|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1651-1986 |
2.83e-170 |
|
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: 527.82 E-value: 2.83e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1651 YTYEYQGNAPKLVYTPLTDKCYLTLTQAMKMGLGGNPYGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDVKSMGRIFVG 1730
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1731 LVKCGAWGCFDEFNRLEEAVLSAVSMQIQTIQDALKNHRSVCELLGKEVEINANSGIFITMNPagkGYGGRQKLPDNLKQ 1810
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNP---GYAGRTELPDNLKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1811 LFRPVAMSRPDNDLIAEVILYSEGFKDAKELGRKLVAIFNLSRELLTPQQHYDWGLRALKTVLRGSGNLLRQLkksgtkQ 1890
Cdd:pfam12774 158 LFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSN------P 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1891 DVNENHIVVQALRLNTMSKFTFADCTRFDALIKDVFPGIDFKEVEYNELSSALKQVFEEANYEVIPNQMKKALELYEQLR 1970
Cdd:pfam12774 232 NLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETML 311
|
330
....*....|....*.
gi 2007538485 1971 QRTGVVIVGPSGAGKS 1986
Cdd:pfam12774 312 VRHGVMLVGPTGSGKT 327
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1361-4015 |
2.44e-162 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 568.46 E-value: 2.44e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1361 LPKEQTRFNKVDEDFRsiMMDIRKDSRVTTLTT-HAGIRNTLLTILDQLQRCQKSLNEFLEEKRSAFPRFyfIGDDDLLE 1439
Cdd:COG5245 644 IPHAVHRKMSLVSGVR--GIYKRVVSGCEAINTiLEDVGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMD 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1440 ILGQSTNPSVIQSHLKKLFAGINSVCFDEEskHITAMRSLEGEVVPFKSKVLLSNNVEA--WLNDlalEMKQTLKQLLKE 1517
Cdd:COG5245 720 RVRELENRVYSYRFFVKKIAKEEMKTVFSS--RIQKKEPFSLDSEAYVGFFRLYEKSIVirGINR---SMGRVLSQYLES 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1518 CVTAGRSSQGAIDPSLFPSQILCLAEQiKFTEDVEDAIrdhslhqiEAQLAaklERYTSVDTSSEDPGNSESGILELKLK 1597
Cdd:COG5245 795 VQEALEIEDGSFFVSRHRVRDGGLEKG-RGCDAWENCF--------DPPLS---EYFRILEKIFPSEEGYFFDEVLKRLD 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1598 ALILDIIHNIDIVKQLNQAQVHTTDDWAWKKQVRFYMKSDHTCYVQMVDSELQYTYEYQGNAPKLVYTPLTDKCYLTLTQ 1677
Cdd:COG5245 863 PGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFE 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1678 AMKMGLGGNpygpAGTGKTESVKALGGLLGRQVlvfncdEGIDVKSmgRIFVGLVKCGAWGcFDEFNRLEEAVLsAVSMQ 1757
Cdd:COG5245 943 AVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR-TILVD 1008
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1758 IQTIQDALKNHRSVCELLGKEVEINANSGIFITMNPagkgyggRQKLPDNLKQLFRPVAMSRPDNdLIAEVilysegfkd 1837
Cdd:COG5245 1009 EYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE-------RNIVLEIGRRALDMFLSNIPFG-AIKSR--------- 1071
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1838 AKELGRKLVAIFNLSRELLTPQQHYDWglRALKTVLRGSGNLLRQlKKSGTKQdvnenhiVVQALRLNTMSkftfadctr 1917
Cdd:COG5245 1072 RESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRMLEE-KTEYLNK-------ILSITGLPLIS--------- 1132
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1918 fDALIKDvfpgIDFKEVEYNELSS-ALKQVFEEANyEVIPNQMKKALELYEQLRQRTGVVIVGPSGAGKSTLWRmlrAAL 1996
Cdd:COG5245 1133 -DTLRER----IDTLDAEWDSFCRiSESLKKYESQ-QVSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYT---DAC 1203
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1997 CKIGKVVKQYTMNPKAMPRHQLLGHIDMDTREWSDGVLTNSARQVVREpqdvsswiicdgdidpEWIESLNSVLDDNRLL 2076
Cdd:COG5245 1204 DYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSKMEYEVE----------------RYVEKTKAEVSSLKLE 1267
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2077 TMPSGERiqfgpnvNFVFETHDlscASPATISRMGMIFLSDEETDLNSLIKSWLRNQPVEYRSNLENWIGDYFSK----A 2152
Cdd:COG5245 1268 LSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRLSTKGVFLDELGDTKRYLDECLDFFSCFEEVQkeidE 1337
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2153 LQWVLKQNDYVVETSLVGTVmnGLSHLHGCKYHDQFIINLI---RGLGGNLNMKSRLEFTKEVFN----WA------RET 2219
Cdd:COG5245 1338 LSMVFCADALRFSADLYHIV--KERRFSGVLAGSDASESLGgksIELAAILEHKDLIVEMKRGINdvlkLRifgdkcRES 1415
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2220 PPDSHRPMDTYFDCDRGQLASY--VLKKPESLTADDFSSGhSLP---------------VIQTPDMQRGLDYFKPWLSse 2282
Cdd:COG5245 1416 TPRFYLISDGDLIKDLNERSDYeeMLIMMFNISAVITNNG-SIAgfelrgervmlrkevVIPTSDTGFVDSFSNEALN-- 1492
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2283 TKQPFILVGPEGCGKGMLLRYAFSQLRSTEIATIHCSAQTTSRHLLQKLSQTcMVISTNTG--RVYRPKDCERLVLYLKD 2360
Cdd:COG5245 1493 TLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERE-TEYYPNTGvvRLYPKPVVKDLVLFCDE 1571
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2361 INLPKLDKWGTSTLVAFLQQVLTYQGFYDE-NLEWVGLENIQIVASMSAGGRLGRHKLTTRFTSIVRLCAVDYPEREQLQ 2439
Cdd:COG5245 1572 INLPYGFEYYPPTVIVFLRPLVERQGFWSSiAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLR 1651
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2440 TIYGAYLEAVLHKNLKNHSIwgssskIYLLAGSMVQVYEQVRAKFTVDDYSHYFFTPCILTQWVLGLFRYDLEGgsSNHP 2519
Cdd:COG5245 1652 NIYEAVLMGSYLCFDEFNRL------SEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETR--IDTP 1723
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2520 LDYVLEIVAYEARRLFRDKIVGVKElhlfdniltsvlqGDWGSDILDNMADSFYVTWGAQHISGAKIAPGQPLPPHGKPL 2599
Cdd:COG5245 1724 DVSLIIDWYCEAIREKIDRLVQQKE-------------SSTSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFGMACL 1790
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2600 GKlssADLKDVIKKGLIHYGRDNQNLDILLFQEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTVTSLVSHMHGAVLFSP 2679
Cdd:COG5245 1791 LK---KDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREI 1867
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2680 KISRGYEPKQFRTDLKHVLHLAGIEAQQVVLLLEDYQFVHPTFLEMINSLLSSGEVPGLYTLEELEPLLLPLKDQASQDG 2759
Cdd:COG5245 1868 FGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTS 1947
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2760 FF----GPVFNYFTYRIQQNLHIVL-IMDSANLNFIINCESnPALHKKCQVLWMEGWSDSSMKKIPEMLFSEA--DIEEK 2832
Cdd:COG5245 1948 LEkdteATLTRVFLVYMEENLPVVFsACCSQDTSVLAGIRS-PALKNRCFIDFKKLWDTEEMSQYANSVETLSrdGGRVF 2026
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2833 YEKKRKDEKKKSSVDPDFIKSFLLIHES-------CKAYGATPSRYMTFLRVYSAISSSKRKELLKRQSHLQAGVSKLNE 2905
Cdd:COG5245 2027 FINGELGVGKGALISEVFGDDAVVIEGRgfeismiEGSLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNE 2106
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2906 AKALVDELNRKAGEQSILLRIKQDEADSALQEITVSMQDASEQKTELERLKHRIAEEVVKIEERKSKIDDELKEVQPLVN 2985
Cdd:COG5245 2107 YGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVL 2186
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2986 EAKLAVGNIRPESLSEIRSLRMPPDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVREDIATFD-ARNIPKEIRESVEE 3064
Cdd:COG5245 2187 EAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPdEIEFDLEARRFREA 2266
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3065 LLFKNkASFDPKNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELK 3144
Cdd:COG5245 2267 RECSD-PSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRR 2345
