALFNRC 3032
Cdd:cd00009 115 RIDRENVRvigatnrpLLGDLDRALYDRL 143
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
3123-3423 |
1.28e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.11 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3123 IKQFMSLFHEKRSDLEEEKIHLNIglnKISETEEQVKELQKSLKlksNELQEKKEAANLKLKEMLGDQQKA-------EE 3195
Cdd:pfam05483 192 IEKMILAFEELRVQAENARLEMHF---KLKEDHEKIQHLEEEYK---KEINDKEKQVSLLLIQITEKENKMkdltfllEE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3196 EKKFSEQLQKEL---AEQLKQMAEKKTFVENDLAQVEPAVAEA-----------QTAVQGI------KKSQLVEVKSMSS 3255
Cdd:pfam05483 266 SRDKANQLEEKTklqDENLKELIEKKDHLTKELEDIKMSLQRSmstqkaleedlQIATKTIcqlteeKEAQMEELNKAKA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3256 PPVTVKLTLEAICILLGENVGTDwkaiRQVMMKDDFMTRILQFDTELLTPEiLKQMEKYIQNPDWEFDKVNRasvacgpm 3335
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELLRTE----QQRLEKNEDQLKIITMELQKKSSE-LEEMTKFKNNKEVELEELKK-------- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3336 VKWARAQLLYSTmlHKVEPLRNELKRLEQEAAK--KTQEGKVVDVritELEESIGKYKEEYaqLIGQAENIKQDLlsVQE 3413
Cdd:pfam05483 413 ILAEDEKLLDEK--KQFEKIAEELKGKEQELIFllQAREKEIHDL---EIQLTAIKTSEEH--YLKEVEDLKTEL--EKE 483
|
330
....*....|
gi 17506419 3414 KVnRSTELLS 3423
Cdd:pfam05483 484 KL-KNIELTA 492
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2532-2671 |
4.00e-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: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2532 PLVLCGPPGSGKTM--TLLAALRSQQEMEVvnVNFSSSTTPELLLRTFDHYCEYRRTPNGVVLAPVQLSQwlVIFCDEIN 2609
Cdd:pfam07728 1 GVLLVGPPGTGKTElaERLAAALSNRPVFY--VQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAAREGE--IAVLDEIN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17506419 2610 LPAPDKYGTQRVISFLRQLVELNGFYRTSdhswVSLERIQFVGACNPPtDPGRHPMTSRFLR 2671
Cdd:pfam07728 77 RANPDVLNSLLSLLDERRLLLPDGGELVK----AAPDGFRLIATMNPL-DRGLNELSPALRS 133
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3130-3434 |
4.17e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3130 FHEKRSDLEEEKIHLNIglnKISETEEQVKELQKSL---KLKSNELQEKKEAANLKLKEMLGDQQKAEEEKKF------- 3199
Cdd:TIGR02168 237 LREELEELQEELKEAEE---ELEELTAELQELEEKLeelRLEVSELEEEIEELQKELYALANEISRLEQQKQIlrerlan 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3200 SEQLQKELAEQLKQMAEKKTFVENDLAQVEPAVAEAQTAVQGIKKsqlvEVKSMSsppvtvkltleaicillgenvgtdw 3279
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA----ELEELE------------------------- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3280 kairqvmmkddfmtrilqfdtelltpEILKQMEKYIQNPDWEFDKVNRASVACGPMVKWARAQLLYstmlhkvepLRNEL 3359
Cdd:TIGR02168 365 --------------------------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER---------LEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3360 KRLEQEAAKKTQEG-----KVVDVRITELEESIGKYKEEYAQLIGQAENIKQDLLSVQEKVNRSTELLSSLRSERDRWSS 3434
Cdd:TIGR02168 410 ERLEDRRERLQQEIeellkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3132-3471 |
8.34e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3132 EKRSDLEEEKIHLNIGLNKISETEEQVKELQKSLKLKSNELQEKKEAANLKLKEMlgDQQKAEEEKKFSEQLQkELAEQL 3211
