|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1613-1940 |
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: 596.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1613 YQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKG 1692
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1693 LAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINF 1772
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1773 RSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYKLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRANPMDTESTIV 1852
Cdd:pfam12774 160 RPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1853 MRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELEAAISRQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTL 1932
Cdd:pfam12774 240 LRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLV 319
|
....*...
gi 1034644034 1933 GPSGAGKT 1940
Cdd:pfam12774 320 GPTGSGKT 327
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
1-473 |
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: 581.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1 MDIRITDATNEAKDNVKYLYTLEKCCDPLYS-SDPLSMMDAIPTLINAIKMIYSISHYYNTSEKITSLFVKVTNQIISAC 79
Cdd:pfam08385 77 LDTELTDALNEAKDNVKYLKTLERPFEDLEElTDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQC 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 80 KAYITNNGtasIWNQPQDVVEEKILSAIKLKQEYQLCFHKTKQKLKQNPNAKQFDFSEMYIFGKFETFHRRLAKIIDIFT 159
Cdd:pfam08385 157 KKYLSPEG---IFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWDFSERYIFGRFDAFLERLEKILELFE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 160 TLKTYSVLQDS------TIEG-LEDMATKYQGIVATIKKKEYNFLDQRKMDFDQDYEEFCKQTNDLHNELRKFMDVTFAK 232
Cdd:pfam08385 234 TIEQFSKLEKIggtkgpELEGvIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 233 IQNTNQALRMLKKFE-RLNIPNL--GIDDKYQLILENYGADIDMISKLYTKQKYDP-PLARNQPPIAGKILWARQLFHRI 308
Cdd:pfam08385 314 ARSTESAFKLLRIFEfLLERPIIrgALEEKYTDLLQMFKKELDAVKKIFDKQKYNPsPIAKNMPPVAGAIIWARQLFRRI 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 309 QQPMQLFQQHPAVLSTAEAKPIIRSYNRMAKVLLEFEVLFHRAWLRQIEEIHVG-LEASLLVKAPGTGELF-VNFDPQIL 386
Cdd:pfam08385 394 QEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGnLKRPLLVRHPETGKLLsVNFDPQLL 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 387 ILFRETECMAQMGLEVSPLATSLFQKRDRYKRNFSNMKMMLAEYQRVKSKIPAAIEQLIVPHLAKVDEALQPGLAALTWT 466
Cdd:pfam08385 474 ALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTWN 553
|
....*..
gi 1034644034 467 SLNIEAY 473
Cdd:pfam08385 554 SLGIDEY 560
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1073-1478 |
5.33e-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: 467.12 E-value: 5.33e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1073 LLEIKKQLNLLQKIYTLYNSVIETVNSYYDILWSEVNIEKINNELLEFQNRCRKLPRALKDWQAFLDLKKIIDDFSECCP 1152
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1153 LLEYMASKAMMERHWERITTLTGHSLDVGNESFKLRNIMEAPLLKYKEEIEDICISAVKERDIEQKLKQVINEWDNKTFT 1232
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1233 FGSFKTRGELLLRGdsTSEIIANMEDSLMLLGSLLSNRYNMPFKAQIQKWVQYLSNSTDIIESWMTVQNLWIYLEAVFVG 1312
Cdd:pfam08393 161 LVPYKDTGTFILKG--WDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1313 GDIAKQLPKEAKRFSNIDKSWVKIMTRAHEVPSVVQCCvGDETLGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVS 1392
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEAC-NIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1393 DPALLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiYDRILSISSQEGETIELDKP-VMAEGNVEVWLNSLLEESQSSL 1471
Cdd:pfam08393 318 NDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE--NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 1034644034 1472 HLVIRQA 1478
Cdd:pfam08393 396 RDLLKEA 402
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4000-4292 |
8.64e-126 |
|
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: 398.92 E-value: 8.64e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 4000 AKDVLDTILGIQPKDTSG--GGDETREAVVARLADDMLEKLPPDYvPFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSL 4077
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGggGGGSSREEIVLELAKDILEKLPEPF-DIEEAEEKYPVGYEDPLNTVLLQEIERFNKLLKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 4078 VRSTLTELKLAIDGTIIMSENLRDALDCMFDARIPAWWKKASWISS-TLGFWFTELIERNSQFTSWVF-NGRPHCFWMTG 4155
Cdd:pfam18199 83 IRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLkPLGSWIRDLLERLKQLQDWLDdEGPPKVFWLSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 4156 FFNPQGFLTAMRQEITRANKgWALDNMVLCNEVTKWM-KDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFEL 4234
Cdd:pfam18199 163 FFFPQAFLTAVLQNYARKNG-WPIDKLSFDFEVTKKVsPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFSP 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 4235 MPVIRIYAENNTL--RDPRFYSCPIYKKPVRTDLNYIAAVDLRTAQTPEHWVLRGVALLC 4292
Cdd:pfam18199 242 LPVIHLKPVESDKkkLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1314-3956 |
1.56e-124 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 444.43 E-value: 1.56e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1314 DIAKQLPKEAKRFSNIDKSWVKIMTRahevpsVVQCCVGDETL----GQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFF 1389
Cdd:COG5245 639 DLMPLIPHAVHRKMSLVSGVRGIYKR------VVSGCEAINTIledvGDDLDLFYKEMDQVFMSIEKVLGLRWREVERAS 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1390 FVSDpaLLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiyDRILSISSQEGETIELDKPVMAEGNVEV--WLN----SL 1463
Cdd:COG5245 713 EVEE--LMDRVRELENRVYSYRFFVKKIAKEEMKTVFS---SRIQKKEPFSLDSEAYVGFFRLYEKSIVirGINrsmgRV 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1464 LEESQSSLhlvirQAAANIQETGFqlteFLSSFPAQVGLLGIQMiWTRDSEEALRNA------KFDKKIMQKTNQAFLEL 1537
Cdd:COG5245 788 LSQYLESV-----QEALEIEDGSF----FVSRHRVRDGGLEKGR-GCDAWENCFDPPlseyfrILEKIFPSEEGYFFDEV 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1538 LNtlidvttrdlsstervKYETLITIHVHQRDIFDDLCHMHIKSPMDFEWLKQCRFYFNEDsDKMMIHITDVAFIYQNEF 1617
