|
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: 654.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 250 LGKIEDCMKVWIKQTEQVLAENNQLLKEaddvGPRAELEHWKKRLSKFNYLLEQLKSPDVKAVLAVLAAAKSKLLKTWRE 329
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNP----GPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 330 MDIRITDATNEAKDNVKYLYTLEKCCDPLYS-SDPLSMMDAIPTLINAIKMIYSISHYYNTSEKITSLFVKVTNQIISAC 408
Cdd:pfam08385 77 LDTELTDALNEAKDNVKYLKTLERPFEDLEElTDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 409 KAYITNNGtasIWNQPQDVVEEKILSAIKLKQEYQLCFHKTKQKLKQNPNAKQFDFSEMYIFGKFETFHRRLAKIIDIFT 488
Cdd:pfam08385 157 KKYLSPEG---IFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWDFSERYIFGRFDAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 489 TLKTYSVLQDS------TIEG-LEDMATKYQGIVATIKKKEYNFLDQRKMDFDQDYEEFCKQTNDLHNELRKFMDVTFAK 561
Cdd:pfam08385 234 TIEQFSKLEKIggtkgpELEGvIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 562 IQNTNQALRMLKKFE-RLNIPNL--GIDDKYQLILENYGADIDMISKLYTKQKYDP-PLARNQPPIAGKILWARQLFHRI 637
Cdd:pfam08385 314 ARSTESAFKLLRIFEfLLERPIIrgALEEKYTDLLQMFKKELDAVKKIFDKQKYNPsPIAKNMPPVAGAIIWARQLFRRI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 638 QQPMQLFQQHPAVLSTAEAKPIIRSYNRMAKVLLEFEVLFHRAWLRQIEEIHVG-LEASLLVKAPGTGELF-VNFDPQIL 715
Cdd:pfam08385 394 QEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGnLKRPLLVRHPETGKLLsVNFDPQLL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 716 ILFRETECMAQMGLEVSPLATSLFQKRDRYKRNFSNMKMMLAEYQRVKSKIPAAIEQLIVPHLAKVDEALQPGLAALTWT 795
Cdd:pfam08385 474 ALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTWN 553
|
....*..
gi 19115954 796 SLNIEAY 802
Cdd:pfam08385 554 SLGIDEY 560
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1942-2269 |
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 19115954 1942 YQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKG 2021
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2022 LAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINF 2101
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2102 RSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYKLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRANPMDTESTIV 2181
Cdd:pfam12774 160 RPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2182 MRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELEAAISRQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTL 2261
Cdd:pfam12774 240 LRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLV 319
|
....*...
gi 19115954 2262 GPSGAGKT 2269
Cdd:pfam12774 320 GPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1402-1807 |
6.24e-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: 6.24e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1402 LLEIKKQLNLLQKIYTLYNSVIETVNSYYDILWSEVNIEKINNELLEFQNRCRKLPRALKDWQAFLDLKKIIDDFSECCP 1481
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1482 LLEYMASKAMMERHWERITTLTGHSLDVGNESFKLRNIMEAPLLKYKEEIEDICISAVKERDIEQKLKQVINEWDNKTFT 1561
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1562 FGSFKTRGELLLRGdsTSEIIANMEDSLMLLGSLLSNRYNMPFKAQIQKWVQYLSNSTDIIESWMTVQNLWIYLEAVFVG 1641
Cdd:pfam08393 161 LVPYKDTGTFILKG--WDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1642 GDIAKQLPKEAKRFSNIDKSWVKIMTRAHEVPSVVQCCvGDETLGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVS 1721
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEAC-NIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1722 DPALLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiYDRILSISSQEGETIELDKP-VMAEGNVEVWLNSLLEESQSSL 1800
Cdd:pfam08393 318 NDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE--NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 19115954 1801 HLVIRQA 1807
Cdd:pfam08393 396 RDLLKEA 402
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4329-4621 |
8.81e-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: 8.81e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4329 AKDVLDTILGIQPKDTSG--GGDETREAVVARLADDMLEKLPPDYvPFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSL 4406
