|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1688-2014 |
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: 631.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1688 YCYEYLGNSPRLVITPLTDRCYITLTQSLHLTMSGAPAGPAGTGKTETTKDLGRALGMMVYVFNCSEQMDYRSIGNIYKG 1767
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1768 LVQTGAWGCFDEFNRIAVEVLSVVAVQVKMIHDAIRSRRRRFVFLGETIPLKPSVGIFITLNPGYAGRTELPENLKALFR 1847
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1848 PCAMVAPDTELICEIMLVAEGFVDARSLARKFISLYTLCDELLSKQDHYDWGLRAIKSVLVVAGSLKRGDKNRPEDQVLM 1927
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1928 RALRDFNMPKIVTDDVPVFLGLVSDLFPALDVPRQRKPHFEQMVKQSTLELRLQPEESFILKVVQLEELLAVRHSIFVVG 2007
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 1958786731 2008 NAGTGKS 2014
Cdd:pfam12774 321 PTGSGKT 327
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
46-617 |
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: 611.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 46 LHAIESVVIKWSHQIQEIIEKDSAqpllsGLHPTPETELDFWTMRHDNLKCIYHQLQAPIVLKMVKILRTRQSSYLPALK 125
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQ-----GRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 126 GIFTTVENALLEARDVELHLRPLRKHIQGLQEA-DFPQTGILIAPLIHTICLIWSHSKFYNSPARVIVLLQEFCNLFIDQ 204
Cdd:pfam08385 76 ALDTELTDALNEAKDNVKYLKTLERPFEDLEELtDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 205 ARAYLSPEDLLKGEIEDALEKVQVAIGVLRMFQNSFFKYRRGLTSYFTGdteqRPWDFQSHLVFSRFNKFLDRLVKIEDM 284
Cdd:pfam08385 156 CKKYLSPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRE----RPWDFSERYIFGRFDAFLERLEKILEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 285 FVTILEFEKLERLefGGSKGAVLNAQIHSMKEEFIECCNVFRQSIYDPSDCDSMEFESDYFQFKSKTLDFDRRLGTLLCE 364
Cdd:pfam08385 232 FETIEQFSKLEKI--GGTKGPELEGVIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 365 GLSNCSGLESAFKLLTIFGNFLEKPVVMEIFSPHYSTLLNMFNAELDMCKRLYDEHMKQiehgHEILNKNMPFTSGNIKW 444
Cdd:pfam08385 310 AFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQKYN----PSPIAKNMPPVAGAIIW 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 445 ARMLLERLQMFWSNFTSLHYLFpDSPDEAAVCQKYAEMTTLLDQFESRIYSEWRRNVDKTCEFNLNQPL-VKFSPINGLL 523
Cdd:pfam08385 386 ARQLFRRIQEPMKRFKEELGLL-KHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGNLKRPLlVRHPETGKLL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 524 SVNFDPKLVAVLREVKYLLMLkKSNIPDSALGIFQKKNIILKHIGNLELLVQGYNKLKQTLLEVEYPLIEKELGAIDEQL 603
Cdd:pfam08385 465 SVNFDPQLLALLREVKYLQKL-GFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKL 543
|
570
....*....|....
gi 1958786731 604 RVAATWLTWQDDFW 617
Cdd:pfam08385 544 EPGLTTLTWNSLGI 557
|
|
| MT super family |
cl37598 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
2921-3265 |
4.93e-171 |
|
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.
The actual alignment was detected with superfamily member pfam12777:
Pssm-ID: 463699 [Multi-domain] Cd Length: 344 Bit Score: 530.80 E-value: 4.93e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2921 EHLGNGIQKLQTTASQVGNLKARLASQEAELQLRNQDAEALITKIGLQTEKVSREKAIADAEERKVAAIQTEASQKQREC 3000
Cdd:pfam12777 1 ERLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3001 EADLLKAEPALVAATAALNTLNRVNLTELKTFPNPPNAVTNVTAAVMVLLAPRGRVPKDRSWKAARIFMGKVDDFLQALI 3080
Cdd:pfam12777 81 EEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGGKIPKDKSWKAAKIMMAKVDGFLDSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3081 NYDKEHIPENCLKVVnEQYLKDPEFNPNLIRTKSFAAAGLCAWVINIIKFYEVYCDVEPKRQALAQTNLDLAAATEKLEA 3160
Cdd:pfam12777 161 KFDKEHIHEACLKAF-KPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3161 VRRKLVDLDHNLRRLTASFEKATAEKVRCQEEVNQTNKTIDLANRLVSELESEKIRWGQSIKSFETQEKTLCGDVLLTAA 3240
Cdd:pfam12777 240 IKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISA 319
|
330 340
....*....|....*....|....*
gi 1958786731 3241 FVSYIGSFTRQYRQELVDCKWIPFL 3265
Cdd:pfam12777 320 FISYLGFFTKKYRNELLDKFWIPYI 344
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1122-1548 |
1.01e-138 |
|
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: 440.54 E-value: 1.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1122 MKQCRREVRLLKELWDIIVYVRRSIDNWTETRWRQVNMEQMDLELRRFAKEIWSLDKAVRVWDAYSGLEGTVKDMTTSLR 1201
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1202 AVAELQNPALRDRHWQQLTNAIGVRF-SINDSTTLADLLAVQLHQVEEDVRDIVDKAVKELGTEKVITDVSHTWEALEFS 1280
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFdPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1281 YEVHHRTGTPLLKSDEQLFETLEHNQSFLLGLGTSwlateplgsayshagilqvqlqtllqsKYVEYFIDQVLSWQNKLN 1360
Cdd:pfam08393 161 LVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSS---------------------------PYVKPFEEEVSEWEKKLS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1361 VADAVIFTWMQVQRTWSHLESIFVcSEDIRIQLVEDAQRFDEVDAEFKELMFKTAKIKNVLEATCRPHLYEKLKDFQHRL 1440
Cdd:pfam08393 214 LLQEILDEWLKVQRKWLYLEPIFS-SEDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1441 SLCEKALAEYLETKRVTFSRFYFISSADLLDLLSKGAQPKQVTRHLVKLFDSISDLQFEDNPEVstckaVGMFSKEKEYV 1520
Cdd:pfam08393 293 EKIQKSLNEYLEKKRLAFPRFYFLSNDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDENKEI-----TGMISKEGEVV 367
|
410 420
....*....|....*....|....*....