Cdd:COG5245 858 LK----------------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLY-KRFIKVRSSYRSAEMFAK 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1618 LGCTDRLVITPLTDRCYITLAQALGMSMggapAGPAGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSG 1697
Cdd:COG5245 921 NTIPFFVFEHSMDTSQHQKLFEAVCDEV----CRFVDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEE 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1698 SWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEHKKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSV 1775
Cdd:COG5245 989 ERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMF 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1776 AMMVPDRQIIIRVKlascgfidnvVLARKFFTLYKLCEEQLSKQVHYDFglrnilsvlRTL-GAAKRANPMDTESTivmr 1854
Cdd:COG5245 1060 LSNIPFGAIKSRRE----------SLDREIGAFNNEVDGIAREEDELMF---------YPMfKSLKAKHRMLEEKT---- 1116
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1855 vlrdMNLSKLIdedEPLFLSLIEDLFPNI--LLDKAGYPELEAAISRQVEEAGLINHPPWKlKVIQLFETQRVRHGMMTL 1932
Cdd:COG5245 1117 ----EYLNKIL---SITGLPLISDTLRERidTLDAEWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGAFHAEY 1188
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1933 GPSGAGKTTCIHTLMRAMTDCGKPHREMRMnpkaitapqmfgrLDvATNDWTdGIFSTLWRKTLRAK-KGEHIWIILDGp 2011
Cdd:COG5245 1189 FRVFLCKIKHYTDACDYLWHVKSPYVKKKY-------------FD-ADMELR-QFFLMFNREDMEARlADSKMEYEVER- 1252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2012 vdaiWIENLNSVLDDNKTLTLANGDRipmapncKIIFEphNIDnASPATVSRNGMVFMSSSILDWSPILEGFL------- 2084
Cdd:COG5245 1253 ----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgdtkryl 1318
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2085 -KKRSPQEAEILRQLYTESF-----PDLYRFCIQ-----------NLEYKMEVLEAfVITQSINMLQGLiplKEQGGEVs 2147
Cdd:COG5245 1319 dECLDFFSCFEEVQKEIDELsmvfcADALRFSADlyhivkerrfsGVLAGSDASES-LGGKSIELAAIL---EHKDLIV- 1393
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2148 qaHLGRLFVFALLWSAGAALELDGRRRLELWLR---SRPTGTLELPPPAGPGDTAFDYYVAPDGTWTHWNTRTQEYLYPS 2224
Cdd:COG5245 1394 --EMKRGINDVLKLRIFGDKCRESTPRFYLISDgdlIKDLNERSDYEEMLIMMFNISAVITNNGSIAGFELRGERVMLRK 1471
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2225 DttpeygsILVPNVDNVRTDFLIQTIAKQGKAVLLIGEQGTAKTVIIKG-FMSKYDPEchmIKSLNFS-SATTPLM---F 2299
Cdd:COG5245 1472 E-------VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPsLRSELITE---VKYFNFStCTMTPSKlsvL 1541
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2300 QRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPIINEWGDQVTNEIVRQLMEQNGFYN-LEKpgEFTSIVDIqFLAAMI 2378
Cdd:COG5245 1542 ERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGAC 1618
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2379 HPGG--GRNDIPQRLKRQFSIFNCTLPSEASVDKIFGVIGVGHYCTQRGFSEEVRDSVTKLVPLTRRLWQMTKikmlpTP 2456
Cdd:COG5245 1619 NPGTdeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTK-----FF 1693
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2457 AKFHYVFNLRDLSRVWQGMLNTTSEVIKEPN-DLLKLWKHECKRVIADRFTVSSDVTWFDKALVSLVEEEFGE------- 2528
Cdd:COG5245 1694 LQMNYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREmiaghig 1773
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2529 EKKLLVDcgiDTYFVDFlrdapeaagetsEEADAETPKIYepiesfshLKERLNMFlqlYNESIRgagMDMVFFADAMVH 2608
Cdd:COG5245 1774 EAEITFS---MILFFGM------------ACLLKKDLAVF--------VEEVRKIF---GSSHLD---VEAVAYKDALLH 1824
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2609 LVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNE 2688
Cdd:COG5245 1825 ILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESI 1904
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2689 IKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfPRCLPTNENLHDYFMSRVRQNLHIVL-CFSPVGEKFR 2767
Cdd:COG5245 1905 PVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVL 1983
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2768 NRALkFPALISGCTIDWFSRWPKDALVAVSEHFLT-SYDIDCSLEIKKEVVQCMGS-FQDGVAEKCVDYFQR-FRRSTHV 2844
Cdd:COG5245 1984 AGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVETlSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIE 2062
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2845 --TPKSYLSFIQG---YKFIYGEKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMK 2919
Cdd:COG5245 2063 gsLGESKIKFIGGlkvYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGE 2142
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2920 AQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMD--CV 2997
Cdd:COG5245 2143 RLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCD 2222
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2998 LLLFQRKVsavkidleksctmpsWQESLKLMTAGNFLQNLQQFPKDT-INEEVIEFL-SPYFEMPDYNIETAKR---VCG 3072
Cdd:COG5245 2223 LLGFEAKI---------------WFGEQQSLRRDDFIRIIGKYPDEIeFDLEARRFReARECSDPSFTGSILNRaskACG 2287
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3073 NvagLCSWTKAMASFFSINKEVLPLKANLVVQENRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAER 3152
Cdd:COG5245 2288 P---LKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDT 2364
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3153 CRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKRLVGDVLLATAFLSYSGPFNQEFRDLLLNDwRKEMKARKIPFGKNL 3232
Cdd:COG5245 2365 VHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIR 2443
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3233 NLSEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSL 3312
Cdd:COG5245 2444 RRQFITEGVQKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQAR 2523
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3313 SLGRPLLIEDvGEELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMK 3392
Cdd:COG5245 2524 REGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVL 2602
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3393 GLEDQLLGRVILTEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEVTQKLEI 3472
Cdd:COG5245 2603 GCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESE 2682
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3473 SAETEVQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLFDlsLARSVKSpitskRIANIIEHMTYEVYK 3552