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEELE-ELQQRL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3212 KQMAEKKTFVENDLAQVEPAVAEAQTAVQGIKKSQLVEVKSMSSPPVTVKLTLEAICILLGENVGTdWKAIRQVMMKDDF 3291
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT-IAGVLFLVLGLLA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3292 MTRILQFDTELLTPEILKQMEKYIQNPDWEFDKVNRASVACG--PMVKWARAQLLYSTMLHKVEPLRN--------ELKR 3361
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlpPDLSPEELLELLDRIEELQELLREaeeleeelQLEE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3362 LEQEAAKKTQEGKVVDvrITELEEsIGKYKEEYAQLIGQAENIKQDLLS----------------VQEKVNRSTELLSSL 3425
Cdd:COG4717 368 LEQEIAALLAEAGVED--EEELRA-ALEQAEEYQELKEELEELEEQLEEllgeleellealdeeeLEEELEELEEELEEL 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 17506419 3426 RSERDRWSSGSAGFSQQMDSLVGDALLSSAFLAYagyydQMLRDEI 3471
Cdd:COG4717 445 EEELEELREELAELEAELEQLEEDGELAELLQEL-----EELKAEL 485
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1197-1596 |
2.90e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.74 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1197 ASIQTQMMNLQTKFAQEDELVEKRTVETLTEWNKSKPVEGAQRPQEALNVITAFEAKLNKLTEERNKMRKARVALDLSDS 1276
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1277 AHAPSEGDKLTVATEELAAMKdvWKALQPVYTGiDEAKEKTWLSVQPRKIRQSLDELMNQLKQLPVKC----RTYKSYEH 1352
Cdd:TIGR00618 418 AFRDLQGQLAHAKKQQELQQR--YAELCAAAIT-CTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHlqetRKKAVVLA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1353 VKQMLhtygkmnmlvAELKSEALK-ERHWHQMMKEM--------RVNWNLSDLTLGQVWDADiLRHEHT-IKKIL--LVA 1420
Cdd:TIGR00618 495 RLLEL----------QEEPCPLCGsCIHPNPARQDIdnpgpltrRMQRGEQTYAQLETSEED-VYHQLTsERKQRasLKE 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1421 QGEMALEEFLReMREYWQNYEVELVNYQNKTRLIKGWDDLFNKLKehqnslsamklspyyKQFEESAQSWDEKLNKINAM 1500
Cdd:TIGR00618 564 QMQEIQQSFSI-LTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE---------------DMLACEQHALLRKLQPEQDL 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 1501 FDVWIDVQRRWVYLEGLFSGSAEISTLLPFESSRFATITTDVLalmKKVAASPRILDVVNMQGAQRLLERLADMLAKIQK 1580
Cdd:TIGR00618 628 QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVL---PKELLASRQLALQKMQSEKEQLTYWKEMLAQCQT 704
|
410
....*....|....*.
gi 17506419 1581 ALGEYLERERSSFPRF 1596
Cdd:TIGR00618 705 LLRELETHIEEYDREF 720
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2875-3032 |
4.93e-05 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 46.13 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2875 HLLLIGTAGAGKTTLS-RFVAWLNGLSVFQLKVHSKYTAADF----DEDMRT------VLRRAGcRNEKLCFImDESNML 2943
Cdd:pfam07728 1 GVLLVGPPGTGKTELAeRLAAALSNRPVFYVQLTRDTTEEDLfgrrNIDPGGaswvdgPLVRAA-REGEIAVL-DEINRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2944 DTGFLERLNTLLANGEVpglfegdehttlmtQIKEGAQRQGLILDshdelykwftqqvmrNLHVVFTMNPSGsglRERAS 3023
Cdd:pfam07728 79 NPDVLNSLLSLLDERRL--------------LLPDGGELVKAAPD---------------GFRLIATMNPLD---RGLNE 126
|
....*....
