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Conserved domains on  [gi|1958754096|ref|XP_038959491|]
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dynein axonemal heavy chain 5 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DHC_N1 pfam08385
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ...
235-787 0e+00

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: 648.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  235 VEKVECCMRVWIKQMEQILAENNQLRKEaddvGPRAELEHWKKRLSKFNYLLDQLKSPDVKAVLAMLAAAKSKLLKVWRD 314
Cdd:pfam08385    1 LHALESVVIKWTKQIQDVLKEDSQGRNP----GPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  315 ADIRVTDAANEAKDNVKYLYTLEKCCDPLYS-SDPVTMVDAIPTLINAIKMIYSISHYYNTSERITSLFVKVTNQMISAC 393
Cdd:pfam08385   77 LDTELTDALNEAKDNVKYLKTLERPFEDLEElTDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  394 KAHITNNGtatIWSQPQDIVMQKIAAAIKLKQGYQCCFQETKQKLKQNPSEKQFDFSEMYIFGKFETFHQRLAKIMDIFT 473
Cdd:pfam08385  157 KKYLSPEG---IFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWDFSERYIFGRFDAFLERLEKILELFE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  474 TFKTYSVLQDSK------IEG-LEDMVTKYQDVVAGIKKKEYNFLDQRKMDFDQDYDEFCKQTNELHSELQRFMDTTFEK 546
Cdd:pfam08385  234 TIEQFSKLEKIGgtkgpeLEGvIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDD 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  547 IQSTRQALSTLKKFE-RLNIPNL--GIEAKYQIVFQNFGTDIDMISKLYTKQKYDP-PLARDQPPIAGKILWARQLFHRL 622
Cdd:pfam08385  314 ARSTESAFKLLRIFEfLLERPIIrgALEEKYTDLLQMFKKELDAVKKIFDKQKYNPsPIAKNMPPVAGAIIWARQLFRRI 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  623 EQPMQLFQQHPFVLRTVEAKPVIRSYNRIAKVLLEFEVLYHRAWLQQIEEIHVG-LEASLLVKAPGTGQLF-VNFDPQIL 700
Cdd:pfam08385  394 QEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGnLKRPLLVRHPETGKLLsVNFDPQLL 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  701 ILFRETQCMSQMGLPVSPFAAALFEKRDMYKKNFSDMKMMLSEYQRVKLKMPPAIEQLMLPHLARVDEALQPGLAVLTWT 780
Cdd:pfam08385  474 ALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTWN 553

                   ....*..
gi 1958754096  781 SLNIGTY 787
Cdd:pfam08385  554 SLGIDEY 560
AAA_6 pfam12774
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ...
1924-2251 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: 592.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1924 YQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKG 2003
Cdd:pfam12774    1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2004 LAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINF 2083
Cdd:pfam12774   81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2084 RSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYQLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRASHTDTESTIV 2163
Cdd:pfam12774  160 RPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2164 MRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELETAISKQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTL 2243
Cdd:pfam12774  240 LRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLV 319

                   ....*...
gi 1958754096 2244 GPSGSGKT 2251
Cdd:pfam12774  320 GPTGSGKT 327
DHC_N2 pfam08393
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ...
1384-1789 3.96e-147

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: 464.81  E-value: 3.96e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1384 LLEIKKQLNLLQKIYSLYNNVIETVNSYQDTLWSEVNIEKINSELLEFQNRCRKLPRALKDWQAFLDMKKTIDDFSECCP 1463
Cdd:pfam08393    1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1464 LLEYMASNAMVERHWQRITTLTGHSLDVGNETFKLRNIMEVPLLKYKEEIEDICISAVKERDIEQKLKQVINEWDNKTLT 1543
Cdd:pfam08393   81 LIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1544 FSSFKTRGELLLRGdsTSEVIASMEDSLMLLGSLLSNRYNMPFKAQIQNWVQCLSNSTDIIENWMTVQNLWIYLEAVFVG 1623
Cdd:pfam08393  161 LVPYKDTGTFILKG--WDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1624 GDIAKQLPKEAKRFSNIDKSWVKIMTRAHEIPNVVQCCvGDETMGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVS 1703
Cdd:pfam08393  239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEAC-NIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLS 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1704 DPALLEILGQASDSHTIQAHLLNVFDNIKTVKFHDkiYDRILSISSREGETIELDKP-VMAEGNVEVWLNSLLEESQSSL 1782
Cdd:pfam08393  318 NDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE--NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMRETL 395

                   ....*..
gi 1958754096 1783 HLVIRQA 1789
Cdd:pfam08393  396 RDLLKEA 402
DYN1 super family cl34955
Dynein, heavy chain [Cytoskeleton];
1625-4267 1.26e-127

Dynein, heavy chain [Cytoskeleton];


The actual alignment was detected with superfamily member COG5245:

Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 454.83  E-value: 1.26e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1625 DIAKQLPKEAKRFSNIDKSWVKIMTRaheipnVVQCCVGDETM----GQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFF 1700
Cdd:COG5245    639 DLMPLIPHAVHRKMSLVSGVRGIYKR------VVSGCEAINTIledvGDDLDLFYKEMDQVFMSIEKVLGLRWREVERAS 712
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1701 FVSDpaLLEILGQASDSHTIQAHLLNVFDNIKTVKFhdkIYDRILSISSREGETIELDKPVMAEGNVEV--WLN----SL 1774
Cdd:COG5245    713 EVEE--LMDRVRELENRVYSYRFFVKKIAKEEMKTV---FSSRIQKKEPFSLDSEAYVGFFRLYEKSIVirGINrsmgRV 787
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1775 LEESQSSLhlvirQAAANIQESGFqlieFLSSFPAQVGLLGIQMlWTRDSEEALQNA------KFDKKIMQKTNQSFLEL 1848
Cdd:COG5245    788 LSQYLESV-----QEALEIEDGSF----FVSRHRVRDGGLEKGR-GCDAWENCFDPPlseyfrILEKIFPSEEGYFFDEV 857
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1849 LNmliemttkdlssmervKYETLITIHVHQRDIFDDLCHMHVKSPTDFEWLKQCRFYFKEDsDKTMIHITDVAFTYQNEF 1928
Cdd:COG5245    858 LK----------------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLY-KRFIKVRSSYRSAEMFAK 920
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1929 LGCTDRLVITPLTDRCYITLAQALGMSMggapAGPAGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSG 2008
Cdd:COG5245    921 NTIPFFVFEHSMDTSQHQKLFEAVCDEV----CRFVDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEE 988
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2009 SWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEHKKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSV 2086
Cdd:COG5245    989 ERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMF 1059
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2087 AMMVPDRQIIIRVKlascgfidnvVLARKFFTLYQLCEEQLSKQVHYDFglrnilsvlRTLGAAKRASH------TDTES 2160
Cdd:COG5245   1060 LSNIPFGAIKSRRE----------SLDREIGAFNNEVDGIAREEDELMF---------YPMFKSLKAKHrmleekTEYLN 1120
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2161 TIVmrvlrdmnlsklidedEPLFLSLIEDLFPNI--LLDKAGYPELETAISKQVEEAGLINHPPWKlKVIQLFETQRVRH 2238
Cdd:COG5245   1121 KIL----------------SITGLPLISDTLRERidTLDAEWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGA 1183
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2239 GMMTLGPSGSGKTSCIHTLMKAMTDCGKPHREMRMnpkaitapqmfgrLDvATNDWTdGIFSTLWRKTLKAK-KGEHIWI 2317
Cdd:COG5245   1184 FHAEYFRVFLCKIKHYTDACDYLWHVKSPYVKKKY-------------FD-ADMELR-QFFLMFNREDMEARlADSKMEY 1248
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2318 VLDGpvdaiWIENLNSVLDDNKTLTLANGDRipmapncKIVFEphNIDnASPATVSRNGMVFMSSSVLDWSPILEGFL-- 2395
Cdd:COG5245   1249 EVER-----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgd 1313
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2396 ------KRRSPQEAEILRQLYAETF-----PDLYRFS--IQNLEFKMEILEAFVITQ-STHMLQGLIPTKEQAGDVD-PE 2460
Cdd:COG5245   1314 tkryldECLDFFSCFEEVQKEIDELsmvfcADALRFSadLYHIVKERRFSGVLAGSDaSESLGGKSIELAAILEHKDlIV 1393
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2461 HLGRLFVFAMMWSVGAVLELEGRRRMELWLRSREGptLHLPQLTDPGDT---MFDYyvapDGTWRHWSMcIPEYVYPPDT 2537
Cdd:COG5245   1394 EMKRGINDVLKLRIFGDKCRESTPRFYLISDGDLI--KDLNERSDYEEMlimMFNI----SAVITNNGS-IAGFELRGER 1466
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2538 TPEYGSILVPNVDNVRTDFLIKTIAKQGKAVLLIGEQGTAKTVIIKG-FMSKFDPEshtVKNLNFS-SATTPLM---FQR 2612
Cdd:COG5245   1467 VMLRKEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPsLRSELITE---VKYFNFStCTMTPSKlsvLER 1543
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2613 TIESYVDKRMGTTYGPPAGKKMAVFIDDLNMPVINEWGDQVTNEIVRQLMEQNGFYN-LEKpgEFTSIVDIqFLAAMIHP 2691
Cdd:COG5245   1544 ETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGACNP 1620
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2692 GG--GRNDIPQRLKRQFSIFNCTLPSDASMDKIFGVIGEGYYCAQRGFSKEVQDAVIKLVPLTRRLWQMTKlkmlpTPAK 2769
Cdd:COG5245   1621 GTdeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTK-----FFLQ 1695
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2770 FHYVFNLRDLSRIWQGMLNITSEVIKDTD-ELLRLWKHECKRVIADRFSMSSDVTWFDKAVVSLVEEEFGEEKTPVVDCG 2848
Cdd:COG5245   1696 MNYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEA 1775
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2849 ----VDAYFVDFlrdapeatgetpeetdAEMPKlyepiASL-NHLQERLSVFlqlYNESIRGTgmdMVFFRDAMVHLVKI 2923
Cdd:COG5245   1776 eitfSMILFFGM----------------ACLLK-----KDLaVFVEEVRKIF---GSSHLDVE---AVAYKDALLHILRS 1828
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2924 SRVIRTPRGNALLVGVGGSGKQSLTRLASFIAGYTSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNEIKEE 3003
Cdd:COG5245   1829 RRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVES 1908
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3004 SFLEYMNNVLSSGEVSNLFARDEIDEINSDLTSIMKKEhPKRPPTNDNLYEYFMSRVRGNLHIVL-CFSPVGEKFRNRAL 3082
Cdd:COG5245   1909 SFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVLAGIR 1987
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3083 kFPALISGCTIDWFSRWPKDALVAVSEHFLS-SYNIDCTAEIKKELVQCMGS-FQDGVAEKCADYFQR-FRRSTHV--TP 3157
Cdd:COG5245   1988 -SPALKNRCFIDFKKLWDTEEMSQYANSVETlSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIEgsLG 2066
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3158 KSYLSFIQG---YKFIYEEKHVEVQSLANRMNTGLEKLKEASESVAALSQELAVKEKELQVANEKADMVLKEVTMKAQAA 3234
Cdd:COG5245   2067 ESKIKFIGGlkvYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLER 2146
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3235 EKVKAEVQKVKDKAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIKPSDIATVRTLGRPPHLIMRIMD--CVLLLF 3312
Cdd:COG5245   2147 EVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCDLLGF 2226
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3313 HRRVnavkidldksctvpsWQESLKLMTAGNFLQNLQQFPkDTIN--------EEVIEFLSPYFEMSDYNieTAKRVCGN 3384
Cdd:COG5245   2227 EAKI---------------WFGEQQSLRRDDFIRIIGKYP-DEIEfdlearrfREARECSDPSFTGSILN--RASKACGP 2288
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3385 vagLCSWTKAMASFFSINKEVLPLKANLIVQENRHALAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDADRC 3464
Cdd:COG5245   2289 ---LKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTV 2365
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3465 RHKMQTASTLISGLAGEKERWTEQSKEFAAQIKRLVGDVLLATAFLSYSGPFNQEFRDLLLNDWKKEMkARKIPFGNDLN 3544
Cdd:COG5245   2366 HKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGMSFIRI-SKEFRDKEIRR 2444
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3545 LNEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTKASRSPLLIDPQTQGKIWIRNKESQNELQITSLNHKYFRNHLEDSLS 3624
Cdd:COG5245   2445 RQFITEGVQKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARR 2524
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3625 LGRPLLIEDvGEELDPALDNVLEKNFIKTGSTFKVKVGDKEVDVMDGFKLYITTKLPNPAYTPEISARTAIIDFTVTVKG 3704
Cdd:COG5245   2525 EGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLG 2603
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3705 LEDQLLGRVILTEKQELEKERTHLLEEVTANKRRTKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKKTAEEVTQKLEIS 3784
Cdd:COG5245   2604 CETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESES 2683
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3785 GETEIQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLFDlsLARSVKSPITSKrigniIEHMTYEVFKY 3864
Cdd:COG5245   2684 MEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFE--KWRRMKSKYLCA-----IRYMLMSSEWI 2756
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3865 avqgLYEEhkflFTLLLTLKIDIQRNLVKHEEFLTLIK-GGASLDLKACPHKPSKWILD-------MTWLNLVELSKLKQ 3936
Cdd:COG5245   2757 ----LDHE----DRSGFIHRLDVSFLLRTKRFVSTLLEdKNYRQVLSSCSLYGNDVISHscdrfdrDVYRALKHQMDNRT 2828
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3937 FSDILDQISRNEklwriWFDKEnpeeeplpnaydksldcfrrlLLIRSWcpdrtiaqARKYIMDSMGENYaegvilDLEK 4016
Cdd:COG5245   2829 HSTILTSNSKTN-----PYKEY---------------------TYNDSW--------AEAFEVEDSGDLY------KFEE 2868
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4017 -TWEESDPRTPLICLLsMGSDPTDSIIalgKRLKIETRyvsmgqgqEVHARKLLHQTMANGGWVLLQNCHLGLDFLDELM 4095
Cdd:COG5245   2869 gLLELIVGHAPLIYAH-KKSLENERNV---DRLGSKEN--------EVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYV 2936
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4096 -DVVTET---ETVHDTFRLWITTEVHKQFPITLLQMSIKFANEppqglraglrrTYGGVSQDLLDVsVGAQWKPMLYA-- 4169
Cdd:COG5245   2937 eDVVYPIkasRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSS-----------TYPETGCGYADL-VEIDRYPFDYTlv 3004
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4170 --------VAFLHSTVQERRKFGPLGWNIPYEFNQADFNATVQFIQNHLdDMDIKKGVSWTTVRYMIGEIQYGGR----- 4236
Cdd:COG5245   3005 iacddafyLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNIL-FLNHLNARKWGNNRDLIFTIVYGKKhslme 3083
                         2730      2740      2750
                   ....*....|....*....|....*....|....
gi 1958754096 4237 ---VTDDYDKRLLNTFAKVWFSENMFGPDFTFYQ 4267
Cdd:COG5245   3084 dskVVDKYCRGYGAHETSSQILASVPGGDPELVK 3117
Dynein_C pfam18199
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ...
4311-4603 8.41e-125

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: 396.22  E-value: 8.41e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4311 AKDVLDTILGIQPKDSSG--GGDETREAVVARLADDMLEKLPEDYSpFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSL 4388
Cdd:pfam18199    4 TNELLSTLLSLQPRSDSGggGGGSSREEIVLELAKDILEKLPEPFD-IEEAEEKYPVGYEDPLNTVLLQEIERFNKLLKV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4389 VRSTLTELKLAVDGTIIMSDNLRDALDCMFDARIPARWKKASWVSS-TLGFWFTELLERNCQFTSWVS-NGRPHCFWMTG 4466
Cdd:pfam18199   83 IRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLkPLGSWIRDLLERLKQLQDWLDdEGPPKVFWLSG 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4467 FFNPQGFLTAMRQEITRANKgWALDNMVLCNEVTKFM-KDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFEL 4545
Cdd:pfam18199  163 FFFPQAFLTAVLQNYARKNG-WPIDKLSFDFEVTKKVsPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFSP 241
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4546 MPVIRIFAENNT--ARDPRLYCCPIYKKPVRTDLNYIAAVDLKTAQAPEHWILRGVALLC 4603
Cdd:pfam18199  242 LPVIHLKPVESDkkKLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVALLL 301
 
Name Accession Description Interval E-value
DHC_N1 pfam08385
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ...
235-787 0e+00