Cdd:COG5245 2683 SMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFE--KWRRMKS-----KYLCAIRYMLMSSEW 2755
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3553 YaargLYEEhkflFTLLLTLKIDIQRN-RVKHEEFLTLIKGGASLDLKACppkpskwilDITWLNLVELSKLRQFSDVLD 3631
Cdd:COG5245 2756 I----LDHE----DRSGFIHRLDVSFLlRTKRFVSTLLEDKNYRQVLSSC---------SLYGNDVISHSCDRFDRDVYR 2818
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3632 QISRNEKMWKIWFDKenpeeeplpnAYDKSLDCFRRLLLIRSWcpdrtiaqARKYIVDSMGEKYaegvilDLEK-TWEES 3710
Cdd:COG5245 2819 ALKHQMDNRTHSTIL----------TSNSKTNPYKEYTYNDSW--------AEAFEVEDSGDLY------KFEEgLLELI 2874
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3711 DPRTPLICLLsMGSDPTDSIIalgKRLKIETRyvsmgqgqEVHARKLLQQTMANGGWALLQNCHLGLDFMDELMDIIIE- 3789
Cdd:COG5245 2875 VGHAPLIYAH-KKSLENERNV---DRLGSKEN--------EVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYVEDVVYp 2942
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3790 ---TELVHDAFRLWMTTEAHKQFPITLLQMSIKFANDPPQGLRAGLKrtysgvsqDLLdvssGSQWKPMLYA-------- 3858
Cdd:COG5245 2943 ikaSRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYA--------DLV----EIDRYPFDYTlviacdda 3010
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3859 --VAFLHSTVQERRKFGALGWNIPYEFNQADFNATVQFIQNHLdDMDVKKGVSWTTIRYMIGEIQYGGR--------VTD 3928
Cdd:COG5245 3011 fyLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNIL-FLNHLNARKWGNNRDLIFTIVYGKKhslmedskVVD 3089
|
2730 2740
....*....|....*....|....*...
gi 1034644034 3929 DYDKRLLNTFAKVWFSENMFGPDFSFYQ 3956
Cdd:COG5245 3090 KYCRGYGAHETSSQILASVPGGDPELVK 3117
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3245-3466 |
4.12e-116 |
|
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: 367.54 E-value: 4.12e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3245 SEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVG 3324
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3325 EELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMKGLEDQLLGRVIL 3404
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034644034 3405 TEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEV 3466
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
2850-2971 |
1.41e-06 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 51.49 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2850 LSFIQGYKFIYGEKHVEvRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQA-----AE 2924
Cdd:PRK07352 29 LAIVIGLLYYFGRGFLG-KILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAiraeiEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034644034 2925 KVKAEVQKVKDRAQAIVDSiSKDKAIAEEKLEAAKPALEEAEAALQT 2971
Cdd:PRK07352 108 QAIEDMARLKQTAAADLSA-EQERVIAQLRREAAELAIAKAESQLPG 153
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2879-2968 |
2.99e-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: 49.46 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2879 EKLKEASESVAALSKELEAKEKELQVANDKADmvlKEVTMKAQAAEKVKAEVQKVKDRAQAivdsisKDKAIAEEKLeAA 2958
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEA------KAKAEAEAKA-KA 191
|
90
....*....|
gi 1034644034 2959 KPALEEAEAA 2968
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 ... |
2868-2970 |
5.06e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.81 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2868 RTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKE-----VTMKAQAAEKVKAEVQKVKDRAQAIVD 2942
Cdd:cd06503 26 KALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEAERILEQAKAEIE 105
|
90 100
....*....|....*....|....*...
gi 1034644034 2943 SiSKDKAIAEEKLEAAKPALEEAEAALQ 2970
Cdd:cd06503 106 Q-EKEKALAELRKEVADLAVEAAEKILG 132
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1613-1940 |
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: 596.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1613 YQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKG 1692
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1693 LAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINF 1772
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1773 RSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYKLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRANPMDTESTIV 1852
Cdd:pfam12774 160 RPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1853 MRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELEAAISRQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTL 1932
Cdd:pfam12774 240 LRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLV 319
|
....*...
gi 1034644034 1933 GPSGAGKT 1940
Cdd:pfam12774 320 GPTGSGKT 327
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
1-473 |
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: 581.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1 MDIRITDATNEAKDNVKYLYTLEKCCDPLYS-SDPLSMMDAIPTLINAIKMIYSISHYYNTSEKITSLFVKVTNQIISAC 79
Cdd:pfam08385 77 LDTELTDALNEAKDNVKYLKTLERPFEDLEElTDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQC 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 80 KAYITNNGtasIWNQPQDVVEEKILSAIKLKQEYQLCFHKTKQKLKQNPNAKQFDFSEMYIFGKFETFHRRLAKIIDIFT 159
Cdd:pfam08385 157 KKYLSPEG---IFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWDFSERYIFGRFDAFLERLEKILELFE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 160 TLKTYSVLQDS------TIEG-LEDMATKYQGIVATIKKKEYNFLDQRKMDFDQDYEEFCKQTNDLHNELRKFMDVTFAK 232
Cdd:pfam08385 234 TIEQFSKLEKIggtkgpELEGvIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 233 IQNTNQALRMLKKFE-RLNIPNL--GIDDKYQLILENYGADIDMISKLYTKQKYDP-PLARNQPPIAGKILWARQLFHRI 308
Cdd:pfam08385 314 ARSTESAFKLLRIFEfLLERPIIrgALEEKYTDLLQMFKKELDAVKKIFDKQKYNPsPIAKNMPPVAGAIIWARQLFRRI 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 309 QQPMQLFQQHPAVLSTAEAKPIIRSYNRMAKVLLEFEVLFHRAWLRQIEEIHVG-LEASLLVKAPGTGELF-VNFDPQIL 386
Cdd:pfam08385 394 QEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGnLKRPLLVRHPETGKLLsVNFDPQLL 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 387 ILFRETECMAQMGLEVSPLATSLFQKRDRYKRNFSNMKMMLAEYQRVKSKIPAAIEQLIVPHLAKVDEALQPGLAALTWT 466
Cdd:pfam08385 474 ALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTWN 553
|
....*..