gi 17506419 3024 TSPALFNRC 3032
Cdd:pfam07728 127 LSPALRSRF 135
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3132-3428 |
5.44e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3132 EKRSDLEEEKIHLNIGLNK----ISETEEQVKELQKSLKLKSNELQEKK---EAANLKLKEMLGDQQKAEEE-----KKF 3199
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEktteISNTQTQLNQLKDEQNKIKKQLSEKQkelEQNNKKIKELEKQLNQLKSEisdlnNQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3200 SEQLQKELAEQLKQMAEKKTFVENDLAQVEPAVAEAQTAVQGIKKsqlvEVKSMSSPPVTVKLTLE----AICILLGENV 3275
Cdd:TIGR04523 305 EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK----ELTNSESENSEKQRELEekqnEIEKLKKENQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3276 GTDWKAIRQVMMKDDFMTRILQFDtelltpEILKQMEKYIQNPDWEFDKVNRasvacgpmvkwaRAQLLYSTmlhkVEPL 3355
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQE------KLNQQKDEQIKKLQQEKELLEK------------EIERLKET----IIKN 438
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17506419 3356 RNELKRLEQEAAKKTQEGKVVDVRITELEESIGKYKEEYaqligqaENIKQDLLSVQEKVNRSTELLSSLRSE 3428
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI-------NKIKQNLEQKQKELKSKEKELKKLNEE 504
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3159-3244 |
9.17e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3159 KELQKSLKLKSNELQEKKEAANLKLKEMLGDQQKAEEEKKFSEQLQKELAEQLKQmAEKKTFVENDLAQVEpAVAEAQTA 3238
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQ-AEEAAAKAAAAAKAK-AEAEAKRA 156
|
....*.
gi 17506419 3239 VQGIKK 3244
Cdd:PRK09510 157 AAAAKK 162
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
3150-3225 |
1.12e-04 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 44.70 E-value: 1.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17506419 3150 KISETEEQVKELQKSLKLKSNELQEKKEAANlKLKEMLGDQQKAEEEKKFSEQLQKELAEQLKQMAEKKTFVENDL 3225
Cdd:pfam04871 2 KKSELESEASSLKNENTELKAELQELSKQYN-SLEQKESQAKELEAEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3149-3244 |
1.28e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.53 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3149 NKISETEEQVKELQKSLKLKSNELQEKKEAANLKLKEmLGDQQKAEEEKKFSEQLQKELAEQLKQMAEKKTFVENDLAQV 3228
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKE-LEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAK 135
|
90
....*....|....*.
gi 17506419 3229 EPAVAEAQTAVQGIKK 3244
Cdd:TIGR02794 136 AEAEAERKAKEEAAKQ 151
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
3132-3252 |
1.44e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 47.32 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3132 EKRSDLEEEKIHLNIGLNKISETEEQVKELQKSLKLKSNELQE-KKEAANLKLKEMLGDQQKAEEEKKFSEQLQKELAEQ 3210
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQlEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEEL 230
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 17506419 3211 LKQMAEKKTFVE---NDLAQVEPAVAEAQTAVQGIKKSQLVEVKS 3252
Cdd:smart00787 231 EEELQELESKIEdltNKKSELNTEIAEAEKKLEQCRGFTFKEIEK 275
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3149-3463 |
2.73e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3149 NKISETEEQVKELQKSLklksNELQEKKEAANLKLKEMLGDQQKAEEEkkfSEQLQKELAEQLKQMAEKKtfvendlAQV 3228
Cdd:COG3883 23 KELSELQAELEAAQAEL----DALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAEIEERR-------EEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3229 EPAVAEAQTAvqgikksqlvevkSMSSPPVTVkltleaicILLGENVGTdwkAIRQVmmkdDFMTRILQFDTELLtpEIL 3308
Cdd:COG3883 89 GERARALYRS-------------GGSVSYLDV--------LLGSESFSD---FLDRL----SALSKIADADADLL--EEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3309 KQMEKYIQNpdwefdkvnrasvacgpmvkwARAQLlySTMLHKVEPLRNELKRLEQEAAKKTQEgkvVDVRITELEESIG 3388
