|
Name |
Accession |
Description |
Interval |
E-value |
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
250-802 |
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: 632.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 250 VEKVECCMRVWIKQMEQILAENSQLRKEaddvGPRAELEHWKQRLSRFNYLLDQLKSPDVKAALALLAAAKSKLLKVWRD 329
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNP----GPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 330 TDIRITDAANEAKDNVKYLYTLEKCCDPLYS-SDPVTMIDAIPTLINAIKMVYSISHYYNTSEKITSLFVKVTNQMISAC 408
Cdd:pfam08385 77 LDTELTDALNEAKDNVKYLKTLERPFEDLEElTDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 409 KAHITNNGtatIWSQPQEIVMQKIAAVIKLKQGYQSCFQETKQKLKQNPSEKQFDFSEMYIFGKFETFHRRLAKIMDIFT 488
Cdd:pfam08385 157 KKYLSPEG---IFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWDFSERYIFGRFDAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 489 TFKTYSVLQDSK------IEG-LEDMATKYQDIVAAIKKKEYNFLDQREMDFDQDYEEFCKRINELHNDLQRFMDITFEK 561
Cdd:pfam08385 234 TIEQFSKLEKIGgtkgpeLEGvIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 562 IPSTRQALSTLKKFE-RLNIPNL--GIEEKYQIIFQNFATDIDTISKLYTKQKYDP-PLARNQPPIAGKILWARQLFHRL 637
Cdd:pfam08385 314 ARSTESAFKLLRIFEfLLERPIIrgALEEKYTDLLQMFKKELDAVKKIFDKQKYNPsPIAKNMPPVAGAIIWARQLFRRI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 638 EQPMQLFQQHPFVLRTAEAKPVIRSYNRIAKVLLEFEVLYHRAWLQQIEEIHAG-LEASLLVKAPGTGELF-VNFDPQIL 715
Cdd:pfam08385 394 QEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGnLKRPLLVRHPETGKLLsVNFDPQLL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 716 VLFRETQCMSQLGLPVSPFAAALFQKRDMFKKNFSDMKMMLSEYERVKLKMPPAIEQLMFPHLARVDEALQPGLAVLTWT 795
Cdd:pfam08385 474 ALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTWN 553
|
....*..
gi 342672105 796 SLNIGGY 802
Cdd:pfam08385 554 SLGIDEY 560
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1939-2266 |
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: 598.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1939 YQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKG 2018
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2019 LAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINF 2098
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2099 RSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYQLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRASPTDTESTIV 2178
Cdd:pfam12774 160 RPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2179 MRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELETAISKQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTL 2258
Cdd:pfam12774 240 LRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLV 319
|
....*...
gi 342672105 2259 GPSGSGKT 2266
Cdd:pfam12774 320 GPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1399-1804 |
2.99e-148 |
|
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: 467.89 E-value: 2.99e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1399 LLEIKRQLNLLQKIYSLYNNVIETVNSYQDTLWSDVNIEKINNELLEFQNRCRKLPRALKDWQAFLDLKKTIDDFSECCP 1478
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1479 LLEYMASNAMVERHWQRITALTGHSLDVGNETFKLRNIMEAPLLKYKEEIEDICISAVKERDIEQKLRQVINEWDNKTLT 1558
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1559 FSGFKTRGELLLRGdsTSEVIASMEDSLMLLGSLLSNRYNMPFKAQIQKWVQCLSNSTDIIENWMTVQNLWIYLEAVFVG 1638
Cdd:pfam08393 161 LVPYKDTGTFILKG--WDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1639 GDIAKQLPKEAKRFSNIDKSWVKIMTRAHEIPNVVQCCvGDETMGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVS 1718
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEAC-NIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1719 DPALLEILGQASDSHTIQAHLLNVFDNIKTVKFHDkiYDRILSISSREGETIELDKP-VMAEGNVEVWLNSLLEESQSSL 1797
Cdd:pfam08393 318 NDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE--NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 342672105 1798 HLVIRQA 1804
Cdd:pfam08393 396 RDLLKEA 402
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1640-4282 |
3.55e-127 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 453.29 E-value: 3.55e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1640 DIAKQLPKEAKRFSNIDKSWVKIMTRaheipnVVQCCVGDETM----GQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFF 1715
Cdd:COG5245 639 DLMPLIPHAVHRKMSLVSGVRGIYKR------VVSGCEAINTIledvGDDLDLFYKEMDQVFMSIEKVLGLRWREVERAS 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1716 FVSDpaLLEILGQASDSHTIQAHLLNVFDNIKTVKFhdkIYDRILSISSREGETIELDKPVMAEGNVEV--WLN----SL 1789
Cdd:COG5245 713 EVEE--LMDRVRELENRVYSYRFFVKKIAKEEMKTV---FSSRIQKKEPFSLDSEAYVGFFRLYEKSIVirGINrsmgRV 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1790 LEESQSSLhlvirQAAANIQEPGFqlieFLSSFPAQVGLLGIQMlWTRDSEEALRNA------KFDKKIMQKTNQAFLEL 1863
Cdd:COG5245 788 LSQYLESV-----QEALEIEDGSF----FVSRHRVRDGGLEKGR-GCDAWENCFDPPlseyfrILEKIFPSEEGYFFDEV 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1864 LNmlieittkdlssmervKYETLITIHVHQRDIFDDLCHMHVKSPTDFEWLKQCRFYFKEDsDKTMIHITDVAFIYQNEF 1943
Cdd:COG5245 858 LK----------------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLY-KRFIKVRSSYRSAEMFAK 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1944 LGCTDRLVITPLTDRCYITLAQALGMSMggapAGPAGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSG 2023