gi 1034644034 467 SLNIEAY 473
Cdd:pfam08385 554 SLGIDEY 560
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1073-1478 |
5.33e-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: 467.12 E-value: 5.33e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1073 LLEIKKQLNLLQKIYTLYNSVIETVNSYYDILWSEVNIEKINNELLEFQNRCRKLPRALKDWQAFLDLKKIIDDFSECCP 1152
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1153 LLEYMASKAMMERHWERITTLTGHSLDVGNESFKLRNIMEAPLLKYKEEIEDICISAVKERDIEQKLKQVINEWDNKTFT 1232
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1233 FGSFKTRGELLLRGdsTSEIIANMEDSLMLLGSLLSNRYNMPFKAQIQKWVQYLSNSTDIIESWMTVQNLWIYLEAVFVG 1312
Cdd:pfam08393 161 LVPYKDTGTFILKG--WDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1313 GDIAKQLPKEAKRFSNIDKSWVKIMTRAHEVPSVVQCCvGDETLGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVS 1392
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEAC-NIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1393 DPALLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiYDRILSISSQEGETIELDKP-VMAEGNVEVWLNSLLEESQSSL 1471
Cdd:pfam08393 318 NDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE--NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 1034644034 1472 HLVIRQA 1478
Cdd:pfam08393 396 RDLLKEA 402
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4000-4292 |
8.64e-126 |
|
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: 398.92 E-value: 8.64e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 4000 AKDVLDTILGIQPKDTSG--GGDETREAVVARLADDMLEKLPPDYvPFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSL 4077
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGggGGGSSREEIVLELAKDILEKLPEPF-DIEEAEEKYPVGYEDPLNTVLLQEIERFNKLLKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 4078 VRSTLTELKLAIDGTIIMSENLRDALDCMFDARIPAWWKKASWISS-TLGFWFTELIERNSQFTSWVF-NGRPHCFWMTG 4155
Cdd:pfam18199 83 IRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLkPLGSWIRDLLERLKQLQDWLDdEGPPKVFWLSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 4156 FFNPQGFLTAMRQEITRANKgWALDNMVLCNEVTKWM-KDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFEL 4234
Cdd:pfam18199 163 FFFPQAFLTAVLQNYARKNG-WPIDKLSFDFEVTKKVsPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFSP 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 4235 MPVIRIYAENNTL--RDPRFYSCPIYKKPVRTDLNYIAAVDLRTAQTPEHWVLRGVALLC 4292
Cdd:pfam18199 242 LPVIHLKPVESDKkkLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1314-3956 |
1.56e-124 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 444.43 E-value: 1.56e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1314 DIAKQLPKEAKRFSNIDKSWVKIMTRahevpsVVQCCVGDETL----GQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFF 1389
Cdd:COG5245 639 DLMPLIPHAVHRKMSLVSGVRGIYKR------VVSGCEAINTIledvGDDLDLFYKEMDQVFMSIEKVLGLRWREVERAS 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1390 FVSDpaLLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiyDRILSISSQEGETIELDKPVMAEGNVEV--WLN----SL 1463
Cdd:COG5245 713 EVEE--LMDRVRELENRVYSYRFFVKKIAKEEMKTVFS---SRIQKKEPFSLDSEAYVGFFRLYEKSIVirGINrsmgRV 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1464 LEESQSSLhlvirQAAANIQETGFqlteFLSSFPAQVGLLGIQMiWTRDSEEALRNA------KFDKKIMQKTNQAFLEL 1537
Cdd:COG5245 788 LSQYLESV-----QEALEIEDGSF----FVSRHRVRDGGLEKGR-GCDAWENCFDPPlseyfrILEKIFPSEEGYFFDEV 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1538 LNtlidvttrdlsstervKYETLITIHVHQRDIFDDLCHMHIKSPMDFEWLKQCRFYFNEDsDKMMIHITDVAFIYQNEF 1617
Cdd:COG5245 858 LK----------------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLY-KRFIKVRSSYRSAEMFAK 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1618 LGCTDRLVITPLTDRCYITLAQALGMSMggapAGPAGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSG 1697
Cdd:COG5245 921 NTIPFFVFEHSMDTSQHQKLFEAVCDEV----CRFVDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEE 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1698 SWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEHKKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSV 1775
Cdd:COG5245 989 ERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMF 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1776 AMMVPDRQIIIRVKlascgfidnvVLARKFFTLYKLCEEQLSKQVHYDFglrnilsvlRTL-GAAKRANPMDTESTivmr 1854
Cdd:COG5245 1060 LSNIPFGAIKSRRE----------SLDREIGAFNNEVDGIAREEDELMF---------YPMfKSLKAKHRMLEEKT---- 1116
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1855 vlrdMNLSKLIdedEPLFLSLIEDLFPNI--LLDKAGYPELEAAISRQVEEAGLINHPPWKlKVIQLFETQRVRHGMMTL 1932
Cdd:COG5245 1117 ----EYLNKIL---SITGLPLISDTLRERidTLDAEWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGAFHAEY 1188
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1933 GPSGAGKTTCIHTLMRAMTDCGKPHREMRMnpkaitapqmfgrLDvATNDWTdGIFSTLWRKTLRAK-KGEHIWIILDGp 2011
Cdd:COG5245 1189 FRVFLCKIKHYTDACDYLWHVKSPYVKKKY-------------FD-ADMELR-QFFLMFNREDMEARlADSKMEYEVER- 1252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2012 vdaiWIENLNSVLDDNKTLTLANGDRipmapncKIIFEphNIDnASPATVSRNGMVFMSSSILDWSPILEGFL------- 2084
Cdd:COG5245 1253 ----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgdtkryl 1318
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2085 -KKRSPQEAEILRQLYTESF-----PDLYRFCIQ-----------NLEYKMEVLEAfVITQSINMLQGLiplKEQGGEVs 2147
Cdd:COG5245 1319 dECLDFFSCFEEVQKEIDELsmvfcADALRFSADlyhivkerrfsGVLAGSDASES-LGGKSIELAAIL---EHKDLIV- 1393
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2148 qaHLGRLFVFALLWSAGAALELDGRRRLELWLR---SRPTGTLELPPPAGPGDTAFDYYVAPDGTWTHWNTRTQEYLYPS 2224