Cdd:COG3883 139 KADKAELEA---------------------KKAEL--EAKLAELEALKAELEAAKAELEAQQAE---QEALLAQLSAEEA 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17506419 3389 KYKEEYAQLIGQAENIKQDLLSVQEKVNRSTELLSSLRSERDRWSSGSAGFSQQMDSLVGDALLSSAFLAYAGYY 3463
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGA 267
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
3132-3251 |
2.85e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.96 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3132 EKRSDLEEEKihlnigLNKISETEEQVKELQKSLKLKSNELQEKKEAANLKLKEMLG-DQQKAEEEKKFSEQLQKELAEQ 3210
Cdd:COG3064 66 QRAAELAAEA------AKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAaEKEKAEEAKRKAEEEAKRKAEE 139
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 17506419 3211 LKQMAEKKTFVENDLAQVEPAVAEAQTAVQGIKKSQLVEVK 3251
Cdd:COG3064 140 ERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAA 180
|
|
| AAA_lid_1 |
pfam17857 |
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3. |
2715-2800 |
3.04e-04 |
|
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: 43.00 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2715 MVDVYLASQEHFTQDDQP-----HYVYSPRELTRWVRGIseAITPLESL-SAEQLVRLWAHEAIRLFQDRLVTEEEREWT 2788
Cdd:pfam17857 1 LIAAALAFHQKIAATFLPtaikfHYIFNLRDFANIFQGI--LFSSAECLkSPLDLIRLWLHESERVYGDKMVDEKDFDLF 78
|
90
....*....|..
gi 17506419 2789 DKLVDTTAERYF 2800
Cdd:pfam17857 79 DKIQMASLKKFF 90
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3132-3403 |
3.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3132 EKRSDLEEEKIHLNIGLNKISETEEQVKELQKSLKLKSNELQEKKEAANLKLKEMLGDQQKAEEEKKFSEQLQKELAEQL 3211
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3212 KQMAEKKTFVENDLAQVEPAVAEAQTAV---------------QGIKKSQLVEVKSMSSppvTVKLTLEAIcillgenvg 3276
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrKELLEEYTAELKRIEK---ELKEIEEKE--------- 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3277 tdwKAIRQVMMKddfMTRILQFDTELLTpeiLKQMEKYIQNPDWEFDKVNrasvacgpMVKWARAQLLYSTMLHKVEPLR 3356
Cdd:PRK03918 476 ---RKLRKELRE---LEKVLKKESELIK---LKELAEQLKELEEKLKKYN--------LEELEKKAEEYEKLKEKLIKLK 538
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17506419 3357 NELKRLEQEAAKKtqegKVVDVRITELEESIGKYKEEYAQLIGQAEN 3403
Cdd:PRK03918 539 GEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| RecA-like_VCP_r2 |
cd19529 |
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ... |
2531-2675 |
3.93e-04 |
|
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410937 [Multi-domain] Cd Length: 159 Bit Score: 44.02 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2531 KPLVLCGPPGSGKTMtLLAALRSQQemevvNVNFSSSTTPELLLR----TFDHYCEYRRTPNGVvlAPVqlsqwlVIFCD 2606
Cdd:cd19529 28 KGILLYGPPGTGKTL-LAKAVATES-----NANFISVKGPELLSKwvgeSEKAIREIFRKARQV--APC------VIFFD 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17506419 2607 EINLPAP------DKYGTQRVISFLrqLVELNGFyrtsdhswVSLERIQFVGACNPP--TDPG--RhpmTSRFLRHVPI 2675
Cdd:cd19529 94 EIDSIAPrrgttgDSGVTERVVNQL--LTELDGL--------EEMNGVVVIAATNRPdiIDPAllR---AGRFDRLIYI 159
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
2870-2955 |
4.40e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 43.10 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2870 RQSQGHLLLIGTAGAGKTTLSR-FVAWLNGLSVFQLKV--HSKYTAADFDED------------------MRTVLRRAGC 2928
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRrLLEQLPEVRDSVVFVdlPSGTSPKDLLRAllralglplsgrlskeelLAALQQLLLA 81
|
90 100
....*....|....*....|....*..