Cdd:COG5245 921 NTIPFFVFEHSMDTSQHQKLFEAVCDEV----CRFVDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEE 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2024 SWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEHKKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSV 2101
Cdd:COG5245 989 ERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMF 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2102 AMMVPDRQIIIRVKlascgfidnvVLARKFFTLYQLCEEQLSKQVHYDFglRNILSVLRtlgAAKR--ASPTDTESTIVm 2179
Cdd:COG5245 1060 LSNIPFGAIKSRRE----------SLDREIGAFNNEVDGIAREEDELMF--YPMFKSLK---AKHRmlEEKTEYLNKIL- 1123
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2180 rvlrdmnlsklidedEPLFLSLIEDLFPNI--LLDKAGYPELETAISKQVEEAGLINHPPWKlKVIQLFETQRVRHGMMT 2257
Cdd:COG5245 1124 ---------------SITGLPLISDTLRERidTLDAEWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGAFHAE 1187
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2258 LGPSGSGKTTCIHTLMKAMTDCGKPHREMRMnpkaitapqmfgrLDvATNDWTdGIFSTLWRKTLKAK-KGEHIWIVLDG 2336
Cdd:COG5245 1188 YFRVFLCKIKHYTDACDYLWHVKSPYVKKKY-------------FD-ADMELR-QFFLMFNREDMEARlADSKMEYEVER 1252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2337 pvdaiWIENLNSVLDDNKTLTLANGDRipmapncKIVFEphNIDnASPATVSRNGMVFMSSSVLDWSPILEGFL------ 2410
Cdd:COG5245 1253 -----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgdtkry 1317
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2411 --KRRSPQEAEILRQLYAETF-----PDLYRFSIqNLEFKMEVLEAFVITQSTHMLQGLIPPKEQAGEV--DPE---HLG 2478
Cdd:COG5245 1318 ldECLDFFSCFEEVQKEIDELsmvfcADALRFSA-DLYHIVKERRFSGVLAGSDASESLGGKSIELAAIleHKDlivEMK 1396
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2479 RLFVFAMMWSVGAVLELEGRRRMELWLRSREGptLHLPQLTDAGDT---MF--DYYVAPNGTWRHWSLCTPEYVYPPDtt 2553
Cdd:COG5245 1397 RGINDVLKLRIFGDKCRESTPRFYLISDGDLI--KDLNERSDYEEMlimMFniSAVITNNGSIAGFELRGERVMLRKE-- 1472
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2554 peygsILVPNVDNVRTDFLIKTIAKQGKAVLLIGEQGTAKTVIIKG-FMSKFDPEshmVKNLNFSSATTP----VMFQRT 2628
Cdd:COG5245 1473 -----VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPsLRSELITE---VKYFNFSTCTMTpsklSVLERE 1544
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2629 IESYVDKRMGTTYGPPAGKKMAVFIDDLNMPVINEWGDQVTNEIVRQLMEQSGFYN-LEKpgEFTSIVDIqFLAAMIHPG 2707
Cdd:COG5245 1545 TEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGACNPG 1621
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2708 G--GRNDIPQRLKRQFSIFNCTLPSDASMDKIF-GVIGAGYYCAQ--RGFSEEVQDALIKLVPLTRRLWQmTKLKMlptp 2782
Cdd:COG5245 1622 TdeGRVKYYERFIRKPVFVFCCYPELASLRNIYeAVLMGSYLCFDefNRLSEETMSASVELYLSSKDKTK-FFLQM---- 1696
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2783 akfHYVFNLRDLSRIWQGMLNITSEVIKDTD-ELLRLWKHECKRVIADRFSMSSDVTWFDKAVVSLVEEEFGEEKAPVVD 2861
Cdd:COG5245 1697 ---NYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIG 1773
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2862 CG----VDAYFVDFlrdapeatgetpeeadAEMPKlyepiASL-NHLRERLSVFlqlYNESIRGTgmdMVFFIDAMVHLV 2936
Cdd:COG5245 1774 EAeitfSMILFFGM----------------ACLLK-----KDLaVFVEEVRKIF---GSSHLDVE---AVAYKDALLHIL 1826
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2937 KISRVIRTPRGNALLVGVGGSGKQSLTRLASFIAGYTSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNEIK 3016
Cdd:COG5245 1827 RSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPV 1906
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3017 EESFLEYMNNVLSSGEVSNLFARDEIDEINSDLTPIMKKEhPRRPPTNDNLYEYFMSRVRGNLHIVL-CFSPVGEKFRNR 3095
Cdd:COG5245 1907 ESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVLAG 1985
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3096 ALkFPALISGCTIDWFSRWPKDALVAVSEHFLS-SYTIDCTAEIKKELVQCMGS-FQDGVAEKCADYFQR-FRRSTHV-- 3170
Cdd:COG5245 1986 IR-SPALKNRCFIDFKKLWDTEEMSQYANSVETlSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIEgs 2064
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3171 TPKSYLSFIQG---YKFIYEEKHMEVQSLANRMNTGLEKLKEASESVAALSKELAGKEKELQVANEKADTVLKEVTMKAQ 3247
Cdd:COG5245 2065 LGESKIKFIGGlkvYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERL 2144
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3248 AAEKVKAEVQKVKDKAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIKPSDIATVRTLGRPPHLIMRIMD--CVLL 3325
Cdd:COG5245 2145 EREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCDLL 2224
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3326 LFQRRVnavkidvdkgctmpsWQESLKLMTAGNFLQNLQQFPkDTIN--------EEVIEFLNPYFEMSDYNieTAKRVC 3397
Cdd:COG5245 2225 GFEAKI---------------WFGEQQSLRRDDFIRIIGKYP-DEIEfdlearrfREARECSDPSFTGSILN--RASKAC 2286
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3398 GNvagLCSWTKAMASFFSINKEVLPLKANLIVQENRHILAMQDLQKAQAELDAKQAELDVVQAEYEQAMAEKQTLLEDAD 3477
Cdd:COG5245 2287 GP---LKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMD 2363
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3478 RCRHKMQTASTLISGLAGEKERWTEQSKEFAAQTKRLVGDVLLATAFLSYSGPFNQEFRDLLLHDWK----KEMKARKIp 3553
Cdd:COG5245 2364 TVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGMSFirisKEFRDKEI- 2442
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3554 fGNGLNLNEMLidaPTISEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESQNELQITSLNHKYFRNH 3633
Cdd:COG5245 2443 -RRRQFITEGV---QKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFG 2518