Cdd:COG5245 1394 --EMKRGINDVLKLRIFGDKCRESTPRFYLISDgdlIKDLNERSDYEEMLIMMFNISAVITNNGSIAGFELRGERVMLRK 1471
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2225 DttpeygsILVPNVDNVRTDFLIQTIAKQGKAVLLIGEQGTAKTVIIKG-FMSKYDPEchmIKSLNFS-SATTPLM---F 2299
Cdd:COG5245 1472 E-------VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPsLRSELITE---VKYFNFStCTMTPSKlsvL 1541
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2300 QRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPIINEWGDQVTNEIVRQLMEQNGFYN-LEKpgEFTSIVDIqFLAAMI 2378
Cdd:COG5245 1542 ERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGAC 1618
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2379 HPGG--GRNDIPQRLKRQFSIFNCTLPSEASVDKIFGVIGVGHYCTQRGFSEEVRDSVTKLVPLTRRLWQMTKikmlpTP 2456
Cdd:COG5245 1619 NPGTdeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTK-----FF 1693
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2457 AKFHYVFNLRDLSRVWQGMLNTTSEVIKEPN-DLLKLWKHECKRVIADRFTVSSDVTWFDKALVSLVEEEFGE------- 2528
Cdd:COG5245 1694 LQMNYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREmiaghig 1773
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2529 EKKLLVDcgiDTYFVDFlrdapeaagetsEEADAETPKIYepiesfshLKERLNMFlqlYNESIRgagMDMVFFADAMVH 2608
Cdd:COG5245 1774 EAEITFS---MILFFGM------------ACLLKKDLAVF--------VEEVRKIF---GSSHLD---VEAVAYKDALLH 1824
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2609 LVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNE 2688
Cdd:COG5245 1825 ILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESI 1904
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2689 IKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfPRCLPTNENLHDYFMSRVRQNLHIVL-CFSPVGEKFR 2767
Cdd:COG5245 1905 PVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVL 1983
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2768 NRALkFPALISGCTIDWFSRWPKDALVAVSEHFLT-SYDIDCSLEIKKEVVQCMGS-FQDGVAEKCVDYFQR-FRRSTHV 2844
Cdd:COG5245 1984 AGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVETlSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIE 2062
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2845 --TPKSYLSFIQG---YKFIYGEKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMK 2919
Cdd:COG5245 2063 gsLGESKIKFIGGlkvYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGE 2142
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2920 AQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMD--CV 2997
Cdd:COG5245 2143 RLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCD 2222
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2998 LLLFQRKVsavkidleksctmpsWQESLKLMTAGNFLQNLQQFPKDT-INEEVIEFL-SPYFEMPDYNIETAKR---VCG 3072
Cdd:COG5245 2223 LLGFEAKI---------------WFGEQQSLRRDDFIRIIGKYPDEIeFDLEARRFReARECSDPSFTGSILNRaskACG 2287
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3073 NvagLCSWTKAMASFFSINKEVLPLKANLVVQENRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAER 3152
Cdd:COG5245 2288 P---LKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDT 2364
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3153 CRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKRLVGDVLLATAFLSYSGPFNQEFRDLLLNDwRKEMKARKIPFGKNL 3232
Cdd:COG5245 2365 VHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIR 2443
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3233 NLSEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSL 3312
Cdd:COG5245 2444 RRQFITEGVQKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQAR 2523
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3313 SLGRPLLIEDvGEELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMK 3392
Cdd:COG5245 2524 REGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVL 2602
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3393 GLEDQLLGRVILTEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEVTQKLEI 3472
Cdd:COG5245 2603 GCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESE 2682
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3473 SAETEVQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLFDlsLARSVKSpitskRIANIIEHMTYEVYK 3552
Cdd:COG5245 2683 SMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFE--KWRRMKS-----KYLCAIRYMLMSSEW 2755
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3553 YaargLYEEhkflFTLLLTLKIDIQRN-RVKHEEFLTLIKGGASLDLKACppkpskwilDITWLNLVELSKLRQFSDVLD 3631
Cdd:COG5245 2756 I----LDHE----DRSGFIHRLDVSFLlRTKRFVSTLLEDKNYRQVLSSC---------SLYGNDVISHSCDRFDRDVYR 2818
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3632 QISRNEKMWKIWFDKenpeeeplpnAYDKSLDCFRRLLLIRSWcpdrtiaqARKYIVDSMGEKYaegvilDLEK-TWEES 3710
Cdd:COG5245 2819 ALKHQMDNRTHSTIL----------TSNSKTNPYKEYTYNDSW--------AEAFEVEDSGDLY------KFEEgLLELI 2874
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3711 DPRTPLICLLsMGSDPTDSIIalgKRLKIETRyvsmgqgqEVHARKLLQQTMANGGWALLQNCHLGLDFMDELMDIIIE- 3789
Cdd:COG5245 2875 VGHAPLIYAH-KKSLENERNV---DRLGSKEN--------EVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYVEDVVYp 2942
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3790 ---TELVHDAFRLWMTTEAHKQFPITLLQMSIKFANDPPQGLRAGLKrtysgvsqDLLdvssGSQWKPMLYA-------- 3858
Cdd:COG5245 2943 ikaSRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYA--------DLV----EIDRYPFDYTlviacdda 3010
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3859 --VAFLHSTVQERRKFGALGWNIPYEFNQADFNATVQFIQNHLdDMDVKKGVSWTTIRYMIGEIQYGGR--------VTD 3928
Cdd:COG5245 3011 fyLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNIL-FLNHLNARKWGNNRDLIFTIVYGKKhslmedskVVD 3089
|
2730 2740
....*....|....*....|....*...