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3145 EKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLPKRAQLAAAFITYLSAAPEGLR--- 3221
Cdd:COG5245 2346 SYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRaie 2425
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3222 KNCLEEWTKAAGLEKFDLRRFLCTESEQLIWKSEGLP-SDDLSIENALVILQSR-VCPFLIDPSSQATEWLKTHLKDSHL 3299
Cdd:COG5245 2426 FGMSFIRISKEFRDKEIRRRQFITEGVQKIEDFKEEAcSTDYGLENSRIRKDLQdLTAVLNDPSSKIVTSQRQMYDEKKA 2505
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3300 EVINQQDSNFITALELAVRFGKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEDFRLFLSTRNPNPFIP 3379
Cdd:COG5245 2506 ILGSFREMEFAFGLSQARREGSDKIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMG 2585
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3380 PDAASIVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLARLEESLLETLATSQGNILENKDLIES 3459
Cdd:COG5245 2586 SIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVL 2665
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3460 LNQTKASSALIQDSLKESYKLQISLDQERDAYLPLAESASKMYFIISDLSKINNMYRFSLASFLRLFQRALQNKqdseST 3539
Cdd:COG5245 2666 LHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWRRMK----SK 2741
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3540 EQR-IQCLVNSLKHMVYEYIcRCLF----------KADQLMFALHFVRGMHPEFfqENEWDTFTGVVVgdmlrkaDSQQR 3608
Cdd:COG5245 2742 YLCaIRYMLMSSEWILDHED-RSGFihrldvsfllRTKRFVSTLLEDKNYRQVL--SSCSLYGNDVIS-------HSCDR 2811
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3609 I-RDQLPSWIDQERSWAVATLKislpgLYQTLCFEDGTlwRTYYH--HSMCEQEFPSILAKkvslFQQvlvvqalrpdrl 3685
Cdd:COG5245 2812 FdRDVYRALKHQMDNRTHSTIL-----TSNSKTNPYKE--YTYNDswAEAFEVEDSGDLYK----FEE------------ 2868
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3686 qsamalfackalGLKELSPLPLNLKRLYKETLEIEPIliiispgadpsqeLQELANAERSSecyhqvamgqgqadLAIQM 3765
Cdd:COG5245 2869 ------------GLLELIVGHAPLIYAHKKSLENERN-------------VDRLGSKENEV--------------YAVLN 2909
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3766 LKECARNGDWLCLKNLHLVVSWL-----PVLEKELNTLQPKESFRLWLTAEVHPNFTPILLQSSLKITYESPPGLKKNLM 3840
Cdd:COG5245 2910 SLFSRKEKSWFEVYNISLSFGWFkryveDVVYPIKASRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYA 2989
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3841 RTYES-WTPEQISKkdnIHRAHALFSLAWFHAACQERRNFIPQGWTKFYEFSLSDLRAGYHVIDR-LFDGSKD-VQWEFV 3917
Cdd:COG5245 2990 DLVEIdRYPFDYTL---VIACDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNiLFLNHLNaRKWGNN 3066
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3918 HGLLENSIYGGRIDNYFDLRVLQSYLKQFF----NSSIID--VLNQRNKKSIFPYSISLpnscsiLDYRAVIEKLPEDDK 3991
Cdd:COG5245 3067 RDLIFTIVYGKKHSLMEDSKVVDKYCRGYGahetSSQILAsvPGGDPELVKFHMEEMCR------SSAFGVIGQLPDLAL 3140
|
2730 2740
....*....|....*....|....
gi 2007538485 3992 PSFFGLPANIARSSQRMTSSQVIS 4015
Cdd:COG5245 3141 CAWLMGPCDSEYLKAIVYSSRIDM 3164
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1120-1518 |
2.02e-126 |
|
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: 405.10 E-value: 2.02e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1120 ISKDIESCAQIWALYEEFQQGLQEMAKEDWITyrTKIYIFEEFLINWHERLRKVE---EHSVMTVKLQSEVDRYKIIIPI 1196
Cdd:pfam08393 4 IKKELEPLKKLWDLVSEWQESLEEWKNGPFSD--LDVEELEEELEEFLKELKKLPkelRDWDVAEELKKKIDDFKKSLPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1197 LKYVRGEHLSPDHWLDLFRLLGLPRGTSLEKLLFGDLLRVadTIVEKASDLKDLNSRAQGEVTIREALRELDLWGVGAVF 1276
Cdd:pfam08393 82 IEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDL--NLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1277 SLIDYEDsqnRTIKLIKDWKDIVNQVGDNRCLLQSLKDSPYYKGFEDKVSIWERKLAQLDEYLQNLNHIQRKWVYLEPIF 1356
Cdd:pfam08393 160 ELVPYKD---TGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1357 G----RGALPKEQTRFNKVDEDFRSIMMDIRKDSRVTTLTTHAGIRNTLLTILDQLQRCQKSLNEFLEEKRSAFPRFYFI 1432
Cdd:pfam08393 237 SsediRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1433 GDDDLLEILGQSTNPSVIQSHLKKLFAGINSVCFDeESKHITAMRSLEGEVVPF-KSKVLLSNNVEAWLNDLALEMKQTL 1511
Cdd:pfam08393 317 SNDELLEILSQTKDPTRVQPHLKKCFEGIASLEFD-ENKEITGMISKEGEVVPFsKPPVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 2007538485 1512 KQLLKEC 1518
Cdd:pfam08393 396 RDLLKEA 402
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3252-3470 |
1.28e-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: 311.68 E-value: 1.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3252 WKSEGLPSDDLSIENALVILQSRVCPFLIDPSSQATEWLKTHLKDSHLEVINQQDSNFITALELAVRFGKTLIIQEM-DG 3330
Cdd:pfam12781 3 WNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVgEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3331 VEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEDFRLFLSTRNPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHE 3410
Cdd:pfam12781 83 LDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVKKE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3411 KPDLEEQKTKLLQQEEDKKIQLARLEESLLETLATSQGNILENKDLIESLNQTKASSALI 3470
Cdd:pfam12781 163 RPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4007-4303 |
6.71e-54 |
|
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: 192.45 E-value: 6.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 4007 RMTSSQVISQLRILGRSVTAGCKFDREiwSNElSPVLNLWKKLNQ---NSNLIHQKVSPPNDRQGSPILSFIILEQFNAI 4083
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGGS--SRE-EIVLELAKDILEklpEPFDIEEAEEKYPVGYEDPLNTVLLQEIERFN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 4084 RLVQSVHQSLAALSKVIRGTTLLSSEVQKLASALLNQKCPLTWQSKWEGPEDPL-QYLRGLVARTLAIQNWVEKAEKQAl 4162
Cdd:pfam18199 78 KLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLgSWIRDLLERLKQLQDWLDDEGPPK- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 4163 ladTLDLSELFHPDTFLNALRQETARATGCSVDSLKFVASWKGRLQEAKLQIK------ISGLLLEGCSFDGSR--LSEn 4234
Cdd:pfam18199 157 ---VFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSPEEVTEPpedgvyVHGLFLEGARWDRKNgcLVE- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2007538485 4235 QHDSPSVSSVLPCYMgwTPQGSYGPYSPDECISLPVYTSAERDC--VVTNIDVPCGGNQDQWIQCGAALFL 4303
Cdd:pfam18199 233 SEPKELFSPLPVIHL--KPVESDKKKLDENTYECPVYKTSERHStnFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
161-674 |
5.94e-23 |
|
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: 106.89 E-value: 5.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 161 LKEDDTRGILTPSDEFQFWIEQA--------HRGSKQISK-----ERA--SY---FKELFE-----------------TI 205
Cdd:pfam08385 19 LKEDSQGRNPGPLAEIEFWKSREanlssiyeQLKSPEVKKvleilEAAksSYlpaFKALDTeltdalneakdnvkylkTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 206 AREFYNLDSL-SLLEVVDLVETTRDVVDDVWRQTEHdhYPES-RMLHLLDVIGGSFGRFVQKKLGSLKLWEDPYYLVKEN 283
Cdd:pfam08385 99 ERPFEDLEELtDPPEIIEAIPPLMNTIRLIWSISRY--YNTSeRMTVLLEKISNQLIEQCKKYLSPEGIFDGDVEEALEK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 284 LKAGISICEQWVIVCSHLTGQVWQRYVPHPWK-SEKYFPETLDRLGKRLEEVLAIRTIHEKLLYFLPASEERIVCLSRVF 362