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3634 LEDSLSLGRPLLIEDvGEELDPALDNVLEKNFIKTGSTFKVKVGDKEVDVMDGFKLYITTKLPNPAYTPEISARTSIIDF 3713
Cdd:COG5245 2519 LSQARREGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMF 2597
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3714 TVTVKGLEDQLLGRVILTEKQELEKERTHLLEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIIVLSNTKKTAEEVT 3793
Cdd:COG5245 2598 VSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIE 2677
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3794 QKLEISGETEIQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLFDlsLARSVKSpitskRIANIIEHMT 3873
Cdd:COG5245 2678 EEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFE--KWRRMKS-----KYLCAIRYML 2750
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3874 YEVFKYaargLYEEhkflFTLLLTLKIDIQRNLVKHEEFLTLIK-GGASLDLKACppkpskwildmtWLNLVELsklkqF 3952
Cdd:COG5245 2751 MSSEWI----LDHE----DRSGFIHRLDVSFLLRTKRFVSTLLEdKNYRQVLSSC------------SLYGNDV-----I 2805
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3953 SDILDQISRNekMWRVWFDKENPEEEPLPNAYDKSLDCFRRLLLIRSWcpdrtiaqARKYIMDSMGENYaegvilDLEK- 4031
Cdd:COG5245 2806 SHSCDRFDRD--VYRALKHQMDNRTHSTILTSNSKTNPYKEYTYNDSW--------AEAFEVEDSGDLY------KFEEg 2869
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4032 TWEESDPRTPLICLLsMGSDPTDSIIalgKRLKIETRyvsmgqgqEVHARKLLHQTMANGGWVLLQNCHLGLDFLDELM- 4110
Cdd:COG5245 2870 LLELIVGHAPLIYAH-KKSLENERNV---DRLGSKEN--------EVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYVe 2937
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4111 DVVTET---ETVHDTFRLWITTEVHKQFPITLLQMSIKFANEppqglraglrrTYGGVSQDLLDVsVGAQWKPMLYA--- 4184
Cdd:COG5245 2938 DVVYPIkasRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSS-----------TYPETGCGYADL-VEIDRYPFDYTlvi 3005
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4185 -------VAFLHSTVQERRKFGPLGWNIPYEFNQADFNATVQFIQNHLdDMDVKKGVSWTTVRYMIGEIQYGGR------ 4251
Cdd:COG5245 3006 acddafyLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNIL-FLNHLNARKWGNNRDLIFTIVYGKKhslmed 3084
|
2730 2740 2750
....*....|....*....|....*....|...
gi 342672105 4252 --VTDDYDKRLLNTFAKVWFSENMFGPDFTFYQ 4282
Cdd:COG5245 3085 skVVDKYCRGYGAHETSSQILASVPGGDPELVK 3117
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4326-4618 |
1.14e-124 |
|
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: 395.84 E-value: 1.14e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4326 AKDVLDTILGIQPKDSSG--GGDETREAVVARLADDMLEKLPEDYSpFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSL 4403
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGggGGGSSREEIVLELAKDILEKLPEPFD-IEEAEEKYPVGYEDPLNTVLLQEIERFNKLLKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4404 VRSTLTELKLAVDGTIIMSENLRDALDCMFDARIPARWKKASWVSS-TLGFWFTELLERNCQFTSWVS-NGRPHCFWMTG 4481
Cdd:pfam18199 83 IRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLkPLGSWIRDLLERLKQLQDWLDdEGPPKVFWLSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4482 FFNPQGFLTAMRQEITRANKgWALDNMVLCNEVTKFM-KDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFEL 4560
Cdd:pfam18199 163 FFFPQAFLTAVLQNYARKNG-WPIDKLSFDFEVTKKVsPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFSP 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4561 MPVIRIFAENNT--ARDPRLYCCPIYKKPVRTDLNYIAAVDLKTAQAPEHWVLRGVALLC 4618
Cdd:pfam18199 242 LPVIHLKPVESDkkKLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3571-3792 |
4.27e-117 |
|
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: 370.62 E-value: 4.27e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3571 SEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESQNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVG 3650
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3651 EELDPALDNVLEKNFIKTGSTFKVKVGDKEVDVMDGFKLYITTKLPNPAYTPEISARTSIIDFTVTVKGLEDQLLGRVIL 3730
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 342672105 3731 TEKQELEKERTHLLEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIIVLSNTKKTAEEV 3792
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
3196-3297 |
4.05e-07 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 53.04 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3196 LANRMNTGLEKLKEASESVAALSKELAGKEKELQVANEKADTVLKEVTMKAQA-----AEKVKAEVQKVKDKAQAIVDSi 3270
Cdd:PRK07352 48 LEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAiraeiEKQAIEDMARLKQTAAADLSA- 126
|
90 100
....*....|....*....|....*..
gi 342672105 3271 SKDKAIAEEKLEAAKPALEEAEAALQT 3297
Cdd:PRK07352 127 EQERVIAQLRREAAELAIAKAESQLPG 153
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3205-3294 |
8.57e-05 |
|
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: 48.30 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3205 EKLKEASESVAALSKELAGKEKELQVANEKADtvlKEVTMKAQAAEKVKAEVQKVKDKAQAivdsisKDKAIAEEKLeAA 3284
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEA------KAKAEAEAKA-KA 191
|
90
....*....|
gi 342672105 3285 KPALEEAEAA 3294
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 ... |
3196-3296 |
2.25e-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: 43.97 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3196 LANRMNTGLEKLKEASESVAALSKELAGKEKELQVANEKADTVLKE-----VTMKAQAAEKVKAEVQKVKDKAQAIVDSi 3270
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEAERILEQAKAEIEQ- 106
|
90 100
....*....|....*....|....*.