gi 1958786731 1521 SF-QAGCECIGHVESWLLQLEQTMKETVR 1548
Cdd:pfam08393 368 PFsKPPVEAKGNVEEWLNELEEEMRETLR 396
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4043-4338 |
1.35e-121 |
|
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: 386.98 E-value: 1.35e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 4043 TVTSNMLFRTLLEMQPRNAVSNEEQGQSTEDKVKNILDDILERLPEEFNMAEIMQKNP--NRSPYILVCFQECERMNVLL 4120
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGGSSREEIVLELAKDILEKLPEPFDIEEAEEKYPvgYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 4121 REIRVSLQHLDLGLKGELTLSPDVETQLSALSYDRVPDTWNKLAYPSTYGLAQWFNDLLLRCRELDTWTQDLTLPAVVWL 4200
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 4201 SGLFNPQSFLTAIMQTMARKNEWPLDRMCLTIDVTKK-TKEDYGHPPREGAYLHGLHLEGARWDIQSGALVDARLKELTS 4279
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKvSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958786731 4280 TMPVIFAKAIPADRQEVKHA-YECPVYKTKARGLT-YVWTFRLRSKDRIAKWVLAGVALLL 4338
Cdd:pfam18199 241 PLPVIHLKPVESDKKKLDENtYECPVYKTSERHSTnFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DYN1 super family |
cl34955 |
Dynein, heavy chain [Cytoskeleton]; |
1376-3990 |
3.70e-116 |
|
Dynein, heavy chain [Cytoskeleton];
The actual alignment was detected with superfamily member COG5245:
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 417.08 E-value: 3.70e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1376 WSHLESIFVCSEDIRIQLVEDAQRFDEVDAEFKELMFKTAKIKNVLEATCRPhLYEKLKDFQHRLSLCEKALAEYLETKR 1455
Cdd:COG5245 627 RLDEYLMMMSLEDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQVFMSIEKVLGLRW 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1456 VTFSRFyfISSADLLDLLSKGAQPKQVTRHLVKLFDSISDLQFEDnpevSTCKAVGMFSKEKE-YVSFQAGCECIgHVES 1534
Cdd:COG5245 706 REVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEEMKTVFS----SRIQKKEPFSLDSEaYVGFFRLYEKS-IVIR 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1535 WLlqlEQTMKETVRLAIAEAIAAYEEKPRELWIFDFPAQVALTGSQIWwtTDVgiafsrLEEGYETALKDFHKkqisQLN 1614
Cdd:COG5245 779 GI---NRSMGRVLSQYLESVQEALEIEDGSFFVSRHRVRDGGLEKGRG--CDA------WENCFDPPLSEYFR----ILE 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1615 TLITLLLGELSPGDRQKVMTICTIDVHARDVVAKLISQKVVSPRAFTWLSqLRHEWEESRKHCIVNICDAHFQYCYEYLG 1694
Cdd:COG5245 844 KIFPSEEGYFFDEVLKRLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVS-ISELPQGLYKRFIKVRSSYRSAEMFAKNT 922
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1695 NSPRLVITPLTDRCYITLTQSLHLTMSGApagpAGTGKTETTKDLGRALGMMVyvfncsEQMDYRSigNIYKGLVQTGAW 1774
Cdd:COG5245 923 IPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEER 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1775 GcFDEFNRIAvEVLSVVAVQVKMIHDAIRSRRRRFVFLGETIPLKPSVGIFITLNPgyagRTELPENLKALFRPCAMVAP 1854
Cdd:COG5245 991 G-TEESALLD-EISRTILVDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIP 1064
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1855 dteliceimlvaEGFVDAR--SLARKFISLYTLCDELLSKQDHYDWglRAIKSVLVVAGSLKRgDKNRPEDQVLmralRD 1932
Cdd:COG5245 1065 ------------FGAIKSRreSLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRMLE-EKTEYLNKIL----SI 1125
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1933 FNMPKIvtDDVPVFLglvSDLFPALDVPRQRKPHFEQMVKQSTLELRLQPEESFILKVVQLEELLAVrhsifvVGNAGTG 2012
Cdd:COG5245 1126 TGLPLI--SDTLRER---IDTLDAEWDSFCRISESLKKYESQQVSGLDVAQFVSFLRSVDTGAFHAE------YFRVFLC 1194
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2013 KSKILRTL-------NRTYVnmkqkpvwndlnpkavtTDELFgfihHATREWKdGLLSSILREQANLT-HDGPTWIVLDG 2084
Cdd:COG5245 1195 KIKHYTDAcdylwhvKSPYV-----------------KKKYF----DADMELR-QFFLMFNREDMEARlADSKMEYEVER 1252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2085 didplWIESLNTVMDDNKVLTLASNERvaltpsmRLLFEthHLQTaTPATVSRAGILY----------VNPQDLG-WNPY 2153
Cdd:COG5245 1253 -----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLGS-IGDKVGRCLVEYdsisrlstkgVFLDELGdTKRY 1317
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2154 VASWIDRRRHQSEKANLTILFDkyIPVCLEKLRTSFKAITSVPEsslvQTICTLLECLLTPENIPSDSPKETYEVYFVFA 2233
Cdd:COG5245 1318 LDECLDFFSCFEEVQKEIDELS--MVFCADALRFSADLYHIVKE----RRFSGVLAGSDASESLGGKSIELAAILEHKDL 1391
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2234 CVWTFGG-------TLLRDQLSDYQADFSRW----WHKEMKAVKFPSQGTIFDYYLDHKTKKFLPwtdkVPQFTMDADAP 2302
Cdd:COG5245 1392 IVEMKRGindvlklRIFGDKCRESTPRFYLIsdgdLIKDLNERSDYEEMLIMMFNISAVITNNGS----IAGFELRGERV 1467
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2303 L--KTVLVHTPETTRLRYFTELLLNKGKPLMLVGNAGVGKTVFLSDTLASiSEDYIVSRVPFNYYTTSADLQRILEKPLE 2380
Cdd:COG5245 1468 MlrKEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS-ELITEVKYFNFSTCTMTPSKLSVLERETE 1546
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2381 K----KAGRNYGPRGNKKLVYFIDDLNMPEVDLYGTVQPHALLRQHIDY-GHWYDRHKvMLKEIRNCQYVACMNPMAGSF 2455
Cdd:COG5245 1547 YypntGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERqGFWSSIAV-SWVTICGIILYGACNPGTDEG 1625
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2456 TVD--PRLKRHFTVLAFNFPSLDTLTTIYgqifSFYLQQQAFC-PSVLRTGPSLIQATIAFHQTMAENFvPTAIKFHYNF 2532
Cdd:COG5245 1626 RVKyyERFIRKPVFVFCCYPELASLRNIY----EAVLMGSYLCfDEFNRLSEETMSASVELYLSSKDKT-KFFLQMNYGY 1700
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2533 NLRDLSNIFQGILFASPECLKCPE-DLARLWLHETSRVYGDRLVDANDSDLFQRKMLEAAHKYFKGADANTLQQQPLVYc 2611
Cdd:COG5245 1701 KPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEITF- 1779
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2612 hfaSGREDPCYEPVkDWEGLKAVLTEMMGNYNELHSEMHLVLFEDAMQHVCRISRILRTPQGHALLVGVGGSGKQSLSRL 2691
Cdd:COG5245 1780 ---SMILFFGMACL-LKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREF 1855
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2692 AAYICSLEVFQITLTEGYGTQDLRVDLANLYVRTGAKNMPTVFLLTDAHVLDESFLVLINDLLASGDIPGLFSDEDTDKI 2771
Cdd:COG5245 1856 VCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRI 1935
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2772 ISGIRNEVRGLGIT-DSRENCWAFFLARVRLQLKMVFCFSPVGHTLRVRARKFPALVNCTAIDWFHAWPQEALVSVSRRF 2850
Cdd:COG5245 1936 PENLRFVFESTSLEkDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGIRSPALKNRCFIDFKKLWDTEEMSQYANSV 2015
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2851 I-EEIEG-----IEPQHK--DSISLFMAYVHTSVKEVSAWYYQNERR-YNYTTPRSFLEQISLFKSLLKKKRGEVQRKKE 2921
Cdd:COG5245 2016 EtLSRDGgrvffINGELGvgKGALISEVFGDDAVVIEGRGFEISMIEgSLGESKIKFIGGLKVYDARCVIYIEELDCTNV 2095
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2922 HLGNGIQKLQTTASQVGNLKARLASQEAELQLRNQDAEALITKIgLQTEKVSREKAIADAEERKVAAIQTEASQKQRECE 3001
Cdd:COG5245 2096 NLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGT-PGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSV 2174
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3002 ADLLK-AEPALVAATAALNTLNRVNLTELKTFPNPPNAVTNVTAAVMVLLaprGRVPKDrsWKAARIFMgKVDDFLQALI 3080
Cdd:COG5245 2175 MKFKSsKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLL---GFEAKI--WFGEQQSL-RRDDFIRIIG 2248
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3081 NYDKE-HIPENCLKVVNEQYLKDPEFNPNLIRTKSFAAAGLCAWVINIIKFYEVYCDVEPKRQALAQTNLDLAAATEKLE 3159
Cdd:COG5245 2249 KYPDEiEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLT 2328
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3160 AVRRKLVDLDHNLRRLTASFEKATAEKVRCQEEVNQTNKTIDLANRLVSELESEKIRWGQSIKSFETQEKTLCGDVLLTA 3239
Cdd:COG5245 2329 LGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSS 2408