gi 17506419 2929 RNEKLCFIMDESNMLDTGFLERLNTLL 2955
Cdd:pfam13401 82 LAVAVVLIIDEAQHLSLEALEELRDLL 108
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3123-3427 |
5.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3123 IKQFMSLFHEKRSDLEEEKIHLNiglNKISETEEQVKELQkSLKLKSNELQEKKEAANLKLKEMLGDQQKAEEEKKFSEQ 3202
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLE---EEINGIEERIKELE-EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3203 LQK-----------ELAEQLKQMAEKKTFVENDLAQVEPAVAEAQTAVQGIKKSqLVEVKSMssppvtvkltlEAICILL 3271
Cdd:PRK03918 374 LERlkkrltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA-IEELKKA-----------KGKCPVC 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3272 GENVGTDWKAirqvmmkddfmtrilqfdtELL---TPEiLKQMEKYIQNPDWEFDKVNRASVACGPMVKWARAQLLYSTM 3348
Cdd:PRK03918 442 GRELTEEHRK-------------------ELLeeyTAE-LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKEL 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17506419 3349 LHKVEPLRNELKRLEQEAAKKTQEgkvvdvritELEesigKYKEEYAQLIGQAENIKQDLLSVQEKVNRSTELLSSLRS 3427
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEELEKKAE---------EYE----KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
2533-2634 |
6.10e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 42.71 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2533 LVLCGPPGSGKTMTL--LAALRSQQEMEVVNVNFSSSTTPELLLRT----FDHYCEYRRTPNGVVLAPVQLSQ----WLV 2602
Cdd:pfam13401 8 LVLTGESGTGKTTLLrrLLEQLPEVRDSVVFVDLPSGTSPKDLLRAllraLGLPLSGRLSKEELLAALQQLLLalavAVV 87
|
90 100 110
....*....|....*....|....*....|...
gi 17506419 2603 IFCDEI-NLPAPdkygtqrVISFLRQLVELNGF 2634
Cdd:pfam13401 88 LIIDEAqHLSLE-------ALEELRDLLNLSSK 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3132-3251 |
6.53e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3132 EKRSDLEEEKIhlniglnKISETEEQVKELQKSLKLKSNELQEKKEAANLKLKEMLGDQQKAEEEKKFSEQLQKelAEQL 3211
Cdd:PTZ00121 1610 EEAKKAEEAKI-------KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK--AEEA 1680
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 17506419 3212 KQMAEKKTFVENDLAQVEpavaEAQTAVQGIKKSQLVEVK 3251
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEA----EEAKKAEELKKKEAEEKK 1716
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3132-3246 |
1.07e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3132 EKRSDLEEEKIHLNIGLNKISETEEQVKELQKSLKLKSNELQEKKEAANLKLKEMLGDQQKAEEEKKFSEQLQKELAEQL 3211
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110
....*....|....*....|....*....|....*
gi 17506419 3212 KQMAEKKTFVENDLAQVEPAVAEAQTAVQGIKKSQ 3246
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3130-3214 |
1.13e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3130 FHEKRSDLEEEkihLNIGLNKISETEEQVKELQKSLKLKSNELqEKKEAANLKLKEMLGDQQKAEEEKKfsEQLQKELAE 3209
Cdd:PRK12704 66 IHKLRNEFEKE---LRERRNELQKLEKRLLQKEENLDRKLELL-EKREEELEKKEKELEQKQQELEKKE--EELEELIEE 139
|
....*
gi 17506419 3210 QLKQM 3214
Cdd:PRK12704 140 QLQEL 144
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3132-3244 |
2.24e-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: 42.99 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3132 EKRSDLEEEKIHLNiglNKISETEEQVKELQKSLKLKSNELQEKKEAANlKLKEMLGDQQKAEE-------------EKK 3198