Cdd:pfam08385 177 LQECIELLEAWKEEYKKTREKLEESPRERPWDfSERYIFGRFDAFLERLEKILELFETIEQFSKLEKIGGTKGPELEGVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 363 EP--------FTGVNPVQYNP--YTEPLWKAAVSQYEKIIAPAEQKIAGKLKNYISEIQdSPQQLLQAFLKYKELVKRPT 432
Cdd:pfam08385 257 EEileefqeaYKVFKSKTYDIldVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDDAR-STESAFKLLRIFEFLLERPI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 433 ISKELMLERETLLARLGDSAKDFRLDFENrcrgipGDASGPLSGKNLSEVVNNIVWVRQLELKVDDTIKIAEALLSDLSg 512
Cdd:pfam08385 336 IRGALEEKYTDLLQMFKKELDAVKKIFDK------QKYNPSPIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLLK- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 513 frsfHRSAEDLLDQF-------KLYEQEQFDDWSREVqsglsDSRSGLCIEANsrIMELDPNDGAL-KVHYSDRLVILLR 584
Cdd:pfam08385 409 ----HAEGKKVIKKYnelakklDEYERLIYEAWLKEV-----EEASEGNLKRP--LLVRHPETGKLlSVNFDPQLLALLR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 585 EVRQLSALGFVIPAKIQQVANVAQKFCKQAIILKQVAHFYNSIDQQMIQSQRPMMLQSALAFEQIIKNskagsgGKSQIT 664
Cdd:pfam08385 478 EVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEP------GLTTLT 551
|
570
....*....|
gi 2007538485 665 WDNpKELEGY 674
Cdd:pfam08385 552 WNS-LGIDEY 560
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2885-3237 |
7.45e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2885 KRKELLKRQSHLQAGVSKLNEAKALVDELNRkageqsillrIKQDEADSALQEITVSMQDASEQKTELErlkhriaEEVV 2964
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKEELER----------LKKRLTGLTPEKLEKELEELEKAKEEIE-------EEIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2965 KIEERKSKIDDELKEVQPLVNEAKLAVG---------------NIRPESLSEIRSLRMPPDVIRDILEGVLRLMgifdts 3029
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKEL------ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3030 wVSMKSFLAKRgvREDIATfdaRNIPKEIRESVEELlfknkASFDPKNAKrastaaaplaawvKANVQYSHVLERIQPLE 3109
Cdd:PRK03918 483 -RELEKVLKKE--SELIKL---KELAEQLKELEEKL-----KKYNLEELE-------------KKAEEYEKLKEKLIKLK 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3110 TEQSGLELNLKKTEDRKRKLEdllnsvgqkvsELKEKFQSRTSEAAKLEAEVSK-AQETIKAAEVLISQLDREHRRWNA- 3187
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLA-----------ELEKKLDELEEELAELLKELEElGFESVEELEERLKELEPFYNEYLEl 607
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2007538485 3188 -----QVAEIAEELATLPKRAQLAAAFITYLSAAPEGLRKNcLEEWTKAAGLEKF 3237
Cdd:PRK03918 608 kdaekELEREEKELKKLEEELDKAFEELAETEKRLEELRKE-LEELEKKYSEEEY 661
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2883-3223 |
1.17e-06 |
|
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: 55.07 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2883 SSKRKELLKRQSHLQAGVSKLNEAKALVDELNRK-----AGEQsilLRIKQDEAD-SALQEITVSMQDASEQktELERLK 2956
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgEEEQ---LRVKEKIGElEAEIASLERSIAEKER--ELEDAE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2957 HRIAEEVVKIEERKSKIDDELKEVQPLvneaklavgNIRPESLSEIrslrmppdvirdilegvlrlmgifdtswvsmksF 3036
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEE---------RKRRDKLTEE---------------------------------Y 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3037 LAKRGVREDIATfDARNIPKEIRESVEELlfknkasfdpknakrastaaaplaawVKANVQYSHVLERIQPLETEQSGLE 3116
Cdd:TIGR02169 360 AELKEELEDLRA-ELEEVDKEFAETRDEL--------------------------KDYREKLEKLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3117 LNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEEL 3196
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
330 340
....*....|....*....|....*..
gi 2007538485 3197 ATLPKRAQLAAAFITYLSAAPEGLRKN 3223
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLKAS 519
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
1942-1988 |
1.98e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 42.77 E-value: 1.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1942 ALKQVFEEANYEVIPNQMKKAL---ELYEQLRQRTgVVIVGPSGAGKSTL 1988
Cdd:cd01854 53 ELLEIYEKLGYPVLAVSAKTGEgldELRELLKGKT-SVLVGQSGVGKSTL 101
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1944-1996 |
5.16e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.48 E-value: 5.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2007538485 1944 KQVFEEANYEVIPNQMkkalelyeqlrqrtgVVIVGPSGAGKSTLWRMLRAAL 1996
Cdd:COG2401 43 RYVLRDLNLEIEPGEI---------------VLIVGASGSGKSTLLRLLAGAL 80
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1651-1986 |
2.83e-170 |
|
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: 527.82 E-value: 2.83e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1651 YTYEYQGNAPKLVYTPLTDKCYLTLTQAMKMGLGGNPYGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDVKSMGRIFVG 1730
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1731 LVKCGAWGCFDEFNRLEEAVLSAVSMQIQTIQDALKNHRSVCELLGKEVEINANSGIFITMNPagkGYGGRQKLPDNLKQ 1810
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNP---GYAGRTELPDNLKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1811 LFRPVAMSRPDNDLIAEVILYSEGFKDAKELGRKLVAIFNLSRELLTPQQHYDWGLRALKTVLRGSGNLLRQLkksgtkQ 1890
Cdd:pfam12774 158 LFRPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSN------P 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1891 DVNENHIVVQALRLNTMSKFTFADCTRFDALIKDVFPGIDFKEVEYNELSSALKQVFEEANYEVIPNQMKKALELYEQLR 1970
Cdd:pfam12774 232 NLNEDVLLLRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETML 311
|
330
....*....|....*.
gi 2007538485 1971 QRTGVVIVGPSGAGKS 1986
Cdd:pfam12774 312 VRHGVMLVGPTGSGKT 327
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1361-4015 |
2.44e-162 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 568.46 E-value: 2.44e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1361 LPKEQTRFNKVDEDFRsiMMDIRKDSRVTTLTT-HAGIRNTLLTILDQLQRCQKSLNEFLEEKRSAFPRFyfIGDDDLLE 1439
Cdd:COG5245 644 IPHAVHRKMSLVSGVR--GIYKRVVSGCEAINTiLEDVGDDLDLFYKEMDQVFMSIEKVLGLRWREVERA--SEVEELMD 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1440 ILGQSTNPSVIQSHLKKLFAGINSVCFDEEskHITAMRSLEGEVVPFKSKVLLSNNVEA--WLNDlalEMKQTLKQLLKE 1517
Cdd:COG5245 720 RVRELENRVYSYRFFVKKIAKEEMKTVFSS--RIQKKEPFSLDSEAYVGFFRLYEKSIVirGINR---SMGRVLSQYLES 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1518 CVTAGRSSQGAIDPSLFPSQILCLAEQiKFTEDVEDAIrdhslhqiEAQLAaklERYTSVDTSSEDPGNSESGILELKLK 1597
Cdd:COG5245 795 VQEALEIEDGSFFVSRHRVRDGGLEKG-RGCDAWENCF--------DPPLS---EYFRILEKIFPSEEGYFFDEVLKRLD 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1598 ALILDIIHNIDIVKQLNQAQVHTTDDWAWKKQVRFYMKSDHTCYVQMVDSELQYTYEYQGNAPKLVYTPLTDKCYLTLTQ 1677
Cdd:COG5245 863 PGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFE 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1678 AMKMGLGGNpygpAGTGKTESVKALGGLLGRQVlvfncdEGIDVKSmgRIFVGLVKCGAWGcFDEFNRLEEAVLsAVSMQ 1757
Cdd:COG5245 943 AVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISR-TILVD 1008
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1758 IQTIQDALKNHRSVCELLGKEVEINANSGIFITMNPagkgyggRQKLPDNLKQLFRPVAMSRPDNdLIAEVilysegfkd 1837
Cdd:COG5245 1009 EYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE-------RNIVLEIGRRALDMFLSNIPFG-AIKSR--------- 1071
