|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1765-2091 |
0e+00 |
|
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: 641.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1765 YNYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGIYVIVVNCSEGLDYKSMGRMYSG 1844
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1845 LAQTGAWGCFDEFNRINIEVLSVVAHQILCILSALAAGLTHFHFDGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFR 1924
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1925 PIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLTDEEVLL 2004
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2005 LSMRDMNIAKLTSVDAPLFNAIVQDLFPNIELPVIDYGKLRETVEQEIRDMGLQSTPFTLTKVFQLYETKNSRHSTMIVG 2084
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 75677365 2085 CTGSGKT 2091
Cdd:pfam12774 321 PTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1220-1628 |
5.76e-170 |
|
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: 530.29 E-value: 5.76e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1220 LQNLEKELDALQQIWEIARDWEENWNEWKTGRFLILQTETMETTAHGLFRRLTKLAKEYKDrnWEIIETTRSKIEQFKRT 1299
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRD--WDVAEELKKKIDDFKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1300 MPLISDLRNPALRERHWDQVRDEIQREFDQESESFTLEQIVELGMDQHVEKIGEISASATKELAIEVALQNIAKTWDVTQ 1379
Cdd:pfam08393 79 LPLIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1380 LDIVPYKDKGHHRLRGTEEVFQALEDNQVALSTMKASRFVKAFEKDVDHWERCLSLILEVIEMILTVQRQWMYLENIFLG 1459
Cdd:pfam08393 159 FELVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1460 EDIRKQLPNESTLFDQVNSNWKAIMDRMNKDNNALRSTHHPGLLDTLIEMNTILEDIQKSLDMYLETKRHIFPRFYFLSN 1539
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1540 DDLLEILGQSRNPEAVQPHLKKCFDNIKLLRIQKvggpssKWEAVGMFSGDGEYIDFLHS-VFLEGPVESWLGDVEQTMR 1618
Cdd:pfam08393 319 DELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE------NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMR 392
|
410
....*....|
gi 75677365 1619 VTLRDLLRNC 1628
Cdd:pfam08393 393 ETLRDLLKEA 402
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1292-4108 |
9.22e-143 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 504.52 E-value: 9.22e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1292 KIEQFKRTMPLISDL-----RNPALRE---RHWDQV----RDEIQREFdqesesftLEQIVELGMDQHV--EKIGEISAS 1357
Cdd:COG5245 486 KLCKIMRMFSFFNSLemfsrRTLANRMaivKYLSSVvrtgPLFLQRDF--------FGRMSELLMARDMfmEVDGVLRLF 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1358 ATKELA--IEVALQNIAKTWDVTQLDivpykdkghhrlrgtEEVFQALEDNQVALSTMKASRFvkaFEKDVDhWERCLSL 1435
Cdd:COG5245 558 FGGEWSgiVQLSGIRRAKRCVERQID---------------DEIREWCSSVLSDDFLEERAVR---VERGAD-GARRLRA 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1436 ILEvIEMILTVQRQWMYLENiflgEDIRKQLPNESTLFDQVNSNWKAIMDRMNKDNNALRSTHHPgLLDTLIEMNTILED 1515
Cdd:COG5245 619 SSG-SPVLRRLDEYLMMMSL----EDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQ 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1516 IQKSLDMYLETKRHIFPRFyfLSNDDLLEILGQSRNPEAVQPHLKKCFDNIKLLRIQkvggpSSKWEAVGMFSGDGEYID 1595
Cdd:COG5245 693 VFMSIEKVLGLRWREVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEEMKTVF-----SSRIQKKEPFSLDSEAYV 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1596 FLHSVFLEGPVESWLGDVEQTMRVTLRDllrnchlALRKFLNKRDkwvkewaGQVVITASQIQ--------WTADVTKCL 1667
Cdd:COG5245 766 GFFRLYEKSIVIRGINRSMGRVLSQYLE-------SVQEALEIED-------GSFFVSRHRVRdgglekgrGCDAWENCF 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1668 LTAKERADKKILKVMKknqvSILNKYSEAIRGnltkimrlKIVALVTIEIHARDVLEKLYKSGLMDVNSFDWLSQLRFYw 1747
Cdd:COG5245 832 DPPLSEYFRILEKIFP----SEEGYFFDEVLK--------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP- 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1748 eKDLDDCVIR-QTNTQFQYNYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSpkgpAGTGKTETVKDLGKALGIYViv 1826
Cdd:COG5245 899 -QGLYKRFIKvRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY-- 971
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1827 vncsEGLDYKSmgRMYSGLAQTGAWGcFDEFNRINIEVLSVVAHQILcILSALAAGLTHFHFDGFEINLVWSCGIFITMN 1906
Cdd:COG5245 972 ----DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTILVDEYL-NSDEFRMLEELNSAVVEHGLKSPSTPVEMIIN 1043
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1907 PgyagRTELPENLKSMFRPIAMVVPDSTlIAEIIlfgegfgncKILAKKVYTLYSLAVQQLSRQDHYDFglRALTSLLRy 1986
Cdd:COG5245 1044 E----RNIVLEIGRRALDMFLSNIPFGA-IKSRR---------ESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLK- 1106
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1987 agKKRRLQPDLTDEEVLLLSmrdmnIAKLTSVDAPLFNAIvqDLFPNIELPVIdygklRETVEQEIRDMGlQSTPFTLTK 2066
Cdd:COG5245 1107 --AKHRMLEEKTEYLNKILS-----ITGLPLISDTLRERI--DTLDAEWDSFC-----RISESLKKYESQ-QVSGLDVAQ 1171
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2067 VFQLYETKNSRHSTMIVGCTGSGKTASWRIlqaslsslcragdpnfniVREFPLNPKALSLGELYGEYDLstnEWTdGIL 2146
Cdd:COG5245 1172 FVSFLRSVDTGAFHAEYFRVFLCKIKHYTD------------------ACDYLWHVKSPYVKKKYFDADM---ELR-QFF 1229
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2147 SSVMRTACADEKPDEK-WILFDGpvdtlWIENMNSVMDDNKVLTLINGERiampeqvSLLFEVEDlamASPATVSRCGMV 2225
Cdd:COG5245 1230 LMFNREDMEARLADSKmEYEVER-----YVEKTKAEVSSLKLELSSVGEG-------QVVVSNLG---SIGDKVGRCLVE 1294
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2226 YTDYADLGWKPYVQSWLEKRPKAEVEPLQrMFE------KLINK-MLAFKKDNCKELVPLPEYSGITSLCKLYSALATPE 2298
Cdd:COG5245 1295 YDSISRLSTKGVFLDELGDTKRYLDECLD-FFScfeevqKEIDElSMVFCADALRFSADLYHIVKERRFSGVLAGSDASE 1373
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2299 NGVNPA----------DGENYVTMVemtFVFSMIWSVCASVDEEGRKRIDSYLREIEGSFPNKDTVYEYF------VDPK 2362
Cdd:COG5245 1374 SLGGKSielaailehkDLIVEMKRG---INDVLKLRIFGDKCRESTPRFYLISDGDLIKDLNERSDYEEMlimmfnISAV 1450
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2363 IRSWTSFEDKLPKSWR--YPPNapfykIMVPTVDTVRYNYLVSSLVANQNPILLVGPVGTGKTSIAQSVLQSlpSSQWSV 2440
Cdd:COG5245 1451 ITNNGSIAGFELRGERvmLRKE-----VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS--ELITEV 1523
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2441 LVVNMSAQTTSNNVQSIIESRVEK-RTKGVYVPFGG---KSMITFMDDLNMPAKDMFGSQPPLELIR-LWIDYGFWYDRT 2515
Cdd:COG5245 1524 KYFNFSTCTMTPSKLSVLERETEYyPNTGVVRLYPKpvvKDLVLFCDEINLPYGFEYYPPTVIVFLRpLVERQGFWSSIA 1603
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2516 KQtIKYIREMFLMAAMGPPGG-GRTVISPRLRSRFNIINMTFPTKSQIIRIFGTMINQKLQDFEEEVKPIGNVVTEATlD 2594
Cdd:COG5245 1604 VS-WVTICGIILYGACNPGTDeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASV-E 1681