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: 648.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  235 VEKVECCMRVWIKQMEQILAENNQLRKEaddvGPRAELEHWKKRLSKFNYLLDQLKSPDVKAVLAMLAAAKSKLLKVWRD 314
Cdd:pfam08385    1 LHALESVVIKWTKQIQDVLKEDSQGRNP----GPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  315 ADIRVTDAANEAKDNVKYLYTLEKCCDPLYS-SDPVTMVDAIPTLINAIKMIYSISHYYNTSERITSLFVKVTNQMISAC 393
Cdd:pfam08385   77 LDTELTDALNEAKDNVKYLKTLERPFEDLEElTDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  394 KAHITNNGtatIWSQPQDIVMQKIAAAIKLKQGYQCCFQETKQKLKQNPSEKQFDFSEMYIFGKFETFHQRLAKIMDIFT 473
Cdd:pfam08385  157 KKYLSPEG---IFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWDFSERYIFGRFDAFLERLEKILELFE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  474 TFKTYSVLQDSK------IEG-LEDMVTKYQDVVAGIKKKEYNFLDQRKMDFDQDYDEFCKQTNELHSELQRFMDTTFEK 546
Cdd:pfam08385  234 TIEQFSKLEKIGgtkgpeLEGvIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDD 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  547 IQSTRQALSTLKKFE-RLNIPNL--GIEAKYQIVFQNFGTDIDMISKLYTKQKYDP-PLARDQPPIAGKILWARQLFHRL 622
Cdd:pfam08385  314 ARSTESAFKLLRIFEfLLERPIIrgALEEKYTDLLQMFKKELDAVKKIFDKQKYNPsPIAKNMPPVAGAIIWARQLFRRI 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  623 EQPMQLFQQHPFVLRTVEAKPVIRSYNRIAKVLLEFEVLYHRAWLQQIEEIHVG-LEASLLVKAPGTGQLF-VNFDPQIL 700
Cdd:pfam08385  394 QEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGnLKRPLLVRHPETGKLLsVNFDPQLL 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  701 ILFRETQCMSQMGLPVSPFAAALFEKRDMYKKNFSDMKMMLSEYQRVKLKMPPAIEQLMLPHLARVDEALQPGLAVLTWT 780
Cdd:pfam08385  474 ALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTWN 553

                   ....*..
gi 1958754096  781 SLNIGTY 787
Cdd:pfam08385  554 SLGIDEY 560
AAA_6 pfam12774
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ...
1924-2251 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: 592.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1924 YQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKG 2003
Cdd:pfam12774    1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2004 LAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINF 2083
Cdd:pfam12774   81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2084 RSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYQLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRASHTDTESTIV 2163
Cdd:pfam12774  160 RPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2164 MRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELETAISKQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTL 2243
Cdd:pfam12774  240 LRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLV 319

                   ....*...
gi 1958754096 2244 GPSGSGKT 2251
Cdd:pfam12774  320 GPTGSGKT 327
DHC_N2 pfam08393
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ...
1384-1789 3.96e-147

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: 464.81  E-value: 3.96e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1384 LLEIKKQLNLLQKIYSLYNNVIETVNSYQDTLWSEVNIEKINSELLEFQNRCRKLPRALKDWQAFLDMKKTIDDFSECCP 1463
Cdd:pfam08393    1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1464 LLEYMASNAMVERHWQRITTLTGHSLDVGNETFKLRNIMEVPLLKYKEEIEDICISAVKERDIEQKLKQVINEWDNKTLT 1543
Cdd:pfam08393   81 LIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1544 FSSFKTRGELLLRGdsTSEVIASMEDSLMLLGSLLSNRYNMPFKAQIQNWVQCLSNSTDIIENWMTVQNLWIYLEAVFVG 1623
Cdd:pfam08393  161 LVPYKDTGTFILKG--WDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1624 GDIAKQLPKEAKRFSNIDKSWVKIMTRAHEIPNVVQCCvGDETMGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVS 1703
Cdd:pfam08393  239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEAC-NIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLS 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1704 DPALLEILGQASDSHTIQAHLLNVFDNIKTVKFHDkiYDRILSISSREGETIELDKP-VMAEGNVEVWLNSLLEESQSSL 1782
Cdd:pfam08393  318 NDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE--NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMRETL 395

                   ....*..
gi 1958754096 1783 HLVIRQA 1789
Cdd:pfam08393  396 RDLLKEA 402
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
1625-4267 1.26e-127