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1838 AKELGRKLVAIFNLSRELLTPQQHYDWglRALKTVLRGSGNLLRQlKKSGTKQdvnenhiVVQALRLNTMSkftfadctr 1917
Cdd:COG5245 1072 RESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRMLEE-KTEYLNK-------ILSITGLPLIS--------- 1132
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1918 fDALIKDvfpgIDFKEVEYNELSS-ALKQVFEEANyEVIPNQMKKALELYEQLRQRTGVVIVGPSGAGKSTLWRmlrAAL 1996
Cdd:COG5245 1133 -DTLRER----IDTLDAEWDSFCRiSESLKKYESQ-QVSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHYT---DAC 1203
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1997 CKIGKVVKQYTMNPKAMPRHQLLGHIDMDTREWSDGVLTNSARQVVREpqdvsswiicdgdidpEWIESLNSVLDDNRLL 2076
Cdd:COG5245 1204 DYLWHVKSPYVKKKYFDADMELRQFFLMFNREDMEARLADSKMEYEVE----------------RYVEKTKAEVSSLKLE 1267
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2077 TMPSGERiqfgpnvNFVFETHDlscASPATISRMGMIFLSDEETDLNSLIKSWLRNQPVEYRSNLENWIGDYFSK----A 2152
Cdd:COG5245 1268 LSSVGEG-------QVVVSNLG---SIGDKVGRCLVEYDSISRLSTKGVFLDELGDTKRYLDECLDFFSCFEEVQkeidE 1337
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2153 LQWVLKQNDYVVETSLVGTVmnGLSHLHGCKYHDQFIINLI---RGLGGNLNMKSRLEFTKEVFN----WA------RET 2219
Cdd:COG5245 1338 LSMVFCADALRFSADLYHIV--KERRFSGVLAGSDASESLGgksIELAAILEHKDLIVEMKRGINdvlkLRifgdkcRES 1415
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2220 PPDSHRPMDTYFDCDRGQLASY--VLKKPESLTADDFSSGhSLP---------------VIQTPDMQRGLDYFKPWLSse 2282
Cdd:COG5245 1416 TPRFYLISDGDLIKDLNERSDYeeMLIMMFNISAVITNNG-SIAgfelrgervmlrkevVIPTSDTGFVDSFSNEALN-- 1492
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2283 TKQPFILVGPEGCGKGMLLRYAFSQLRSTEIATIHCSAQTTSRHLLQKLSQTcMVISTNTG--RVYRPKDCERLVLYLKD 2360
Cdd:COG5245 1493 TLRSYIYCGPPGSGKEMLMCPSLRSELITEVKYFNFSTCTMTPSKLSVLERE-TEYYPNTGvvRLYPKPVVKDLVLFCDE 1571
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2361 INLPKLDKWGTSTLVAFLQQVLTYQGFYDE-NLEWVGLENIQIVASMSAGGRLGRHKLTTRFTSIVRLCAVDYPEREQLQ 2439
Cdd:COG5245 1572 INLPYGFEYYPPTVIVFLRPLVERQGFWSSiAVSWVTICGIILYGACNPGTDEGRVKYYERFIRKPVFVFCCYPELASLR 1651
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2440 TIYGAYLEAVLHKNLKNHSIwgssskIYLLAGSMVQVYEQVRAKFTVDDYSHYFFTPCILTQWVLGLFRYDLEGgsSNHP 2519
Cdd:COG5245 1652 NIYEAVLMGSYLCFDEFNRL------SEETMSASVELYLSSKDKTKFFLQMNYGYKPRELTRSLRAIFGYAETR--IDTP 1723
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2520 LDYVLEIVAYEARRLFRDKIVGVKElhlfdniltsvlqGDWGSDILDNMADSFYVTWGAQHISGAKIAPGQPLPPHGKPL 2599
Cdd:COG5245 1724 DVSLIIDWYCEAIREKIDRLVQQKE-------------SSTSRQDLYDFGLRAIREMIAGHIGEAEITFSMILFFGMACL 1790
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2600 GKlssADLKDVIKKGLIHYGRDNQNLDILLFQEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTVTSLVSHMHGAVLFSP 2679
Cdd:COG5245 1791 LK---KDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREI 1867
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2680 KISRGYEPKQFRTDLKHVLHLAGIEAQQVVLLLEDYQFVHPTFLEMINSLLSSGEVPGLYTLEELEPLLLPLKDQASQDG 2759
Cdd:COG5245 1868 FGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTS 1947
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2760 FF----GPVFNYFTYRIQQNLHIVL-IMDSANLNFIINCESnPALHKKCQVLWMEGWSDSSMKKIPEMLFSEA--DIEEK 2832
Cdd:COG5245 1948 LEkdteATLTRVFLVYMEENLPVVFsACCSQDTSVLAGIRS-PALKNRCFIDFKKLWDTEEMSQYANSVETLSrdGGRVF 2026
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2833 YEKKRKDEKKKSSVDPDFIKSFLLIHES-------CKAYGATPSRYMTFLRVYSAISSSKRKELLKRQSHLQAGVSKLNE 2905
Cdd:COG5245 2027 FINGELGVGKGALISEVFGDDAVVIEGRgfeismiEGSLGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNE 2106
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2906 AKALVDELNRKAGEQSILLRIKQDEADSALQEITVSMQDASEQKTELERLKHRIAEEVVKIEERKSKIDDELKEVQPLVN 2985
Cdd:COG5245 2107 YGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVL 2186
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2986 EAKLAVGNIRPESLSEIRSLRMPPDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVREDIATFD-ARNIPKEIRESVEE 3064
Cdd:COG5245 2187 EAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAKIWFGEQQSLRRDDFIRIIGKYPdEIEFDLEARRFREA 2266
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3065 LLFKNkASFDPKNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELK 3144
Cdd:COG5245 2267 RECSD-PSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRR 2345
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3145 EKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLPKRAQLAAAFITYLSAAPEGLR--- 3221
Cdd:COG5245 2346 SYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRaie 2425
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3222 KNCLEEWTKAAGLEKFDLRRFLCTESEQLIWKSEGLP-SDDLSIENALVILQSR-VCPFLIDPSSQATEWLKTHLKDSHL 3299
Cdd:COG5245 2426 FGMSFIRISKEFRDKEIRRRQFITEGVQKIEDFKEEAcSTDYGLENSRIRKDLQdLTAVLNDPSSKIVTSQRQMYDEKKA 2505
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3300 EVINQQDSNFITALELAVRFGKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEDFRLFLSTRNPNPFIP 3379
Cdd:COG5245 2506 ILGSFREMEFAFGLSQARREGSDKIIGDAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMG 2585
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3380 PDAASIVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLARLEESLLETLATSQGNILENKDLIES 3459
Cdd:COG5245 2586 SIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVL 2665
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3460 LNQTKASSALIQDSLKESYKLQISLDQERDAYLPLAESASKMYFIISDLSKINNMYRFSLASFLRLFQRALQNKqdseST 3539
Cdd:COG5245 2666 LHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFEKWRRMK----SK 2741
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3540 EQR-IQCLVNSLKHMVYEYIcRCLF----------KADQLMFALHFVRGMHPEFfqENEWDTFTGVVVgdmlrkaDSQQR 3608
Cdd:COG5245 2742 YLCaIRYMLMSSEWILDHED-RSGFihrldvsfllRTKRFVSTLLEDKNYRQVL--SSCSLYGNDVIS-------HSCDR 2811
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3609 I-RDQLPSWIDQERSWAVATLKislpgLYQTLCFEDGTlwRTYYH--HSMCEQEFPSILAKkvslFQQvlvvqalrpdrl 3685
Cdd:COG5245 2812 FdRDVYRALKHQMDNRTHSTIL-----TSNSKTNPYKE--YTYNDswAEAFEVEDSGDLYK----FEE------------ 2868
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3686 qsamalfackalGLKELSPLPLNLKRLYKETLEIEPIliiispgadpsqeLQELANAERSSecyhqvamgqgqadLAIQM 3765
Cdd:COG5245 2869 ------------GLLELIVGHAPLIYAHKKSLENERN-------------VDRLGSKENEV--------------YAVLN 2909
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3766 LKECARNGDWLCLKNLHLVVSWL-----PVLEKELNTLQPKESFRLWLTAEVHPNFTPILLQSSLKITYESPPGLKKNLM 3840
Cdd:COG5245 2910 SLFSRKEKSWFEVYNISLSFGWFkryveDVVYPIKASRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYA 2989
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3841 RTYES-WTPEQISKkdnIHRAHALFSLAWFHAACQERRNFIPQGWTKFYEFSLSDLRAGYHVIDR-LFDGSKD-VQWEFV 3917
Cdd:COG5245 2990 DLVEIdRYPFDYTL---VIACDDAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNiLFLNHLNaRKWGNN 3066
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3918 HGLLENSIYGGRIDNYFDLRVLQSYLKQFF----NSSIID--VLNQRNKKSIFPYSISLpnscsiLDYRAVIEKLPEDDK 3991
Cdd:COG5245 3067 RDLIFTIVYGKKHSLMEDSKVVDKYCRGYGahetSSQILAsvPGGDPELVKFHMEEMCR------SSAFGVIGQLPDLAL 3140
|
2730 2740
....*....|....*....|....