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2595 MYNTVVQRFlPTPTKMHYLFNLRDISKVFQGMLRANKDFHDTKS-SITRLWIHECFRVFSDRLVDAADTEAFMGIISDKL 2673
Cdd:COG5245 1682 LYLSSKDKT-KFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFG 1760
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2674 GSFF-DLTFHHLcpSKRPPIFGDFLKEPKVYEDLTDLTV-LKTVMETAlneYNLSPSVvpmQLVLFREAIEHITRIVRVI 2751
Cdd:COG5245 1761 LRAIrEMIAGHI--GEAEITFSMILFFGMACLLKKDLAVfVEEVRKIF---GSSHLDV---EAVAYKDALLHILRSRRGL 1832
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2752 GQPRGNMLLVGIGGSGRQSLARLASSICDYTTFQIEVTKHYRKQEFRDDIKRLYRQAGVELKTTSFIFVDTQIADESFLE 2831
Cdd:COG5245 1833 LVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLE 1912
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2832 DINNILSSGEVPNLYKPDEFEEIQSHIIDQARVEQVP-ESSDSLFAYLIERVQNNLHIVLCL-SPMGDPFRNWIRqYPAL 2909
Cdd:COG5245 1913 DFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEkDTEATLTRVFLVYMEENLPVVFSAcCSQDTSVLAGIR-SPAL 1991
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2910 VNCTTINWFSEWPQEALLEVAEKCL-----------IGVDLGTQE--NIHRKVAQIFVTMHWSVaqYSQKMLLELrrhNY 2976
Cdd:COG5245 1992 KNRCFIDFKKLWDTEEMSQYANSVEtlsrdggrvffINGELGVGKgaLISEVFGDDAVVIEGRG--FEISMIEGS---LG 2066
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2977 VTPTKYLELLSGYKKLLGEKRQELLAQANKLRTGLFKIDETREKVQVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREA 3056
Cdd:COG5245 2067 ESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLER 2146
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3057 DEQQKAVTANSEKIAVEEIKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGN 3136
Cdd:COG5245 2147 EVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGF 2226
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3137 EPT-WAEAKRQLGEQNFIKSLINFDKD-NISDKVLKKIGA-YCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVV 3213
Cdd:COG5245 2227 EAKiWFGEQQSLRRDDFIRIIGKYPDEiEFDLEARRFREArECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVK 2306
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3214 EPKRIRMNAALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARW 3293
Cdd:COG5245 2307 IPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEW 2386
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3294 EETVQGLEEDLGYLVGDCLLAAAFLSYMGPflTNYRDEIVNQIWIGKIWELQVPCSPSFAIDNFLCNPTKVRDWNIQGLP 3373
Cdd:COG5245 2387 GGVFSEVPKLMVELDGDGHPSSCLHPYIGT--LGFLCRAIEFGMSFIRISKEFRDKEIRRRQFITEGVQKIEDFKEEACS 2464
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3374 SDAFSTENGIIVTRGNRWALMIDPQAQALKWIKNMEGGQGLKIIDLQMSDYLRILEHAIHFGYPVLLQnVQEYLDPTLNP 3453
Cdd:COG5245 2465 TDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIG-DAEALDEEIGR 2543
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3454 MLNKSVARIGGRLLMRIGDKEVEYNTNFRFYITTKLSNPHYSPETSAKTTIVNFAVKEQGLEAQLLGIVVRKERPELEEQ 3533
Cdd:COG5245 2544 LIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVH 2623
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3534 KDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLHTSKITATEVTEQLETSETTEINTDLAREAYRPCAQR 3613
Cdd:COG5245 2624 EKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKR 2703
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3614 ASILFFVLNDMGCIDPMYQFSLDAYISLF-ILSIDKSHRSNKLEDRIDYLNDYhtyavyrytcrtLFERHKLLFSFhmca 3692
Cdd:COG5245 2704 LESIRVEIAMFDEKALMYNKSICELSSEFeKWRRMKSKYLCAIRYMLMSSEWI------------LDHEDRSGFIH---- 2767
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3693 kILETSGKLNMDEynfFLRGGVVLDREGQMDNPCSSWLADAYWDNITELDKLTNFhglMNSFEQYPRDWHLWYTnaapek 3772
Cdd:COG5245 2768 -RLDVSFLLRTKR---FVSTLLEDKNYRQVLSSCSLYGNDVISHSCDRFDRDVYR---ALKHQMDNRTHSTILT------ 2834
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3773 amlpgeWENACNEMQRMLIVRSLRQ-DRVAFCVTSFIITnlgsrfieppvlnmKSVLEDSTPRSPLVFILSPGVDptsaL 3851
Cdd:COG5245 2835 ------SNSKTNPYKEYTYNDSWAEaFEVEDSGDLYKFE--------------EGLLELIVGHAPLIYAHKKSLE----N 2890
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3852 LQLAEHMGMAQRfhaLSLGQGQAPIAArllregvTQGHWVFLANCHLSLSWMPN-LDKLVEQLQVEDPHPSF-RLWLSSI 3929
Cdd:COG5245 2891 ERNVDRLGSKEN---EVYAVLNSLFSR-------KEKSWFEVYNISLSFGWFKRyVEDVVYPIKASRVCGKVkNMWTSMV 2960
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3930 PHPDFPISILQVSIKMTTEPPKGLKANMTRLYQLMsepQFSRCSKPAKYKKLLFSLCFFHSVLLERKKFLQLGWNIIYGF 4009
Cdd:COG5245 2961 DADMLPIQLLIAIDSFVSSTYPETGCGYADLVEID---RYPFDYTLVIACDDAFYLSWEHAAVASVISAGPKENNEEIYF 3037
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 4010 NDSDFEVSENLLS--LYLDEYEETPWDALKYLIAGINYGGHVTDDWDRRLLTTYINDYFC--DQSLSTPFHRLSALETYF 4085
Cdd:COG5245 3038 GDKDFEFKTHLLKniLFLNHLNARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGAheTSSQILASVPGGDPELVK 3117
|
2890 2900
....*....|....*....|....
gi 75677365 4086 I-PKDGSLASYKEYISLLPGMDPP 4108
Cdd:COG5245 3118 FhMEEMCRSSAFGVIGQLPDLALC 3141
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4123-4423 |
4.52e-128 |
|
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: 405.47 E-value: 4.52e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 4123 ITEAQTLFDTLLSLQPQITPTRAGG-QTREEKVLELAADVKQKIPEMIDYE-GTQKLLALDPSPLNVVLLQEIQRYNTLM 4200
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGgSSREEIVLELAKDILEKLPEPFDIEeAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 4201 QTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLW-GKAYPSQKPLAAWTRDLAMRVEQFELWASRARPPVIFWL 4279
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWaKKSYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 4280 SGFTFPTGFLTAVLQSSARQNNVSVDSLSWEFIV-STVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVC 4358
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVtKKVSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75677365 4359 LMPTIHFRPAE-SRKKSAKGMYSCPCYYYPNRAGSsdraSFVIGIDLRSGaMTPDHWIKRGTALLM 4423
Cdd:pfam18199 241 PLPVIHLKPVEsDKKKLDENTYECPVYKTSERHST----NFVFSVDLPTD-KPPDHWILRGVALLL 301
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2732-2992 |
8.60e-123 |
|
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: 388.50 E-value: 8.60e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2732 MQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICDYTTFQIEVTKHYRKQEFRDDIKRLYRQAGVE 2811
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2812 LKTTSFIFVDTQIADESFLEDINNILSSGEVPNLYKPDEFEEIQSHIIDQARVEQVPESSDSLFAYLIERVQNNLHIVLC 2891
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2892 LSPMGDPFRNWIRQYPALVNCTTINWFSEWPQEALLEVAEKCLigVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLEL 2971
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFL--EDIEIPEELKSNVVKVFVYVHSSVEDMSKKFYEEL 238
|
250 260
....*....|....*....|.