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 454.83  E-value: 1.26e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1625 DIAKQLPKEAKRFSNIDKSWVKIMTRaheipnVVQCCVGDETM----GQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFF 1700
Cdd:COG5245    639 DLMPLIPHAVHRKMSLVSGVRGIYKR------VVSGCEAINTIledvGDDLDLFYKEMDQVFMSIEKVLGLRWREVERAS 712
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1701 FVSDpaLLEILGQASDSHTIQAHLLNVFDNIKTVKFhdkIYDRILSISSREGETIELDKPVMAEGNVEV--WLN----SL 1774
Cdd:COG5245    713 EVEE--LMDRVRELENRVYSYRFFVKKIAKEEMKTV---FSSRIQKKEPFSLDSEAYVGFFRLYEKSIVirGINrsmgRV 787
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1775 LEESQSSLhlvirQAAANIQESGFqlieFLSSFPAQVGLLGIQMlWTRDSEEALQNA------KFDKKIMQKTNQSFLEL 1848
Cdd:COG5245    788 LSQYLESV-----QEALEIEDGSF----FVSRHRVRDGGLEKGR-GCDAWENCFDPPlseyfrILEKIFPSEEGYFFDEV 857
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1849 LNmliemttkdlssmervKYETLITIHVHQRDIFDDLCHMHVKSPTDFEWLKQCRFYFKEDsDKTMIHITDVAFTYQNEF 1928
Cdd:COG5245    858 LK----------------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLY-KRFIKVRSSYRSAEMFAK 920
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1929 LGCTDRLVITPLTDRCYITLAQALGMSMggapAGPAGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSG 2008
Cdd:COG5245    921 NTIPFFVFEHSMDTSQHQKLFEAVCDEV----CRFVDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEE 988
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2009 SWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEHKKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSV 2086
Cdd:COG5245    989 ERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMF 1059
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2087 AMMVPDRQIIIRVKlascgfidnvVLARKFFTLYQLCEEQLSKQVHYDFglrnilsvlRTLGAAKRASH------TDTES 2160
Cdd:COG5245   1060 LSNIPFGAIKSRRE----------SLDREIGAFNNEVDGIAREEDELMF---------YPMFKSLKAKHrmleekTEYLN 1120
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2161 TIVmrvlrdmnlsklidedEPLFLSLIEDLFPNI--LLDKAGYPELETAISKQVEEAGLINHPPWKlKVIQLFETQRVRH 2238
Cdd:COG5245   1121 KIL----------------SITGLPLISDTLRERidTLDAEWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGA 1183
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2239 GMMTLGPSGSGKTSCIHTLMKAMTDCGKPHREMRMnpkaitapqmfgrLDvATNDWTdGIFSTLWRKTLKAK-KGEHIWI 2317
Cdd:COG5245   1184 FHAEYFRVFLCKIKHYTDACDYLWHVKSPYVKKKY-------------FD-ADMELR-QFFLMFNREDMEARlADSKMEY 1248
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2318 VLDGpvdaiWIENLNSVLDDNKTLTLANGDRipmapncKIVFEphNIDnASPATVSRNGMVFMSSSVLDWSPILEGFL-- 2395
Cdd:COG5245   1249 EVER-----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgd 1313
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2396 ------KRRSPQEAEILRQLYAETF-----PDLYRFS--IQNLEFKMEILEAFVITQ-STHMLQGLIPTKEQAGDVD-PE 2460
Cdd:COG5245   1314 tkryldECLDFFSCFEEVQKEIDELsmvfcADALRFSadLYHIVKERRFSGVLAGSDaSESLGGKSIELAAILEHKDlIV 1393
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2461 HLGRLFVFAMMWSVGAVLELEGRRRMELWLRSREGptLHLPQLTDPGDT---MFDYyvapDGTWRHWSMcIPEYVYPPDT 2537
Cdd:COG5245   1394 EMKRGINDVLKLRIFGDKCRESTPRFYLISDGDLI--KDLNERSDYEEMlimMFNI----SAVITNNGS-IAGFELRGER 1466
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2538 TPEYGSILVPNVDNVRTDFLIKTIAKQGKAVLLIGEQGTAKTVIIKG-FMSKFDPEshtVKNLNFS-SATTPLM---FQR 2612
Cdd:COG5245   1467 VMLRKEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPsLRSELITE---VKYFNFStCTMTPSKlsvLER 1543
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2613 TIESYVDKRMGTTYGPPAGKKMAVFIDDLNMPVINEWGDQVTNEIVRQLMEQNGFYN-LEKpgEFTSIVDIqFLAAMIHP 2691
Cdd:COG5245   1544 ETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGACNP 1620
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2692 GG--GRNDIPQRLKRQFSIFNCTLPSDASMDKIFGVIGEGYYCAQRGFSKEVQDAVIKLVPLTRRLWQMTKlkmlpTPAK 2769
Cdd:COG5245   1621 GTdeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTK-----FFLQ 1695
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2770 FHYVFNLRDLSRIWQGMLNITSEVIKDTD-ELLRLWKHECKRVIADRFSMSSDVTWFDKAVVSLVEEEFGEEKTPVVDCG 2848
Cdd:COG5245   1696 MNYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEA 1775
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2849 ----VDAYFVDFlrdapeatgetpeetdAEMPKlyepiASL-NHLQERLSVFlqlYNESIRGTgmdMVFFRDAMVHLVKI 2923
Cdd:COG5245   1776 eitfSMILFFGM----------------ACLLK-----KDLaVFVEEVRKIF---GSSHLDVE---AVAYKDALLHILRS 1828
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2924 SRVIRTPRGNALLVGVGGSGKQSLTRLASFIAGYTSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNEIKEE 3003
Cdd:COG5245   1829 RRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVES 1908
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3004 SFLEYMNNVLSSGEVSNLFARDEIDEINSDLTSIMKKEhPKRPPTNDNLYEYFMSRVRGNLHIVL-CFSPVGEKFRNRAL 3082
Cdd:COG5245   1909 SFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVLAGIR 1987
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3083 kFPALISGCTIDWFSRWPKDALVAVSEHFLS-SYNIDCTAEIKKELVQCMGS-FQDGVAEKCADYFQR-FRRSTHV--TP 3157
Cdd:COG5245   1988 -SPALKNRCFIDFKKLWDTEEMSQYANSVETlSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIEgsLG 2066
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3158 KSYLSFIQG---YKFIYEEKHVEVQSLANRMNTGLEKLKEASESVAALSQELAVKEKELQVANEKADMVLKEVTMKAQAA 3234
Cdd:COG5245   2067 ESKIKFIGGlkvYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLER 2146
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3235 EKVKAEVQKVKDKAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIKPSDIATVRTLGRPPHLIMRIMD--CVLLLF 3312
Cdd:COG5245   2147 EVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCDLLGF 2226
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3313 HRRVnavkidldksctvpsWQESLKLMTAGNFLQNLQQFPkDTIN--------EEVIEFLSPYFEMSDYNieTAKRVCGN 3384
Cdd:COG5245   2227 EAKI---------------WFGEQQSLRRDDFIRIIGKYP-DEIEfdlearrfREARECSDPSFTGSILN--RASKACGP 2288
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3385 vagLCSWTKAMASFFSINKEVLPLKANLIVQENRHALAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDADRC 3464
Cdd:COG5245   2289 ---LKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTV 2365
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3465 RHKMQTASTLISGLAGEKERWTEQSKEFAAQIKRLVGDVLLATAFLSYSGPFNQEFRDLLLNDWKKEMkARKIPFGNDLN 3544
Cdd:COG5245   2366 HKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGMSFIRI-SKEFRDKEIRR 2444
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3545 LNEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTKASRSPLLIDPQTQGKIWIRNKESQNELQITSLNHKYFRNHLEDSLS 3624
Cdd:COG5245   2445 RQFITEGVQKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARR 2524
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3625 LGRPLLIEDvGEELDPALDNVLEKNFIKTGSTFKVKVGDKEVDVMDGFKLYITTKLPNPAYTPEISARTAIIDFTVTVKG 3704
Cdd:COG5245   2525 EGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLG 2603
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3705 LEDQLLGRVILTEKQELEKERTHLLEEVTANKRRTKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKKTAEEVTQKLEIS 3784
Cdd:COG5245   2604 CETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESES 2683
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3785 GETEIQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLFDlsLARSVKSPITSKrigniIEHMTYEVFKY 3864
Cdd:COG5245   2684 MEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFE--KWRRMKSKYLCA-----IRYMLMSSEWI 2756
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3865 avqgLYEEhkflFTLLLTLKIDIQRNLVKHEEFLTLIK-GGASLDLKACPHKPSKWILD-------MTWLNLVELSKLKQ 3936
Cdd:COG5245   2757 ----LDHE----DRSGFIHRLDVSFLLRTKRFVSTLLEdKNYRQVLSSCSLYGNDVISHscdrfdrDVYRALKHQMDNRT 2828
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3937 FSDILDQISRNEklwriWFDKEnpeeeplpnaydksldcfrrlLLIRSWcpdrtiaqARKYIMDSMGENYaegvilDLEK 4016
Cdd:COG5245   2829 HSTILTSNSKTN-----PYKEY---------------------TYNDSW--------AEAFEVEDSGDLY------KFEE 2868
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4017 -TWEESDPRTPLICLLsMGSDPTDSIIalgKRLKIETRyvsmgqgqEVHARKLLHQTMANGGWVLLQNCHLGLDFLDELM 4095
Cdd:COG5245   2869 gLLELIVGHAPLIYAH-KKSLENERNV---DRLGSKEN--------EVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYV 2936
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4096 -DVVTET---ETVHDTFRLWITTEVHKQFPITLLQMSIKFANEppqglraglrrTYGGVSQDLLDVsVGAQWKPMLYA-- 4169
Cdd:COG5245   2937 eDVVYPIkasRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSS-----------TYPETGCGYADL-VEIDRYPFDYTlv 3004
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4170 --------VAFLHSTVQERRKFGPLGWNIPYEFNQADFNATVQFIQNHLdDMDIKKGVSWTTVRYMIGEIQYGGR----- 4236
Cdd:COG5245   3005 iacddafyLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNIL-FLNHLNARKWGNNRDLIFTIVYGKKhslme 3083
                         2730      2740      2750
                   ....*....|....*....|....*....|....
gi 1958754096 4237 ---VTDDYDKRLLNTFAKVWFSENMFGPDFTFYQ 4267
Cdd:COG5245   3084 dskVVDKYCRGYGAHETSSQILASVPGGDPELVK 3117
Dynein_C pfam18199
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ...
4311-4603 8.41e-125

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: 396.22  E-value: 8.41e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4311 AKDVLDTILGIQPKDSSG--GGDETREAVVARLADDMLEKLPEDYSpFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSL 4388
Cdd:pfam18199    4 TNELLSTLLSLQPRSDSGggGGGSSREEIVLELAKDILEKLPEPFD-IEEAEEKYPVGYEDPLNTVLLQEIERFNKLLKV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4389 VRSTLTELKLAVDGTIIMSDNLRDALDCMFDARIPARWKKASWVSS-TLGFWFTELLERNCQFTSWVS-NGRPHCFWMTG 4466
Cdd:pfam18199   83 IRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLkPLGSWIRDLLERLKQLQDWLDdEGPPKVFWLSG 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4467 FFNPQGFLTAMRQEITRANKgWALDNMVLCNEVTKFM-KDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFEL 4545
Cdd:pfam18199  163 FFFPQAFLTAVLQNYARKNG-WPIDKLSFDFEVTKKVsPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFSP 241
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4546 MPVIRIFAENNT--ARDPRLYCCPIYKKPVRTDLNYIAAVDLKTAQAPEHWILRGVALLC 4603
Cdd:pfam18199  242 LPVIHLKPVESDkkKLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVALLL 301
AAA_9 pfam12781
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ...
3556-3777 2.25e-114

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: 362.92  E-value: 2.25e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3556 SEWNLQGLPNDDLSIQNGIIVTKASRSPLLIDPQTQGKIWIRNKESQNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVG 3635
Cdd:pfam12781    1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3636 EELDPALDNVLEKNFIKTGSTFKVKVGDKEVDVMDGFKLYITTKLPNPAYTPEISARTAIIDFTVTVKGLEDQLLGRVIL 3715
Cdd:pfam12781   81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958754096 3716 TEKQELEKERTHLLEEVTANKRRTKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKKTAEEV 3777
Cdd:pfam12781  161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
3181-3282 2.12e-07

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 53.81  E-value: 2.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3181 LANRMNTGLEKLKEASESVAALSQELAVKEKELQVANEKADMVLKEVTMKAQA-----AEKVKAEVQKVKDKAQAIVDSi 3255
Cdd:PRK07352    48 LEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAiraeiEKQAIEDMARLKQTAAADLSA- 126
                           90       100
                   ....*....|....*....|....*..
gi 1958754096 3256 SKDKAIAEEKLEAAKPALEEAEAALQT 3282
Cdd:PRK07352   127 EQERVIAQLRREAAELAIAKAESQLPG 153
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
3190-3279 1.21e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.92  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3190 EKLKEASESVAALSQELAVKEKElqVANEKADmvlKEVTMKAQAAEKVKAEVQKVKDKAQAivdsisKDKAIAEEKLeAA 3269
Cdd:TIGR02794  124 AKAKQAAEAKAKAEAEAERKAKE--EAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEA------KAKAEAEAKA-KA 191
                           90
                   ....*....|
gi 1958754096 3270 KPALEEAEAA 3279
Cdd:TIGR02794  192 EEAKAKAEAA 201
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
3181-3281 8.30e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 42.42  E-value: 8.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3181 LANRMNTGLEKLKEASESVAALSQELAVKEKELQVANEKADMVLKE-----VTMKAQAAEKVKAEVQKVKDKAQAIVDSi 3255
Cdd:cd06503     28 LDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEAERILEQAKAEIEQ- 106
                           90       100
                   ....*....|....*....|....*.
gi 1958754096 3256 SKDKAIAEEKLEAAKPALEEAEAALQ 3281
Cdd:cd06503    107 EKEKALAELRKEVADLAVEAAEKILG 132
 