gi 2007538485 3992 PSFFGLPANIARSSQRMTSSQVIS 4015
Cdd:COG5245 3141 CAWLMGPCDSEYLKAIVYSSRIDM 3164
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1120-1518 |
2.02e-126 |
|
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: 405.10 E-value: 2.02e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1120 ISKDIESCAQIWALYEEFQQGLQEMAKEDWITyrTKIYIFEEFLINWHERLRKVE---EHSVMTVKLQSEVDRYKIIIPI 1196
Cdd:pfam08393 4 IKKELEPLKKLWDLVSEWQESLEEWKNGPFSD--LDVEELEEELEEFLKELKKLPkelRDWDVAEELKKKIDDFKKSLPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1197 LKYVRGEHLSPDHWLDLFRLLGLPRGTSLEKLLFGDLLRVadTIVEKASDLKDLNSRAQGEVTIREALRELDLWGVGAVF 1276
Cdd:pfam08393 82 IEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDL--NLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1277 SLIDYEDsqnRTIKLIKDWKDIVNQVGDNRCLLQSLKDSPYYKGFEDKVSIWERKLAQLDEYLQNLNHIQRKWVYLEPIF 1356
Cdd:pfam08393 160 ELVPYKD---TGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1357 G----RGALPKEQTRFNKVDEDFRSIMMDIRKDSRVTTLTTHAGIRNTLLTILDQLQRCQKSLNEFLEEKRSAFPRFYFI 1432
Cdd:pfam08393 237 SsediRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1433 GDDDLLEILGQSTNPSVIQSHLKKLFAGINSVCFDeESKHITAMRSLEGEVVPF-KSKVLLSNNVEAWLNDLALEMKQTL 1511
Cdd:pfam08393 317 SNDELLEILSQTKDPTRVQPHLKKCFEGIASLEFD-ENKEITGMISKEGEVVPFsKPPVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 2007538485 1512 KQLLKEC 1518
Cdd:pfam08393 396 RDLLKEA 402
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3252-3470 |
1.28e-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: 311.68 E-value: 1.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3252 WKSEGLPSDDLSIENALVILQSRVCPFLIDPSSQATEWLKTHLKDSHLEVINQQDSNFITALELAVRFGKTLIIQEM-DG 3330
Cdd:pfam12781 3 WNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVgEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3331 VEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNEDFRLFLSTRNPNPFIPPDAASIVTEVNFTTTRSGLRGQLLALTIQHE 3410
Cdd:pfam12781 83 LDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVKKE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3411 KPDLEEQKTKLLQQEEDKKIQLARLEESLLETLATSQGNILENKDLIESLNQTKASSALI 3470
Cdd:pfam12781 163 RPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4007-4303 |
6.71e-54 |
|
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: 192.45 E-value: 6.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 4007 RMTSSQVISQLRILGRSVTAGCKFDREiwSNElSPVLNLWKKLNQ---NSNLIHQKVSPPNDRQGSPILSFIILEQFNAI 4083
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGGS--SRE-EIVLELAKDILEklpEPFDIEEAEEKYPVGYEDPLNTVLLQEIERFN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 4084 RLVQSVHQSLAALSKVIRGTTLLSSEVQKLASALLNQKCPLTWQSKWEGPEDPL-QYLRGLVARTLAIQNWVEKAEKQAl 4162
Cdd:pfam18199 78 KLLKVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLgSWIRDLLERLKQLQDWLDDEGPPK- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 4163 ladTLDLSELFHPDTFLNALRQETARATGCSVDSLKFVASWKGRLQEAKLQIK------ISGLLLEGCSFDGSR--LSEn 4234
Cdd:pfam18199 157 ---VFWLSGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKVSPEEVTEPpedgvyVHGLFLEGARWDRKNgcLVE- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2007538485 4235 QHDSPSVSSVLPCYMgwTPQGSYGPYSPDECISLPVYTSAERDC--VVTNIDVPCGGNQDQWIQCGAALFL 4303
Cdd:pfam18199 233 SEPKELFSPLPVIHL--KPVESDKKKLDENTYECPVYKTSERHStnFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
3863-4001 |
3.51e-50 |
|
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: 175.34 E-value: 3.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3863 LFSLAWFHAACQERRNFIPQGWTKFYEFSLSDLRAGYHVIDRLFDGSKD-VQWEFVHGLLENSIYGGRIDNYFDLRVLQS 3941
Cdd:pfam18198 5 LFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYDEkIPWDALRYLIGEINYGGRVTDDWDRRLLNT 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3942 YLKQFFNSSIIDvlnqrNKKSIFPYSISLPNSCSILDYRAVIEKLPEDDKPSFFGLPANI 4001
Cdd:pfam18198 85 YLEEFFNPEVLE-----EDFKFSPSLYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2625-2811 |
1.15e-43 |
|
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: 161.24 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2625 LDILLFQEVLEYMSRIDRVLSFPGGSLLLAGRSGVGRRTVTSLVSHMHGAVLFSPKISRGYEPKQFRTDLKHVLHLAGIE 2704
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2705 AQQVVLLLEDYQFVHPTFLEMINSLLSSGEVPGLYTLEELEPLLLPLKDQASQDGFFGP---VFNYFTYRIQQNLHIVLI 2781
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSreaVYNYFVKRCRNNLHIVLC 160
|
170 180 190
....*....|....*....|....*....|
gi 2007538485 2782 MDSANLNFIINCESNPALHKKCQVLWMEGW 2811
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEW 190
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
3729-3828 |
1.26e-39 |
|
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: 144.12 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3729 GADPSQELQELANAERSSECYHQVAMGQGQADLAIQMLKECARNGDWLCLKNLHLVVSWLPVLEKELNTLQPK---ESFR 3805
Cdd:pfam03028 13 GSDPTADLEKLAKKLGFGGKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILEELPEEtlhPDFR 92
|
90 100
....*....|....*....|...
gi 2007538485 3806 LWLTAEVHPNFTPILLQSSLKIT 3828
Cdd:pfam03028 93 LWLTSEPSPKFPISILQNSIKIT 115
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1974-2110 |
9.10e-30 |
|
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: 117.01 E-value: 9.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1974 GVVIVGPSGAGKSTLWRMLRAALCKigkVVKQYTMNPKAMPRHQLLGHIDMDTR--EWSDGVLTNSARqvvrepqdvSSW 2051
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSN---RPVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAAR---------EGE 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2007538485 2052 IICDGDID---PEWIESLNSVLDDNRLLTMPSGERIQFGP-NVNFVFETHDL----SCASPATISRM 2110
Cdd:pfam07728 69 IAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMNPLdrglNELSPALRSRF 135
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
2896-3228 |
8.26e-26 |
|
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: 112.09 E-value: 8.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2896 LQAGVSKLNEAKALVDELNRKAGEQSILLRIKQDEADSALQEITVSMQDASEQKTELERLKHRIAEEVVKIEERKSKIDD 2975
Cdd:pfam12777 3 LENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2976 ELKEVQPLVNEAKLAVGNIRPESLSEIRSLRMPPDVIRDILEGVLRLMGIF-----DTSWVSMKSFLAK-RGVREDIATF 3049
Cdd:pfam12777 83 DLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGgkipkDKSWKAAKIMMAKvDGFLDSLIKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3050 DARNIPKEIRESVEEllFKNKASFDPKNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKL 3129
Cdd:pfam12777 163 DKEHIHEACLKAFKP--YLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3130 EDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLPKRAQLAAAF 3209
Cdd:pfam12777 241 KAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISAF 320
|
330 340
....*....|....*....|
gi 2007538485 3210 ITYLSAAPEGLRKNCLEE-W 3228
Cdd:pfam12777 321 ISYLGFFTKKYRNELLDKfW 340
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
161-674 |
5.94e-23 |
|
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: 106.89 E-value: 5.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 161 LKEDDTRGILTPSDEFQFWIEQA--------HRGSKQISK-----ERA--SY---FKELFE-----------------TI 205
Cdd:pfam08385 19 LKEDSQGRNPGPLAEIEFWKSREanlssiyeQLKSPEVKKvleilEAAksSYlpaFKALDTeltdalneakdnvkylkTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 206 AREFYNLDSL-SLLEVVDLVETTRDVVDDVWRQTEHdhYPES-RMLHLLDVIGGSFGRFVQKKLGSLKLWEDPYYLVKEN 283
Cdd:pfam08385 99 ERPFEDLEELtDPPEIIEAIPPLMNTIRLIWSISRY--YNTSeRMTVLLEKISNQLIEQCKKYLSPEGIFDGDVEEALEK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 284 LKAGISICEQWVIVCSHLTGQVWQRYVPHPWK-SEKYFPETLDRLGKRLEEVLAIRTIHEKLLYFLPASEERIVCLSRVF 362
Cdd:pfam08385 177 LQECIELLEAWKEEYKKTREKLEESPRERPWDfSERYIFGRFDAFLERLEKILELFETIEQFSKLEKIGGTKGPELEGVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 363 EP--------FTGVNPVQYNP--YTEPLWKAAVSQYEKIIAPAEQKIAGKLKNYISEIQdSPQQLLQAFLKYKELVKRPT 432
Cdd:pfam08385 257 EEileefqeaYKVFKSKTYDIldVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDDAR-STESAFKLLRIFEFLLERPI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 433 ISKELMLERETLLARLGDSAKDFRLDFENrcrgipGDASGPLSGKNLSEVVNNIVWVRQLELKVDDTIKIAEALLSDLSg 512
Cdd:pfam08385 336 IRGALEEKYTDLLQMFKKELDAVKKIFDK------QKYNPSPIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLLK- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 513 frsfHRSAEDLLDQF-------KLYEQEQFDDWSREVqsglsDSRSGLCIEANsrIMELDPNDGAL-KVHYSDRLVILLR 584