gi 75677365 2972 RRHNYVTPTKYLELLSGYKKL 2992
Cdd:pfam12780 239 KRKNYVTPKSYLELLRLYKNL 259
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
242-717 |
6.54e-113 |
|
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: 372.68 E-value: 6.54e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 242 VQRLETSMIHWTRQIKEMLSAQETvetGENLGPLEEIEFWRNRCMDLSGISKQLVKKGVKHVESILHLAKSSYLAPFMKL 321
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQ---GRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 322 AQQIQDGSRQAQSNLTFLSILKEPYQELAFMK-PKDISSKLPKLISLIRIIWVNSPHYNTRERLTSLFRKVC-------- 392
Cdd:pfam08385 78 DTELTDALNEAKDNVKYLKTLERPFEDLEELTdPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISnqlieqck 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 393 ---------------------DCQYHFARWED------------GKQGP------------------------------- 408
Cdd:pfam08385 158 kylspegifdgdveealeklqECIELLEAWKEeykktrekleesPRERPwdfseryifgrfdaflerlekilelfetieq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 409 ---LPCFFGAQGPQITRNLLEIEDIFHKNLHTLRAVRGGILDVKNTCWHEDYNKFRAGIKDLEVMTQNLITSAFELVRDV 485
Cdd:pfam08385 238 fskLEKIGGTKGPELEGVIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDDARST 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 486 PHGVLLLDTFHRLASREAIKRTYDKKAVDLYMLFNSELALVNR--ERNKKWPD-LEPYVAQYSGKARWVHILRRRIDRVM 562
Cdd:pfam08385 318 ESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKifDKQKYNPSpIAKNMPPVAGAIIWARQLFRRIQEPM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 563 TCLAGAHFLPRIGTGKESVHTYQQMVQAIDELVRKTFQEWTSSLDKDCIRRLDTPLLRISQEKAGMLDVNFDKSLLILFA 642
Cdd:pfam08385 398 KRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGNLKRPLLVRHPETGKLLSVNFDPQLLALLR 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75677365 643 EIDYWERLLFETPHYVVNVAERAEDLRILRENLLLVARDYNRIIAMLSPDEQALFKERIRLLDKKIHPGLKKLHW 717
Cdd:pfam08385 478 EVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTW 552
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2410-2552 |
2.00e-08 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 56.39 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2410 NPILLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPfgGKSMITFMDDLNMPA 2489
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK--AKPGVLFIDEIDSLS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75677365 2490 KDMFGSQppLELIRLWIDYGFWYDRTKqtikyiremFLMAAMGPPGGGrtvISPRLRSRFNII 2552
Cdd:cd00009 98 RGAQNAL--LRVLETLNDLRIDRENVR---------VIGATNRPLLGD---LDRALYDRLDIR 146
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2990-3303 |
1.15e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2990 KKLLGEKRQELLAQANKLRTGLFKIDETREKVQVMSLELEDAKKKVAEFQKQCEEYLVI------IVQQKREADEQQKAV 3063
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdeakkkAEEDKKKADELKKAA 1414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3064 TAN-----------------------SEKIAVEEIKCQA----LADNAQKDLEEALPAlEEAMRALESLNKKDIGEIKSY 3116
Cdd:PTZ00121 1415 AAKkkadeakkkaeekkkadeakkkaEEAKKADEAKKKAeeakKAEEAKKKAEEAKKA-DEAKKKAEEAKKADEAKKKAE 1493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3117 GRPPAQVEIVMQAVMILRGNEPTWAEAKRQLGEQNFIKSLINFDKDNISDKVLKKIGAYCAQPDFQPDIIGRVSLAAKS- 3195
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAe 1573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3196 --LCMWVRAMElygrLYRVVEPKRI-----------RMNAALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQK 3262
Cdd:PTZ00121 1574 edKNMALRKAE----EAKKAEEARIeevmklyeeekKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 75677365 3263 EELRKKSEEMELKLERagmlVSGLAGEKARWEETVQGLEED 3303
Cdd:PTZ00121 1650 EELKKAEEENKIKAAE----EAKKAEEDKKKAEEAKKAEED 1686
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2983-3286 |
6.50e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2983 LELLSGYKKLLGEKRQELLAQANKLRTglfKIDETREKVQVMSLELEDAKKKVAEFQKQCEEY------LVIIV----QQ 3052
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEE---ELEELTAELQELEEKLEELRLEVSELEEEIEELqkelyaLANEIsrleQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3053 KREADEQQKAVTANSEKIAVEEIKCQALADNAQKDLEEALPALEEAMRALESLNKKdigeiksygrppaqveivmqavmi 3132
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE------------------------ 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3133 LRGNEPTWAEAKRQLGEQNfiKSLINFDKDniSDKVLKKIGAycaqpdfqpdIIGRVSLAAKSLCMWVRAMElygRLYRV 3212
Cdd:TIGR02168 360 LEELEAELEELESRLEELE--EQLETLRSK--VAQLELQIAS----------LNNEIERLEARLERLEDRRE---RLQQE 422
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75677365 3213 VE-----PKRIRMNAALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKlaqKEELRKKSEEMELKLERAGMLVSGL 3286
Cdd:TIGR02168 423 IEellkkLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA---EQALDAAERELAQLQARLDSLERLQ 498
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2410-2468 |
2.62e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.29 E-value: 2.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 75677365 2410 NPILLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKG 2468
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG 61
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
923-1455 |
2.99e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 923 PIQTVVEQ-DEDIKKIQTQISSGMTNNASLLQNYLKtwdmyreiweinkdsfiHRYQRlnppvssfvADIARYTEVANNV 1001
Cdd:TIGR00618 297 AHIKAVTQiEQQAQRIHTELQSKMRSRAKLLMKRAA-----------------HVKQQ---------SSIEEQRRLLQTL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1002 QKEETV----TNIQFVLLDCSHLKFSLVQHCNEWQNKFATLL-REMAAGRLLElhtylKENAEKISRPPQTLEElgvslq 1076
Cdd:TIGR00618 351 HSQEIHirdaHEVATSIREISCQQHTLTQHIHTLQQQKTTLTqKLQSLCKELD-----ILQREQATIDTRTSAF------ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1077 lvDALKHDLANVETQIPPIHEQFAILEKYEvpveDSVLEMLDSLNGEWVVFQQTLLDSKQMLKKHKEkfktglIHSADDF 1156
Cdd:TIGR00618 420 --RDLQGQLAHAKKQQELQQRYAELCAAAI----TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ------IHLQETR 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1157 KKKAHtlledfefkGHFtsnvgymsALDQITQVRAMLMAMREEENSLRAnLGIFKIEQPPskdLQNLEKELDALQQiwei 1236
Cdd:TIGR00618 488 KKAVV---------LAR--------LLELQEEPCPLCGSCIHPNPARQD-IDNPGPLTRR---MQRGEQTYAQLET---- 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1237 ardweenwnewktgrflilqteTMETTAHGLfRRLTKLAKEYKDRNWEIIETTRSKIEQFKRTMPLISDLRNPALRERHW 1316
Cdd:TIGR00618 543 ----------------------SEEDVYHQL-TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1317 DQVRDEIQREFDQESEsftlEQIVELGMDQHVEKIGEISASATKELAIEVAlqniAKTWDVTQLdivPYKDKGHHRLRGT 1396
Cdd:TIGR00618 600 TEKLSEAEDMLACEQH----ALLRKLQPEQDLQDVRLHLQQCSQELALKLT----ALHALQLTL---TQERVREHALSIR 668
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 75677365 1397 EEVFQALEDNQVALSTMKASRFVKAFEKDVdhWERCLSLILEVIEMILTVQRQWMYLEN 1455
Cdd:TIGR00618 669 VLPKELLASRQLALQKMQSEKEQLTYWKEM--LAQCQTLLRELETHIEEYDREFNEIEN 725
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1765-2091 |
0e+00 |
|
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: 641.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1765 YNYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGIYVIVVNCSEGLDYKSMGRMYSG 1844
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1845 LAQTGAWGCFDEFNRINIEVLSVVAHQILCILSALAAGLTHFHFDGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFR 1924
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1925 PIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLTDEEVLL 2004
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2005 LSMRDMNIAKLTSVDAPLFNAIVQDLFPNIELPVIDYGKLRETVEQEIRDMGLQSTPFTLTKVFQLYETKNSRHSTMIVG 2084
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 75677365 2085 CTGSGKT 2091
Cdd:pfam12774 321 PTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1220-1628 |