Name Accession Description Interval E-value
DHC_N1 pfam08385
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ...
235-787 0e+00

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: 648.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  235 VEKVECCMRVWIKQMEQILAENNQLRKEaddvGPRAELEHWKKRLSKFNYLLDQLKSPDVKAVLAMLAAAKSKLLKVWRD 314
Cdd:pfam08385    1 LHALESVVIKWTKQIQDVLKEDSQGRNP----GPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  315 ADIRVTDAANEAKDNVKYLYTLEKCCDPLYS-SDPVTMVDAIPTLINAIKMIYSISHYYNTSERITSLFVKVTNQMISAC 393
Cdd:pfam08385   77 LDTELTDALNEAKDNVKYLKTLERPFEDLEElTDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQC 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  394 KAHITNNGtatIWSQPQDIVMQKIAAAIKLKQGYQCCFQETKQKLKQNPSEKQFDFSEMYIFGKFETFHQRLAKIMDIFT 473
Cdd:pfam08385  157 KKYLSPEG---IFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWDFSERYIFGRFDAFLERLEKILELFE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  474 TFKTYSVLQDSK------IEG-LEDMVTKYQDVVAGIKKKEYNFLDQRKMDFDQDYDEFCKQTNELHSELQRFMDTTFEK 546
Cdd:pfam08385  234 TIEQFSKLEKIGgtkgpeLEGvIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDD 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  547 IQSTRQALSTLKKFE-RLNIPNL--GIEAKYQIVFQNFGTDIDMISKLYTKQKYDP-PLARDQPPIAGKILWARQLFHRL 622
Cdd:pfam08385  314 ARSTESAFKLLRIFEfLLERPIIrgALEEKYTDLLQMFKKELDAVKKIFDKQKYNPsPIAKNMPPVAGAIIWARQLFRRI 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  623 EQPMQLFQQHPFVLRTVEAKPVIRSYNRIAKVLLEFEVLYHRAWLQQIEEIHVG-LEASLLVKAPGTGQLF-VNFDPQIL 700
Cdd:pfam08385  394 QEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGnLKRPLLVRHPETGKLLsVNFDPQLL 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096  701 ILFRETQCMSQMGLPVSPFAAALFEKRDMYKKNFSDMKMMLSEYQRVKLKMPPAIEQLMLPHLARVDEALQPGLAVLTWT 780
Cdd:pfam08385  474 ALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTWN 553

                   ....*..
gi 1958754096  781 SLNIGTY 787
Cdd:pfam08385  554 SLGIDEY 560
AAA_6 pfam12774
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ...
1924-2251 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: 592.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1924 YQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKG 2003
Cdd:pfam12774    1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2004 LAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINF 2083
Cdd:pfam12774   81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2084 RSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYQLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRASHTDTESTIV 2163
Cdd:pfam12774  160 RPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2164 MRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELETAISKQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTL 2243
Cdd:pfam12774  240 LRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLV 319

                   ....*...
gi 1958754096 2244 GPSGSGKT 2251
Cdd:pfam12774  320 GPTGSGKT 327
DHC_N2 pfam08393
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ...
1384-1789 3.96e-147

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: 464.81  E-value: 3.96e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1384 LLEIKKQLNLLQKIYSLYNNVIETVNSYQDTLWSEVNIEKINSELLEFQNRCRKLPRALKDWQAFLDMKKTIDDFSECCP 1463
Cdd:pfam08393    1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1464 LLEYMASNAMVERHWQRITTLTGHSLDVGNETFKLRNIMEVPLLKYKEEIEDICISAVKERDIEQKLKQVINEWDNKTLT 1543
Cdd:pfam08393   81 LIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1544 FSSFKTRGELLLRGdsTSEVIASMEDSLMLLGSLLSNRYNMPFKAQIQNWVQCLSNSTDIIENWMTVQNLWIYLEAVFVG 1623
Cdd:pfam08393  161 LVPYKDTGTFILKG--WDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1624 GDIAKQLPKEAKRFSNIDKSWVKIMTRAHEIPNVVQCCvGDETMGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVS 1703
Cdd:pfam08393  239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEAC-NIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLS 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1704 DPALLEILGQASDSHTIQAHLLNVFDNIKTVKFHDkiYDRILSISSREGETIELDKP-VMAEGNVEVWLNSLLEESQSSL 1782
Cdd:pfam08393  318 NDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE--NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMRETL 395

                   ....*..
gi 1958754096 1783 HLVIRQA 1789
Cdd:pfam08393  396 RDLLKEA 402
DYN1 COG5245
Dynein, heavy chain [Cytoskeleton];
1625-4267 1.26e-127

Dynein, heavy chain [Cytoskeleton];