Cdd:pfam08385 409 ----HAEGKKVIKKYnelakklDEYERLIYEAWLKEV-----EEASEGNLKRP--LLVRHPETGKLlSVNFDPQLLALLR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 585 EVRQLSALGFVIPAKIQQVANVAQKFCKQAIILKQVAHFYNSIDQQMIQSQRPMMLQSALAFEQIIKNskagsgGKSQIT 664
Cdd:pfam08385 478 EVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEP------GLTTLT 551
|
570
....*....|
gi 2007538485 665 WDNpKELEGY 674
Cdd:pfam08385 552 WNS-LGIDEY 560
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2284-2423 |
1.65e-20 |
|
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: 91.68 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2284 KQPFILVGPEGCGKGMLLRYAFSQLRSTE--IATIHCSAQTTSrhllqklSQTCMVISTN----TGRVYRPKDCERLVLY 2357
Cdd:pfam12775 31 GKPVLLVGPTGTGKTVIIQNLLRKLDKEKylPLFINFSAQTTS-------NQTQDIIESKlekrRKGVYGPPGGKKLVVF 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2007538485 2358 LKDINLPKLDKWGTSTLVAFLQQVLTYQGFYD-ENLEWVGLENIQIVASMS-AGGrlGRHKLTTRFTS 2423
Cdd:pfam12775 104 IDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDrKKLTFKEIVDVQFVAAMGpPGG--GRNDITPRLLR 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2885-3237 |
7.45e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2885 KRKELLKRQSHLQAGVSKLNEAKALVDELNRkageqsillrIKQDEADSALQEITVSMQDASEQKTELErlkhriaEEVV 2964
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKEELER----------LKKRLTGLTPEKLEKELEELEKAKEEIE-------EEIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2965 KIEERKSKIDDELKEVQPLVNEAKLAVG---------------NIRPESLSEIRSLRMPPDVIRDILEGVLRLMgifdts 3029
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKEL------ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3030 wVSMKSFLAKRgvREDIATfdaRNIPKEIRESVEELlfknkASFDPKNAKrastaaaplaawvKANVQYSHVLERIQPLE 3109
Cdd:PRK03918 483 -RELEKVLKKE--SELIKL---KELAEQLKELEEKL-----KKYNLEELE-------------KKAEEYEKLKEKLIKLK 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3110 TEQSGLELNLKKTEDRKRKLEdllnsvgqkvsELKEKFQSRTSEAAKLEAEVSK-AQETIKAAEVLISQLDREHRRWNA- 3187
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLA-----------ELEKKLDELEEELAELLKELEElGFESVEELEERLKELEPFYNEYLEl 607
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2007538485 3188 -----QVAEIAEELATLPKRAQLAAAFITYLSAAPEGLRKNcLEEWTKAAGLEKF 3237
Cdd:PRK03918 608 kdaekELEREEKELKKLEEELDKAFEELAETEKRLEELRKE-LEELEKKYSEEEY 661
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3091-3208 |
1.42e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3091 WVKANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKA 3170
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110
....*....|....*....|....*....|....*...
gi 2007538485 3171 AEVLISQLDREHRRWNAQVAEIAEELATLpkRAQLAAA 3208
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEEL--EEELEEA 349
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2883-3223 |
1.17e-06 |
|
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: 55.07 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2883 SSKRKELLKRQSHLQAGVSKLNEAKALVDELNRK-----AGEQsilLRIKQDEAD-SALQEITVSMQDASEQktELERLK 2956
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgEEEQ---LRVKEKIGElEAEIASLERSIAEKER--ELEDAE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2957 HRIAEEVVKIEERKSKIDDELKEVQPLvneaklavgNIRPESLSEIrslrmppdvirdilegvlrlmgifdtswvsmksF 3036
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEE---------RKRRDKLTEE---------------------------------Y 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3037 LAKRGVREDIATfDARNIPKEIRESVEELlfknkasfdpknakrastaaaplaawVKANVQYSHVLERIQPLETEQSGLE 3116
Cdd:TIGR02169 360 AELKEELEDLRA-ELEEVDKEFAETRDEL--------------------------KDYREKLEKLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3117 LNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEEL 3196
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
330 340
....*....|....*....|....*..
gi 2007538485 3197 ATLPKRAQLAAAFITYLSAAPEGLRKN 3223
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLKAS 519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2885-3255 |
8.23e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2885 KRKELLKRQSHLQagvSKLNEAKALVDELNRKAGEQSillriKQDEADSALQEITVSMQDASEQKTELERLKHriAEEVV 2964
Cdd:PTZ00121 1309 KKAEEAKKADEAK---KKAEEAKKKADAAKKKAEEAK-----KAAEAAKAEAEAAADEAEAAEEKAEAAEKKK--EEAKK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2965 KIEERKSKIDDELK--EVQPLVNEAKLavgniRPESLSEIRSLRMPPDVIRDILEGVlrlmgifdtswvsMKSFLAKRGV 3042
Cdd:PTZ00121 1379 KADAAKKKAEEKKKadEAKKKAEEDKK-----KADELKKAAAAKKKADEAKKKAEEK-------------KKADEAKKKA 1440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3043 REDIATFDARNIPKEIRESvEELLFKNKASFDPKNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLElNLKKT 3122
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKA-EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD-EAKKA 1518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3123 EDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEElatlPKR 3202
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE----ARI 1594
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2007538485 3203 AQLAAAFITYLSAAPEGLRKNcLEEWTKAAGLEKFDLRRflcTESEQLIWKSE 3255
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAEEEK---KKVEQLKKKEA 1643
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2885-3206 |
9.49e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2885 KRKELLKRQSHLQagvSKLNEAKALVDELNRKAGEQSillriKQDEADSALQEitvsmQDASEQKTELERLKhriAEEVV 2964
Cdd:PTZ00121 1477 KKAEEAKKADEAK---KKAEEAKKKADEAKKAAEAKK-----KADEAKKAEEA-----KKADEAKKAEEAKK---ADEAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2965 KIEERKSKidDELKEVQPLVN-EAKLAVGNIRPESLSEIRSLRMPpDVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVR 3043
Cdd:PTZ00121 1541 KAEEKKKA--DELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3044 EDIATFDARNiPKEIRESVEELlfKNKASFDPKNA----KRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELNL 3119
Cdd:PTZ00121 1618 AKIKAEELKK-AEEEKKKVEQL--KKKEAEEKKKAeelkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3120 KKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLisQLDREHRRWNAQVAEIAEELATL 3199
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEE 1772
|
....*..
gi 2007538485 3200 PKRAQLA 3206
Cdd:PTZ00121 1773 IRKEKEA 1779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2863-3201 |
1.80e-05 |
|
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: 51.22 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2863 AYGATPSRYMTFLRVYSAISSSKRKE--LLKRQSHLQagvSKLNEAKALVDELNRKAGEQSILLRIKQDEADSALQEITV 2940
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELssLQSELRRIE---NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2941 SMQDASEQKTELERLKHRIAEEVVKIEERKSKIDDELKEVQPLvnEAKLAvGNIRPESLSEIRSLRmppDVIRDIlEGVL 3020
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLS-HSRIPEIQAELSKLE---EEVSRI-EARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3021 RlmgifdtswvSMKSFLAKRGVREDIAtfdarnipkeiRESVEELLFKNKASFDPKNAKRastaaaplaawvkanvqysh 3100
Cdd:TIGR02169 815 R----------EIEQKLNRLTLEKEYL-----------EKEIQELQEQRIDLKEQIKSIE-------------------- 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3101 vlERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIK----AAEVLIS 3176
Cdd:TIGR02169 854 --KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSelkaKLEALEE 931
|
330 340
....*....|....*....|....*
gi 2007538485 3177 QLDrEHRRWNAQVAEIAEELATLPK 3201
Cdd:TIGR02169 932 ELS-EIEDPKGEDEEIPEEELSLED 955
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2885-3208 |
1.80e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2885 KRKELLKRQshLQAGVSKLNEAKALVDELNRKAGEQSILLRIKQDEADSALQEITVSMQDASEQKTELERLKHRIAEEvv 2964
Cdd:COG4717 146 ERLEELEER--LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE-- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2965 kIEERKSKIDDELKEVQPLVNEAKLAVGNIRPESLSEIRSLRMPPDVIRDILE---GVLRLMG--IFDTSWVSMKSFLAK 3039
Cdd:COG4717 222 -LEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiaGVLFLVLglLALLFLLLAREKASL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3040 RGVREDIATFDARNI--PKEIRESVEELLFKNKASfdpknAKRASTAAAPLAAWVKANVQYSHVLER--IQPLETEQSGL 3115
Cdd:COG4717 301 GKEAEELQALPALEEleEEELEELLAALGLPPDLS-----PEELLELLDRIEELQELLREAEELEEElqLEELEQEIAAL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3116 eLNLKKTED---------RKRKLEDLLnsvgQKVSELKEKFQSRTSEAAKLEAEVSKAQ--ETIKAAEVLISQLDREHRR 3184
Cdd:COG4717 376 -LAEAGVEDeeelraaleQAEEYQELK----EELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEELEE 450
|
330 340
....*....|....*....|....