5.76e-170 |
|
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: 530.29 E-value: 5.76e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1220 LQNLEKELDALQQIWEIARDWEENWNEWKTGRFLILQTETMETTAHGLFRRLTKLAKEYKDrnWEIIETTRSKIEQFKRT 1299
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRD--WDVAEELKKKIDDFKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1300 MPLISDLRNPALRERHWDQVRDEIQREFDQESESFTLEQIVELGMDQHVEKIGEISASATKELAIEVALQNIAKTWDVTQ 1379
Cdd:pfam08393 79 LPLIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1380 LDIVPYKDKGHHRLRGTEEVFQALEDNQVALSTMKASRFVKAFEKDVDHWERCLSLILEVIEMILTVQRQWMYLENIFLG 1459
Cdd:pfam08393 159 FELVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1460 EDIRKQLPNESTLFDQVNSNWKAIMDRMNKDNNALRSTHHPGLLDTLIEMNTILEDIQKSLDMYLETKRHIFPRFYFLSN 1539
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1540 DDLLEILGQSRNPEAVQPHLKKCFDNIKLLRIQKvggpssKWEAVGMFSGDGEYIDFLHS-VFLEGPVESWLGDVEQTMR 1618
Cdd:pfam08393 319 DELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE------NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMR 392
|
410
....*....|
gi 75677365 1619 VTLRDLLRNC 1628
Cdd:pfam08393 393 ETLRDLLKEA 402
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1292-4108 |
9.22e-143 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 504.52 E-value: 9.22e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1292 KIEQFKRTMPLISDL-----RNPALRE---RHWDQV----RDEIQREFdqesesftLEQIVELGMDQHV--EKIGEISAS 1357
Cdd:COG5245 486 KLCKIMRMFSFFNSLemfsrRTLANRMaivKYLSSVvrtgPLFLQRDF--------FGRMSELLMARDMfmEVDGVLRLF 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1358 ATKELA--IEVALQNIAKTWDVTQLDivpykdkghhrlrgtEEVFQALEDNQVALSTMKASRFvkaFEKDVDhWERCLSL 1435
Cdd:COG5245 558 FGGEWSgiVQLSGIRRAKRCVERQID---------------DEIREWCSSVLSDDFLEERAVR---VERGAD-GARRLRA 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1436 ILEvIEMILTVQRQWMYLENiflgEDIRKQLPNESTLFDQVNSNWKAIMDRMNKDNNALRSTHHPgLLDTLIEMNTILED 1515
Cdd:COG5245 619 SSG-SPVLRRLDEYLMMMSL----EDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQ 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1516 IQKSLDMYLETKRHIFPRFyfLSNDDLLEILGQSRNPEAVQPHLKKCFDNIKLLRIQkvggpSSKWEAVGMFSGDGEYID 1595
Cdd:COG5245 693 VFMSIEKVLGLRWREVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEEMKTVF-----SSRIQKKEPFSLDSEAYV 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1596 FLHSVFLEGPVESWLGDVEQTMRVTLRDllrnchlALRKFLNKRDkwvkewaGQVVITASQIQ--------WTADVTKCL 1667
Cdd:COG5245 766 GFFRLYEKSIVIRGINRSMGRVLSQYLE-------SVQEALEIED-------GSFFVSRHRVRdgglekgrGCDAWENCF 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1668 LTAKERADKKILKVMKknqvSILNKYSEAIRGnltkimrlKIVALVTIEIHARDVLEKLYKSGLMDVNSFDWLSQLRFYw 1747
Cdd:COG5245 832 DPPLSEYFRILEKIFP----SEEGYFFDEVLK--------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP- 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1748 eKDLDDCVIR-QTNTQFQYNYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSpkgpAGTGKTETVKDLGKALGIYViv 1826
Cdd:COG5245 899 -QGLYKRFIKvRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY-- 971
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1827 vncsEGLDYKSmgRMYSGLAQTGAWGcFDEFNRINIEVLSVVAHQILcILSALAAGLTHFHFDGFEINLVWSCGIFITMN 1906
Cdd:COG5245 972 ----DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTILVDEYL-NSDEFRMLEELNSAVVEHGLKSPSTPVEMIIN 1043
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1907 PgyagRTELPENLKSMFRPIAMVVPDSTlIAEIIlfgegfgncKILAKKVYTLYSLAVQQLSRQDHYDFglRALTSLLRy 1986
Cdd:COG5245 1044 E----RNIVLEIGRRALDMFLSNIPFGA-IKSRR---------ESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLK- 1106
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1987 agKKRRLQPDLTDEEVLLLSmrdmnIAKLTSVDAPLFNAIvqDLFPNIELPVIdygklRETVEQEIRDMGlQSTPFTLTK 2066
Cdd:COG5245 1107 --AKHRMLEEKTEYLNKILS-----ITGLPLISDTLRERI--DTLDAEWDSFC-----RISESLKKYESQ-QVSGLDVAQ 1171
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2067 VFQLYETKNSRHSTMIVGCTGSGKTASWRIlqaslsslcragdpnfniVREFPLNPKALSLGELYGEYDLstnEWTdGIL 2146
Cdd:COG5245 1172 FVSFLRSVDTGAFHAEYFRVFLCKIKHYTD------------------ACDYLWHVKSPYVKKKYFDADM---ELR-QFF 1229
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2147 SSVMRTACADEKPDEK-WILFDGpvdtlWIENMNSVMDDNKVLTLINGERiampeqvSLLFEVEDlamASPATVSRCGMV 2225
Cdd:COG5245 1230 LMFNREDMEARLADSKmEYEVER-----YVEKTKAEVSSLKLELSSVGEG-------QVVVSNLG---SIGDKVGRCLVE 1294
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2226 YTDYADLGWKPYVQSWLEKRPKAEVEPLQrMFE------KLINK-MLAFKKDNCKELVPLPEYSGITSLCKLYSALATPE 2298
Cdd:COG5245 1295 YDSISRLSTKGVFLDELGDTKRYLDECLD-FFScfeevqKEIDElSMVFCADALRFSADLYHIVKERRFSGVLAGSDASE 1373
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2299 NGVNPA----------DGENYVTMVemtFVFSMIWSVCASVDEEGRKRIDSYLREIEGSFPNKDTVYEYF------VDPK 2362
Cdd:COG5245 1374 SLGGKSielaailehkDLIVEMKRG---INDVLKLRIFGDKCRESTPRFYLISDGDLIKDLNERSDYEEMlimmfnISAV 1450
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2363 IRSWTSFEDKLPKSWR--YPPNapfykIMVPTVDTVRYNYLVSSLVANQNPILLVGPVGTGKTSIAQSVLQSlpSSQWSV 2440
Cdd:COG5245 1451 ITNNGSIAGFELRGERvmLRKE-----VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS--ELITEV 1523
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2441 LVVNMSAQTTSNNVQSIIESRVEK-RTKGVYVPFGG---KSMITFMDDLNMPAKDMFGSQPPLELIR-LWIDYGFWYDRT 2515
Cdd:COG5245 1524 KYFNFSTCTMTPSKLSVLERETEYyPNTGVVRLYPKpvvKDLVLFCDEINLPYGFEYYPPTVIVFLRpLVERQGFWSSIA 1603
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2516 KQtIKYIREMFLMAAMGPPGG-GRTVISPRLRSRFNIINMTFPTKSQIIRIFGTMINQKLQDFEEEVKPIGNVVTEATlD 2594
Cdd:COG5245 1604 VS-WVTICGIILYGACNPGTDeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASV-E 1681
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2595 MYNTVVQRFlPTPTKMHYLFNLRDISKVFQGMLRANKDFHDTKS-SITRLWIHECFRVFSDRLVDAADTEAFMGIISDKL 2673
Cdd:COG5245 1682 LYLSSKDKT-KFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFG 1760
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2674 GSFF-DLTFHHLcpSKRPPIFGDFLKEPKVYEDLTDLTV-LKTVMETAlneYNLSPSVvpmQLVLFREAIEHITRIVRVI 2751
Cdd:COG5245 1761 LRAIrEMIAGHI--GEAEITFSMILFFGMACLLKKDLAVfVEEVRKIF---GSSHLDV---EAVAYKDALLHILRSRRGL 1832
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2752 GQPRGNMLLVGIGGSGRQSLARLASSICDYTTFQIEVTKHYRKQEFRDDIKRLYRQAGVELKTTSFIFVDTQIADESFLE 2831
Cdd:COG5245 1833 LVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLE 1912
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2832 DINNILSSGEVPNLYKPDEFEEIQSHIIDQARVEQVP-ESSDSLFAYLIERVQNNLHIVLCL-SPMGDPFRNWIRqYPAL 2909
Cdd:COG5245 1913 DFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEkDTEATLTRVFLVYMEENLPVVFSAcCSQDTSVLAGIR-SPAL 1991
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2910 VNCTTINWFSEWPQEALLEVAEKCL-----------IGVDLGTQE--NIHRKVAQIFVTMHWSVaqYSQKMLLELrrhNY 2976
Cdd:COG5245 1992 KNRCFIDFKKLWDTEEMSQYANSVEtlsrdggrvffINGELGVGKgaLISEVFGDDAVVIEGRG--FEISMIEGS---LG 2066
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2977 VTPTKYLELLSGYKKLLGEKRQELLAQANKLRTGLFKIDETREKVQVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREA 3056
Cdd:COG5245 2067 ESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLER 2146
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3057 DEQQKAVTANSEKIAVEEIKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGN 3136
Cdd:COG5245 2147 EVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGF 2226
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3137 EPT-WAEAKRQLGEQNFIKSLINFDKD-NISDKVLKKIGA-YCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVV 3213
Cdd:COG5245 2227 EAKiWFGEQQSLRRDDFIRIIGKYPDEiEFDLEARRFREArECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVK 2306
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3214 EPKRIRMNAALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARW 3293