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGggGGGSSREEIVLELAKDILEKLPEPF-DIEEAEEKYPVGYEDPLNTVLLQEIERFNKLLKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4407 VRSTLTELKLAIDGTIIMSENLRDALDCMFDARIPAWWKKASWISS-TLGFWFTELIERNSQFTSWVF-NGRPHCFWMTG 4484
Cdd:pfam18199 83 IRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLkPLGSWIRDLLERLKQLQDWLDdEGPPKVFWLSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4485 FFNPQGFLTAMRQEITRANKgWALDNMVLCNEVTKWM-KDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFEL 4563
Cdd:pfam18199 163 FFFPQAFLTAVLQNYARKNG-WPIDKLSFDFEVTKKVsPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFSP 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4564 MPVIRIYAENNTL--RDPRFYSCPIYKKPVRTDLNYIAAVDLRTAQTPEHWVLRGVALLC 4621
Cdd:pfam18199 242 LPVIHLKPVESDKkkLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1643-4285 |
1.83e-124 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 444.43 E-value: 1.83e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1643 DIAKQLPKEAKRFSNIDKSWVKIMTRahevpsVVQCCVGDETL----GQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFF 1718
Cdd:COG5245 639 DLMPLIPHAVHRKMSLVSGVRGIYKR------VVSGCEAINTIledvGDDLDLFYKEMDQVFMSIEKVLGLRWREVERAS 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1719 FVSDpaLLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiyDRILSISSQEGETIELDKPVMAEGNVEV--WLN----SL 1792
Cdd:COG5245 713 EVEE--LMDRVRELENRVYSYRFFVKKIAKEEMKTVFS---SRIQKKEPFSLDSEAYVGFFRLYEKSIVirGINrsmgRV 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1793 LEESQSSLhlvirQAAANIQETGFqlteFLSSFPAQVGLLGIQMiWTRDSEEALRNA------KFDKKIMQKTNQAFLEL 1866
Cdd:COG5245 788 LSQYLESV-----QEALEIEDGSF----FVSRHRVRDGGLEKGR-GCDAWENCFDPPlseyfrILEKIFPSEEGYFFDEV 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1867 LNtlidvttrdlsstervKYETLITIHVHQRDIFDDLCHMHIKSPMDFEWLKQCRFYFNEDsDKMMIHITDVAFIYQNEF 1946
Cdd:COG5245 858 LK----------------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLY-KRFIKVRSSYRSAEMFAK 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1947 LGCTDRLVITPLTDRCYITLAQALGMSMggapAGPAGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSG 2026
Cdd:COG5245 921 NTIPFFVFEHSMDTSQHQKLFEAVCDEV----CRFVDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEE 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2027 SWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEHKKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSV 2104
Cdd:COG5245 989 ERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMF 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2105 AMMVPDRQIIIRVKlascgfidnvVLARKFFTLYKLCEEQLSKQVHYDFglrnilsvlRTL-GAAKRANPMDTESTivmr 2183
Cdd:COG5245 1060 LSNIPFGAIKSRRE----------SLDREIGAFNNEVDGIAREEDELMF---------YPMfKSLKAKHRMLEEKT---- 1116
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2184 vlrdMNLSKLIdedEPLFLSLIEDLFPNI--LLDKAGYPELEAAISRQVEEAGLINHPPWKlKVIQLFETQRVRHGMMTL 2261
Cdd:COG5245 1117 ----EYLNKIL---SITGLPLISDTLRERidTLDAEWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGAFHAEY 1188
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2262 GPSGAGKTTCIHTLMRAMTDCGKPHREMRMnpkaitapqmfgrLDvATNDWTdGIFSTLWRKTLRAK-KGEHIWIILDGp 2340
Cdd:COG5245 1189 FRVFLCKIKHYTDACDYLWHVKSPYVKKKY-------------FD-ADMELR-QFFLMFNREDMEARlADSKMEYEVER- 1252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2341 vdaiWIENLNSVLDDNKTLTLANGDRipmapncKIIFEphNIDnASPATVSRNGMVFMSSSILDWSPILEGFL------- 2413
Cdd:COG5245 1253 ----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgdtkryl 1318
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2414 -KKRSPQEAEILRQLYTESF-----PDLYRFCIQ-----------NLEYKMEVLEAfVITQSINMLQGLiplKEQGGEVs 2476
Cdd:COG5245 1319 dECLDFFSCFEEVQKEIDELsmvfcADALRFSADlyhivkerrfsGVLAGSDASES-LGGKSIELAAIL---EHKDLIV- 1393
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2477 qaHLGRLFVFALLWSAGAALELDGRRRLELWLR---SRPTGTLELPPPAGPGDTAFDYYVAPDGTWTHWNTRTQEYLYPS 2553
Cdd:COG5245 1394 --EMKRGINDVLKLRIFGDKCRESTPRFYLISDgdlIKDLNERSDYEEMLIMMFNISAVITNNGSIAGFELRGERVMLRK 1471
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2554 DttpeygsILVPNVDNVRTDFLIQTIAKQGKAVLLIGEQGTAKTVIIKG-FMSKYDPEchmIKSLNFS-SATTPLM---F 2628