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3240 AFVSYIGSFTRQYRQ-ELVDCKwiPFLQQKVSIP-------IAEGLDMIatlTDDATIATWNNQGLPSDRMSTENATILt 3311
Cdd:COG5245 2409 CLHPYIGTLGFLCRAiEFGMSF--IRISKEFRDKeirrrqfITEGVQKI---EDFKEEACSTDYGLENSRIRKDLQDLT- 2482
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3312 hckrwPLMIDPQQQGIKWIKNKYGPdlKVTHLG---QKGFLNAIEMALAFGDVILIENlKETVDPVLGPLLGRNTIKKGK 3388
Cdd:COG5245 2483 -----AVLNDPSSKIVTSQRQMYDE--KKAILGsfrEMEFAFGLSQARREGSDKIIGD-AEALDEEIGRLIKEEFKSNLS 2554
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3389 YIR--IGDKECEFNKNFRLILHTKLANPHYKPELQAQTTLLNFTVTEDGLEGQLLAEVVSVERPDLERLKLVLTKHQNDF 3466
Cdd:COG5245 2555 EVKvmINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACG 2634
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3467 KIELRHLEEDLLLRLSAAEGSFLDDTDLVERLETTKATAAEIEHKVIEARENERKINETRECYRPVAARASLMYFVISDL 3546
Cdd:COG5245 2635 SLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMF 2714
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3547 RKINPVYQFSLKAFKTLFHRAIEQADKVEDTQERIcaLMESVTYatflhasqaLFEKDKLTFlsqmafqillrrneIHPL 3626
Cdd:COG5245 2715 DEKALMYNKSICELSSEFEKWRRMKSKYLCAIRYM--LMSSEWI---------LDHEDRSGF--------------IHRL 2769
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3627 ELDFLLRFTVEHTYSSPVDFLTAQSWSAVKAV--ALMEEFRGLDRDVEgSAKQWRKWVESECPEKEKLPQ-EWKKKSLIQ 3703
Cdd:COG5245 2770 DVSFLLRTKRFVSTLLEDKNYRQVLSSCSLYGndVISHSCDRFDRDVY-RALKHQMDNRTHSTILTSNSKtNPYKEYTYN 2848
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3704 KLIILRavrpdrmtyalrnFVEEKLGTKYvertrlDLGKAFGESSPGT-PVFFILSPGVDALKDLEVLGKRlgftidsgk 3782
Cdd:COG5245 2849 DSWAEA-------------FEVEDSGDLY------KFEEGLLELIVGHaPLIYAHKKSLENERNVDRLGSK--------- 2900
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3783 fhnvslgqGQELVAEMALEKAAIGGHWVFLQNVHLVAKWlgtLEKLLEKFSQGS-----HRDYRVFLSAEAAPSQhepvI 3857
Cdd:COG5245 2901 --------ENEVYAVLNSLFSRKEKSWFEVYNISLSFGW---FKRYVEDVVYPIkasrvCGKVKNMWTSMVDADM----L 2965
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3858 PQGLLENSIKITNEPPTGMLANLhAALYNFDQ---DTLEMCSKDqefksILFSLCYFHGCVAGRLRFGPQGWSRSYPFSP 3934
Cdd:COG5245 2966 PIQLLIAIDSFVSSTYPETGCGY-ADLVEIDRypfDYTLVIACD-----DAFYLSWEHAAVASVISAGPKENNEEIYFGD 3039
|
2650 2660 2670 2680 2690 2700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958786731 3935 GDLTICT----NILY-NHLEAnphVPWEDLRYLFGEIIYGGHITDAWD----RKLCRVYLEEFMN 3990
Cdd:COG5245 3040 KDFEFKThllkNILFlNHLNA---RKWGNNRDLIFTIVYGKKHSLMEDskvvDKYCRGYGAHETS 3101
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1688-2014 |
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: 631.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1688 YCYEYLGNSPRLVITPLTDRCYITLTQSLHLTMSGAPAGPAGTGKTETTKDLGRALGMMVYVFNCSEQMDYRSIGNIYKG 1767
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1768 LVQTGAWGCFDEFNRIAVEVLSVVAVQVKMIHDAIRSRRRRFVFLGETIPLKPSVGIFITLNPGYAGRTELPENLKALFR 1847
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1848 PCAMVAPDTELICEIMLVAEGFVDARSLARKFISLYTLCDELLSKQDHYDWGLRAIKSVLVVAGSLKRGDKNRPEDQVLM 1927
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1928 RALRDFNMPKIVTDDVPVFLGLVSDLFPALDVPRQRKPHFEQMVKQSTLELRLQPEESFILKVVQLEELLAVRHSIFVVG 2007
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 1958786731 2008 NAGTGKS 2014
Cdd:pfam12774 321 PTGSGKT 327
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
46-617 |
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: 611.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 46 LHAIESVVIKWSHQIQEIIEKDSAqpllsGLHPTPETELDFWTMRHDNLKCIYHQLQAPIVLKMVKILRTRQSSYLPALK 125
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQ-----GRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 126 GIFTTVENALLEARDVELHLRPLRKHIQGLQEA-DFPQTGILIAPLIHTICLIWSHSKFYNSPARVIVLLQEFCNLFIDQ 204
Cdd:pfam08385 76 ALDTELTDALNEAKDNVKYLKTLERPFEDLEELtDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 205 ARAYLSPEDLLKGEIEDALEKVQVAIGVLRMFQNSFFKYRRGLTSYFTGdteqRPWDFQSHLVFSRFNKFLDRLVKIEDM 284
Cdd:pfam08385 156 CKKYLSPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRE----RPWDFSERYIFGRFDAFLERLEKILEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 285 FVTILEFEKLERLefGGSKGAVLNAQIHSMKEEFIECCNVFRQSIYDPSDCDSMEFESDYFQFKSKTLDFDRRLGTLLCE 364
Cdd:pfam08385 232 FETIEQFSKLEKI--GGTKGPELEGVIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 365 GLSNCSGLESAFKLLTIFGNFLEKPVVMEIFSPHYSTLLNMFNAELDMCKRLYDEHMKQiehgHEILNKNMPFTSGNIKW 444
Cdd:pfam08385 310 AFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQKYN----PSPIAKNMPPVAGAIIW 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 445 ARMLLERLQMFWSNFTSLHYLFpDSPDEAAVCQKYAEMTTLLDQFESRIYSEWRRNVDKTCEFNLNQPL-VKFSPINGLL 523
Cdd:pfam08385 386 ARQLFRRIQEPMKRFKEELGLL-KHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGNLKRPLlVRHPETGKLL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 524 SVNFDPKLVAVLREVKYLLMLkKSNIPDSALGIFQKKNIILKHIGNLELLVQGYNKLKQTLLEVEYPLIEKELGAIDEQL 603
Cdd:pfam08385 465 SVNFDPQLLALLREVKYLQKL-GFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKL 543
|
570
....*....|....
gi 1958786731 604 RVAATWLTWQDDFW 617
Cdd:pfam08385 544 EPGLTTLTWNSLGI 557
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
2921-3265 |
4.93e-171 |
|
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: 530.80 E-value: 4.93e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2921 EHLGNGIQKLQTTASQVGNLKARLASQEAELQLRNQDAEALITKIGLQTEKVSREKAIADAEERKVAAIQTEASQKQREC 3000
Cdd:pfam12777 1 ERLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3001 EADLLKAEPALVAATAALNTLNRVNLTELKTFPNPPNAVTNVTAAVMVLLAPRGRVPKDRSWKAARIFMGKVDDFLQALI 3080
Cdd:pfam12777 81 EEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGGKIPKDKSWKAAKIMMAKVDGFLDSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3081 NYDKEHIPENCLKVVnEQYLKDPEFNPNLIRTKSFAAAGLCAWVINIIKFYEVYCDVEPKRQALAQTNLDLAAATEKLEA 3160
Cdd:pfam12777 161 KFDKEHIHEACLKAF-KPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3161 VRRKLVDLDHNLRRLTASFEKATAEKVRCQEEVNQTNKTIDLANRLVSELESEKIRWGQSIKSFETQEKTLCGDVLLTAA 3240
Cdd:pfam12777 240 IKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISA 319
|
330 340
....*....|....*....|....*
gi 1958786731 3241 FVSYIGSFTRQYRQELVDCKWIPFL 3265
Cdd:pfam12777 320 FISYLGFFTKKYRNELLDKFWIPYI 344
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1122-1548 |
1.01e-138 |
|
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: 440.54 E-value: 1.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1122 MKQCRREVRLLKELWDIIVYVRRSIDNWTETRWRQVNMEQMDLELRRFAKEIWSLDKAVRVWDAYSGLEGTVKDMTTSLR 1201
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1202 AVAELQNPALRDRHWQQLTNAIGVRF-SINDSTTLADLLAVQLHQVEEDVRDIVDKAVKELGTEKVITDVSHTWEALEFS 1280
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFdPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1281 YEVHHRTGTPLLKSDEQLFETLEHNQSFLLGLGTSwlateplgsayshagilqvqlqtllqsKYVEYFIDQVLSWQNKLN 1360
Cdd:pfam08393 161 LVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSS---------------------------PYVKPFEEEVSEWEKKLS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1361 VADAVIFTWMQVQRTWSHLESIFVcSEDIRIQLVEDAQRFDEVDAEFKELMFKTAKIKNVLEATCRPHLYEKLKDFQHRL 1440
Cdd:pfam08393 214 LLQEILDEWLKVQRKWLYLEPIFS-SEDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1441 SLCEKALAEYLETKRVTFSRFYFISSADLLDLLSKGAQPKQVTRHLVKLFDSISDLQFEDNPEVstckaVGMFSKEKEYV 1520
Cdd:pfam08393 293 EKIQKSLNEYLEKKRLAFPRFYFLSNDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDENKEI-----TGMISKEGEVV 367
|
410 420
....*....|....*....|....*....