gi 342672105 3271 SKDKAIAEEKLEAAKPALEEAEAALQ 3296
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 ... |
250-802 |
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: 632.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 250 VEKVECCMRVWIKQMEQILAENSQLRKEaddvGPRAELEHWKQRLSRFNYLLDQLKSPDVKAALALLAAAKSKLLKVWRD 329
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNP----GPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 330 TDIRITDAANEAKDNVKYLYTLEKCCDPLYS-SDPVTMIDAIPTLINAIKMVYSISHYYNTSEKITSLFVKVTNQMISAC 408
Cdd:pfam08385 77 LDTELTDALNEAKDNVKYLKTLERPFEDLEElTDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 409 KAHITNNGtatIWSQPQEIVMQKIAAVIKLKQGYQSCFQETKQKLKQNPSEKQFDFSEMYIFGKFETFHRRLAKIMDIFT 488
Cdd:pfam08385 157 KKYLSPEG---IFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWDFSERYIFGRFDAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 489 TFKTYSVLQDSK------IEG-LEDMATKYQDIVAAIKKKEYNFLDQREMDFDQDYEEFCKRINELHNDLQRFMDITFEK 561
Cdd:pfam08385 234 TIEQFSKLEKIGgtkgpeLEGvIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 562 IPSTRQALSTLKKFE-RLNIPNL--GIEEKYQIIFQNFATDIDTISKLYTKQKYDP-PLARNQPPIAGKILWARQLFHRL 637
Cdd:pfam08385 314 ARSTESAFKLLRIFEfLLERPIIrgALEEKYTDLLQMFKKELDAVKKIFDKQKYNPsPIAKNMPPVAGAIIWARQLFRRI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 638 EQPMQLFQQHPFVLRTAEAKPVIRSYNRIAKVLLEFEVLYHRAWLQQIEEIHAG-LEASLLVKAPGTGELF-VNFDPQIL 715
Cdd:pfam08385 394 QEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGnLKRPLLVRHPETGKLLsVNFDPQLL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 716 VLFRETQCMSQLGLPVSPFAAALFQKRDMFKKNFSDMKMMLSEYERVKLKMPPAIEQLMFPHLARVDEALQPGLAVLTWT 795
Cdd:pfam08385 474 ALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTWN 553
|
....*..
gi 342672105 796 SLNIGGY 802
Cdd:pfam08385 554 SLGIDEY 560
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1939-2266 |
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: 598.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1939 YQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKG 2018
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2019 LAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINF 2098
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2099 RSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYQLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRASPTDTESTIV 2178
Cdd:pfam12774 160 RPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2179 MRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELETAISKQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTL 2258
Cdd:pfam12774 240 LRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLV 319
|
....*...
gi 342672105 2259 GPSGSGKT 2266
Cdd:pfam12774 320 GPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1399-1804 |
2.99e-148 |
|
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: 467.89 E-value: 2.99e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1399 LLEIKRQLNLLQKIYSLYNNVIETVNSYQDTLWSDVNIEKINNELLEFQNRCRKLPRALKDWQAFLDLKKTIDDFSECCP 1478
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1479 LLEYMASNAMVERHWQRITALTGHSLDVGNETFKLRNIMEAPLLKYKEEIEDICISAVKERDIEQKLRQVINEWDNKTLT 1558
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1559 FSGFKTRGELLLRGdsTSEVIASMEDSLMLLGSLLSNRYNMPFKAQIQKWVQCLSNSTDIIENWMTVQNLWIYLEAVFVG 1638
Cdd:pfam08393 161 LVPYKDTGTFILKG--WDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1639 GDIAKQLPKEAKRFSNIDKSWVKIMTRAHEIPNVVQCCvGDETMGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVS 1718
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEAC-NIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1719 DPALLEILGQASDSHTIQAHLLNVFDNIKTVKFHDkiYDRILSISSREGETIELDKP-VMAEGNVEVWLNSLLEESQSSL 1797
Cdd:pfam08393 318 NDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE--NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 342672105 1798 HLVIRQA 1804
Cdd:pfam08393 396 RDLLKEA 402
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1640-4282 |
3.55e-127 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 453.29 E-value: 3.55e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1640 DIAKQLPKEAKRFSNIDKSWVKIMTRaheipnVVQCCVGDETM----GQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFF 1715
Cdd:COG5245 639 DLMPLIPHAVHRKMSLVSGVRGIYKR------VVSGCEAINTIledvGDDLDLFYKEMDQVFMSIEKVLGLRWREVERAS 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1716 FVSDpaLLEILGQASDSHTIQAHLLNVFDNIKTVKFhdkIYDRILSISSREGETIELDKPVMAEGNVEV--WLN----SL 1789
Cdd:COG5245 713 EVEE--LMDRVRELENRVYSYRFFVKKIAKEEMKTV---FSSRIQKKEPFSLDSEAYVGFFRLYEKSIVirGINrsmgRV 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1790 LEESQSSLhlvirQAAANIQEPGFqlieFLSSFPAQVGLLGIQMlWTRDSEEALRNA------KFDKKIMQKTNQAFLEL 1863
Cdd:COG5245 788 LSQYLESV-----QEALEIEDGSF----FVSRHRVRDGGLEKGR-GCDAWENCFDPPlseyfrILEKIFPSEEGYFFDEV 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1864 LNmlieittkdlssmervKYETLITIHVHQRDIFDDLCHMHVKSPTDFEWLKQCRFYFKEDsDKTMIHITDVAFIYQNEF 1943
Cdd:COG5245 858 LK----------------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLY-KRFIKVRSSYRSAEMFAK 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 1944 LGCTDRLVITPLTDRCYITLAQALGMSMggapAGPAGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSG 2023
Cdd:COG5245 921 NTIPFFVFEHSMDTSQHQKLFEAVCDEV----CRFVDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEE 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2024 SWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEHKKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSV 2101
Cdd:COG5245 989 ERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMF 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2102 AMMVPDRQIIIRVKlascgfidnvVLARKFFTLYQLCEEQLSKQVHYDFglRNILSVLRtlgAAKR--ASPTDTESTIVm 2179
Cdd:COG5245 1060 LSNIPFGAIKSRRE----------SLDREIGAFNNEVDGIAREEDELMF--YPMFKSLK---AKHRmlEEKTEYLNKIL- 1123
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2180 rvlrdmnlsklidedEPLFLSLIEDLFPNI--LLDKAGYPELETAISKQVEEAGLINHPPWKlKVIQLFETQRVRHGMMT 2257
Cdd:COG5245 1124 ---------------SITGLPLISDTLRERidTLDAEWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGAFHAE 1187
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2258 LGPSGSGKTTCIHTLMKAMTDCGKPHREMRMnpkaitapqmfgrLDvATNDWTdGIFSTLWRKTLKAK-KGEHIWIVLDG 2336