Cdd:COG5245 2307 IPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEW 2386
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3294 EETVQGLEEDLGYLVGDCLLAAAFLSYMGPflTNYRDEIVNQIWIGKIWELQVPCSPSFAIDNFLCNPTKVRDWNIQGLP 3373
Cdd:COG5245 2387 GGVFSEVPKLMVELDGDGHPSSCLHPYIGT--LGFLCRAIEFGMSFIRISKEFRDKEIRRRQFITEGVQKIEDFKEEACS 2464
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3374 SDAFSTENGIIVTRGNRWALMIDPQAQALKWIKNMEGGQGLKIIDLQMSDYLRILEHAIHFGYPVLLQnVQEYLDPTLNP 3453
Cdd:COG5245 2465 TDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIG-DAEALDEEIGR 2543
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3454 MLNKSVARIGGRLLMRIGDKEVEYNTNFRFYITTKLSNPHYSPETSAKTTIVNFAVKEQGLEAQLLGIVVRKERPELEEQ 3533
Cdd:COG5245 2544 LIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVH 2623
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3534 KDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLHTSKITATEVTEQLETSETTEINTDLAREAYRPCAQR 3613
Cdd:COG5245 2624 EKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKR 2703
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3614 ASILFFVLNDMGCIDPMYQFSLDAYISLF-ILSIDKSHRSNKLEDRIDYLNDYhtyavyrytcrtLFERHKLLFSFhmca 3692
Cdd:COG5245 2704 LESIRVEIAMFDEKALMYNKSICELSSEFeKWRRMKSKYLCAIRYMLMSSEWI------------LDHEDRSGFIH---- 2767
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3693 kILETSGKLNMDEynfFLRGGVVLDREGQMDNPCSSWLADAYWDNITELDKLTNFhglMNSFEQYPRDWHLWYTnaapek 3772
Cdd:COG5245 2768 -RLDVSFLLRTKR---FVSTLLEDKNYRQVLSSCSLYGNDVISHSCDRFDRDVYR---ALKHQMDNRTHSTILT------ 2834
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3773 amlpgeWENACNEMQRMLIVRSLRQ-DRVAFCVTSFIITnlgsrfieppvlnmKSVLEDSTPRSPLVFILSPGVDptsaL 3851
Cdd:COG5245 2835 ------SNSKTNPYKEYTYNDSWAEaFEVEDSGDLYKFE--------------EGLLELIVGHAPLIYAHKKSLE----N 2890
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3852 LQLAEHMGMAQRfhaLSLGQGQAPIAArllregvTQGHWVFLANCHLSLSWMPN-LDKLVEQLQVEDPHPSF-RLWLSSI 3929
Cdd:COG5245 2891 ERNVDRLGSKEN---EVYAVLNSLFSR-------KEKSWFEVYNISLSFGWFKRyVEDVVYPIKASRVCGKVkNMWTSMV 2960
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3930 PHPDFPISILQVSIKMTTEPPKGLKANMTRLYQLMsepQFSRCSKPAKYKKLLFSLCFFHSVLLERKKFLQLGWNIIYGF 4009
Cdd:COG5245 2961 DADMLPIQLLIAIDSFVSSTYPETGCGYADLVEID---RYPFDYTLVIACDDAFYLSWEHAAVASVISAGPKENNEEIYF 3037
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 4010 NDSDFEVSENLLS--LYLDEYEETPWDALKYLIAGINYGGHVTDDWDRRLLTTYINDYFC--DQSLSTPFHRLSALETYF 4085
Cdd:COG5245 3038 GDKDFEFKTHLLKniLFLNHLNARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGAheTSSQILASVPGGDPELVK 3117
|
2890 2900
....*....|....*....|....
gi 75677365 4086 I-PKDGSLASYKEYISLLPGMDPP 4108
Cdd:COG5245 3118 FhMEEMCRSSAFGVIGQLPDLALC 3141
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4123-4423 |
4.52e-128 |
|
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: 405.47 E-value: 4.52e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 4123 ITEAQTLFDTLLSLQPQITPTRAGG-QTREEKVLELAADVKQKIPEMIDYE-GTQKLLALDPSPLNVVLLQEIQRYNTLM 4200
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGgSSREEIVLELAKDILEKLPEPFDIEeAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 4201 QTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLW-GKAYPSQKPLAAWTRDLAMRVEQFELWASRARPPVIFWL 4279
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWaKKSYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 4280 SGFTFPTGFLTAVLQSSARQNNVSVDSLSWEFIV-STVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVC 4358
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVtKKVSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75677365 4359 LMPTIHFRPAE-SRKKSAKGMYSCPCYYYPNRAGSsdraSFVIGIDLRSGaMTPDHWIKRGTALLM 4423
Cdd:pfam18199 241 PLPVIHLKPVEsDKKKLDENTYECPVYKTSERHST----NFVFSVDLPTD-KPPDHWILRGVALLL 301
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2732-2992 |
8.60e-123 |
|
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: 388.50 E-value: 8.60e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2732 MQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICDYTTFQIEVTKHYRKQEFRDDIKRLYRQAGVE 2811
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2812 LKTTSFIFVDTQIADESFLEDINNILSSGEVPNLYKPDEFEEIQSHIIDQARVEQVPESSDSLFAYLIERVQNNLHIVLC 2891
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2892 LSPMGDPFRNWIRQYPALVNCTTINWFSEWPQEALLEVAEKCLigVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLEL 2971
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFL--EDIEIPEELKSNVVKVFVYVHSSVEDMSKKFYEEL 238
|
250 260
....*....|....*....|.
gi 75677365 2972 RRHNYVTPTKYLELLSGYKKL 2992
Cdd:pfam12780 239 KRKNYVTPKSYLELLRLYKNL 259
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3365-3586 |
4.64e-120 |
|
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: 379.09 E-value: 4.64e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3365 RDWNIQGLPSDAFSTENGIIVTRGNRWALMIDPQAQALKWIKNMEGGQGLKIIDLQMSDYLRILEHAIHFGYPVLLQNVQ 3444
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3445 EYLDPTLNPMLNKSVARIGGRLLMRIGDKEVEYNTNFRFYITTKLSNPHYSPETSAKTTIVNFAVKEQGLEAQLLGIVVR 3524
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75677365 3525 KERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLHTSKITATEV 3586
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
242-717 |
6.54e-113 |
|
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: 372.68 E-value: 6.54e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 242 VQRLETSMIHWTRQIKEMLSAQETvetGENLGPLEEIEFWRNRCMDLSGISKQLVKKGVKHVESILHLAKSSYLAPFMKL 321
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQ---GRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 322 AQQIQDGSRQAQSNLTFLSILKEPYQELAFMK-PKDISSKLPKLISLIRIIWVNSPHYNTRERLTSLFRKVC-------- 392
Cdd:pfam08385 78 DTELTDALNEAKDNVKYLKTLERPFEDLEELTdPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISnqlieqck 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 393 ---------------------DCQYHFARWED------------GKQGP------------------------------- 408
Cdd:pfam08385 158 kylspegifdgdveealeklqECIELLEAWKEeykktrekleesPRERPwdfseryifgrfdaflerlekilelfetieq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 409 ---LPCFFGAQGPQITRNLLEIEDIFHKNLHTLRAVRGGILDVKNTCWHEDYNKFRAGIKDLEVMTQNLITSAFELVRDV 485
Cdd:pfam08385 238 fskLEKIGGTKGPELEGVIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDDARST 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 486 PHGVLLLDTFHRLASREAIKRTYDKKAVDLYMLFNSELALVNR--ERNKKWPD-LEPYVAQYSGKARWVHILRRRIDRVM 562
Cdd:pfam08385 318 ESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKifDKQKYNPSpIAKNMPPVAGAIIWARQLFRRIQEPM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 563 TCLAGAHFLPRIGTGKESVHTYQQMVQAIDELVRKTFQEWTSSLDKDCIRRLDTPLLRISQEKAGMLDVNFDKSLLILFA 642
Cdd:pfam08385 398 KRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGNLKRPLLVRHPETGKLLSVNFDPQLLALLR 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75677365 643 EIDYWERLLFETPHYVVNVAERAEDLRILRENLLLVARDYNRIIAMLSPDEQALFKERIRLLDKKIHPGLKKLHW 717
Cdd:pfam08385 478 EVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTW 552
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2379-2557 |
1.10e-100 |
|
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: 321.65 E-value: 1.10e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2379 YPPNAPFYKIMVPTVDTVRYNYLVSSLVANQNPILLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSII 2458
Cdd:pfam12775 1 IPPDVPFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQDII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2459 ESRVEKRTKGVYVPFGGKSMITFMDDLNMPAKDMFGSQPPLELIRLWIDYGFWYDRTKQTIKYIREMFLMAAMGPPGGGR 2538
Cdd:pfam12775 81 ESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPGGGR 160
|
170
....*....|....*....