Cdd:COG1579 31 AELAELEDELAALE---ARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVRNNKEyealqkeieslkrRIS 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 17506419 3199 FSEQLQKELAEQLKQMAEKKTFVENDLAQVEPAVAEAQTAVQGIKK 3244
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
|
| RecA-like_PEX6_r2 |
cd19527 |
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ... |
2510-2657 |
2.56e-03 |
|
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410935 [Multi-domain] Cd Length: 160 Bit Score: 41.73 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2510 VVPTIDT-VRHEMLLAAWLAEHKPLVLCGPPGSGKTMtLLAALRSQqemevVNVNFSSSTTPELL-LRTFDHYCEYRRtp 2587
Cdd:cd19527 5 ILDTIQLpLEHPELFSSGLRKRSGILLYGPPGTGKTL-LAKAIATE-----CSLNFLSVKGPELInMYIGESEANVRE-- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17506419 2588 ngvVLAPVQLSQWLVIFCDEINLPAPDKyGTQ--------RVISFLrqLVELNGFYRTSDHSWVsleriqfVGACNPP 2657
Cdd:cd19527 77 ---VFQKARDAKPCVIFFDELDSLAPSR-GNSgdsggvmdRVVSQL--LAELDGMSSSGQDVFV-------IGATNRP 141
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3120-3240 |
2.65e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3120 LDFIKQFMSLFHEKRSDLEEEKIHLNIGLNKISETEEQVKELQKSLKLKSNELQEKKEAANLKLKEMLGDQQKAEEEKKF 3199
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 17506419 3200 SEQLQKE---LAEQLKQMAEKKTFVENDLAQVEPAVAEAQTAVQ 3240
Cdd:COG4372 117 LEELQKErqdLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
3159-3240 |
2.94e-03 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 40.34 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3159 KELQKSLKLKSNELQEkkeaanlKLKEMLGD-QQKAEEEKKFSEQLQKELAEQLKQMAEK-KTFVENDLAQVEPAVAEAQ 3236
Cdd:COG4980 30 KETRKKLKDKADDLKD-------KAEDLKDElKEKASELSEEAKEKLDELIEEIKEKIEElKEEVEPKIEELKEEAEKLQ 102
|
....
gi 17506419 3237 TAVQ 3240
Cdd:COG4980 103 KEVE 106
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
2518-2662 |
3.27e-03 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 41.50 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2518 RHEMLLAAWLAEHKPLVLCGPPGSGKTMtLLAALRSQQEMEVVNVNFSSSTTP------ELLLRTFDhycEYRRtpngvv 2591
Cdd:cd19481 14 RGSRLRRYGLGLPKGILLYGPPGTGKTL-LAKALAGELGLPLIVVKLSSLLSKyvgeseKNLRKIFE---RARR------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2592 LAPVqlsqwlVIFCDEINLPAPDKYG------TQRVISFLrqLVELNGFYrtsdhswvSLERIQFVGACNPP-------T 2658
Cdd:cd19481 84 LAPC------ILFIDEIDAIGRKRDSsgesgeLRRVLNQL--LTELDGVN--------SRSKVLVIAATNRPdlldpalL 147
|
....
gi 17506419 2659 DPGR 2662
Cdd:cd19481 148 RPGR 151
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3351-3434 |
4.90e-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: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3351 KVEPLRNELKRLEQEAAKKTQEGKVVDVRITELEESIGKYKEEyaqligqAENIKQDLLsvQEKVNRSTELLSSLRSERD 3430
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA-------LNDLEARLS--HSRIPEIQAELSKLEEEVS 808
|
....
gi 17506419 3431 RWSS 3434
Cdd:TIGR02169 809 RIEA 812
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3132-3247 |
4.90e-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: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3132 EKRSDLEEEKIHLNIGLNKISETEEQVKELQK---SLKLKSNELQEKKEAANLKLKEMLGDQQKAEEEKKFSEQLQKELA 3208
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
90 100 110
....*....|....*....|....*....|....*....