gi 1034644034 3929 DYDKRLLNTFAKVWFSENMFGPDFSFYQ 3956
Cdd:COG5245 3090 KYCRGYGAHETSSQILASVPGGDPELVK 3117
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3245-3466 |
4.12e-116 |
|
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: 367.54 E-value: 4.12e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3245 SEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVG 3324
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3325 EELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMKGLEDQLLGRVIL 3404
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034644034 3405 TEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEV 3466
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 ... |
2597-2857 |
5.35e-99 |
|
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: 320.32 E-value: 5.35e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2597 MDMVFFADAMVHLVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQ 2676
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2677 GKGITFIFTDNEIKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfpRCLPTNENLHDYFMSRVRQNLHIV 2756
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQ--NIEDSREAVYNYFVKRCRNNLHIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2757 LCFSPVGEKFRNRALKFPALISGCTIDWFSRWPKDALVAVSEHFLTsyDIDCSLEIKKEVVQCMGSFQDGVAEKCVDYFQ 2836
Cdd:pfam12780 159 LCMSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLE--DIEIPEELKSNVVKVFVYVHSSVEDMSKKFYE 236
|
250 260
....*....|....*....|.
gi 1034644034 2837 RFRRSTHVTPKSYLSFIQGYK 2857
Cdd:pfam12780 237 ELKRKNYVTPKSYLELLRLYK 257
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2222-2403 |
1.06e-87 |
|
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: 284.28 E-value: 1.06e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2222 YPSDTtpEYGSILVPNVDNVRTDFLIQTIAKQGKAVLLIGEQGTAKTVIIKGFMSKYDPECHMIKSLNFSSATTPLMFQR 2301
Cdd:pfam12775 1 IPPDV--PFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2302 TIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPIINEWGDQVTNEIVRQLMEQNGFYNLEKPgEFTSIVDIQFLAAMIHPG 2381
Cdd:pfam12775 79 IIESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKL-TFKEIVDVQFVAAMGPPG 157
|
170 180
....*....|....*....|..
gi 1034644034 2382 GGRNDIPQRLKRQFSIFNCTLP 2403
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 ... |
3852-3991 |
7.36e-75 |
|
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: 245.83 E-value: 7.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3852 WKPMLYAVAFLHSTVQERRKFGALGWNIPYEFNQADFNATVQFIQNHLDdmDVKKGVSWTTIRYMIGEIQYGGRVTDDYD 3931
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLD--EYDEKIPWDALRYLIGEINYGGRVTDDWD 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034644034 3932 KRLLNTFAKVWFSENMFGPDFSFYQG-YNIPKCSTVDNYLQYIQSLPAYDSPEVFGLHPNA 3991
Cdd:pfam18198 79 RRLLNTYLEEFFNPEVLEEDFKFSPSlYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
3711-3820 |
1.27e-50 |
|
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: 175.71 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3711 DPRTPLICLLSMGSDPTDSIIALGKRLKIETRY--VSMGQGQEVHARKLLQQTMANGGWALLQNCHLGLDFMDELMDII- 3787
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGFGGKLhsISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILe 80
|
90 100 110
....*....|....*....|....*....|....
gi 1034644034 3788 -IETELVHDAFRLWMTTEAHKQFPITLLQMSIKF 3820
Cdd:pfam03028 81 eLPEETLHPDFRLWLTSEPSPKFPISILQNSIKI 114
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
2873-3218 |
1.86e-47 |
|
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This family is the region between D4 and D5 and is the two predicted alpha-helical coiled coil segments that form the stalk supporting the ATP-sensitive microtubule binding component.
Pssm-ID: 463699 [Multi-domain] Cd Length: 344 Bit Score: 175.26 E-value: 1.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2873 RMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAE 2952
Cdd:pfam12777 2 RLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2953 EKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMDCVLLLFqrkVSAVKIDLEKsctmpSWQESlKLMTA-- 3030
Cdd:pfam12777 82 EDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILM---APGGKIPKDK-----SWKAA-KIMMAkv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3031 GNFLQNLQQFPKDTINEEVIEFLSPYFEMPDYNIETAKRVCGNVAGLCSWTKAMASFFSINKEVLPlKANLVVQENRHLL 3110
Cdd:pfam12777 153 DGFLDSLIKFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAP-KRQALEEANADLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3111 AMQD-LQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAERCRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKRLV 3189
Cdd:pfam12777 232 AAQEkLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLC 311
|
330 340 350
....*....|....*....|....*....|
gi 1034644034 3190 GDVLLATAFLSYSGPFNQEFRDLLLND-WR 3218
Cdd:pfam12777 312 GDILLISAFISYLGFFTKKYRNELLDKfWI 341
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2095-2214 |
4.27e-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: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2095 LRQLYTESFPDLYRFCIQNLEYKMEVLEAFVITQSINMLQGLIP-------LKEQGGEVSQAHLGRLFVFALLWSAGAAL 2167
Cdd:pfam17852 1 LEPLFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDevleyngVHPLSPDKLKEYLEKLFLFALVWSIGGTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1034644034 2168 ELDGRRRLELWLRSRPTGtLELPPPagPGDTAFDYYV-APDGTWTHWN 2214
Cdd:pfam17852 81 DEDSRKKFDEFLRELFSG-LDLPPP--EKGTVYDYFVdLEKGEWVPWS 125
|
|
| AAA_lid_1 |
pfam17857 |
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3. |
2437-2526 |
2.44e-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: 79.98 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2437 LVPLTRRLWQMTKIKMLPTPAKFHYVFNLRDLSRVWQGMLNTTSEVIKEPNDLLKLWKHECKRVIADRFTVSSDVTWFDK 2516
Cdd:pfam17857 1 LIAAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDK 80
|
90
....*....|
gi 1034644034 2517 ALVSLVEEEF 2526