gi 75677365 2539 TVISPRLRSRFNIINMTFP 2557
Cdd:pfam12775 161 NDITPRLLRHFNVFNITFP 179
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
3978-4117 |
1.99e-73 |
|
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: 241.98 E-value: 1.99e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3978 YKKLLFSLCFFHSVLLERKKFLQLGWNIIYGFNDSDFEVSENLLSLYLDEY-EETPWDALKYLIAGINYGGHVTDDWDRR 4056
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYdEKIPWDALRYLIGEINYGGRVTDDWDRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75677365 4057 LLTTYINDYFCDQSLSTPFHrLSALeTYFIPKDGSLASYKEYISLLPGMDPPEAFGQHPNA 4117
Cdd:pfam18198 81 LLNTYLEEFFNPEVLEEDFK-FSPS-LYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
3832-3946 |
5.20e-64 |
|
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: 213.85 E-value: 5.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3832 TPRSPLVFILSPGVDPTSALLQLAEHMGMAQRFHALSLGQGQAPIAARLLREGVTQGHWVFLANCHLSLSWMPNLDKLVE 3911
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGFGGKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILE 80
|
90 100 110
....*....|....*....|....*....|....*
gi 75677365 3912 QLQVEDPHPSFRLWLSSIPHPDFPISILQVSIKMT 3946
Cdd:pfam03028 81 ELPEETLHPDFRLWLTSEPSPKFPISILQNSIKIT 115
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
3006-3338 |
9.29e-58 |
|
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: 205.31 E-value: 9.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3006 KLRTGLFKIDETREKVqvmslelEDAKKKVA----EFQKQCE--EYLVIIVQQKREADEQQKAVTANSE-KIAVEEIKCQ 3078
Cdd:pfam12777 2 RLENGLLKLHSTAAQV-------DDLKAKLAaqeaELKQKNEdaDKLIQVVGIEADKVSKEKAIADEEEqKVAVIMKEVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3079 ALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMIL---RGNEP---TWAEAKRQLGE-QN 3151
Cdd:pfam12777 75 EKQKACEEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILmapGGKIPkdkSWKAAKIMMAKvDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3152 FIKSLINFDKDNISDKVLKKIGAYCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRIRMNAALAQLREKQ 3231
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3232 AALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDC 3311
Cdd:pfam12777 235 EKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDI 314
|
330 340
....*....|....*....|....*..
gi 75677365 3312 LLAAAFLSYMGPFLTNYRDEIVNQIWI 3338
Cdd:pfam12777 315 LLISAFISYLGFFTKKYRNELLDKFWI 341
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2253-2371 |
9.29e-33 |
|
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA domain 5 in the dynein heavy chain. This domain is composed of 8 alpha helices.
Pssm-ID: 465532 [Multi-domain] Cd Length: 126 Bit Score: 125.09 E-value: 9.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2253 LQRMFEKLINKMLAFKKDNCKELVPLPEYSGITSLCKLYSALATP---ENGVNPADGENYVTMVEMTFVFSMIWSVCASV 2329
Cdd:pfam17852 1 LEPLFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDEvleYNGVHPLSPDKLKEYLEKLFLFALVWSIGGTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 75677365 2330 DEEGRKRIDSYLREIEGS----FPNKDTVYEYFVDPKIRSWTSFED 2371
Cdd:pfam17852 81 DEDSRKKFDEFLRELFSGldlpPPEKGTVYDYFVDLEKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2411-2549 |
5.07e-24 |
|
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: 100.44 E-value: 5.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2411 PILLVGPVGTGKTSIAQSVLQSLpsSQWSVLVVNMSAQTTSNNVQSIIESRVE--KRTKGVYVPFGGKSMITFMDDLNMP 2488
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL--SNRPVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75677365 2489 AKDMFGSQ-PPLELIRLWIDYGFWYDRTKQTikyirEMFLMAAMGPPGGGRTVISPRLRSRF 2549
Cdd:pfam07728 79 NPDVLNSLlSLLDERRLLLPDGGELVKAAPD-----GFRLIATMNPLDRGLNELSPALRSRF 135
|
|
| AAA_lid_1 |
pfam17857 |
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3. |
2590-2678 |
5.41e-17 |
|
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3.
Pssm-ID: 465535 [Multi-domain] Cd Length: 100 Bit Score: 79.21 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2590 EATLDMYNTVVQRFLPTPTKMHYLFNLRDISKVFQGMLRANKDFHDTKSSITRLWIHECFRVFSDRLVDAADTEAFMGII 2669
Cdd:pfam17857 3 AAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDKIQ 82
|
....*....
gi 75677365 2670 SDKLGSFFD 2678
Cdd:pfam17857 83 MASLKKFFD 91
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2410-2552 |
2.00e-08 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 56.39 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2410 NPILLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPfgGKSMITFMDDLNMPA 2489
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK--AKPGVLFIDEIDSLS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75677365 2490 KDMFGSQppLELIRLWIDYGFWYDRTKqtikyiremFLMAAMGPPGGGrtvISPRLRSRFNII 2552
Cdd:cd00009 98 RGAQNAL--LRVLETLNDLRIDRENVR---------VIGATNRPLLGD---LDRALYDRLDIR 146
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2990-3303 |
1.15e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2990 KKLLGEKRQELLAQANKLRTGLFKIDETREKVQVMSLELEDAKKKVAEFQKQCEEYLVI------IVQQKREADEQQKAV 3063
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdeakkkAEEDKKKADELKKAA 1414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3064 TAN-----------------------SEKIAVEEIKCQA----LADNAQKDLEEALPAlEEAMRALESLNKKDIGEIKSY 3116
Cdd:PTZ00121 1415 AAKkkadeakkkaeekkkadeakkkaEEAKKADEAKKKAeeakKAEEAKKKAEEAKKA-DEAKKKAEEAKKADEAKKKAE 1493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3117 GRPPAQVEIVMQAVMILRGNEPTWAEAKRQLGEQNFIKSLINFDKDNISDKVLKKIGAYCAQPDFQPDIIGRVSLAAKS- 3195
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAe 1573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3196 --LCMWVRAMElygrLYRVVEPKRI-----------RMNAALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQK 3262
Cdd:PTZ00121 1574 edKNMALRKAE----EAKKAEEARIeevmklyeeekKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 75677365 3263 EELRKKSEEMELKLERagmlVSGLAGEKARWEETVQGLEED 3303
Cdd:PTZ00121 1650 EELKKAEEENKIKAAE----EAKKAEEDKKKAEEAKKAEED 1686
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2081-2222 |
5.64e-07 |
|
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: 51.52 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2081 MIVGCTGSGKTASWRILqasLSSLCRAgdpNFNIVrefpLNPKALSLGELYGEYDLSTN--EWTDGILSSVMRtacadek 2158
Cdd:pfam07728 3 LLVGPPGTGKTELAERL---AAALSNR---PVFYV----QLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAAR------- 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75677365 2159 pdEKWILFDGPVDTL---WIENMNSVMDDNKVLTLINGERI-AMPEQVSLLFEVEDL----AMASPATVSRC 2222
Cdd:pfam07728 66 --EGEIAVLDEINRAnpdVLNSLLSLLDERRLLLPDGGELVkAAPDGFRLIATMNPLdrglNELSPALRSRF 135
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2967-3310 |
1.86e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2967 MLLELRRHNyvtptKYLELLSGYKKLLGEKRQELLAQANKLRTglfKIDETREKVQVMSLELEDAKKKVAEFQKQCEEyl 3046
Cdd:COG1196 230 LLLKLRELE-----AELEELEAELEELEAELEELEAELAELEA---ELEELRLELEELELELEEAQAEEYELLAELAR-- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3047 viIVQQKREADEQQKAVTANSEKIAVEEIKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKsygrppAQVEIV 3126
Cdd:COG1196 300 --LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE------ALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3127 MQAVMILRGNEPTWAEAKRQLGEQNFIKSLINFDKDNISDKVLKKIgaycaqpdfqpdiigrvslaakslcmwvRAMELY 3206
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE----------------------------RLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3207 GRLYRVVEPKRIRMNAALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGL 3286
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
330 340
....*....|....*....|....