Pssm-ID: 227570 [Multi-domain]  Cd Length: 3164  Bit Score: 454.83  E-value: 1.26e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1625 DIAKQLPKEAKRFSNIDKSWVKIMTRaheipnVVQCCVGDETM----GQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFF 1700
Cdd:COG5245    639 DLMPLIPHAVHRKMSLVSGVRGIYKR------VVSGCEAINTIledvGDDLDLFYKEMDQVFMSIEKVLGLRWREVERAS 712
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1701 FVSDpaLLEILGQASDSHTIQAHLLNVFDNIKTVKFhdkIYDRILSISSREGETIELDKPVMAEGNVEV--WLN----SL 1774
Cdd:COG5245    713 EVEE--LMDRVRELENRVYSYRFFVKKIAKEEMKTV---FSSRIQKKEPFSLDSEAYVGFFRLYEKSIVirGINrsmgRV 787
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1775 LEESQSSLhlvirQAAANIQESGFqlieFLSSFPAQVGLLGIQMlWTRDSEEALQNA------KFDKKIMQKTNQSFLEL 1848
Cdd:COG5245    788 LSQYLESV-----QEALEIEDGSF----FVSRHRVRDGGLEKGR-GCDAWENCFDPPlseyfrILEKIFPSEEGYFFDEV 857
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1849 LNmliemttkdlssmervKYETLITIHVHQRDIFDDLCHMHVKSPTDFEWLKQCRFYFKEDsDKTMIHITDVAFTYQNEF 1928
Cdd:COG5245    858 LK----------------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLY-KRFIKVRSSYRSAEMFAK 920
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 1929 LGCTDRLVITPLTDRCYITLAQALGMSMggapAGPAGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSG 2008
Cdd:COG5245    921 NTIPFFVFEHSMDTSQHQKLFEAVCDEV----CRFVDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEE 988
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2009 SWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEHKKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSV 2086
Cdd:COG5245    989 ERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMF 1059
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2087 AMMVPDRQIIIRVKlascgfidnvVLARKFFTLYQLCEEQLSKQVHYDFglrnilsvlRTLGAAKRASH------TDTES 2160
Cdd:COG5245   1060 LSNIPFGAIKSRRE----------SLDREIGAFNNEVDGIAREEDELMF---------YPMFKSLKAKHrmleekTEYLN 1120
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2161 TIVmrvlrdmnlsklidedEPLFLSLIEDLFPNI--LLDKAGYPELETAISKQVEEAGLINHPPWKlKVIQLFETQRVRH 2238
Cdd:COG5245   1121 KIL----------------SITGLPLISDTLRERidTLDAEWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGA 1183
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2239 GMMTLGPSGSGKTSCIHTLMKAMTDCGKPHREMRMnpkaitapqmfgrLDvATNDWTdGIFSTLWRKTLKAK-KGEHIWI 2317
Cdd:COG5245   1184 FHAEYFRVFLCKIKHYTDACDYLWHVKSPYVKKKY-------------FD-ADMELR-QFFLMFNREDMEARlADSKMEY 1248
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2318 VLDGpvdaiWIENLNSVLDDNKTLTLANGDRipmapncKIVFEphNIDnASPATVSRNGMVFMSSSVLDWSPILEGFL-- 2395
Cdd:COG5245   1249 EVER-----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgd 1313
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2396 ------KRRSPQEAEILRQLYAETF-----PDLYRFS--IQNLEFKMEILEAFVITQ-STHMLQGLIPTKEQAGDVD-PE 2460
Cdd:COG5245   1314 tkryldECLDFFSCFEEVQKEIDELsmvfcADALRFSadLYHIVKERRFSGVLAGSDaSESLGGKSIELAAILEHKDlIV 1393
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2461 HLGRLFVFAMMWSVGAVLELEGRRRMELWLRSREGptLHLPQLTDPGDT---MFDYyvapDGTWRHWSMcIPEYVYPPDT 2537
Cdd:COG5245   1394 EMKRGINDVLKLRIFGDKCRESTPRFYLISDGDLI--KDLNERSDYEEMlimMFNI----SAVITNNGS-IAGFELRGER 1466
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2538 TPEYGSILVPNVDNVRTDFLIKTIAKQGKAVLLIGEQGTAKTVIIKG-FMSKFDPEshtVKNLNFS-SATTPLM---FQR 2612
Cdd:COG5245   1467 VMLRKEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPsLRSELITE---VKYFNFStCTMTPSKlsvLER 1543
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2613 TIESYVDKRMGTTYGPPAGKKMAVFIDDLNMPVINEWGDQVTNEIVRQLMEQNGFYN-LEKpgEFTSIVDIqFLAAMIHP 2691
Cdd:COG5245   1544 ETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGACNP 1620
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2692 GG--GRNDIPQRLKRQFSIFNCTLPSDASMDKIFGVIGEGYYCAQRGFSKEVQDAVIKLVPLTRRLWQMTKlkmlpTPAK 2769
Cdd:COG5245   1621 GTdeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTK-----FFLQ 1695
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2770 FHYVFNLRDLSRIWQGMLNITSEVIKDTD-ELLRLWKHECKRVIADRFSMSSDVTWFDKAVVSLVEEEFGEEKTPVVDCG 2848
Cdd:COG5245   1696 MNYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEA 1775
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2849 ----VDAYFVDFlrdapeatgetpeetdAEMPKlyepiASL-NHLQERLSVFlqlYNESIRGTgmdMVFFRDAMVHLVKI 2923
Cdd:COG5245   1776 eitfSMILFFGM----------------ACLLK-----KDLaVFVEEVRKIF---GSSHLDVE---AVAYKDALLHILRS 1828
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2924 SRVIRTPRGNALLVGVGGSGKQSLTRLASFIAGYTSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNEIKEE 3003
Cdd:COG5245   1829 RRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVES 1908
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3004 SFLEYMNNVLSSGEVSNLFARDEIDEINSDLTSIMKKEhPKRPPTNDNLYEYFMSRVRGNLHIVL-CFSPVGEKFRNRAL 3082
Cdd:COG5245   1909 SFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVLAGIR 1987
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3083 kFPALISGCTIDWFSRWPKDALVAVSEHFLS-SYNIDCTAEIKKELVQCMGS-FQDGVAEKCADYFQR-FRRSTHV--TP 3157
Cdd:COG5245   1988 -SPALKNRCFIDFKKLWDTEEMSQYANSVETlSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIEgsLG 2066
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3158 KSYLSFIQG---YKFIYEEKHVEVQSLANRMNTGLEKLKEASESVAALSQELAVKEKELQVANEKADMVLKEVTMKAQAA 3234
Cdd:COG5245   2067 ESKIKFIGGlkvYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLER 2146
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3235 EKVKAEVQKVKDKAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIKPSDIATVRTLGRPPHLIMRIMD--CVLLLF 3312
Cdd:COG5245   2147 EVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCDLLGF 2226
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3313 HRRVnavkidldksctvpsWQESLKLMTAGNFLQNLQQFPkDTIN--------EEVIEFLSPYFEMSDYNieTAKRVCGN 3384
Cdd:COG5245   2227 EAKI---------------WFGEQQSLRRDDFIRIIGKYP-DEIEfdlearrfREARECSDPSFTGSILN--RASKACGP 2288
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3385 vagLCSWTKAMASFFSINKEVLPLKANLIVQENRHALAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDADRC 3464
Cdd:COG5245   2289 ---LKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTV 2365
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3465 RHKMQTASTLISGLAGEKERWTEQSKEFAAQIKRLVGDVLLATAFLSYSGPFNQEFRDLLLNDWKKEMkARKIPFGNDLN 3544
Cdd:COG5245   2366 HKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGMSFIRI-SKEFRDKEIRR 2444
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3545 LNEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTKASRSPLLIDPQTQGKIWIRNKESQNELQITSLNHKYFRNHLEDSLS 3624
Cdd:COG5245   2445 RQFITEGVQKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARR 2524
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3625 LGRPLLIEDvGEELDPALDNVLEKNFIKTGSTFKVKVGDKEVDVMDGFKLYITTKLPNPAYTPEISARTAIIDFTVTVKG 3704
Cdd:COG5245   2525 EGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLG 2603
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3705 LEDQLLGRVILTEKQELEKERTHLLEEVTANKRRTKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKKTAEEVTQKLEIS 3784
Cdd:COG5245   2604 CETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESES 2683
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3785 GETEIQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLFDlsLARSVKSPITSKrigniIEHMTYEVFKY 3864
Cdd:COG5245   2684 MEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFE--KWRRMKSKYLCA-----IRYMLMSSEWI 2756
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3865 avqgLYEEhkflFTLLLTLKIDIQRNLVKHEEFLTLIK-GGASLDLKACPHKPSKWILD-------MTWLNLVELSKLKQ 3936
Cdd:COG5245   2757 ----LDHE----DRSGFIHRLDVSFLLRTKRFVSTLLEdKNYRQVLSSCSLYGNDVISHscdrfdrDVYRALKHQMDNRT 2828
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3937 FSDILDQISRNEklwriWFDKEnpeeeplpnaydksldcfrrlLLIRSWcpdrtiaqARKYIMDSMGENYaegvilDLEK 4016
Cdd:COG5245   2829 HSTILTSNSKTN-----PYKEY---------------------TYNDSW--------AEAFEVEDSGDLY------KFEE 2868
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4017 -TWEESDPRTPLICLLsMGSDPTDSIIalgKRLKIETRyvsmgqgqEVHARKLLHQTMANGGWVLLQNCHLGLDFLDELM 4095
Cdd:COG5245   2869 gLLELIVGHAPLIYAH-KKSLENERNV---DRLGSKEN--------EVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYV 2936
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4096 -DVVTET---ETVHDTFRLWITTEVHKQFPITLLQMSIKFANEppqglraglrrTYGGVSQDLLDVsVGAQWKPMLYA-- 4169
Cdd:COG5245   2937 eDVVYPIkasRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSS-----------TYPETGCGYADL-VEIDRYPFDYTlv 3004
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4170 --------VAFLHSTVQERRKFGPLGWNIPYEFNQADFNATVQFIQNHLdDMDIKKGVSWTTVRYMIGEIQYGGR----- 4236
Cdd:COG5245   3005 iacddafyLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNIL-FLNHLNARKWGNNRDLIFTIVYGKKhslme 3083
                         2730      2740      2750
                   ....*....|....*....|....*....|....
gi 1958754096 4237 ---VTDDYDKRLLNTFAKVWFSENMFGPDFTFYQ 4267
Cdd:COG5245   3084 dskVVDKYCRGYGAHETSSQILASVPGGDPELVK 3117
Dynein_C pfam18199
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ...
4311-4603 8.41e-125

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: 396.22  E-value: 8.41e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4311 AKDVLDTILGIQPKDSSG--GGDETREAVVARLADDMLEKLPEDYSpFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSL 4388
Cdd:pfam18199    4 TNELLSTLLSLQPRSDSGggGGGSSREEIVLELAKDILEKLPEPFD-IEEAEEKYPVGYEDPLNTVLLQEIERFNKLLKV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4389 VRSTLTELKLAVDGTIIMSDNLRDALDCMFDARIPARWKKASWVSS-TLGFWFTELLERNCQFTSWVS-NGRPHCFWMTG 4466
Cdd:pfam18199   83 IRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLkPLGSWIRDLLERLKQLQDWLDdEGPPKVFWLSG 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4467 FFNPQGFLTAMRQEITRANKgWALDNMVLCNEVTKFM-KDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFEL 4545
Cdd:pfam18199  163 FFFPQAFLTAVLQNYARKNG-WPIDKLSFDFEVTKKVsPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFSP 241
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4546 MPVIRIFAENNT--ARDPRLYCCPIYKKPVRTDLNYIAAVDLKTAQAPEHWILRGVALLC 4603
Cdd:pfam18199  242 LPVIHLKPVESDkkKLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVALLL 301
AAA_9 pfam12781
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ...
3556-3777 2.25e-114