gi 1958786731 1521 SF-QAGCECIGHVESWLLQLEQTMKETVR 1548
Cdd:pfam08393 368 PFsKPPVEAKGNVEEWLNELEEEMRETLR 396
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4043-4338 |
1.35e-121 |
|
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: 386.98 E-value: 1.35e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 4043 TVTSNMLFRTLLEMQPRNAVSNEEQGQSTEDKVKNILDDILERLPEEFNMAEIMQKNP--NRSPYILVCFQECERMNVLL 4120
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGGSSREEIVLELAKDILEKLPEPFDIEEAEEKYPvgYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 4121 REIRVSLQHLDLGLKGELTLSPDVETQLSALSYDRVPDTWNKLAYPSTYGLAQWFNDLLLRCRELDTWTQDLTLPAVVWL 4200
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 4201 SGLFNPQSFLTAIMQTMARKNEWPLDRMCLTIDVTKK-TKEDYGHPPREGAYLHGLHLEGARWDIQSGALVDARLKELTS 4279
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKvSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958786731 4280 TMPVIFAKAIPADRQEVKHA-YECPVYKTKARGLT-YVWTFRLRSKDRIAKWVLAGVALLL 4338
Cdd:pfam18199 241 PLPVIHLKPVESDKKKLDENtYECPVYKTSERHSTnFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1376-3990 |
3.70e-116 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 417.08 E-value: 3.70e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1376 WSHLESIFVCSEDIRIQLVEDAQRFDEVDAEFKELMFKTAKIKNVLEATCRPhLYEKLKDFQHRLSLCEKALAEYLETKR 1455
Cdd:COG5245 627 RLDEYLMMMSLEDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQVFMSIEKVLGLRW 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1456 VTFSRFyfISSADLLDLLSKGAQPKQVTRHLVKLFDSISDLQFEDnpevSTCKAVGMFSKEKE-YVSFQAGCECIgHVES 1534
Cdd:COG5245 706 REVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEEMKTVFS----SRIQKKEPFSLDSEaYVGFFRLYEKS-IVIR 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1535 WLlqlEQTMKETVRLAIAEAIAAYEEKPRELWIFDFPAQVALTGSQIWwtTDVgiafsrLEEGYETALKDFHKkqisQLN 1614
Cdd:COG5245 779 GI---NRSMGRVLSQYLESVQEALEIEDGSFFVSRHRVRDGGLEKGRG--CDA------WENCFDPPLSEYFR----ILE 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1615 TLITLLLGELSPGDRQKVMTICTIDVHARDVVAKLISQKVVSPRAFTWLSqLRHEWEESRKHCIVNICDAHFQYCYEYLG 1694
Cdd:COG5245 844 KIFPSEEGYFFDEVLKRLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVS-ISELPQGLYKRFIKVRSSYRSAEMFAKNT 922
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1695 NSPRLVITPLTDRCYITLTQSLHLTMSGApagpAGTGKTETTKDLGRALGMMVyvfncsEQMDYRSigNIYKGLVQTGAW 1774
Cdd:COG5245 923 IPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEER 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1775 GcFDEFNRIAvEVLSVVAVQVKMIHDAIRSRRRRFVFLGETIPLKPSVGIFITLNPgyagRTELPENLKALFRPCAMVAP 1854
Cdd:COG5245 991 G-TEESALLD-EISRTILVDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIP 1064
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1855 dteliceimlvaEGFVDAR--SLARKFISLYTLCDELLSKQDHYDWglRAIKSVLVVAGSLKRgDKNRPEDQVLmralRD 1932
Cdd:COG5245 1065 ------------FGAIKSRreSLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRMLE-EKTEYLNKIL----SI 1125
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1933 FNMPKIvtDDVPVFLglvSDLFPALDVPRQRKPHFEQMVKQSTLELRLQPEESFILKVVQLEELLAVrhsifvVGNAGTG 2012
Cdd:COG5245 1126 TGLPLI--SDTLRER---IDTLDAEWDSFCRISESLKKYESQQVSGLDVAQFVSFLRSVDTGAFHAE------YFRVFLC 1194
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2013 KSKILRTL-------NRTYVnmkqkpvwndlnpkavtTDELFgfihHATREWKdGLLSSILREQANLT-HDGPTWIVLDG 2084
Cdd:COG5245 1195 KIKHYTDAcdylwhvKSPYV-----------------KKKYF----DADMELR-QFFLMFNREDMEARlADSKMEYEVER 1252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2085 didplWIESLNTVMDDNKVLTLASNERvaltpsmRLLFEthHLQTaTPATVSRAGILY----------VNPQDLG-WNPY 2153
Cdd:COG5245 1253 -----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLGS-IGDKVGRCLVEYdsisrlstkgVFLDELGdTKRY 1317
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2154 VASWIDRRRHQSEKANLTILFDkyIPVCLEKLRTSFKAITSVPEsslvQTICTLLECLLTPENIPSDSPKETYEVYFVFA 2233
Cdd:COG5245 1318 LDECLDFFSCFEEVQKEIDELS--MVFCADALRFSADLYHIVKE----RRFSGVLAGSDASESLGGKSIELAAILEHKDL 1391
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2234 CVWTFGG-------TLLRDQLSDYQADFSRW----WHKEMKAVKFPSQGTIFDYYLDHKTKKFLPwtdkVPQFTMDADAP 2302
Cdd:COG5245 1392 IVEMKRGindvlklRIFGDKCRESTPRFYLIsdgdLIKDLNERSDYEEMLIMMFNISAVITNNGS----IAGFELRGERV 1467
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2303 L--KTVLVHTPETTRLRYFTELLLNKGKPLMLVGNAGVGKTVFLSDTLASiSEDYIVSRVPFNYYTTSADLQRILEKPLE 2380
Cdd:COG5245 1468 MlrKEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS-ELITEVKYFNFSTCTMTPSKLSVLERETE 1546
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2381 K----KAGRNYGPRGNKKLVYFIDDLNMPEVDLYGTVQPHALLRQHIDY-GHWYDRHKvMLKEIRNCQYVACMNPMAGSF 2455
Cdd:COG5245 1547 YypntGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERqGFWSSIAV-SWVTICGIILYGACNPGTDEG 1625
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2456 TVD--PRLKRHFTVLAFNFPSLDTLTTIYgqifSFYLQQQAFC-PSVLRTGPSLIQATIAFHQTMAENFvPTAIKFHYNF 2532
Cdd:COG5245 1626 RVKyyERFIRKPVFVFCCYPELASLRNIY----EAVLMGSYLCfDEFNRLSEETMSASVELYLSSKDKT-KFFLQMNYGY 1700
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2533 NLRDLSNIFQGILFASPECLKCPE-DLARLWLHETSRVYGDRLVDANDSDLFQRKMLEAAHKYFKGADANTLQQQPLVYc 2611
Cdd:COG5245 1701 KPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEITF- 1779
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2612 hfaSGREDPCYEPVkDWEGLKAVLTEMMGNYNELHSEMHLVLFEDAMQHVCRISRILRTPQGHALLVGVGGSGKQSLSRL 2691
Cdd:COG5245 1780 ---SMILFFGMACL-LKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREF 1855
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2692 AAYICSLEVFQITLTEGYGTQDLRVDLANLYVRTGAKNMPTVFLLTDAHVLDESFLVLINDLLASGDIPGLFSDEDTDKI 2771
Cdd:COG5245 1856 VCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRI 1935
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2772 ISGIRNEVRGLGIT-DSRENCWAFFLARVRLQLKMVFCFSPVGHTLRVRARKFPALVNCTAIDWFHAWPQEALVSVSRRF 2850
Cdd:COG5245 1936 PENLRFVFESTSLEkDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGIRSPALKNRCFIDFKKLWDTEEMSQYANSV 2015
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2851 I-EEIEG-----IEPQHK--DSISLFMAYVHTSVKEVSAWYYQNERR-YNYTTPRSFLEQISLFKSLLKKKRGEVQRKKE 2921
Cdd:COG5245 2016 EtLSRDGgrvffINGELGvgKGALISEVFGDDAVVIEGRGFEISMIEgSLGESKIKFIGGLKVYDARCVIYIEELDCTNV 2095
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2922 HLGNGIQKLQTTASQVGNLKARLASQEAELQLRNQDAEALITKIgLQTEKVSREKAIADAEERKVAAIQTEASQKQRECE 3001
Cdd:COG5245 2096 NLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGT-PGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSV 2174
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3002 ADLLK-AEPALVAATAALNTLNRVNLTELKTFPNPPNAVTNVTAAVMVLLaprGRVPKDrsWKAARIFMgKVDDFLQALI 3080
Cdd:COG5245 2175 MKFKSsKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLL---GFEAKI--WFGEQQSL-RRDDFIRIIG 2248