gi 75677365 3287 AGEKARWEETVQGLEEDLGYLVGD 3310
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVA 527
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2995-3101 |
2.18e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.27 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2995 EKRQELLAQANKLRtglfKIDETREKVQVMSLELEDAKKKVAEFQKQCEEYLVIIVQQ-KREADEQQKAVTANSEKIAvE 3073
Cdd:PRK09510 91 ELQQKQAAEQERLK----QLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAaKAKAEAEAKRAAAAAKKAA-A 165
|
90 100
....*....|....*....|....*...
gi 75677365 3074 EIKCQALADNAQKDLEEALPALEEAMRA 3101
Cdd:PRK09510 166 EAKKKAEAEAAKKAAAEAKKKAEAEAAA 193
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2990-3279 |
4.15e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2990 KKLLGEKRQ--ELLAQANKLRtglfKIDETREKVQVMSLELEDAKKKvAEFQKQCEEylVIIVQQKREADEQQKAVTAN- 3066
Cdd:PTZ00121 1463 KKKAEEAKKadEAKKKAEEAK----KADEAKKKAEEAKKKADEAKKA-AEAKKKADE--AKKAEEAKKADEAKKAEEAKk 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3067 -------SEKIAVEEIKCQALADNAQ--KDLEEALPALEE---AMRALESLNKKDIGEIKSYGRPPAQvEIVMQAVMiLR 3134
Cdd:PTZ00121 1536 adeakkaEEKKKADELKKAEELKKAEekKKAEEAKKAEEDknmALRKAEEAKKAEEARIEEVMKLYEE-EKKMKAEE-AK 1613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3135 GNEPTWAEAKrQLGEQNFIKSLINFDKDNISDKVLKkigAYCAQPDFQPDIIGRVSLAAKSLCMWVRAMELygrlyRVVE 3214
Cdd:PTZ00121 1614 KAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKK---AEELKKAEEENKIKAAEEAKKAEEDKKKAEEA-----KKAE 1684
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75677365 3215 PKRIRMNAALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERA 3279
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2983-3286 |
6.50e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2983 LELLSGYKKLLGEKRQELLAQANKLRTglfKIDETREKVQVMSLELEDAKKKVAEFQKQCEEY------LVIIV----QQ 3052
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEE---ELEELTAELQELEEKLEELRLEVSELEEEIEELqkelyaLANEIsrleQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3053 KREADEQQKAVTANSEKIAVEEIKCQALADNAQKDLEEALPALEEAMRALESLNKKdigeiksygrppaqveivmqavmi 3132
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE------------------------ 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3133 LRGNEPTWAEAKRQLGEQNfiKSLINFDKDniSDKVLKKIGAycaqpdfqpdIIGRVSLAAKSLCMWVRAMElygRLYRV 3212
Cdd:TIGR02168 360 LEELEAELEELESRLEELE--EQLETLRSK--VAQLELQIAS----------LNNEIERLEARLERLEDRRE---RLQQE 422
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75677365 3213 VE-----PKRIRMNAALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKlaqKEELRKKSEEMELKLERAGMLVSGL 3286
Cdd:TIGR02168 423 IEellkkLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA---EQALDAAERELAQLQARLDSLERLQ 498
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2961-3280 |
7.13e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.40 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2961 AQYSQKMLLELRRHNyvtptkylELLSGYKKLLGEKRQ---ELLAQANKLRTGLF---------------KIDETREKVQ 3022
Cdd:pfam01576 21 QQKAESELKELEKKH--------QQLCEEKNALQEQLQaetELCAEAEEMRARLAarkqeleeilhelesRLEEEEERSQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3023 VMSLEledaKKKVAEFQKQCEEYLviivqqKREADEQQK----AVTANSeKIAVEEIKCQALADNAQKDLEEAlPALEEA 3098
Cdd:pfam01576 93 QLQNE----KKKMQQHIQDLEEQL------DEEEAARQKlqleKVTTEA-KIKKLEEDILLLEDQNSKLSKER-KLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3099 MRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMI-LRGNEPTWAE---AKRQL-GEQNFIKSLInfdkdnisdkvlkkig 3173
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEErLKKEEKGRQElekAKRKLeGESTDLQEQI---------------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3174 aycAQPDFQPDIIgRVSLAAKSlcmwvraMELYGRLYRVvEPKRIRMNAALAQLREKQAALAEAQEKL------------ 3241
Cdd:pfam01576 225 ---AELQAQIAEL-RAQLAKKE-------EELQAALARL-EEETAQKNNALKKIRELEAQISELQEDLeseraarnkaek 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 75677365 3242 --REVAEKLEMLKKQYDEKL---AQKEELRKKSEEMELKLERAG 3280
Cdd:pfam01576 293 qrRDLGEELEALKTELEDTLdttAAQQELRSKREQEVTELKKAL 336
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2410-2468 |
2.62e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.29 E-value: 2.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 75677365 2410 NPILLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKG 2468
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG 61
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
923-1455 |
2.99e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 923 PIQTVVEQ-DEDIKKIQTQISSGMTNNASLLQNYLKtwdmyreiweinkdsfiHRYQRlnppvssfvADIARYTEVANNV 1001
Cdd:TIGR00618 297 AHIKAVTQiEQQAQRIHTELQSKMRSRAKLLMKRAA-----------------HVKQQ---------SSIEEQRRLLQTL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1002 QKEETV----TNIQFVLLDCSHLKFSLVQHCNEWQNKFATLL-REMAAGRLLElhtylKENAEKISRPPQTLEElgvslq 1076
Cdd:TIGR00618 351 HSQEIHirdaHEVATSIREISCQQHTLTQHIHTLQQQKTTLTqKLQSLCKELD-----ILQREQATIDTRTSAF------ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1077 lvDALKHDLANVETQIPPIHEQFAILEKYEvpveDSVLEMLDSLNGEWVVFQQTLLDSKQMLKKHKEkfktglIHSADDF 1156
Cdd:TIGR00618 420 --RDLQGQLAHAKKQQELQQRYAELCAAAI----TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ------IHLQETR 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1157 KKKAHtlledfefkGHFtsnvgymsALDQITQVRAMLMAMREEENSLRAnLGIFKIEQPPskdLQNLEKELDALQQiwei 1236
Cdd:TIGR00618 488 KKAVV---------LAR--------LLELQEEPCPLCGSCIHPNPARQD-IDNPGPLTRR---MQRGEQTYAQLET---- 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1237 ardweenwnewktgrflilqteTMETTAHGLfRRLTKLAKEYKDRNWEIIETTRSKIEQFKRTMPLISDLRNPALRERHW 1316
Cdd:TIGR00618 543 ----------------------SEEDVYHQL-TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1317 DQVRDEIQREFDQESEsftlEQIVELGMDQHVEKIGEISASATKELAIEVAlqniAKTWDVTQLdivPYKDKGHHRLRGT 1396
Cdd:TIGR00618 600 TEKLSEAEDMLACEQH----ALLRKLQPEQDLQDVRLHLQQCSQELALKLT----ALHALQLTL---TQERVREHALSIR 668
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 75677365 1397 EEVFQALEDNQVALSTMKASRFVKAFEKDVdhWERCLSLILEVIEMILTVQRQWMYLEN 1455
Cdd:TIGR00618 669 VLPKELLASRQLALQKMQSEKEQLTYWKEM--LAQCQTLLRELETHIEEYDREFNEIEN 725
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2998-3108 |
3.75e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2998 QELLAQANKLRTGLFKIDETREKVQVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIaveeIKC 3077
Cdd:COG1340 146 EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEI----VEA 221
|
90 100 110
....*....|....*....|....*....|.