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: 362.92  E-value: 2.25e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3556 SEWNLQGLPNDDLSIQNGIIVTKASRSPLLIDPQTQGKIWIRNKESQNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVG 3635
Cdd:pfam12781    1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3636 EELDPALDNVLEKNFIKTGSTFKVKVGDKEVDVMDGFKLYITTKLPNPAYTPEISARTAIIDFTVTVKGLEDQLLGRVIL 3715
Cdd:pfam12781   81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958754096 3716 TEKQELEKERTHLLEEVTANKRRTKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKKTAEEV 3777
Cdd:pfam12781  161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
AAA_8 pfam12780
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ...
2908-3168 1.99e-104

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: 336.12  E-value: 1.99e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2908 MDMVFFRDAMVHLVKISRVIRTPRGNALLVGVGGSGKQSLTRLASFIAGYTSFQITLTRSYNTSNLMEDLKVLYRTAGQQ 2987
Cdd:pfam12780    1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2988 GKGITFIFTDNEIKEESFLEYMNNVLSSGEVSNLFARDEIDEINSDLTSIMKKEhpKRPPTNDNLYEYFMSRVRGNLHIV 3067
Cdd:pfam12780   81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQ--NIEDSREAVYNYFVKRCRNNLHIV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3068 LCFSPVGEKFRNRALKFPALISGCTIDWFSRWPKDALVAVSEHFLSSYNIDctAEIKKELVQCMGSFQDGVAEKCADYFQ 3147
Cdd:pfam12780  159 LCMSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDIEIP--EELKSNVVKVFVYVHSSVEDMSKKFYE 236
                          250       260
                   ....*....|....*....|.
gi 1958754096 3148 RFRRSTHVTPKSYLSFIQGYK 3168
Cdd:pfam12780  237 ELKRKNYVTPKSYLELLRLYK 257
AAA_7 pfam12775
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
2533-2714 4.21e-89

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: 288.52  E-value: 4.21e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2533 YPPDTtpEYGSILVPNVDNVRTDFLIKTIAKQGKAVLLIGEQGTAKTVIIKGFMSKFDPESHTVKNLNFSSATTPLMFQR 2612
Cdd:pfam12775    1 IPPDV--PFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2613 TIESYVDKRMGTTYGPPAGKKMAVFIDDLNMPVINEWGDQVTNEIVRQLMEQNGFYNLEKPgEFTSIVDIQFLAAMIHPG 2692
Cdd:pfam12775   79 IIESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKL-TFKEIVDVQFVAAMGPPG 157
                          170       180
                   ....*....|....*....|..
gi 1958754096 2693 GGRNDIPQRLKRQFSIFNCTLP 2714
Cdd:pfam12775  158 GGRNDITPRLLRHFNVFNITFP 179
AAA_lid_11 pfam18198
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ...
4163-4302 8.35e-76

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: 248.91  E-value: 8.35e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4163 WKPMLYAVAFLHSTVQERRKFGPLGWNIPYEFNQADFNATVQFIQNHLDDMDikKGVSWTTVRYMIGEIQYGGRVTDDYD 4242
Cdd:pfam18198    1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYD--EKIPWDALRYLIGEINYGGRVTDDWD 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958754096 4243 KRLLNTFAKVWFSENMFGPDFTFYQG-YNIPKCSTVDGYLQYIQSLPAYDSPEVFGLHPNA 4302
Cdd:pfam18198   79 RRLLNTYLEEFFNPEVLEEDFKFSPSlYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
Dynein_heavy pfam03028
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ...
4022-4131 6.45e-51

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: 176.48  E-value: 6.45e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 4022 DPRTPLICLLSMGSDPTDSIIALGKRLKIETRY--VSMGQGQEVHARKLLHQTMANGGWVLLQNCHLGLDFLDELMDVV- 4098
Cdd:pfam03028    1 SPTTPLIFILSPGSDPTADLEKLAKKLGFGGKLhsISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILe 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958754096 4099 -TETETVHDTFRLWITTEVHKQFPITLLQMSIKF 4131
Cdd:pfam03028   81 eLPEETLHPDFRLWLTSEPSPKFPISILQNSIKI 114
MT pfam12777
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ...
3184-3526 1.02e-47

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: 176.42  E-value: 1.02e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3184 RMNTGLEKLKEASESVAALSQELAVKEKELQVANEKADMVLKEVTMKAQAAEKVKAEVQKVKDKAQAIVDSISKDKAIAE 3263
Cdd:pfam12777    2 RLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3264 EKLEAAKPALEEAEAALQTIKPSDIATVRTLGRPPHLIMRIMDCVLLLFHRRVnavKIDLDKSctvpsWQESlKLMTA-- 3341
Cdd:pfam12777   82 EDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGG---KIPKDKS-----WKAA-KIMMAkv 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3342 GNFLQNLQQFPKDTINEEVIEFLSPYFEMSDYNIETAKRVCGNVAGLCSWTKAMASFFSINKEVLPLKANLIVQENRHAL 3421
Cdd:pfam12777  153 DGFLDSLIKFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAA 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3422 AMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDADRCRHKMQTASTLISGLAGEKERWTEQSKEFAAQIKRLVG 3501
Cdd:pfam12777  233 AQEKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCG 312
                          330       340
                   ....*....|....*....|....*
gi 1958754096 3502 DVLLATAFLSYSGPFNQEFRDLLLN 3526
Cdd:pfam12777  313 DILLISAFISYLGFFTKKYRNELLD 337
Dynein_AAA_lid pfam17852
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ...
2406-2525 2.65e-21

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: 92.35  E-value: 2.65e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2406 LRQLYAETFPDLYRFSIQNLEFKMEILEAFVITQSTHMLQGLIPTKEQAGDVDP-------EHLGRLFVFAMMWSVGAVL 2478
Cdd:pfam17852    1 LEPLFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDEVLEYNGVHPlspdklkEYLEKLFLFALVWSIGGTL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958754096 2479 ELEGRRRMELWLRSREGpTLHLPQltDPGDTMFDYYV-APDGTWRHWS 2525
Cdd:pfam17852   81 DEDSRKKFDEFLRELFS-GLDLPP--PEKGTVYDYFVdLEKGEWVPWS 125
AAA_lid_1 pfam17857
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3.
2748-2844 5.42e-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: 5.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2748 LVPLTRRLWQMTKLKMLPTPAKFHYVFNLRDLSRIWQGMLNITSEVIKDTDELLRLWKHECKRVIADRFSMSSDVTWFDK 2827
Cdd:pfam17857    1 LIAAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDK 80
                           90
                   ....*....|....*..
gi 1958754096 2828 AVVSLVEEEFGEEKTPV 2844
Cdd:pfam17857   81 IQMASLKKFFDDIEDEL 97
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
2239-2374 1.38e-09

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: 59.23  E-value: 1.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2239 GMMTLGPSGSGKTScIHTLMKAMTDCGKPhrEMRMNPKAITAPQMFGRLDVATND--WTDGIFstlwrkTLKAKKGEHIw 2316
Cdd:pfam07728    1 GVLLVGPPGTGKTE-LAERLAAALSNRPV--FYVQLTRDTTEEDLFGRRNIDPGGasWVDGPL------VRAAREGEIA- 70
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958754096 2317 iVLDGpVDAI---WIENLNSVLDDNKTLTLANGDRIPMAPNC-KIVFEPHNID----NASPATVSR 2374
Cdd:pfam07728   71 -VLDE-INRAnpdVLNSLLSLLDERRLLLPDGGELVKAAPDGfRLIATMNPLDrglnELSPALRSR 134
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
3181-3282 2.12e-07

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 53.81  E-value: 2.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3181 LANRMNTGLEKLKEASESVAALSQELAVKEKELQVANEKADMVLKEVTMKAQA-----AEKVKAEVQKVKDKAQAIVDSi 3255
Cdd:PRK07352    48 LEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAiraeiEKQAIEDMARLKQTAAADLSA- 126
                           90       100
                   ....*....|....*....|....*..
gi 1958754096 3256 SKDKAIAEEKLEAAKPALEEAEAALQT 3282
Cdd:PRK07352   127 EQERVIAQLRREAAELAIAKAESQLPG 153
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
3187-3280 1.42e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.98  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3187 TGLEKLKEASESVAALSQELAVKEKELQVANEKADMVLKEVTMKAQAAEKVKAEVQKVKDKAQAIVDSISKDKAIAEEKL 3266
Cdd:COG3883    119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
                           90
                   ....*....|....
gi 1958754096 3267 EAAKPALEEAEAAL 3280
Cdd:COG3883    199 AELEAELAAAEAAA 212
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
3172-3283 4.07e-05