gi 2007538485 3185 WNAQVAEIAEELATLPKRAQLAAA 3208
Cdd:COG4717 451 LREELAELEAELEQLEEDGELAEL 474
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2886-3202 |
1.82e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2886 RKELLKRQSHLQAGVSKLNEAKALVDELNRKAGEqsILLRIKqdEADSALQEITVSMQDASEQKTELERLKHRIAE---E 2962
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEE--VLREIN--EISSELPELREELEKLEKEVKELEELKEEIEElekE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2963 VVKIEERKSKIDDELKEVQPLVNEAKlavgnirpeslSEIRSLRmppDVIRDI--LEGVLRLMGIFDTSWVSMKSFLAKR 3040
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELK-----------KEIEELE---EKVKELkeLKEKAEEYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3041 GVREDIATFDARNIPKEIREsVEELlfKNKASFDPKNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELN-- 3118
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKE-LEEK--EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEkl 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3119 ---LKKTEDRKRKLEDLLNSVGQKVSELKEKfqsrtseaaklEAEVSKAQETIKAAE----VLISQLDREHR-----RWN 3186
Cdd:PRK03918 390 ekeLEELEKAKEEIEEEISKITARIGELKKE-----------IKELKKAIEELKKAKgkcpVCGRELTEEHRkelleEYT 458
|
330
....*....|....*.
gi 2007538485 3187 AQVAEIAEELATLPKR 3202
Cdd:PRK03918 459 AELKRIEKELKEIEEK 474
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2885-3500 |
2.62e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2885 KRKELLKRQSHLQAgvsKLNEAKALVDELNRKAGEQSILLRIKQDEADSALQEITVSMQDASEQKTELERLKHRIAEEVV 2964
Cdd:COG1196 254 ELEELEAELAELEA---ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2965 KIEERKSKIDDELKEVQPLVNEAKLAvgnirpeslseirslrmppdvirdilegvlrlmgifdtswvsmksflakrgvre 3044
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEA------------------------------------------------------ 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3045 diatfdarnipKEIRESVEELLFKNKASFDPKNAKrastaaaplaaWVKANVQYSHVLERIQPLETEQSGLELNLKKTED 3124
Cdd:COG1196 357 -----------EAELAEAEEALLEAEAELAEAEEE-----------LEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3125 RKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLPKRAQ 3204
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3205 LAAAfityLSAAPEGLrkncLEEWTKAAGLEKFDLrrfLCTESEQLIWkseglpsDDLSIENALVILQSRVCPFLIDPSS 3284
Cdd:COG1196 495 LLLE----AEADYEGF----LEGVKAALLLAGLRG---LAGAVAVLIG-------VEAAYEAALEAALAAALQNIVVEDD 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3285 QATEWLKTHLKDSHLEVINQQDSNFITALELAVRfgKTLIIQEMDGVEPVLYPLLRRDLVAQGPRYVVQIGDKIIDYNED 3364
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA--ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3365 FRLFLSTRNPNPFIppdAASIVTEVNFTTTRSGLRGQLLALTIQHEKPDLEEQKTKLLQQEEDKKIQLARLEESLLETLA 3444
Cdd:COG1196 635 ALRRAVTLAGRLRE---VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2007538485 3445 TSQGNILENKDLIESLNQTKASSALIQDSLKESYKLQISLDQERDAYLPLAESASK 3500
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3103-3204 |
4.51e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3103 ERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREH 3182
Cdd:COG4372 73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
90 100
....*....|....*....|..
gi 2007538485 3183 RRWNAQVAEIAEELATLPKRAQ 3204
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQ 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3093-3223 |
4.98e-05 |
|
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: 48.00 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3093 KANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVG---------QKVSELKEKFQSRTSEAAKLEAEVSK 3163
Cdd:COG1579 42 ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealqKEIESLKRRISDLEDEILELMERIEE 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2007538485 3164 AQETIKAAEVLIS----QLDREHRRWNAQVAEIAEELATLP-KRAQLAAAFITYLSAAPEGLRKN 3223
Cdd:COG1579 122 LEEELAELEAELAeleaELEEKKAELDEELAELEAELEELEaEREELAAKIPPELLALYERIRKR 186
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2943-3200 |
1.62e-04 |
|
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: 47.45 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2943 QDASEQKTELERLKHRIAEEVVKIEERKSKIDDELKEVQPLvnEAKLAvgnirpESLSEIRSLRMPPDVIRDILEGVLRL 3022
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--ERRIA------ALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3023 MGIFDTSWVSMKSFLAKRgvrediatfdARNIPKEIRESVEELLFKNKasfDPKNAKRASTaaaplaaWVKANVQYshVL 3102
Cdd:COG4942 92 IAELRAELEAQKEELAEL----------LRALYRLGRQPPLALLLSPE---DFLDAVRRLQ-------YLKYLAPA--RR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3103 ERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDREH 3182
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|....*...
gi 2007538485 3183 RRWNAQVAEIAEELATLP 3200
Cdd:COG4942 230 ARLEAEAAAAAERTPAAG 247
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2853-3199 |
2.91e-04 |
|
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: 46.87 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2853 SFLLIHESCKAYGATPSRYMTFLRVYSaISSSKRKELLKRQSHLQagvsKLNEAKALVDELNRKAGEQSILLRIKQDEAD 2932
Cdd:COG5185 193 SELKKAEPSGTVNSIKESETGNLGSES-TLLEKAKEIINIEEALK----GFQDPESELEDLAQTSDKLEKLVEQNTDLRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2933 SALQEITVSMQDASEQKTEL----ERLKHRIAEEVVKIEERKSkIDDELKEVQPLVNEAKLAvgnirpESLSEIRSlrmp 3008
Cdd:COG5185 268 EKLGENAESSKRLNENANNLikqfENTKEKIAEYTKSIDIKKA-TESLEEQLAAAEAEQELE------ESKRETET---- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3009 pdVIRDILEGVLRLMGIFDTSWVSMKSFLAKRGVREDIATFDAR--NIPKEIRESVEELLFKNKasfDPKNAKRAstaaa 3086
Cdd:COG5185 337 --GIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEEldSFKDTIESTKESLDEIPQ---NQRGYAQE----- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3087 plaawVKANVQySHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKlEAEVSKAQE 3166
Cdd:COG5185 407 -----ILATLE-DTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYD-EINRSVRSK 479
|
330 340 350
....*....|....*....|....*....|...
gi 2007538485 3167 TIKaaevlisqLDREHRRWNAQVAEIAEELATL 3199
Cdd:COG5185 480 KED--------LNEELTQIESRVSTLKATLEKL 504
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3103-3208 |
2.99e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3103 ERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAA----KLEAEVSKAQETIKAAEVLISQL 3178
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAalleALEEELEALEEALAEAEAALRDL 417
|
90 100 110
....*....|....*....|....*....|....*..
gi 2007538485 3179 DREHRRWNAQVAE-------IAEELATLpkRAQLAAA 3208
Cdd:COG4913 418 RRELRELEAEIASlerrksnIPARLLAL--RDALAEA 452
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2945-3202 |
8.57e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2945 ASEQKTELERLKHRIAEEVvkieERKSKIDDELKEVQPLVNEAKLAVGNIRPEslseIRSLRMPPDVIRDILEGVLRLMG 3024
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFI----KRTENIEELIKEKEKELEEVLREINEISSE----LPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3025 IFDTSWVSMKSFLA-KRGVREDIatfdarnipKEIRESVEELlfKNKASFDPKNAKRastaaaplaawvkanvqyshvLE 3103
Cdd:PRK03918 239 EIEELEKELESLEGsKRKLEEKI---------RELEERIEEL--KKEIEELEEKVKE---------------------LK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3104 RIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFqsrtSEAAKLEAEVSKAQETIKAAEVLISQLDREHR 3183
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHE 362
|
250
....*....|....*....