Cdd:COG5245 1188 YFRVFLCKIKHYTDACDYLWHVKSPYVKKKY-------------FD-ADMELR-QFFLMFNREDMEARlADSKMEYEVER 1252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2337 pvdaiWIENLNSVLDDNKTLTLANGDRipmapncKIVFEphNIDnASPATVSRNGMVFMSSSVLDWSPILEGFL------ 2410
Cdd:COG5245 1253 -----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgdtkry 1317
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2411 --KRRSPQEAEILRQLYAETF-----PDLYRFSIqNLEFKMEVLEAFVITQSTHMLQGLIPPKEQAGEV--DPE---HLG 2478
Cdd:COG5245 1318 ldECLDFFSCFEEVQKEIDELsmvfcADALRFSA-DLYHIVKERRFSGVLAGSDASESLGGKSIELAAIleHKDlivEMK 1396
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2479 RLFVFAMMWSVGAVLELEGRRRMELWLRSREGptLHLPQLTDAGDT---MF--DYYVAPNGTWRHWSLCTPEYVYPPDtt 2553
Cdd:COG5245 1397 RGINDVLKLRIFGDKCRESTPRFYLISDGDLI--KDLNERSDYEEMlimMFniSAVITNNGSIAGFELRGERVMLRKE-- 1472
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2554 peygsILVPNVDNVRTDFLIKTIAKQGKAVLLIGEQGTAKTVIIKG-FMSKFDPEshmVKNLNFSSATTP----VMFQRT 2628
Cdd:COG5245 1473 -----VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPsLRSELITE---VKYFNFSTCTMTpsklSVLERE 1544
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2629 IESYVDKRMGTTYGPPAGKKMAVFIDDLNMPVINEWGDQVTNEIVRQLMEQSGFYN-LEKpgEFTSIVDIqFLAAMIHPG 2707
Cdd:COG5245 1545 TEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGACNPG 1621
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2708 G--GRNDIPQRLKRQFSIFNCTLPSDASMDKIF-GVIGAGYYCAQ--RGFSEEVQDALIKLVPLTRRLWQmTKLKMlptp 2782
Cdd:COG5245 1622 TdeGRVKYYERFIRKPVFVFCCYPELASLRNIYeAVLMGSYLCFDefNRLSEETMSASVELYLSSKDKTK-FFLQM---- 1696
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2783 akfHYVFNLRDLSRIWQGMLNITSEVIKDTD-ELLRLWKHECKRVIADRFSMSSDVTWFDKAVVSLVEEEFGEEKAPVVD 2861
Cdd:COG5245 1697 ---NYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIG 1773
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2862 CG----VDAYFVDFlrdapeatgetpeeadAEMPKlyepiASL-NHLRERLSVFlqlYNESIRGTgmdMVFFIDAMVHLV 2936
Cdd:COG5245 1774 EAeitfSMILFFGM----------------ACLLK-----KDLaVFVEEVRKIF---GSSHLDVE---AVAYKDALLHIL 1826
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2937 KISRVIRTPRGNALLVGVGGSGKQSLTRLASFIAGYTSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNEIK 3016
Cdd:COG5245 1827 RSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPV 1906
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3017 EESFLEYMNNVLSSGEVSNLFARDEIDEINSDLTPIMKKEhPRRPPTNDNLYEYFMSRVRGNLHIVL-CFSPVGEKFRNR 3095
Cdd:COG5245 1907 ESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVLAG 1985
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3096 ALkFPALISGCTIDWFSRWPKDALVAVSEHFLS-SYTIDCTAEIKKELVQCMGS-FQDGVAEKCADYFQR-FRRSTHV-- 3170
Cdd:COG5245 1986 IR-SPALKNRCFIDFKKLWDTEEMSQYANSVETlSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIEgs 2064
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3171 TPKSYLSFIQG---YKFIYEEKHMEVQSLANRMNTGLEKLKEASESVAALSKELAGKEKELQVANEKADTVLKEVTMKAQ 3247
Cdd:COG5245 2065 LGESKIKFIGGlkvYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERL 2144
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3248 AAEKVKAEVQKVKDKAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIKPSDIATVRTLGRPPHLIMRIMD--CVLL 3325
Cdd:COG5245 2145 EREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCDLL 2224
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3326 LFQRRVnavkidvdkgctmpsWQESLKLMTAGNFLQNLQQFPkDTIN--------EEVIEFLNPYFEMSDYNieTAKRVC 3397
Cdd:COG5245 2225 GFEAKI---------------WFGEQQSLRRDDFIRIIGKYP-DEIEfdlearrfREARECSDPSFTGSILN--RASKAC 2286
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3398 GNvagLCSWTKAMASFFSINKEVLPLKANLIVQENRHILAMQDLQKAQAELDAKQAELDVVQAEYEQAMAEKQTLLEDAD 3477
Cdd:COG5245 2287 GP---LKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMD 2363
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3478 RCRHKMQTASTLISGLAGEKERWTEQSKEFAAQTKRLVGDVLLATAFLSYSGPFNQEFRDLLLHDWK----KEMKARKIp 3553
Cdd:COG5245 2364 TVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGMSFirisKEFRDKEI- 2442
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3554 fGNGLNLNEMLidaPTISEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESQNELQITSLNHKYFRNH 3633
Cdd:COG5245 2443 -RRRQFITEGV---QKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFG 2518
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3634 LEDSLSLGRPLLIEDvGEELDPALDNVLEKNFIKTGSTFKVKVGDKEVDVMDGFKLYITTKLPNPAYTPEISARTSIIDF 3713
Cdd:COG5245 2519 LSQARREGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMF 2597
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3714 TVTVKGLEDQLLGRVILTEKQELEKERTHLLEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIIVLSNTKKTAEEVT 3793
Cdd:COG5245 2598 VSKVLGCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIE 2677
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3794 QKLEISGETEIQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLFDlsLARSVKSpitskRIANIIEHMT 3873
Cdd:COG5245 2678 EEESESMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFE--KWRRMKS-----KYLCAIRYML 2750
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3874 YEVFKYaargLYEEhkflFTLLLTLKIDIQRNLVKHEEFLTLIK-GGASLDLKACppkpskwildmtWLNLVELsklkqF 3952
Cdd:COG5245 2751 MSSEWI----LDHE----DRSGFIHRLDVSFLLRTKRFVSTLLEdKNYRQVLSSC------------SLYGNDV-----I 2805
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3953 SDILDQISRNekMWRVWFDKENPEEEPLPNAYDKSLDCFRRLLLIRSWcpdrtiaqARKYIMDSMGENYaegvilDLEK- 4031
Cdd:COG5245 2806 SHSCDRFDRD--VYRALKHQMDNRTHSTILTSNSKTNPYKEYTYNDSW--------AEAFEVEDSGDLY------KFEEg 2869
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4032 TWEESDPRTPLICLLsMGSDPTDSIIalgKRLKIETRyvsmgqgqEVHARKLLHQTMANGGWVLLQNCHLGLDFLDELM- 4110
Cdd:COG5245 2870 LLELIVGHAPLIYAH-KKSLENERNV---DRLGSKEN--------EVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYVe 2937
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4111 DVVTET---ETVHDTFRLWITTEVHKQFPITLLQMSIKFANEppqglraglrrTYGGVSQDLLDVsVGAQWKPMLYA--- 4184
Cdd:COG5245 2938 DVVYPIkasRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSS-----------TYPETGCGYADL-VEIDRYPFDYTlvi 3005
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4185 -------VAFLHSTVQERRKFGPLGWNIPYEFNQADFNATVQFIQNHLdDMDVKKGVSWTTVRYMIGEIQYGGR------ 4251
Cdd:COG5245 3006 acddafyLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNIL-FLNHLNARKWGNNRDLIFTIVYGKKhslmed 3084
|
2730 2740 2750
....*....|....*....|....*....|...