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3081 NYDKE-HIPENCLKVVNEQYLKDPEFNPNLIRTKSFAAAGLCAWVINIIKFYEVYCDVEPKRQALAQTNLDLAAATEKLE 3159
Cdd:COG5245 2249 KYPDEiEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLT 2328
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3160 AVRRKLVDLDHNLRRLTASFEKATAEKVRCQEEVNQTNKTIDLANRLVSELESEKIRWGQSIKSFETQEKTLCGDVLLTA 3239
Cdd:COG5245 2329 LGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSS 2408
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3240 AFVSYIGSFTRQYRQ-ELVDCKwiPFLQQKVSIP-------IAEGLDMIatlTDDATIATWNNQGLPSDRMSTENATILt 3311
Cdd:COG5245 2409 CLHPYIGTLGFLCRAiEFGMSF--IRISKEFRDKeirrrqfITEGVQKI---EDFKEEACSTDYGLENSRIRKDLQDLT- 2482
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3312 hckrwPLMIDPQQQGIKWIKNKYGPdlKVTHLG---QKGFLNAIEMALAFGDVILIENlKETVDPVLGPLLGRNTIKKGK 3388
Cdd:COG5245 2483 -----AVLNDPSSKIVTSQRQMYDE--KKAILGsfrEMEFAFGLSQARREGSDKIIGD-AEALDEEIGRLIKEEFKSNLS 2554
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3389 YIR--IGDKECEFNKNFRLILHTKLANPHYKPELQAQTTLLNFTVTEDGLEGQLLAEVVSVERPDLERLKLVLTKHQNDF 3466
Cdd:COG5245 2555 EVKvmINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACG 2634
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3467 KIELRHLEEDLLLRLSAAEGSFLDDTDLVERLETTKATAAEIEHKVIEARENERKINETRECYRPVAARASLMYFVISDL 3546
Cdd:COG5245 2635 SLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMF 2714
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3547 RKINPVYQFSLKAFKTLFHRAIEQADKVEDTQERIcaLMESVTYatflhasqaLFEKDKLTFlsqmafqillrrneIHPL 3626
Cdd:COG5245 2715 DEKALMYNKSICELSSEFEKWRRMKSKYLCAIRYM--LMSSEWI---------LDHEDRSGF--------------IHRL 2769
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3627 ELDFLLRFTVEHTYSSPVDFLTAQSWSAVKAV--ALMEEFRGLDRDVEgSAKQWRKWVESECPEKEKLPQ-EWKKKSLIQ 3703
Cdd:COG5245 2770 DVSFLLRTKRFVSTLLEDKNYRQVLSSCSLYGndVISHSCDRFDRDVY-RALKHQMDNRTHSTILTSNSKtNPYKEYTYN 2848
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3704 KLIILRavrpdrmtyalrnFVEEKLGTKYvertrlDLGKAFGESSPGT-PVFFILSPGVDALKDLEVLGKRlgftidsgk 3782
Cdd:COG5245 2849 DSWAEA-------------FEVEDSGDLY------KFEEGLLELIVGHaPLIYAHKKSLENERNVDRLGSK--------- 2900
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3783 fhnvslgqGQELVAEMALEKAAIGGHWVFLQNVHLVAKWlgtLEKLLEKFSQGS-----HRDYRVFLSAEAAPSQhepvI 3857
Cdd:COG5245 2901 --------ENEVYAVLNSLFSRKEKSWFEVYNISLSFGW---FKRYVEDVVYPIkasrvCGKVKNMWTSMVDADM----L 2965
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3858 PQGLLENSIKITNEPPTGMLANLhAALYNFDQ---DTLEMCSKDqefksILFSLCYFHGCVAGRLRFGPQGWSRSYPFSP 3934
Cdd:COG5245 2966 PIQLLIAIDSFVSSTYPETGCGY-ADLVEIDRypfDYTLVIACD-----DAFYLSWEHAAVASVISAGPKENNEEIYFGD 3039
|
2650 2660 2670 2680 2690 2700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958786731 3935 GDLTICT----NILY-NHLEAnphVPWEDLRYLFGEIIYGGHITDAWD----RKLCRVYLEEFMN 3990
Cdd:COG5245 3040 KDFEFKThllkNILFlNHLNA---RKWGNNRDLIFTIVYGKKHSLMEDskvvDKYCRGYGAHETS 3101
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3290-3508 |
1.67e-109 |
|
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: 348.66 E-value: 1.67e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3290 ATWNNQGLPSDRMSTENATILTHCKRWPLMIDPQQQGIKWIKNKYGP-DLKVTHLGQKGFLNAIEMALAFGDVILIENLK 3368
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDnGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3369 ETVDPVLGPLLGRNTIKKG--KYIRIGDKECEFNKNFRLILHTKLANPHYKPELQAQTTLLNFTVTEDGLEGQLLAEVVS 3446
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGgrKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958786731 3447 VERPDLERLKLVLTKHQNDFKIELRHLEEDLLLRLSAAEGSFLDDTDLVERLETTKATAAEI 3508
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
2928-3022 |
2.39e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 43.56 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2928 QKLQTTASQVGNLKARLASQEAEL-QLRNQDAEALITKIGLQTEKVSREKAIADAEErKVAAIQTEASQKQ----RECEA 3002
Cdd:TIGR04320 247 TPIPNPPNSLAALQAKLATAQADLaAAQTALNTAQAALTSAQTAYAAAQAALATAQK-ELANAQAQALQTAqnnlATAQA 325
|
90 100
....*....|....*....|
gi 1958786731 3003 DLLKAEPALVAATAALNTLN 3022
Cdd:TIGR04320 326 ALANAEARLAKAKEALANLN 345
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1688-2014 |
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: 631.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1688 YCYEYLGNSPRLVITPLTDRCYITLTQSLHLTMSGAPAGPAGTGKTETTKDLGRALGMMVYVFNCSEQMDYRSIGNIYKG 1767
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1768 LVQTGAWGCFDEFNRIAVEVLSVVAVQVKMIHDAIRSRRRRFVFLGETIPLKPSVGIFITLNPGYAGRTELPENLKALFR 1847
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1848 PCAMVAPDTELICEIMLVAEGFVDARSLARKFISLYTLCDELLSKQDHYDWGLRAIKSVLVVAGSLKRGDKNRPEDQVLM 1927
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1928 RALRDFNMPKIVTDDVPVFLGLVSDLFPALDVPRQRKPHFEQMVKQSTLELRLQPEESFILKVVQLEELLAVRHSIFVVG 2007
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 1958786731 2008 NAGTGKS 2014
Cdd:pfam12774 321 PTGSGKT 327
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
46-617 |
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: 611.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 46 LHAIESVVIKWSHQIQEIIEKDSAqpllsGLHPTPETELDFWTMRHDNLKCIYHQLQAPIVLKMVKILRTRQSSYLPALK 125
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQ-----GRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 126 GIFTTVENALLEARDVELHLRPLRKHIQGLQEA-DFPQTGILIAPLIHTICLIWSHSKFYNSPARVIVLLQEFCNLFIDQ 204
Cdd:pfam08385 76 ALDTELTDALNEAKDNVKYLKTLERPFEDLEELtDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 205 ARAYLSPEDLLKGEIEDALEKVQVAIGVLRMFQNSFFKYRRGLTSYFTGdteqRPWDFQSHLVFSRFNKFLDRLVKIEDM 284
Cdd:pfam08385 156 CKKYLSPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRE----RPWDFSERYIFGRFDAFLERLEKILEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 285 FVTILEFEKLERLefGGSKGAVLNAQIHSMKEEFIECCNVFRQSIYDPSDCDSMEFESDYFQFKSKTLDFDRRLGTLLCE 364
Cdd:pfam08385 232 FETIEQFSKLEKI--GGTKGPELEGVIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 365 GLSNCSGLESAFKLLTIFGNFLEKPVVMEIFSPHYSTLLNMFNAELDMCKRLYDEHMKQiehgHEILNKNMPFTSGNIKW 444
Cdd:pfam08385 310 AFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQKYN----PSPIAKNMPPVAGAIIW 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 445 ARMLLERLQMFWSNFTSLHYLFpDSPDEAAVCQKYAEMTTLLDQFESRIYSEWRRNVDKTCEFNLNQPL-VKFSPINGLL 523
Cdd:pfam08385 386 ARQLFRRIQEPMKRFKEELGLL-KHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGNLKRPLlVRHPETGKLL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 524 SVNFDPKLVAVLREVKYLLMLkKSNIPDSALGIFQKKNIILKHIGNLELLVQGYNKLKQTLLEVEYPLIEKELGAIDEQL 603
Cdd:pfam08385 465 SVNFDPQLLALLREVKYLQKL-GFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKL 543
|
570
....*....|....