gi 75677365 3078 QALADNAQKDLEEALPALEEAMRALESLNKK 3108
Cdd:COG1340 222 QEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2983-3316 |
3.84e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2983 LELLSGYKKLLG--EKRQELLAQANKLRTGLFKIDETREKVQVMSLELEDAKKKVAEFQKQCEEYLVI--------IVQQ 3052
Cdd:COG4717 118 LEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslateeeLQDL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3053 KREADEQQKAVTANSEKIAVEEIKCQaladnaqkDLEEALPALEEAMRALESLNKKD---------------IGEIKSYG 3117
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELE--------ELEEELEQLENELEAAALEERLKearlllliaaallalLGLGGSLL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3118 RPPAQVEIVMQAVMILRGNEPTWAEAKRQLGEQNFIKSLINFDKDNISDKVLKKI-GAYCAQPDFQPDIIGRVSLAAKSL 3196
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELlAALGLPPDLSPEELLELLDRIEEL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3197 C-MWVRAMELYGRLYRVVEPKRIR--MNAALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKS--EE 3271
Cdd:COG4717 350 QeLLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEE 429
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 75677365 3272 MELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDCLLAAA 3316
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEL 474
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1802-1923 |
6.14e-04 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 43.05 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 1802 KGPAGTGKTETVKDLGKALGIY-VIVVNCSE---------GLDYKSMG--RMYSGL---AQTGAWGCFDEFNRINIEVLS 1866
Cdd:pfam07728 5 VGPPGTGKTELAERLAAALSNRpVFYVQLTRdtteedlfgRRNIDPGGasWVDGPLvraAREGEIAVLDEINRANPDVLN 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75677365 1867 VVahqiLCILSA----LAAGLTHFHFDGFEINLVwscgifITMNPGYAGRTELPENLKSMF 1923
Cdd:pfam07728 85 SL----LSLLDErrllLPDGGELVKAAPDGFRLI------ATMNPLDRGLNELSPALRSRF 135
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
3219-3279 |
7.32e-04 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 42.19 E-value: 7.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75677365 3219 RMNAALAQLREKQAALAEAQEKLREVAEKLEMLKKQYD---EKLA-QKEELRKKSEEMELKLERA 3279
Cdd:pfam18595 51 KLEEAKKKLKELRDALEEKEIELRELERREERLQRQLEnaqEKLErLREQAEEKREAAQARLEEL 115
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2993-3304 |
9.68e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2993 LGEKRQELLAQANKLRTGLFKIDETREKVQVMSLELEDAKKKVAEFQKQCEEyLVIIVQQKREADEQQKAVTANSEKIAV 3072
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGLSG 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3073 EEikcQALAD--NAQKDLEEALP-ALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAKRQLGE 3149
Cdd:TIGR02168 521 IL---GVLSEliSVDEGYEAAIEaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3150 QNFIKSLINFDKdnisdkvlkkigaycAQPDFQPDIIGRVS--LAAKSLcmwVRAMELYGRL---YRVVEP--KRIRMNA 3222
Cdd:TIGR02168 598 EGFLGVAKDLVK---------------FDPKLRKALSYLLGgvLVVDDL---DNALELAKKLrpgYRIVTLdgDLVRPGG 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3223 ALAQLREKQAALAEAQEK-LREVAEKLEMLKKQYDEKLAQKEELRKKSEEME-------LKLERAGMLVSGLAGEKARWE 3294
Cdd:TIGR02168 660 VITGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlrKELEELSRQISALRKDLARLE 739
|
330
....*....|
gi 75677365 3295 ETVQGLEEDL 3304
Cdd:TIGR02168 740 AEVEQLEERI 749
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3221-3279 |
1.22e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 75677365 3221 NAALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERA 3279
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA 77
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2990-3108 |
1.45e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.07 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2990 KKLLGEKRQELLAQANKLRtglfKIDETREKVQV--MSLELEDAKKKVAEFQKQCEEylviivQQKREADEQQKAVTANS 3067
Cdd:TIGR02794 71 KKLEQQAEEAEKQRAAEQA----RQKELEQRAAAekAAKQAEQAAKQAEEKQKQAEE------AKAKQAAEAKAKAEAEA 140
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 75677365 3068 EKIAVEEIKCQALADNAQKDLEEALPALEEAMRALESLNKK 3108
Cdd:TIGR02794 141 ERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA 181
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
3222-3304 |
1.51e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.47 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3222 AALAQLRE---KQAALA-EAQEKL-REV------AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAgmlvsglageK 3290
Cdd:pfam07926 22 AQLQKLQEdleKQAEIArEAQQNYeRELvlhaedIKALQALREELNELKAEIAELKAEAESAKAELEES----------E 91
|
90
....*....|....
gi 75677365 3291 ARWEETVQGLEEDL 3304
Cdd:pfam07926 92 ESWEEQKKELEKEL 105
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3219-3277 |
1.67e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 1.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75677365 3219 RMNAALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKLA----QKEELRKKSEEMELKLE 3277
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAeleaELEELEAEREELAAKIP 173
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3219-3304 |
1.86e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3219 RMNAALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQ 3298
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
....*.
gi 75677365 3299 GLEEDL 3304
Cdd:COG4372 161 SLQEEL 166
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2995-3295 |
1.92e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 2995 EKRQELLAQANKLRTglfKIDETREKVQVMSLELEDAKKKVAEFQKQCEEYlviivqqKREADEQQKAVTANSEKIavEE 3074
Cdd:COG1340 29 EKRDELNEELKELAE---KRDELNAQVKELREEAQELREKRDELNEKVKEL-------KEERDELNEKLNELREEL--DE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3075 IKcqALADNAQKDLEEaLPALEEAMRALE------SLNKKD----IGEIKSYGRppaQVEIVMQAVmilrgneptwaEAK 3144
Cdd:COG1340 97 LR--KELAELNKAGGS-IDKLRKEIERLEwrqqteVLSPEEekelVEKIKELEK---ELEKAKKAL-----------EKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3145 RQLGE-QNFIKSLinfdKDNISDkVLKKIGAYCAQpdfqpdiIGRVSLAAKSLcmwvramelygrlYRVVEPKRIRMNAA 3223
Cdd:COG1340 160 EKLKElRAELKEL----RKEAEE-IHKKIKELAEE-------AQELHEEMIEL-------------YKEADELRKEADEL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3224 LAQLREKQAALAE-------AQEKLREVAEKLEMLKKQYD--EKLAQKEELRKKSEEMELKLERagmlvsglaGEKARWE 3294
Cdd:COG1340 215 HKEIVEAQEKADElheeiieLQKELRELRKELKKLRKKQRalKREKEKEELEEKAEEIFEKLKK---------GEKLTTE 285
|
.
gi 75677365 3295 E 3295
Cdd:COG1340 286 E 286
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3223-3308 |
2.92e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3223 ALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEE 3302
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
....*.
gi 75677365 3303 DLGYLV 3308
Cdd:TIGR02168 310 RLANLE 315
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3213-3304 |
3.75e-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: 43.51 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677365 3213 VEPKRIRMNAALAQLR----EKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAG 3288
Cdd:TIGR02168 314 LERQLEELEAQLEELEskldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
90
....*....|....*.
gi 75677365 3289 EKARWEETVQGLEEDL 3304
Cdd:TIGR02168 394 QIASLNNEIERLEARL 409
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
3224-3264 |
5.50e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 40.27 E-value: 5.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 75677365 3224 LAQLREKQAA--LAEAQEKLREVAEKLEMLKKQYDEKLAQKEE 3264
Cdd:COG2882 13 LAEKEEDEAAreLGQAQQALEQAEEQLEQLEQYREEYEQRLQQ 55
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
3222-3289 |
9.94e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.94 E-value: 9.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75677365 3222 AALAQLREKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGE 3289
Cdd:pfam05701 121 AAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIE 188
|
|
| |