gi 342672105 4252 --VTDDYDKRLLNTFAKVWFSENMFGPDFTFYQ 4282
Cdd:COG5245 3085 skVVDKYCRGYGAHETSSQILASVPGGDPELVK 3117
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4326-4618 |
1.14e-124 |
|
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: 395.84 E-value: 1.14e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4326 AKDVLDTILGIQPKDSSG--GGDETREAVVARLADDMLEKLPEDYSpFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSL 4403
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGggGGGSSREEIVLELAKDILEKLPEPFD-IEEAEEKYPVGYEDPLNTVLLQEIERFNKLLKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4404 VRSTLTELKLAVDGTIIMSENLRDALDCMFDARIPARWKKASWVSS-TLGFWFTELLERNCQFTSWVS-NGRPHCFWMTG 4481
Cdd:pfam18199 83 IRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLkPLGSWIRDLLERLKQLQDWLDdEGPPKVFWLSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4482 FFNPQGFLTAMRQEITRANKgWALDNMVLCNEVTKFM-KDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFEL 4560
Cdd:pfam18199 163 FFFPQAFLTAVLQNYARKNG-WPIDKLSFDFEVTKKVsPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFSP 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4561 MPVIRIFAENNT--ARDPRLYCCPIYKKPVRTDLNYIAAVDLKTAQAPEHWVLRGVALLC 4618
Cdd:pfam18199 242 LPVIHLKPVESDkkKLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3571-3792 |
4.27e-117 |
|
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: 370.62 E-value: 4.27e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3571 SEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESQNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVG 3650
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3651 EELDPALDNVLEKNFIKTGSTFKVKVGDKEVDVMDGFKLYITTKLPNPAYTPEISARTSIIDFTVTVKGLEDQLLGRVIL 3730
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 342672105 3731 TEKQELEKERTHLLEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIIVLSNTKKTAEEV 3792
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 ... |
2923-3183 |
1.79e-102 |
|
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: 330.34 E-value: 1.79e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2923 MDMVFFIDAMVHLVKISRVIRTPRGNALLVGVGGSGKQSLTRLASFIAGYTSFQITLTRSYNTSNLMEDLKVLYRTAGQQ 3002
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3003 GKGITFIFTDNEIKEESFLEYMNNVLSSGEVSNLFARDEIDEINSDLTPIMKKEHprRPPTNDNLYEYFMSRVRGNLHIV 3082
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQN--IEDSREAVYNYFVKRCRNNLHIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3083 LCFSPVGEKFRNRALKFPALISGCTIDWFSRWPKDALVAVSEHFLSSYTIDctAEIKKELVQCMGSFQDGVAEKCADYFQ 3162
Cdd:pfam12780 159 LCMSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDIEIP--EELKSNVVKVFVYVHSSVEDMSKKFYE 236
|
250 260
....*....|....*....|.
gi 342672105 3163 RFRRSTHVTPKSYLSFIQGYK 3183
Cdd:pfam12780 237 ELKRKNYVTPKSYLELLRLYK 257
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2548-2729 |
1.08e-88 |
|
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: 287.37 E-value: 1.08e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2548 YPPDTtpEYGSILVPNVDNVRTDFLIKTIAKQGKAVLLIGEQGTAKTVIIKGFMSKFDPESHMVKNLNFSSATTPVMFQR 2627
Cdd:pfam12775 1 IPPDV--PFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2628 TIESYVDKRMGTTYGPPAGKKMAVFIDDLNMPVINEWGDQVTNEIVRQLMEQSGFYNLEKPgEFTSIVDIQFLAAMIHPG 2707
Cdd:pfam12775 79 IIESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKL-TFKEIVDVQFVAAMGPPG 157
|
170 180
....*....|....*....|..
gi 342672105 2708 GGRNDIPQRLKRQFSIFNCTLP 2729
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 ... |
4178-4317 |
4.87e-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: 249.29 E-value: 4.87e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4178 WKPMLYAVAFLHSTVQERRKFGPLGWNIPYEFNQADFNATVQFIQNHLDdmDVKKGVSWTTVRYMIGEIQYGGRVTDDYD 4257
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLD--EYDEKIPWDALRYLIGEINYGGRVTDDWD 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 342672105 4258 KRLLNTFAKVWFSENMFGPDFTFYQG-YNIPKCSTVDGYLQYIQSLPAYDSPEVFGLHPNA 4317
Cdd:pfam18198 79 RRLLNTYLEEFFNPEVLEEDFKFSPSlYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
4037-4146 |
5.99e-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: 5.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 4037 DPRTPLICLLSMGSDPTDSIIALGKRLKIETRY--VSMGQGQEVHARKLLHQTMANGGWVLLQNCHLGLDFLDELMDVV- 4113
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGFGGKLhsISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILe 80
|
90 100 110
....*....|....*....|....*....|....