gi 17506419 3209 EQLKQMAEKKTFVENDLAQVEPAVAEAQTAVQGIKKSQL 3247
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
3098-3430 |
5.07e-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: 43.02 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3098 QKFNEMETkkghRVMACTPRHFLDfIKQFMSLFHEKRSDLEEEKIHLNIGLNKISETEEQVKELQKSLKLKSNELQEKKE 3177
Cdd:COG5185 207 IKESETGN----LGSESTLLEKAK-EIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLN 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3178 AANLKLK---EMLGDQQKAEEEKKFSEQLQKELAEQLKQMAEKKTFvendlaqvEPAVAEAQTAVQGIKKSQLVEVKSMS 3254
Cdd:COG5185 282 ENANNLIkqfENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEL--------EESKRETETGIQNLTAEIEQGQESLT 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3255 SPPVTVKLTLEAIcillgenVGTDWKAIRQVMMkDDFMTRI---------LQFDTELLTPEILKQMEKYIQNPDWEFDKV 3325
Cdd:COG5185 354 ENLEAIKEEIENI-------VGEVELSKSSEEL-DSFKDTIestkesldeIPQNQRGYAQEILATLEDTLKAADRQIEEL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3326 NRAsvacgpmVKWARAQllYSTMLHKVEPLRNEL------------KRLEQEAAKKTQEGKV----VDVRITELEESIGK 3389
Cdd:COG5185 426 QRQ-------IEQATSS--NEEVSKLLNELISELnkvmreadeesqSRLEEAYDEINRSVRSkkedLNEELTQIESRVST 496
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 17506419 3390 YKEEYAQLIgqaENIKQDLLSVQEKVNRSTELLSSLRSERD 3430
Cdd:COG5185 497 LKATLEKLR---AKLERQLEGVRSKLDQVAESLKDFMRARG 534
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
3152-3247 |
5.29e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.82 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3152 SETEEQVKELQKSLKlksNELQEKKEAANLKLKEMLgDQQKAEEEKKF----SEQLQKELAEQLKQMAEKKTfvenDLAQ 3227
Cdd:pfam09731 353 REREEIRESYEEKLR---TELERQAEAHEEHLKDVL-VEQEIELQREFlqdiKEKVEEERAGRLLKLNELLA----NLKG 424
|
90 100
....*....|....*....|.
gi 17506419 3228 VEPAVAE-AQTAVQGIKKSQL 3247
Cdd:pfam09731 425 LEKATSShSEVEDENRKAQQL 445
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3130-3240 |
5.43e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3130 FHEKRSDLEEEKIHLNIGLNKISETEEQVKELQKSLKLKSNELQEKKEAANLKLKEMLGDQQKAEEEKKFSEQLQKELAE 3209
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
90 100 110
....*....|....*....|....*....|.
gi 17506419 3210 QLKQMAEKKTFVENDLAQVEPAVAEAQTAVQ 3240
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3129-3244 |
6.32e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3129 LFHEKRSDLEEEKIHLNIGLNKISETEEQVKELQKSLKLKSNELQEKKEAANLKLKEMLGDQQKAEEEKKFSEQLQKELA 3208
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110
....*....|....*....|....*....|....*.