Cdd:pfam17857 81 IQMASLKKFF 90
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1928-2063 |
1.87e-09 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 58.84 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 1928 GMMTLGPSGAGKTTCIHTLMRAMTDCGKphrEMRMNPKAITAPQMFGRLDVATND--WTDGIFstlwrkTLRAKKGehiW 2005
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPV---FYVQLTRDTTEEDLFGRRNIDPGGasWVDGPL------VRAAREG---E 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034644034 2006 IILDGPVDAI---WIENLNSVLDDNKTLTLANGDRIPMAPNC-KIIFEPHNID----NASPATVSR 2063
Cdd:pfam07728 69 IAVLDEINRAnpdVLNSLLSLLDERRLLLPDGGELVKAAPDGfRLIATMNPLDrglnELSPALRSR 134
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2867-2988 |
1.19e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2867 VRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVandkadmvlkevtmKAQAAEKVKAEVQKVKDRAQAIVDSISK 2946
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEA--------------LKAELEAAKAELEAQQAEQEALLAQLSA 189
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1034644034 2947 DKAIAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPH 2988
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
2850-2971 |
1.41e-06 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 51.49 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2850 LSFIQGYKFIYGEKHVEvRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQA-----AE 2924
Cdd:PRK07352 29 LAIVIGLLYYFGRGFLG-KILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAiraeiEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034644034 2925 KVKAEVQKVKDRAQAIVDSiSKDKAIAEEKLEAAKPALEEAEAALQT 2971
Cdd:PRK07352 108 QAIEDMARLKQTAAADLSA-EQERVIAQLRREAAELAIAKAESQLPG 153
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2879-2968 |
2.99e-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: 49.46 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2879 EKLKEASESVAALSKELEAKEKELQVANDKADmvlKEVTMKAQAAEKVKAEVQKVKDRAQAivdsisKDKAIAEEKLeAA 2958
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEA------KAKAEAEAKA-KA 191
|
90
....*....|
gi 1034644034 2959 KPALEEAEAA 2968
Cdd:TIGR02794 192 EEAKAKAEAA 201
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2880-2967 |
1.76e-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: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2880 KLKEAsesvAALSKELEAKEKELQVANDKADMVLK----EVTMKAQAAEKVKAEVQKVKDRAqaivdsiSKDKAIAE--E 2953
Cdd:TIGR02794 143 KAKEE----AAKQAEEEAKAKAAAEAKKKAEEAKKkaeaEAKAKAEAEAKAKAEEAKAKAEA-------AKAKAAAEaaA 211
|
90
....*....|....
gi 1034644034 2954 KLEAAKPALEEAEA 2967
Cdd:TIGR02794 212 KAEAEAAAAAAAEA 225
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3111-3184 |
2.31e-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: 2.31e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034644034 3111 AMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAERcrhKMQTASTLISGLAGEKERWTEQSQEFAAQ 3184
Cdd:COG3883 134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2880-2968 |
2.54e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2880 KLKEASES--VAALSK--ELEAKEKELQVANDKADMVLKEvtmKAQAAEKVKAEV---QKVKDRAQAIVDSISKDKAIAE 2952
Cdd:PRK09510 146 KAKAEAEAkrAAAAAKkaAAEAKKKAEAEAAKKAAAEAKK---KAEAEAAAKAAAeakKKAEAEAKKKAAAEAKKKAAAE 222
|
90
....*....|....*.
gi 1034644034 2953 EKLEAAKPALEEAEAA 2968
Cdd:PRK09510 223 AKAAAAKAAAEAKAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2862-3195 |
2.91e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2862 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRaqaiV 2941
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----I 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2942 DSISKDKAIAEEKLEAAKPALEEAEAALQTIRpSDIATVRTlgrpphLIMRIMDCVLLL------FQRKVSAVKIDL-EK 3014
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAE-AEIEELEA------QIEQLKEELKALrealdeLRAELTLLNEEAaNL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3015 SCTMPSWQESLKLmtAGNFLQNLQQFPKDtiNEEVIEFLSPYFEMPDYNIETAKRvcgnvaGLCSWTKAMASFFSINKEV 3094
Cdd:TIGR02168 823 RERLESLERRIAA--TERRLEDLEEQIEE--LSEDIESLAAEIEELEELIEELES------ELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3095 LPLKANLVVQENRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQ-AMTEKQTLLEDAERcrhKMQTASTLISGLAGEKER 3173
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVrIDNLQERLSEEYSL---TLEEAEALENKIEDDEEE 969
|
330 340
....*....|....*....|..
gi 1034644034 3174 WTEQSQEFAAQTKRLvGDVLLA 3195
Cdd:TIGR02168 970 ARRRLKRLENKIKEL-GPVNLA 990
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2868-2970 |
5.06e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.81 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2868 RTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKE-----VTMKAQAAEKVKAEVQKVKDRAQAIVD 2942
Cdd:cd06503 26 KALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEAERILEQAKAEIE 105
|
90 100
....*....|....*....|....*...
gi 1034644034 2943 SiSKDKAIAEEKLEAAKPALEEAEAALQ 2970
Cdd:cd06503 106 Q-EKEKALAELRKEVADLAVEAAEKILG 132
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2880-2968 |
5.67e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.57 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2880 KLKEASESVAALSKEL--EAKEKELQVANDKAD---MVLKEVTMKAQAAEKVKAEVQ---KVKDRAQAIVDSISKDKAIA 2951
Cdd:PRK09510 118 KQAEEAAKQAALKQKQaeEAAAKAAAAAKAKAEaeaKRAAAAAKKAAAEAKKKAEAEaakKAAAEAKKKAEAEAAAKAAA 197
|
90
....*....|....*..
gi 1034644034 2952 EEKLEAAKPALEEAEAA 2968
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAE 214
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2862-2969 |
6.83e-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: 44.53 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2862 EKHVEVRTLANRmntgLEKLKEASESVA------ALSKELEAKEKELQVANDKadmvLKEVTMKAQAAEKVKAEVQKVKD 2935
Cdd:COG1579 63 RLELEIEEVEAR----IKKYEEQLGNVRnnkeyeALQKEIESLKRRISDLEDE----ILELMERIEELEEELAELEAELA 134
|
90 100 110
....*....|....*....|....*....|....