gi 342672105 4114 -TETETVHDTFRLWITTEVHKQFPITLLQMSIKF 4146
Cdd:pfam03028 81 eLPEETLHPDFRLWLTSEPSPKFPISILQNSIKI 114
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
3199-3540 |
5.38e-48 |
|
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: 177.19 E-value: 5.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3199 RMNTGLEKLKEASESVAALSKELAGKEKELQVANEKADTVLKEVTMKAQAAEKVKAEVQKVKDKAQAIVDSISKDKAIAE 3278
Cdd:pfam12777 2 RLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3279 EKLEAAKPALEEAEAALQTIKPSDIATVRTLGRPPHLIMRIMDCVLLLFQRRvnaVKIDVDKgctmpSWQESlKLMTA-- 3356
Cdd:pfam12777 82 EDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPG---GKIPKDK-----SWKAA-KIMMAkv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3357 GNFLQNLQQFPKDTINEEVIEFLNPYFEMSDYNIETAKRVCGNVAGLCSWTKAMASFFSINKEVLPLKanlivqenrhil 3436
Cdd:pfam12777 153 DGFLDSLIKFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKR------------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3437 amQDLQKAQAELDAKQAELDVVQAE--------------YEQAMAEKQTLLEDADRCRHKMQTASTLISGLAGEKERWTE 3502
Cdd:pfam12777 221 --QALEEANADLAAAQEKLAAIKAKiaelnanlakltaaFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWAD 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 342672105 3503 QSKEFAAQTKRLVGDVLLATAFLSYSGPFNQEFRDLLL 3540
Cdd:pfam12777 299 AVENFKQQERTLCGDILLISAFISYLGFFTKKYRNELL 336
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2421-2540 |
4.21e-22 |
|
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: 94.66 E-value: 4.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2421 LRQLYAETFPDLYRFSIQNLEFKMEVLEAFVITQSTHMLQGLIPPKEQAGEVDP-------EHLGRLFVFAMMWSVGAVL 2493
Cdd:pfam17852 1 LEPLFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDEVLEYNGVHPlspdklkEYLEKLFLFALVWSIGGTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 342672105 2494 ELEGRRRMELWLRSREGpTLHLPQltDAGDTMFDYYV-APNGTWRHWS 2540
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. |
2763-2859 |
5.49e-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: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2763 LVPLTRRLWQMTKLKMLPTPAKFHYVFNLRDLSRIWQGMLNITSEVIKDTDELLRLWKHECKRVIADRFSMSSDVTWFDK 2842
Cdd:pfam17857 1 LIAAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDK 80
|
90
....*....|....*..
gi 342672105 2843 AVVSLVEEEFGEEKAPV 2859
Cdd:pfam17857 81 IQMASLKKFFDDIEDEL 97
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2254-2389 |
7.54e-10 |
|
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: 60.00 E-value: 7.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2254 GMMTLGPSGSGKTTcIHTLMKAMTDCGKPhrEMRMNPKAITAPQMFGRLDVATND--WTDGIFstlwrkTLKAKKGEHIw 2331
Cdd:pfam07728 1 GVLLVGPPGTGKTE-LAERLAAALSNRPV--FYVQLTRDTTEEDLFGRRNIDPGGasWVDGPL------VRAAREGEIA- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 342672105 2332 iVLDGpVDAI---WIENLNSVLDDNKTLTLANGDRIPMAPNC-KIVFEPHNID----NASPATVSR 2389
Cdd:pfam07728 71 -VLDE-INRAnpdVLNSLLSLLDERRLLLPDGGELVKAAPDGfRLIATMNPLDrglnELSPALRSR 134
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
3196-3297 |
4.05e-07 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 53.04 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3196 LANRMNTGLEKLKEASESVAALSKELAGKEKELQVANEKADTVLKEVTMKAQA-----AEKVKAEVQKVKDKAQAIVDSi 3270
Cdd:PRK07352 48 LEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAiraeiEKQAIEDMARLKQTAAADLSA- 126
|
90 100
....*....|....*....|....*..
gi 342672105 3271 SKDKAIAEEKLEAAKPALEEAEAALQT 3297
Cdd:PRK07352 127 EQERVIAQLRREAAELAIAKAESQLPG 153
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3202-3295 |
9.06e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3202 TGLEKLKEASESVAALSKELAGKEKELQVANEKADTVLKEVTMKAQAAEKVKAEVQKVKDKAQAIVDSISKDKAIAEEKL 3281
Cdd:COG3883 119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
90
....*....|....
gi 342672105 3282 EAAKPALEEAEAAL 3295
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 ... |
3187-3298 |
4.81e-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: 48.18 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3187 EEKHMEVQSLANRMNTGLEKLKEASESVA-ALSKELAGKEKELQVANEkadtVLKEVTMKAQAAEKVKAEVQKVKDKAQA 3265
Cdd:pfam06008 147 EAELKAAQDLLSRIQTWFQSPQEENKALAnALRDSLAEYEAKLSDLRE----LLREAAAKTRDANRLNLANQANLREFQR 222
|
90 100 110
....*....|....*....|....*....|...
gi 342672105 3266 IVDSISKDKAIAEEKLEAAKPALEEAEAALQTI 3298
Cdd:pfam06008 223 KKEEVSEQKNQLEETLKTARDSLDAANLLLQEI 255
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3205-3294 |
8.57e-05 |
|
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: 48.30 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3205 EKLKEASESVAALSKELAGKEKELQVANEKADtvlKEVTMKAQAAEKVKAEVQKVKDKAQAivdsisKDKAIAEEKLeAA 3284
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEA------KAKAEAEAKA-KA 191
|
90
....*....|
gi 342672105 3285 KPALEEAEAA 3294
Cdd:TIGR02794 192 EEAKAKAEAA 201
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3206-3293 |
2.14e-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: 47.15 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3206 KLKEASESVA---ALSKELAGKEKELQVANEKADTVLKEvtmKAQAAEKVKAEvqKVKDKAQAivdsiSKDKAIAE--EK 3280
Cdd:TIGR02794 143 KAKEEAAKQAeeeAKAKAAAEAKKKAEEAKKKAEAEAKA---KAEAEAKAKAE--EAKAKAEA-----AKAKAAAEaaAK 212
|
90
....*....|...