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 48.56  E-value: 4.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3172 EEKHVEVQSLANRMNTGLEKLKEASESVA-ALSQELAVKEKELQVANEkadmVLKEVTMKAQAAEKVKAEVQKVKDKAQA 3250
Cdd:pfam06008  147 EAELKAAQDLLSRIQTWFQSPQEENKALAnALRDSLAEYEAKLSDLRE----LLREAAAKTRDANRLNLANQANLREFQR 222
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958754096 3251 IVDSISKDKAIAEEKLEAAKPALEEAEAALQTI 3283
Cdd:pfam06008  223 KKEEVSEQKNQLEETLKTARDSLDAANLLLQEI 255
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
3190-3279 1.21e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.92  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3190 EKLKEASESVAALSQELAVKEKElqVANEKADmvlKEVTMKAQAAEKVKAEVQKVKDKAQAivdsisKDKAIAEEKLeAA 3269
Cdd:TIGR02794  124 AKAKQAAEAKAKAEAEAERKAKE--EAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEA------KAKAEAEAKA-KA 191
                           90
                   ....*....|
gi 1958754096 3270 KPALEEAEAA 3279
Cdd:TIGR02794  192 EEAKAKAEAA 201
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
2568-2706 1.57e-04

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 44.59  E-value: 1.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 2568 VLLIGEQGTAKTVIIKGFMSKFDPESHTVKNLNfsSATTP--LMFQRTIESYVDKRMGTTYGPPAGKKMAVFIDDLNMP- 2644
Cdd:pfam07728    2 VLLVGPPGTGKTELAERLAAALSNRPVFYVQLT--RDTTEedLFGRRNIDPGGASWVDGPLVRAAREGEIAVLDEINRAn 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958754096 2645 --VINEWgDQVTNEIVRQLMEqNGFYNLEKPGEFtsivdiQFLAAMIHPGGGRNDIPQRLKRQF 2706
Cdd:pfam07728   80 pdVLNSL-LSLLDERRLLLPD-GGELVKAAPDGF------RLIATMNPLDRGLNELSPALRSRF 135
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
3191-3279 2.82e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 46.72  E-value: 2.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3191 KLK-EASESVAALSQELAVKEKELQVANEKADMVLKEVTMKAQAAEKVKAEV---QKVKDKAQAIVDSISKDKAIAEEKL 3266
Cdd:PRK09510   146 KAKaEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAeakKKAEAEAKKKAAAEAKKKAAAEAKA 225
                           90
                   ....*....|...
gi 1958754096 3267 EAAKPALEEAEAA 3279
Cdd:PRK09510   226 AAAKAAAEAKAAA 238
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
3422-3497 3.96e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 3.96e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958754096 3422 AMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDADRcrhKMQTASTLISGLAGEKERWTEQSKEFAAQIK 3497
Cdd:COG3883    134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
3191-3278 5.72e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.61  E-value: 5.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3191 KLKEASESVA---ALSQELAVKEKELQVANEKADMVLKEvtmKAQAAEKVKAEvqKVKDKAQAivdsiSKDKAIAE--EK 3265
Cdd:TIGR02794  143 KAKEEAAKQAeeeAKAKAAAEAKKKAEEAKKKAEAEAKA---KAEAEAKAKAE--EAKAKAEA-----AKAKAAAEaaAK 212
                           90
                   ....*....|...
gi 1958754096 3266 LEAAKPALEEAEA 3278
Cdd:TIGR02794  213 AEAEAAAAAAAEA 225
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3167-3284 5.84e-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: 46.20  E-value: 5.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3167 YKFIYEE-KHVEVQSLANRMNTGLEKLKEASESVAALSQELAVKEKELQVANEKadmvLKEVTMKAQAAEKVKAEVQKVK 3245
Cdd:TIGR02168  215 YKELKAElRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK----LEELRLEVSELEEEIEELQKEL 290
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958754096 3246 DKAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIK 3284
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
3181-3281 8.30e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 42.42  E-value: 8.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3181 LANRMNTGLEKLKEASESVAALSQELAVKEKELQVANEKADMVLKE-----VTMKAQAAEKVKAEVQKVKDKAQAIVDSi 3255
Cdd:cd06503     28 LDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEAERILEQAKAEIEQ- 106
                           90       100
                   ....*....|....*....|....*.
gi 1958754096 3256 SKDKAIAEEKLEAAKPALEEAEAALQ 3281
Cdd:cd06503    107 EKEKALAELRKEVADLAVEAAEKILG 132
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
3177-3282 8.99e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 8.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3177 EVQSLANRMNTGLEKLKEASESVAALSQELAVKEKELQVANEKADMVLKEVTMKAQAAEKVKAEVQKVKDKAQAIVDSIS 3256
Cdd:COG4372     39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
                           90       100
                   ....*....|....*....|....*.
gi 1958754096 3257 KDKAiAEEKLEAAKPALEEAEAALQT 3282
Cdd:COG4372    119 ELQK-ERQDLEQQRKQLEAQIAELQS 143
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
3172-3279 9.72e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.18  E-value: 9.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3172 EEKHVEVQSLANRmntglEKLKEASESV--AALSQELA--VKEKELQVANEKADMVLKEVtmkAQAAEKVKAEVQKV-KD 3246
Cdd:PRK09510   102 RLKQLEKERLAAQ-----EQKKQAEEAAkqAALKQKQAeeAAAKAAAAAKAKAEAEAKRA---AAAAKKAAAEAKKKaEA 173
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958754096 3247 KAQAIVDSISKDKAIAEEKLEAAKPALEEAEAA 3279
Cdd:PRK09510   174 EAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAE 206
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
3190-3281 3.13e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 41.31  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3190 EKLKEASESVAALSQELAVKEKELQVANEKADMVLKEVT-----MKAQAAEKVKAEVQKVKDKAQAIVDSIsKDKAIAEE 3264
Cdd:COG0711     38 DGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARkeaeaIAEEAKAEAEAEAERIIAQAEAEIEQE-RAKALAEL 116
                           90
                   ....*....|....*..
gi 1958754096 3265 KLEAAKPALEEAEAALQ 3281
Cdd:COG0711    117 RAEVADLAVAIAEKILG 133
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
3176-3284 3.30e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3176 VEVQSLANRMNTGLEKLKEASESVAALSQELAVKEKELQVANEKADMVLKEVTMKAQAAEKVKAEVQKVKDK-------- 3247
Cdd:COG1579     10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnk 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1958754096 3248 -AQAI---VDSISKDKAIAEEKLEAAKPALEEAEAALQTIK 3284
Cdd:COG1579     90 eYEALqkeIESLKRRISDLEDEILELMERIEELEEELAELE 130
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
3198-3282 4.13e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 42.79  E-value: 4.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3198 SVAALSQELAVKEKEL---QVANEKADMVLKEVTMKAQAAEKVKAEVQKVKDKAQAI--------VDSISKDKAIAEEKL 3266
Cdd:TIGR04320  255 SLAALQAKLATAQADLaaaQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQalqtaqnnLATAQAALANAEARL 334
                           90
                   ....*....|....*.
gi 1958754096 3267 EAAKPALEEAEAALQT 3282
Cdd:TIGR04320  335 AKAKEALANLNADLAK 350
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
3171-3280 7.63e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 7.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3171 YEEKHVEVQSLANRmntgLEKLKEASESVA------ALSQELAVKEKELQVANEKadmvLKEVTMKAQAAEKVKAEVQKV 3244
Cdd:COG1579     61 IKRLELEIEEVEAR----IKKYEEQLGNVRnnkeyeALQKEIESLKRRISDLEDE----ILELMERIEELEEELAELEAE 132
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958754096 3245 KDKAQAIVDSISKDKAIAEEKLEAAKPALEEAEAAL 3280
Cdd:COG1579    133 LAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3408-3499 9.08e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 9.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3408 LKANLIV-----QENRHALAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDADRCRHKMQTASTLISGLAGEK 3482
Cdd:COG1196    225 LEAELLLlklreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
                           90
                   ....*....|....*..
gi 1958754096 3483 ERWTEQSKEFAAQIKRL 3499
Cdd:COG1196    305 ARLEERRRELEERLEEL 321
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
3190-3284 9.94e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 9.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958754096 3190 EKLKEASESVAALSQELAVKEKELQVANEKADMVLKEVtmkaqaaEKVKAEVQKVKDKAQAI---VDSISKDKAIAEEKL 3266
Cdd:COG4372     80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-------EELQKERQDLEQQRKQLeaqIAELQSEIAEREEEL 152
                           90
                   ....*....|....*...
gi 1958754096 3267 EAAKPALEEAEAALQTIK 3284
Cdd:COG4372    153 KELEEQLESLQEELAALE 170
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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