gi 1958786731 604 RVAATWLTWQDDFW 617
Cdd:pfam08385 544 EPGLTTLTWNSLGI 557
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
2921-3265 |
4.93e-171 |
|
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: 530.80 E-value: 4.93e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2921 EHLGNGIQKLQTTASQVGNLKARLASQEAELQLRNQDAEALITKIGLQTEKVSREKAIADAEERKVAAIQTEASQKQREC 3000
Cdd:pfam12777 1 ERLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3001 EADLLKAEPALVAATAALNTLNRVNLTELKTFPNPPNAVTNVTAAVMVLLAPRGRVPKDRSWKAARIFMGKVDDFLQALI 3080
Cdd:pfam12777 81 EEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGGKIPKDKSWKAAKIMMAKVDGFLDSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3081 NYDKEHIPENCLKVVnEQYLKDPEFNPNLIRTKSFAAAGLCAWVINIIKFYEVYCDVEPKRQALAQTNLDLAAATEKLEA 3160
Cdd:pfam12777 161 KFDKEHIHEACLKAF-KPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3161 VRRKLVDLDHNLRRLTASFEKATAEKVRCQEEVNQTNKTIDLANRLVSELESEKIRWGQSIKSFETQEKTLCGDVLLTAA 3240
Cdd:pfam12777 240 IKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISA 319
|
330 340
....*....|....*....|....*
gi 1958786731 3241 FVSYIGSFTRQYRQELVDCKWIPFL 3265
Cdd:pfam12777 320 FISYLGFFTKKYRNELLDKFWIPYI 344
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1122-1548 |
1.01e-138 |
|
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: 440.54 E-value: 1.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1122 MKQCRREVRLLKELWDIIVYVRRSIDNWTETRWRQVNMEQMDLELRRFAKEIWSLDKAVRVWDAYSGLEGTVKDMTTSLR 1201
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1202 AVAELQNPALRDRHWQQLTNAIGVRF-SINDSTTLADLLAVQLHQVEEDVRDIVDKAVKELGTEKVITDVSHTWEALEFS 1280
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFdPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1281 YEVHHRTGTPLLKSDEQLFETLEHNQSFLLGLGTSwlateplgsayshagilqvqlqtllqsKYVEYFIDQVLSWQNKLN 1360
Cdd:pfam08393 161 LVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSS---------------------------PYVKPFEEEVSEWEKKLS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1361 VADAVIFTWMQVQRTWSHLESIFVcSEDIRIQLVEDAQRFDEVDAEFKELMFKTAKIKNVLEATCRPHLYEKLKDFQHRL 1440
Cdd:pfam08393 214 LLQEILDEWLKVQRKWLYLEPIFS-SEDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1441 SLCEKALAEYLETKRVTFSRFYFISSADLLDLLSKGAQPKQVTRHLVKLFDSISDLQFEDNPEVstckaVGMFSKEKEYV 1520
Cdd:pfam08393 293 EKIQKSLNEYLEKKRLAFPRFYFLSNDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDENKEI-----TGMISKEGEVV 367
|
410 420
....*....|....*....|....*....
gi 1958786731 1521 SF-QAGCECIGHVESWLLQLEQTMKETVR 1548
Cdd:pfam08393 368 PFsKPPVEAKGNVEEWLNELEEEMRETLR 396
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4043-4338 |
1.35e-121 |
|
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: 386.98 E-value: 1.35e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 4043 TVTSNMLFRTLLEMQPRNAVSNEEQGQSTEDKVKNILDDILERLPEEFNMAEIMQKNP--NRSPYILVCFQECERMNVLL 4120
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGGSSREEIVLELAKDILEKLPEPFDIEEAEEKYPvgYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 4121 REIRVSLQHLDLGLKGELTLSPDVETQLSALSYDRVPDTWNKLAYPSTYGLAQWFNDLLLRCRELDTWTQDLTLPAVVWL 4200
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 4201 SGLFNPQSFLTAIMQTMARKNEWPLDRMCLTIDVTKK-TKEDYGHPPREGAYLHGLHLEGARWDIQSGALVDARLKELTS 4279
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKvSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958786731 4280 TMPVIFAKAIPADRQEVKHA-YECPVYKTKARGLT-YVWTFRLRSKDRIAKWVLAGVALLL 4338
Cdd:pfam18199 241 PLPVIHLKPVESDKKKLDENtYECPVYKTSERHSTnFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1376-3990 |
3.70e-116 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 417.08 E-value: 3.70e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1376 WSHLESIFVCSEDIRIQLVEDAQRFDEVDAEFKELMFKTAKIKNVLEATCRPhLYEKLKDFQHRLSLCEKALAEYLETKR 1455
Cdd:COG5245 627 RLDEYLMMMSLEDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQVFMSIEKVLGLRW 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1456 VTFSRFyfISSADLLDLLSKGAQPKQVTRHLVKLFDSISDLQFEDnpevSTCKAVGMFSKEKE-YVSFQAGCECIgHVES 1534
Cdd:COG5245 706 REVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEEMKTVFS----SRIQKKEPFSLDSEaYVGFFRLYEKS-IVIR 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1535 WLlqlEQTMKETVRLAIAEAIAAYEEKPRELWIFDFPAQVALTGSQIWwtTDVgiafsrLEEGYETALKDFHKkqisQLN 1614
Cdd:COG5245 779 GI---NRSMGRVLSQYLESVQEALEIEDGSFFVSRHRVRDGGLEKGRG--CDA------WENCFDPPLSEYFR----ILE 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1615 TLITLLLGELSPGDRQKVMTICTIDVHARDVVAKLISQKVVSPRAFTWLSqLRHEWEESRKHCIVNICDAHFQYCYEYLG 1694
Cdd:COG5245 844 KIFPSEEGYFFDEVLKRLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVS-ISELPQGLYKRFIKVRSSYRSAEMFAKNT 922
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1695 NSPRLVITPLTDRCYITLTQSLHLTMSGApagpAGTGKTETTKDLGRALGMMVyvfncsEQMDYRSigNIYKGLVQTGAW 1774
Cdd:COG5245 923 IPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEER 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1775 GcFDEFNRIAvEVLSVVAVQVKMIHDAIRSRRRRFVFLGETIPLKPSVGIFITLNPgyagRTELPENLKALFRPCAMVAP 1854
Cdd:COG5245 991 G-TEESALLD-EISRTILVDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNIP 1064
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1855 dteliceimlvaEGFVDAR--SLARKFISLYTLCDELLSKQDHYDWglRAIKSVLVVAGSLKRgDKNRPEDQVLmralRD 1932
Cdd:COG5245 1065 ------------FGAIKSRreSLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRMLE-EKTEYLNKIL----SI 1125
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1933 FNMPKIvtDDVPVFLglvSDLFPALDVPRQRKPHFEQMVKQSTLELRLQPEESFILKVVQLEELLAVrhsifvVGNAGTG 2012
Cdd:COG5245 1126 TGLPLI--SDTLRER---IDTLDAEWDSFCRISESLKKYESQQVSGLDVAQFVSFLRSVDTGAFHAE------YFRVFLC 1194
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2013 KSKILRTL-------NRTYVnmkqkpvwndlnpkavtTDELFgfihHATREWKdGLLSSILREQANLT-HDGPTWIVLDG 2084
Cdd:COG5245 1195 KIKHYTDAcdylwhvKSPYV-----------------KKKYF----DADMELR-QFFLMFNREDMEARlADSKMEYEVER 1252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2085 didplWIESLNTVMDDNKVLTLASNERvaltpsmRLLFEthHLQTaTPATVSRAGILY----------VNPQDLG-WNPY 2153
Cdd:COG5245 1253 -----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLGS-IGDKVGRCLVEYdsisrlstkgVFLDELGdTKRY 1317
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2154 VASWIDRRRHQSEKANLTILFDkyIPVCLEKLRTSFKAITSVPEsslvQTICTLLECLLTPENIPSDSPKETYEVYFVFA 2233
Cdd:COG5245 1318 LDECLDFFSCFEEVQKEIDELS--MVFCADALRFSADLYHIVKE----RRFSGVLAGSDASESLGGKSIELAAILEHKDL 1391