gi 1034644034 2936 RAQAIVDSISKDKAIAEEKLEAAKPALEEAEAAL 2969
Cdd:COG1579 135 ELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2866-2971 |
9.28e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2866 EVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSIS 2945
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100
....*....|....*....|....*.
gi 1034644034 2946 KDKAiAEEKLEAAKPALEEAEAALQT 2971
Cdd:COG4372 119 ELQK-ERQDLEQQRKQLEAQIAELQS 143
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2878-3197 |
1.08e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2878 LEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVT-MKAQAAEKVKAEVQKVKDRAQAIVDSISKdkaiAEEKLE 2956
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEE----AQEELE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2957 AAKPALEEAEAALQTIRPSD--------------IATVRTLGRPPHLIMRIMDCVLLLFQRKVSAVKIDLEKSCTMPswQ 3022
Cdd:COG4717 224 ELEEELEQLENELEAAALEErlkearlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL--G 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3023 ESLKLMTAGNFLQNLQQfpkdtinEEVIEFLSPYFEMPDYNIETAKRVCGNVAglcSWTKAMASFFSINKEvlpLKANLV 3102
Cdd:COG4717 302 KEAEELQALPALEELEE-------EELEELLAALGLPPDLSPEELLELLDRIE---ELQELLREAEELEEE---LQLEEL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 3103 VQENRHLLAMQD---------LQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLE--DAERCRHKMQTASTLISGLAGEK 3171
Cdd:COG4717 369 EQEIAALLAEAGvedeeelraALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEEL 448
|
330 340
....*....|....*....|....*.
gi 1034644034 3172 ERWTEQSQEFAAQTKRLVGDVLLATA 3197
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELAEL 474
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2879-2968 |
1.10e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.02 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2879 EKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAA 2958
Cdd:pfam05701 370 AKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAI 449
|
90
....*....|
gi 1034644034 2959 KpALEEAEAA 2968
Cdd:pfam05701 450 K-ALQESESS 458
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2257-2395 |
1.22e-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: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2257 VLLIGEQGTAKTVIIKGFMSKYDP-ECHMIkslNFSSATTP--LMFQRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMP 2333
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNrPVFYV---QLTRDTTEedLFGRRNIDPGGASWVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034644034 2334 ---IINEWgDQVTNEIVRQLMEqNGFYNLEKPGEFtsivdiQFLAAMIHPGGGRNDIPQRLKRQF 2395
Cdd:pfam07728 79 npdVLNSL-LSLLDERRLLLPD-GGELVKAAPDGF------RLIATMNPLDRGLNELSPALRSRF 135
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2865-2972 |
2.41e-03 |
|
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: 43.17 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2865 VEVRTLANRMNTGLEKLKEASESVA-ALSKELEAKEKELQVANDkadmVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDS 2943
Cdd:pfam06008 151 KAAQDLLSRIQTWFQSPQEENKALAnALRDSLAEYEAKLSDLRE----LLREAAAKTRDANRLNLANQANLREFQRKKEE 226
|
90 100
....*....|....*....|....*....
gi 1034644034 2944 ISKDKAIAEEKLEAAKPALEEAEAALQTI 2972
Cdd:pfam06008 227 VSEQKNQLEETLKTARDSLDAANLLLQEI 255
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2856-2970 |
2.78e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.31 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2856 YKFIYgeKHVeVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVT-----MKAQAAEKVKAEV 2930
Cdd:COG0711 18 KKFAW--PPI-LKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARkeaeaIAEEAKAEAEAEA 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1034644034 2931 QKVKDRAQAIVDSIsKDKAIAEEKLEAAKPALEEAEAALQ 2970
Cdd:COG0711 95 ERIIAQAEAEIEQE-RAKALAELRAEVADLAVAIAEKILG 133
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2862-2971 |
3.18e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2862 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKadmvLKEVTMKAQAAEKVKAEVQKVKDRAQAIV 2941
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK----LEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110
....*....|....*....|....*....|
gi 1034644034 2942 DSISKDKAIAEEKLEAAKPALEEAEAALQT 2971
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEE 327
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2883-2973 |
3.81e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2883 EASESVAALSKELEAKEKELQVANDKADMVLKEvtmkaqaAEKVKAEVQKVKDRAQAIVDS-ISKDKAIAEEKLEAAKpa 2961
Cdd:PRK00409 513 EDKEKLNELIASLEELERELEQKAEEAEALLKE-------AEKLKEELEEKKEKLQEEEDKlLEEAEKEAQQAIKEAK-- 583
|
90
....*....|..
gi 1034644034 2962 lEEAEAALQTIR 2973
Cdd:PRK00409 584 -KEADEIIKELR 594
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2862-2973 |
4.48e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2862 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDR--AQA 2939
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEA 93
|
90 100 110
....*....|....*....|....*....|....*..
gi 1034644034 2940 I---VDSISKDKAIAEEKLEAAKPALEEAEAALQTIR 2973
Cdd:COG1579 94 LqkeIESLKRRISDLEDEILELMERIEELEEELAELE 130
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2866-2969 |
5.22e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2866 EVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKdraqaivdsis 2945
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE----------- 764
|
90 100
....*....|....*....|....
gi 1034644034 2946 KDKAIAEEKLEAAKPALEEAEAAL 2969
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARL 788
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2866-2968 |
5.23e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2866 EVRTLANRMNTgLEKLKEASES---VAALSKELEAKEKELQvANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVD 2942
Cdd:COG4913 639 ELDALQERREA-LQRLAEYSWDeidVASAEREIAELEAELE-RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIG 716
|
90 100
....*....|....*....|....*.
gi 1034644034 2943 SISKDKAIAEEKLEAAKPALEEAEAA 2968
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEDL 742
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2878-2982 |
7.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644034 2878 LEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISK-DKAIAEEKLE 2956
Cdd:COG4913 677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFA 756
|
90 100
....*....|....*....|....*.
gi 1034644034 2957 AAkpALEEAEAALQTIRPSDIATVRT 2982
Cdd:COG4913 757 AA--LGDAVERELRENLEERIDALRA 780
|
|
| |