gi 342672105 3281 LEAAKPALEEAEA 3293
Cdd:TIGR02794 213 AEAEAAAAAAAEA 225
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
3196-3296 |
2.25e-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: 43.97 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3196 LANRMNTGLEKLKEASESVAALSKELAGKEKELQVANEKADTVLKE-----VTMKAQAAEKVKAEVQKVKDKAQAIVDSi 3270
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEAERILEQAKAEIEQ- 106
|
90 100
....*....|....*....|....*.
gi 342672105 3271 SKDKAIAEEKLEAAKPALEEAEAALQ 3296
Cdd:cd06503 107 EKEKALAELRKEVADLAVEAAEKILG 132
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3192-3299 |
2.26e-04 |
|
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: 46.07 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3192 EVQSLANRMNTGLEKLKEASESVAALSKELAGKEKELQVANEKADTVLKEVTMKAQAAEKVKAEVQKVKDK--------- 3262
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnke 90
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 342672105 3263 AQAI---VDSISKDKAIAEEKLEAAKPALEEAEAALQTIK 3299
Cdd:COG1579 91 YEALqkeIESLKRRISDLEDEILELMERIEELEEELAELE 130
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3437-3510 |
2.45e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 2.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342672105 3437 AMQDLQKAQAELDAKQAELDVVQAEYEQAMAEKQTLLEDADRcrhKMQTASTLISGLAGEKERWTEQSKEFAAQ 3510
Cdd:COG3883 134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3206-3294 |
8.64e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3206 KLK-EASESVAALSKELAGKEKELQVANEKADTVLKEVTMKAQAAEKVKAEVQ-KVK--DKAQAIVDSISKDKAIAEEKL 3281
Cdd:PRK09510 146 KAKaEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEaKKKaeAEAKKKAAAEAKKKAAAEAKA 225
|
90
....*....|...
gi 342672105 3282 EAAKPALEEAEAA 3294
Cdd:PRK09510 226 AAAKAAAEAKAAA 238
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3186-3295 |
1.06e-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: 44.15 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3186 YEEKHMEVQSLANRmntgLEKLKEASESVA------ALSKELAGKEKELQVANEKadtvLKEVTMKAQAAEKVKAEVQKV 3259
Cdd:COG1579 61 IKRLELEIEEVEAR----IKKYEEQLGNVRnnkeyeALQKEIESLKRRISDLEDE----ILELMERIEELEEELAELEAE 132
|
90 100 110
....*....|....*....|....*....|....*.
gi 342672105 3260 KDKAQAIVDSISKDKAIAEEKLEAAKPALEEAEAAL 3295
Cdd:COG1579 133 LAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3192-3297 |
1.21e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3192 EVQSLANRMNTGLEKLKEASESVAALSKELAGKEKELQVANEKADTVLKEVTMKAQAAEKVKAEVQKVKDKAQAIVDSIS 3271
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100
....*....|....*....|....*.
gi 342672105 3272 KDKAiAEEKLEAAKPALEEAEAALQT 3297
Cdd:COG4372 119 ELQK-ERQDLEQQRKQLEAQIAELQS 143
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2583-2721 |
1.33e-03 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 41.89 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 2583 VLLIGEQGTAKTVIIKGFMSKFDPESHMVKNLNfsSATTP--VMFQRTIESYVDKRMGTTYGPPAGKKMAVFIDDLNMP- 2659
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRPVFYVQLT--RDTTEedLFGRRNIDPGGASWVDGPLVRAAREGEIAVLDEINRAn 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342672105 2660 --VINEWgDQVTNEIVRQLMEqSGFYNLEKPGEFtsivdiQFLAAMIHPGGGRNDIPQRLKRQF 2721
Cdd:pfam07728 80 pdVLNSL-LSLLDERRLLLPD-GGELVKAAPDGF------RLIATMNPLDRGLNELSPALRSRF 135
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3182-3299 |
1.37e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3182 YKFIYEE-KHMEVQSLANRMNTGLEKLKEASESVAALSKELAGKEKELQVANEKADTVLKEVtmkaQAAEKVKAEVQKVK 3260
Cdd:TIGR02168 215 YKELKAElRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV----SELEEEIEELQKEL 290
|
90 100 110
....*....|....*....|....*....|....*....
gi 342672105 3261 DKAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIK 3299
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
3207-3299 |
1.71e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.61 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3207 LKEASESVAALSKELAgkEKELQVANEKADTVLKEVTMKAQAAEKVKAEVQKVKDKAQ-----AIVDSISKDKAIAEEKL 3281
Cdd:pfam05262 203 LKERESQEDAKRAQQL--KEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKnlpkpADTSSPKEDKQVAENQK 280
|
90
....*....|....*...
gi 342672105 3282 EAAKPALEEAEAALQTIK 3299
Cdd:pfam05262 281 REIEKAQIEIKKNDEEAL 298
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
3205-3296 |
1.71e-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: 42.08 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3205 EKLKEASESVAALSKELAGKEKELQVANEKADTVLKEVT-----MKAQAAEKVKAEVQKVKDKAQAIVDSIsKDKAIAEE 3279
Cdd:COG0711 38 DGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARkeaeaIAEEAKAEAEAEAERIIAQAEAEIEQE-RAKALAEL 116
|
90
....*....|....*..
gi 342672105 3280 KLEAAKPALEEAEAALQ 3296
Cdd:COG0711 117 RAEVADLAVAIAEKILG 133
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
3213-3297 |
3.67e-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: 43.18 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3213 SVAALSKELAGKEKEL---QVANEKADTVLKEVTMKAQAAEKVKAEVQKVKDKAQAI--------VDSISKDKAIAEEKL 3281
Cdd:TIGR04320 255 SLAALQAKLATAQADLaaaQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQalqtaqnnLATAQAALANAEARL 334
|
90
....*....|....*.
gi 342672105 3282 EAAKPALEEAEAALQT 3297
Cdd:TIGR04320 335 AKAKEALANLNADLAK 350
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3205-3299 |
4.83e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342672105 3205 EKLKEASESVAALSKELAGKEKELQVANEKADTVLKEVtmkaqaaEKVKAEVQKVKDKAQAI---VDSISKDKAIAEEKL 3281
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-------EELQKERQDLEQQRKQLeaqIAELQSEIAEREEEL 152
|
90
....*....|....*...
gi 342672105 3282 EAAKPALEEAEAALQTIK 3299
Cdd:COG4372 153 KELEEQLESLQEELAALE 170
|
|
| |