gi 2007538485 3184 RWNaQVAEIAEELATLPKR 3202
Cdd:PRK03918 363 LYE-EAKAKKEELERLKKR 380
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3119-3223 |
9.89e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3119 LKKTEDRKRKLEDLLNSVGQKVSELKEKfqsrtseAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELAT 3198
Cdd:COG3883 135 LEELKADKAELEAKKAELEAKLAELEAL-------KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
90 100
....*....|....*....|....*
gi 2007538485 3199 LPKRAQLAAAFITYLSAAPEGLRKN 3223
Cdd:COG3883 208 AEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1689-1812 |
1.39e-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: 41.89 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1689 GPAGTGKTESVKALGGLL-GRQVLVFNCDE---------GIDVKSMGRIFVGLV-----KCGAWGCFDEFNRLEEAVLSA 1753
Cdd:pfam07728 6 GPPGTGKTELAERLAAALsNRPVFYVQLTRdtteedlfgRRNIDPGGASWVDGPlvraaREGEIAVLDEINRANPDVLNS 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2007538485 1754 VSMQIQTiqdalkNHRSVCELLGKEVEINANSGIFITMNPAGKgygGRQKLPDNLKQLF 1812
Cdd:pfam07728 86 LLSLLDE------RRLLLPDGGELVKAAPDGFRLIATMNPLDR---GLNELSPALRSRF 135
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
1942-1988 |
1.98e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 42.77 E-value: 1.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1942 ALKQVFEEANYEVIPNQMKKAL---ELYEQLRQRTgVVIVGPSGAGKSTL 1988
Cdd:cd01854 53 ELLEIYEKLGYPVLAVSAKTGEgldELRELLKGKT-SVLVGQSGVGKSTL 101
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3056-3223 |
1.99e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3056 KEIRESVEELlFKNKASFDPKNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDL--- 3132
Cdd:COG4717 49 ERLEKEADEL-FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlql 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3133 -------------LNSVGQKVSELKEKFQSRTS---EAAKLEAEVSKAQETIKAAEVL--------ISQLDREHRRWNAQ 3188
Cdd:COG4717 128 lplyqelealeaeLAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQlslateeeLQDLAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|....*
gi 2007538485 3189 VAEIAEELATLPKRAQLAAAFITYLSAAPEGLRKN 3223
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3109-3181 |
2.99e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 2.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2007538485 3109 ETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDRE 3181
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
1688-1771 |
3.19e-03 |
|
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: 40.98 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 1688 YGPAGTGKTESVKALGGLLGRQ---VLVFNC--------DEGIDVKSMGRIFVGLVKCGAWGC--FDEFNRLEEAVLSAV 1754
Cdd:cd00009 25 YGPPGTGKTTLARAIANELFRPgapFLYLNAsdlleglvVAELFGHFLVRLLFELAEKAKPGVlfIDEIDSLSRGAQNAL 104
|
90
....*....|....*..
gi 2007538485 1755 SMQIQTIQDALKNHRSV 1771
Cdd:cd00009 105 LRVLETLNDLRIDRENV 121
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
1688-1728 |
3.32e-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: 41.11 E-value: 3.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2007538485 1688 YGPAGTGKTESVKALGGLLGRQVLVFNCDEGIDV------KSMGRIF 1728
Cdd:cd19481 32 YGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKyvgeseKNLRKIF 78
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2874-3199 |
3.34e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2874 FLRVYSAISSSKRKELLKRQSHLQagvSKLNEAKALVDELNrkagEQSILLRIKQDEADSAL-------QEITV---SMQ 2943
Cdd:PRK02224 189 LDQLKAQIEEKEEKDLHERLNGLE---SELAELDEEIERYE----EQREQARETRDEADEVLeeheerrEELETleaEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2944 DASEQKTELERLKHRIAEEVVKIEERKSKIDDELKEVQplvneAKLAVGNIRPESLSEIRS-LRMPPDVIRDILEgvlrl 3022
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDLL-----AEAGLDDADAEAVEARREeLEDRDEELRDRLE----- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3023 mgifdTSWVSMKSFLAK-RGVREDIATFDARNipKEIRESVEELlfknkaSFDPKNAKRASTAAAplaawvkanvqyshv 3101
Cdd:PRK02224 332 -----ECRVAAQAHNEEaESLREDADDLEERA--EELREEAAEL------ESELEEAREAVEDRR--------------- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3102 lERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKA----------- 3170
Cdd:PRK02224 384 -EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpve 462
|
330 340 350
....*....|....*....|....*....|...
gi 2007538485 3171 ----AEVLisqldrEHRRwnAQVAEIAEELATL 3199
Cdd:PRK02224 463 gsphVETI------EEDR--ERVEELEAELEDL 487
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2886-3181 |
3.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2886 RKELLKRQSHLQAGVSKLNEAKALVDELNRKAGEQSILLRIKQ-----DEADSALQEITVsmQDASEQKTELERLKhria 2960
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeqlKELEEKLKKYNL--EELEKKAEEYEKLK---- 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2961 EEVVKIEERKSKIDDELKEVQPLvnEAKLAVGNIRPESLSEIRSlrmppDVIRDILEgvlrlmgifdtswVSMKSFlakr 3040
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKLEEL--KKKLAELEKKLDELEEELA-----ELLKELEE-------------LGFESV---- 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3041 gvrediatfdarnipKEIRESVEELLFKNKASFDPKNAKRASTAAaplaawvkanvqyshvLERIQPLETEQSGLELNLK 3120
Cdd:PRK03918 588 ---------------EELEERLKELEPFYNEYLELKDAEKELERE----------------EKELKKLEEELDKAFEELA 636
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2007538485 3121 KTEDRKRKLEDLLNSVGQKVSE-----LKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLDRE 3181
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1975-2013 |
3.93e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.91 E-value: 3.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2007538485 1975 VVIVGPSGAGKSTLWRMLrAALCKI--------GKVVKQytMNPK----AM 2013
Cdd:PRK11650 33 IVLVGPSGCGKSTLLRMV-AGLERItsgeiwigGRVVNE--LEPAdrdiAM 80
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3116-3215 |
4.15e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3116 ELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAAKLEAEVSKAQETIKAAEVLISQLdrehrrwNAQVAEIAEE 3195
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-------EAEIEERREE 87
|
90 100
....*....|....*....|
gi 2007538485 3196 LATLPKRAQLAAAFITYLSA 3215
Cdd:COG3883 88 LGERARALYRSGGSVSYLDV 107
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1944-1996 |
5.16e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.48 E-value: 5.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2007538485 1944 KQVFEEANYEVIPNQMkkalelyeqlrqrtgVVIVGPSGAGKSTLWRMLRAAL 1996
Cdd:COG2401 43 RYVLRDLNLEIEPGEI---------------VLIVGASGSGKSTLLRLLAGAL 80
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1975-1992 |
5.20e-03 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 42.37 E-value: 5.20e-03
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
3095-3172 |
6.63e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 40.72 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3095 NVQysHVLERIQPL----------ETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSEL-------KEKFQSRTSEAAKL 3157
Cdd:pfam05266 86 DVK--APQSRINKLlslkdrqtklLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELerqlalaKEKKEAADKEIARL 163
|
90
....*....|....*
gi 2007538485 3158 EAEVSKAQETIKAAE 3172
Cdd:pfam05266 164 KSEAEKLEQEIQDVE 178
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2885-2990 |
8.64e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.13 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2885 KRKELLKRQSHLQAGVSKLNEA-------KALVDELNRKAGEQSILLRIKQDEADSALQEITVSMQDASEQKTELERLKH 2957
Cdd:pfam20492 7 EKQELEERLKQYEEETKKAQEEleeseetAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELA 86
|
90 100 110
....*....|....*....|....*....|...
gi 2007538485 2958 RIAEEVVKIEERKSKIDDELKEVQPLVNEAKLA 2990
Cdd:pfam20492 87 EAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3076-3222 |
8.75e-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: 42.35 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3076 KNAKRASTAAAPLAAWVKANVQYSHVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEKFQSRTSEAA 3155
Cdd:TIGR02168 219 KAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2007538485 3156 KLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLPKRAQLAAAFITYLSAAPEGLRK 3222
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2915-3209 |
8.98e-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: 42.35 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2915 RKAGEQSILLRikQDEADSALQEITVSMQDASEQKTELERLKHRIAEevvkIEERKSKIDDELKEVQPLVNEAKLAVGNI 2994
Cdd:TIGR02168 665 SAKTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 2995 RPES---LSEIRSLRMPPDVIRDILEGVLRLMGIFDTSWVSMKSFLAKrgVREDIATF-DARNIPKEIRESVEELLFKNK 3070
Cdd:TIGR02168 739 EAEVeqlEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE--LEAQIEQLkEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3071 ASFDpKNAKRASTAAAPLAAWVKANVQyshVLERIQPLETEQSGLELNLKKTEDRKRKLEDLLNSVGQKVSELKEkfqsr 3150
Cdd:TIGR02168 817 EEAA-NLRERLESLERRIAATERRLED---LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE----- 887
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2007538485 3151 tsEAAKLEAEVSKAQETIKAAEVLISQLDREHRRWNAQVAEIAEELATLP-KRAQLAAAF 3209
Cdd:TIGR02168 888 --ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvRIDNLQERL 945
|
|
| |