Cdd:COG5245 1472 E-------VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPsLRSELITE---VKYFNFStCTMTPSKlsvL 1541
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2629 QRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPIINEWGDQVTNEIVRQLMEQNGFYN-LEKpgEFTSIVDIqFLAAMI 2707
Cdd:COG5245 1542 ERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGAC 1618
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2708 HPGG--GRNDIPQRLKRQFSIFNCTLPSEASVDKIFGVIGVGHYCTQRGFSEEVRDSVTKLVPLTRRLWQMTKikmlpTP 2785
Cdd:COG5245 1619 NPGTdeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTK-----FF 1693
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2786 AKFHYVFNLRDLSRVWQGMLNTTSEVIKEPN-DLLKLWKHECKRVIADRFTVSSDVTWFDKALVSLVEEEFGE------- 2857
Cdd:COG5245 1694 LQMNYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREmiaghig 1773
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2858 EKKLLVDcgiDTYFVDFlrdapeaagetsEEADAETPKIYepiesfshLKERLNMFlqlYNESIRgagMDMVFFADAMVH 2937
Cdd:COG5245 1774 EAEITFS---MILFFGM------------ACLLKKDLAVF--------VEEVRKIF---GSSHLD---VEAVAYKDALLH 1824
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2938 LVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNE 3017
Cdd:COG5245 1825 ILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESI 1904
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3018 IKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfPRCLPTNENLHDYFMSRVRQNLHIVL-CFSPVGEKFR 3096
Cdd:COG5245 1905 PVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVL 1983
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3097 NRALkFPALISGCTIDWFSRWPKDALVAVSEHFLT-SYDIDCSLEIKKEVVQCMGS-FQDGVAEKCVDYFQR-FRRSTHV 3173
Cdd:COG5245 1984 AGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVETlSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIE 2062
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3174 --TPKSYLSFIQG---YKFIYGEKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMK 3248
Cdd:COG5245 2063 gsLGESKIKFIGGlkvYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGE 2142
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3249 AQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMD--CV 3326
Cdd:COG5245 2143 RLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCD 2222
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3327 LLLFQRKVsavkidleksctmpsWQESLKLMTAGNFLQNLQQFPKDT-INEEVIEFL-SPYFEMPDYNIETAKR---VCG 3401
Cdd:COG5245 2223 LLGFEAKI---------------WFGEQQSLRRDDFIRIIGKYPDEIeFDLEARRFReARECSDPSFTGSILNRaskACG 2287
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3402 NvagLCSWTKAMASFFSINKEVLPLKANLVVQENRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAER 3481
Cdd:COG5245 2288 P---LKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDT 2364
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3482 CRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKRLVGDVLLATAFLSYSGPFNQEFRDLLLNDwRKEMKARKIPFGKNL 3561
Cdd:COG5245 2365 VHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIR 2443
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3562 NLSEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSL 3641
Cdd:COG5245 2444 RRQFITEGVQKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQAR 2523
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3642 SLGRPLLIEDvGEELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMK 3721
Cdd:COG5245 2524 REGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVL 2602
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3722 GLEDQLLGRVILTEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEVTQKLEI 3801
Cdd:COG5245 2603 GCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESE 2682
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3802 SAETEVQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLFDlsLARSVKSpitskRIANIIEHMTYEVYK 3881
Cdd:COG5245 2683 SMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFE--KWRRMKS-----KYLCAIRYMLMSSEW 2755
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3882 YaargLYEEhkflFTLLLTLKIDIQRN-RVKHEEFLTLIKGGASLDLKACppkpskwilDITWLNLVELSKLRQFSDVLD 3960