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2234 CVWTFGG-------TLLRDQLSDYQADFSRW----WHKEMKAVKFPSQGTIFDYYLDHKTKKFLPwtdkVPQFTMDADAP 2302
Cdd:COG5245 1392 IVEMKRGindvlklRIFGDKCRESTPRFYLIsdgdLIKDLNERSDYEEMLIMMFNISAVITNNGS----IAGFELRGERV 1467
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2303 L--KTVLVHTPETTRLRYFTELLLNKGKPLMLVGNAGVGKTVFLSDTLASiSEDYIVSRVPFNYYTTSADLQRILEKPLE 2380
Cdd:COG5245 1468 MlrKEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS-ELITEVKYFNFSTCTMTPSKLSVLERETE 1546
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2381 K----KAGRNYGPRGNKKLVYFIDDLNMPEVDLYGTVQPHALLRQHIDY-GHWYDRHKvMLKEIRNCQYVACMNPMAGSF 2455
Cdd:COG5245 1547 YypntGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERqGFWSSIAV-SWVTICGIILYGACNPGTDEG 1625
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2456 TVD--PRLKRHFTVLAFNFPSLDTLTTIYgqifSFYLQQQAFC-PSVLRTGPSLIQATIAFHQTMAENFvPTAIKFHYNF 2532
Cdd:COG5245 1626 RVKyyERFIRKPVFVFCCYPELASLRNIY----EAVLMGSYLCfDEFNRLSEETMSASVELYLSSKDKT-KFFLQMNYGY 1700
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2533 NLRDLSNIFQGILFASPECLKCPE-DLARLWLHETSRVYGDRLVDANDSDLFQRKMLEAAHKYFKGADANTLQQQPLVYc 2611
Cdd:COG5245 1701 KPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIGEAEITF- 1779
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2612 hfaSGREDPCYEPVkDWEGLKAVLTEMMGNYNELHSEMHLVLFEDAMQHVCRISRILRTPQGHALLVGVGGSGKQSLSRL 2691
Cdd:COG5245 1780 ---SMILFFGMACL-LKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRGACDAREF 1855
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2692 AAYICSLEVFQITLTEGYGTQDLRVDLANLYVRTGAKNMPTVFLLTDAHVLDESFLVLINDLLASGDIPGLFSDEDTDKI 2771
Cdd:COG5245 1856 VCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFSGNERIRI 1935
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2772 ISGIRNEVRGLGIT-DSRENCWAFFLARVRLQLKMVFCFSPVGHTLRVRARKFPALVNCTAIDWFHAWPQEALVSVSRRF 2850
Cdd:COG5245 1936 PENLRFVFESTSLEkDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGIRSPALKNRCFIDFKKLWDTEEMSQYANSV 2015
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2851 I-EEIEG-----IEPQHK--DSISLFMAYVHTSVKEVSAWYYQNERR-YNYTTPRSFLEQISLFKSLLKKKRGEVQRKKE 2921
Cdd:COG5245 2016 EtLSRDGgrvffINGELGvgKGALISEVFGDDAVVIEGRGFEISMIEgSLGESKIKFIGGLKVYDARCVIYIEELDCTNV 2095
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2922 HLGNGIQKLQTTASQVGNLKARLASQEAELQLRNQDAEALITKIgLQTEKVSREKAIADAEERKVAAIQTEASQKQRECE 3001
Cdd:COG5245 2096 NLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGT-PGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSV 2174
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3002 ADLLK-AEPALVAATAALNTLNRVNLTELKTFPNPPNAVTNVTAAVMVLLaprGRVPKDrsWKAARIFMgKVDDFLQALI 3080
Cdd:COG5245 2175 MKFKSsKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLL---GFEAKI--WFGEQQSL-RRDDFIRIIG 2248
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3081 NYDKE-HIPENCLKVVNEQYLKDPEFNPNLIRTKSFAAAGLCAWVINIIKFYEVYCDVEPKRQALAQTNLDLAAATEKLE 3159
Cdd:COG5245 2249 KYPDEiEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLT 2328
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3160 AVRRKLVDLDHNLRRLTASFEKATAEKVRCQEEVNQTNKTIDLANRLVSELESEKIRWGQSIKSFETQEKTLCGDVLLTA 3239
Cdd:COG5245 2329 LGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSS 2408
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3240 AFVSYIGSFTRQYRQ-ELVDCKwiPFLQQKVSIP-------IAEGLDMIatlTDDATIATWNNQGLPSDRMSTENATILt 3311
Cdd:COG5245 2409 CLHPYIGTLGFLCRAiEFGMSF--IRISKEFRDKeirrrqfITEGVQKI---EDFKEEACSTDYGLENSRIRKDLQDLT- 2482
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3312 hckrwPLMIDPQQQGIKWIKNKYGPdlKVTHLG---QKGFLNAIEMALAFGDVILIENlKETVDPVLGPLLGRNTIKKGK 3388
Cdd:COG5245 2483 -----AVLNDPSSKIVTSQRQMYDE--KKAILGsfrEMEFAFGLSQARREGSDKIIGD-AEALDEEIGRLIKEEFKSNLS 2554
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3389 YIR--IGDKECEFNKNFRLILHTKLANPHYKPELQAQTTLLNFTVTEDGLEGQLLAEVVSVERPDLERLKLVLTKHQNDF 3466
Cdd:COG5245 2555 EVKvmINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACG 2634
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3467 KIELRHLEEDLLLRLSAAEGSFLDDTDLVERLETTKATAAEIEHKVIEARENERKINETRECYRPVAARASLMYFVISDL 3546
Cdd:COG5245 2635 SLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMF 2714
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3547 RKINPVYQFSLKAFKTLFHRAIEQADKVEDTQERIcaLMESVTYatflhasqaLFEKDKLTFlsqmafqillrrneIHPL 3626
Cdd:COG5245 2715 DEKALMYNKSICELSSEFEKWRRMKSKYLCAIRYM--LMSSEWI---------LDHEDRSGF--------------IHRL 2769
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3627 ELDFLLRFTVEHTYSSPVDFLTAQSWSAVKAV--ALMEEFRGLDRDVEgSAKQWRKWVESECPEKEKLPQ-EWKKKSLIQ 3703
Cdd:COG5245 2770 DVSFLLRTKRFVSTLLEDKNYRQVLSSCSLYGndVISHSCDRFDRDVY-RALKHQMDNRTHSTILTSNSKtNPYKEYTYN 2848
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3704 KLIILRavrpdrmtyalrnFVEEKLGTKYvertrlDLGKAFGESSPGT-PVFFILSPGVDALKDLEVLGKRlgftidsgk 3782
Cdd:COG5245 2849 DSWAEA-------------FEVEDSGDLY------KFEEGLLELIVGHaPLIYAHKKSLENERNVDRLGSK--------- 2900
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3783 fhnvslgqGQELVAEMALEKAAIGGHWVFLQNVHLVAKWlgtLEKLLEKFSQGS-----HRDYRVFLSAEAAPSQhepvI 3857
Cdd:COG5245 2901 --------ENEVYAVLNSLFSRKEKSWFEVYNISLSFGW---FKRYVEDVVYPIkasrvCGKVKNMWTSMVDADM----L 2965
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3858 PQGLLENSIKITNEPPTGMLANLhAALYNFDQ---DTLEMCSKDqefksILFSLCYFHGCVAGRLRFGPQGWSRSYPFSP 3934
Cdd:COG5245 2966 PIQLLIAIDSFVSSTYPETGCGY-ADLVEIDRypfDYTLVIACD-----DAFYLSWEHAAVASVISAGPKENNEEIYFGD 3039
|
2650 2660 2670 2680 2690 2700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958786731 3935 GDLTICT----NILY-NHLEAnphVPWEDLRYLFGEIIYGGHITDAWD----RKLCRVYLEEFMN 3990
Cdd:COG5245 3040 KDFEFKThllkNILFlNHLNA---RKWGNNRDLIFTIVYGKKHSLMEDskvvDKYCRGYGAHETS 3101
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3290-3508 |
1.67e-109 |
|
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: 348.66 E-value: 1.67e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3290 ATWNNQGLPSDRMSTENATILTHCKRWPLMIDPQQQGIKWIKNKYGP-DLKVTHLGQKGFLNAIEMALAFGDVILIENLK 3368
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDnGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3369 ETVDPVLGPLLGRNTIKKG--KYIRIGDKECEFNKNFRLILHTKLANPHYKPELQAQTTLLNFTVTEDGLEGQLLAEVVS 3446
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGgrKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958786731 3447 VERPDLERLKLVLTKHQNDFKIELRHLEEDLLLRLSAAEGSFLDDTDLVERLETTKATAAEI 3508
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 ... |
2649-2908 |
5.86e-109 |