gi 17506419 3209 EQLKQMAEKKTFVENDLAQVEPAVAEAQTAVQGIKK 3244
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3102-3475 |
6.48e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3102 EMETKKGHRVMAcTPRHFLDFIKQFMSLFHEKRSDLEEEKIHLNIGLNKISE--------TEEQVKELQKSLKLKsNELQ 3173
Cdd:TIGR00618 534 EQTYAQLETSEE-DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEdipnlqniTVRLQDLTEKLSEAE-DMLA 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3174 EKKEAANLKLKEMLGDQQKAEEEKKFSEQLQKELAeQLKQMAEkkTFVENDLAQVEPAVAEAQTAVQGIKKSQLVEVKSM 3253
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLT-ALHALQL--TLTQERVREHALSIRVLPKELLASRQLALQKMQSE 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3254 SSPPVTVKLTLEAICILLGE---NVGTDWKAIRQVMMKDDFMTRILQFDTELLTPEILKQMEkyiqnpdwEFDKVNRASV 3330
Cdd:TIGR00618 689 KEQLTYWKEMLAQCQTLLREletHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH--------QARTVLKART 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3331 ACGPMVKWARAQLLYStmLHKVEPLRNELKRLEQEAAKKTQEGKvvdvritELEESIGKYKEEYAQ-LIGQAENIKQDLL 3409
Cdd:TIGR00618 761 EAHFNNNEEVTAALQT--GAELSHLAAEIQFFNRLREEDTHLLK-------TLEAEIGQEIPSDEDiLNLQCETLVQEEE 831
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17506419 3410 SVQEKVNRSTELLSSLRSERDRWSSGsagfSQQMDSLVGDALLSSAFLAYAGYYDQ---MLRDEIFHKW 3475
Cdd:TIGR00618 832 QFLSRLEEKSATLGEITHQLLKYEEC----SKQLAQLTQEQAKIIQLSDKLNGINQikiQFDGDALIKF 896
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3123-3240 |
7.42e-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: 42.74 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3123 IKQFMSLFHEKRSDLEEEKIHLNIGLNKISETEEQVKELQKSLKLKSNElQEKKEAANLKLKEMLGDQQKAEEE-KKFSE 3201
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ-LEELEAQLEELESKLDELAEELAElEEKLE 347
|
90 100 110
....*....|....*....|....*....|....*....
gi 17506419 3202 QLQKELAEQLKQMAEKktfvENDLAQVEPAVAEAQTAVQ 3240
Cdd:TIGR02168 348 ELKEELESLEAELEEL----EAELEELESRLEELEEQLE 382
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
2533-2675 |
8.22e-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: 39.50 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 2533 LVLCGPPGSGKTMtLLAALRSQQEMEVVNVNFSSST------TPELLLRTFDHYCEyrrtpngvvLAPVqlsqwlVIFCD 2606
Cdd:pfam00004 1 LLLYGPPGTGKTT-LAKAVAKELGAPFIEISGSELVskyvgeSEKRLRELFEAAKK---------LAPC------VIFID 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17506419 2607 EINLPAPDKYG-----TQRVISFLrqLVELNGFyrTSDHSwvsleRIQFVGACN-PPT-DPgrhPMTSRFLRHVPI 2675
Cdd:pfam00004 65 EIDALAGSRGSggdseSRRVVNQL--LTELDGF--TSSNS-----KVIVIAATNrPDKlDP---ALLGRFDRIIEF 128
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3094-3406 |
9.39e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3094 HKTVQKFNEMETKKGHRVMACTPrhfldfikQFMSLFHEKRSDLEEEKIHLNIGLNKISETEEQVKELQKSLKLKSNELQ 3173
Cdd:TIGR00618 189 KKSLHGKAELLTLRSQLLTLCTP--------CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3174 EKK------------EAANLKLKEMLGDQQKAE---EEKKFSEQLQKELAEQLKQMAEKKTFVENDLAQVEPAVAEAQTA 3238
Cdd:TIGR00618 261 LLKqlrarieelraqEAVLEETQERINRARKAAplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3239 VQGIKKSQlvevksmssppvtvklTLEAICILLGE--NVGTDWKAIRQVMMKDDFMTRILQFDTelltpEILKQMEKYIQ 3316
Cdd:TIGR00618 341 EEQRRLLQ----------------TLHSQEIHIRDahEVATSIREISCQQHTLTQHIHTLQQQK-----TTLTQKLQSLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506419 3317 NpdwEFDKVNRASVACGPMVKWARAQLLYSTMLHKVEPLrnELKRLEQEAAKKTQEGKVVDVRITELEESIGKYKEEyAQ 3396
Cdd:TIGR00618 400 K---ELDILQREQATIDTRTSAFRDLQGQLAHAKKQQEL--QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER-EQ 473
|
330
....*....|
gi 17506419 3397 LIGQAENIKQ 3406
Cdd:TIGR00618 474 QLQTKEQIHL 483
|
|
| |