|
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: 348.83 E-value: 5.86e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2649 MHLVLFEDAMQHVCRISRILRTPQGHALLVGVGGSGKQSLSRLAAYICSLEVFQITLTEGYGTQDLRVDLANLYVRTGAK 2728
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2729 NMPTVFLLTDAHVLDESFLVLINDLLASGDIPGLFSDEDTDKIISGIRNEVRGLGITDSRENCWAFFLARVRLQLKMVFC 2808
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2809 FSPVGHTLRVRARKFPALVNCTAIDWFHAWPQEALVSVSRRFIEEIEGIEpQHKDSISLFMAYVHTSVKEVSAWYYQNER 2888
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDIEIPE-ELKSNVVKVFVYVHSSVEDMSKKFYEELK 239
|
250 260
....*....|....*....|
gi 1958786731 2889 RYNYTTPRSFLEQISLFKSL 2908
Cdd:pfam12780 240 RKNYVTPKSYLELLRLYKNL 259
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2298-2473 |
1.05e-86 |
|
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: 281.59 E-value: 1.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2298 DADAPLKTVLVHTPETTRLRYFTELLLNKGKPLMLVGNAGVGKTVFLSDTLASIS-EDYIVSRVPFNYYTTSADLQRILE 2376
Cdd:pfam12775 2 PPDVPFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDkEKYLPLFINFSAQTTSNQTQDIIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2377 KPLEKKAGRNYGPRGNKKLVYFIDDLNMPEVDLYGTVQPHALLRQHIDYGHWYDRHKVMLKEIRNCQYVACMNPMAGS-F 2455
Cdd:pfam12775 82 SKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPGGGrN 161
|
170
....*....|....*...
gi 1958786731 2456 TVDPRLKRHFTVLAFNFP 2473
Cdd:pfam12775 162 DITPRLLRHFNVFNITFP 179
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
3901-4037 |
3.32e-63 |
|
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: 212.70 E-value: 3.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3901 FKSILFSLCYFHGCVAGRLRFGPQGWSRSYPFSPGDLTICTNILYNHLEANPH-VPWEDLRYLFGEIIYGGHITDAWDRK 3979
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYDEkIPWDALRYLIGEINYGGRVTDDWDRR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958786731 3980 LCRVYLEEFMNPSLIEDELMLAPG-FAAPPYSDYSGYHQYIEDMLPPESPALYGLHPNA 4037
Cdd:pfam18198 81 LLNTYLEEFFNPEVLEEDFKFSPSlYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
3748-3869 |
4.41e-49 |
|
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: 171.09 E-value: 4.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 3748 SPGTPVFFILSPGVDALKDLEVLGKRLGFTidsGKFHNVSLGQGQELVAEMALEKAAIGGHWVFLQNVHLVAKWLGTLEK 3827
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGFG---GKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958786731 3828 LLEKF-SQGSHRDYRVFLSAEAAPSqhepvIPQGLLENSIKIT 3869
Cdd:pfam03028 78 ILEELpEETLHPDFRLWLTSEPSPK-----FPISILQNSIKIT 115
|
|
| AAA_lid_1 |
pfam17857 |
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3. |
2506-2595 |
3.79e-35 |
|
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: 130.83 E-value: 3.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2506 LIQATIAFHQTMAENFVPTAIKFHYNFNLRDLSNIFQGILFASPECLKCPEDLARLWLHETSRVYGDRLVDANDSDLFQR 2585
Cdd:pfam17857 1 LIAAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDK 80
|
90
....*....|
gi 1958786731 2586 KMLEAAHKYF 2595
Cdd:pfam17857 81 IQMASLKKFF 90
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2173-2290 |
2.83e-29 |
|
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: 115.07 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2173 LFDKYIPVCLEKLRTSFKAITSVPESSLVQTICTLLECLLTP-------ENIPSDSPKETYEVYFVFACVWTFGGTLLRD 2245
Cdd:pfam17852 4 LFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDEvleyngvHPLSPDKLKEYLEKLFLFALVWSIGGTLDED 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958786731 2246 QlsdyQADFSRWWHKEMKAVKFP--SQGTIFDYYLDHKTKKFLPWTD 2290
Cdd:pfam17852 84 S----RKKFDEFLRELFSGLDLPppEKGTVYDYFVDLEKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2002-2137 |
5.40e-11 |
|
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: 63.08 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2002 SIFVVGNAGTGKSKILRTLNRTYVNmkqKPVWNDLNPKAVTTDELFGFIHHATR--EWKDGLLSSILREqanlthdgpTW 2079
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSN---RPVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAARE---------GE 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958786731 2080 IVLDGDID---PLWIESLNTVMDDNKVLTLASNERV-ALTPSMRLLFETH----HLQTATPATVSR 2137
Cdd:pfam07728 69 IAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVkAAPDGFRLIATMNpldrGLNELSPALRSR 134
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2329-2465 |
6.01e-08 |
|
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: 54.22 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2329 PLMLVGNAGVGKTvFLSDTLASISEDYIVSRVPFNYYTTSADLQRILEkPLEKKAGRNYGP---RGNKKLVYFIDDLNMP 2405
Cdd:pfam07728 1 GVLLVGPPGTGKT-ELAERLAAALSNRPVFYVQLTRDTTEEDLFGRRN-IDPGGASWVDGPlvrAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958786731 2406 EVDLYGTVQPhaLL---RQHIDYGHWYDRHK---VMLkeirncqyVACMNP-MAGSFTVDPRLKRHF 2465
Cdd:pfam07728 79 NPDVLNSLLS--LLderRLLLPDGGELVKAApdgFRL--------IATMNPlDRGLNELSPALRSRF 135
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1726-1846 |
1.58e-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: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 1726 GPAGTGKTETTKDLGRAL-GMMVYVFNCSEQMDY------RSIGNIYKGLV--------QTGAWGCFDEFNRIAVEVLSV 1790
Cdd:pfam07728 6 GPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEedlfgrRNIDPGGASWVdgplvraaREGEIAVLDEINRANPDVLNS 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958786731 1791 VavqvkmiHDAIRSRRRRFVFLGETIPLKP-SVGIFITLNPGYAGRTELPENLKALF 1846
Cdd:pfam07728 86 L-------LSLLDERRLLLPDGGELVKAAPdGFRLIATMNPLDRGLNELSPALRSRF 135
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
3147-3211 |
5.02e-04 |
|
Laminin Domain II; 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: 368703 [Multi-domain] Cd Length: 138 Bit Score: 43.24 E-value: 5.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958786731 3147 TNLDLAAATEKLEAVRRKLVDLDHNLRRLTASFEKATAEKVRCQEEVNQTNKTIDLANRLVSELE 3211
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLE 65
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
2928-3022 |
2.39e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 43.56 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958786731 2928 QKLQTTASQVGNLKARLASQEAEL-QLRNQDAEALITKIGLQTEKVSREKAIADAEErKVAAIQTEASQKQ----RECEA 3002
Cdd:TIGR04320 247 TPIPNPPNSLAALQAKLATAQADLaAAQTALNTAQAALTSAQTAYAAAQAALATAQK-ELANAQAQALQTAqnnlATAQA 325
|
90 100
....*....|....*....|
gi 1958786731 3003 DLLKAEPALVAATAALNTLN 3022
Cdd:TIGR04320 326 ALANAEARLAKAKEALANLN 345
|
|
| |