Cdd:COG5245 2756 I----LDHE----DRSGFIHRLDVSFLlRTKRFVSTLLEDKNYRQVLSSC---------SLYGNDVISHSCDRFDRDVYR 2818
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3961 QISRNEKMWKIWFDKenpeeeplpnAYDKSLDCFRRLLLIRSWcpdrtiaqARKYIVDSMGEKYaegvilDLEK-TWEES 4039
Cdd:COG5245 2819 ALKHQMDNRTHSTIL----------TSNSKTNPYKEYTYNDSW--------AEAFEVEDSGDLY------KFEEgLLELI 2874
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4040 DPRTPLICLLsMGSDPTDSIIalgKRLKIETRyvsmgqgqEVHARKLLQQTMANGGWALLQNCHLGLDFMDELMDIIIE- 4118
Cdd:COG5245 2875 VGHAPLIYAH-KKSLENERNV---DRLGSKEN--------EVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYVEDVVYp 2942
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4119 ---TELVHDAFRLWMTTEAHKQFPITLLQMSIKFANDPPQGLRAGLKrtysgvsqDLLdvssGSQWKPMLYA-------- 4187
Cdd:COG5245 2943 ikaSRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYA--------DLV----EIDRYPFDYTlviacdda 3010
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4188 --VAFLHSTVQERRKFGALGWNIPYEFNQADFNATVQFIQNHLdDMDVKKGVSWTTIRYMIGEIQYGGR--------VTD 4257
Cdd:COG5245 3011 fyLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNIL-FLNHLNARKWGNNRDLIFTIVYGKKhslmedskVVD 3089
|
2730 2740
....*....|....*....|....*...
gi 19115954 4258 DYDKRLLNTFAKVWFSENMFGPDFSFYQ 4285
Cdd:COG5245 3090 KYCRGYGAHETSSQILASVPGGDPELVK 3117
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3574-3795 |
5.88e-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: 5.88e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3574 SEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVG 3653
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3654 EELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMKGLEDQLLGRVIL 3733
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115954 3734 TEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEV 3795
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
3179-3300 |
1.87e-06 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 51.11 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3179 LSFIQGYKFIYGEKHVEvRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQA-----AE 3253
Cdd:PRK07352 29 LAIVIGLLYYFGRGFLG-KILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAiraeiEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 19115954 3254 KVKAEVQKVKDRAQAIVDSiSKDKAIAEEKLEAAKPALEEAEAALQT 3300
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 ... |
3208-3297 |
3.22e-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: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3208 EKLKEASESVAALSKELEAKEKELQVANDKADmvlKEVTMKAQAAEKVKAEVQKVKDRAQAivdsisKDKAIAEEKLeAA 3287
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEA------KAKAEAEAKA-KA 191
|
90
....*....|
gi 19115954 3288 KPALEEAEAA 3297
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 ... |
3197-3299 |
6.43e-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: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3197 RTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKE-----VTMKAQAAEKVKAEVQKVKDRAQAIVD 3271
Cdd:cd06503 26 KALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEAERILEQAKAEIE 105
|
90 100
....*....|....*....|....*...
gi 19115954 3272 SiSKDKAIAEEKLEAAKPALEEAEAALQ 3299
Cdd:cd06503 106 Q-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: 654.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 250 LGKIEDCMKVWIKQTEQVLAENNQLLKEaddvGPRAELEHWKKRLSKFNYLLEQLKSPDVKAVLAVLAAAKSKLLKTWRE 329
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNP----GPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 330 MDIRITDATNEAKDNVKYLYTLEKCCDPLYS-SDPLSMMDAIPTLINAIKMIYSISHYYNTSEKITSLFVKVTNQIISAC 408
Cdd:pfam08385 77 LDTELTDALNEAKDNVKYLKTLERPFEDLEElTDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 409 KAYITNNGtasIWNQPQDVVEEKILSAIKLKQEYQLCFHKTKQKLKQNPNAKQFDFSEMYIFGKFETFHRRLAKIIDIFT 488
Cdd:pfam08385 157 KKYLSPEG---IFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWDFSERYIFGRFDAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 489 TLKTYSVLQDS------TIEG-LEDMATKYQGIVATIKKKEYNFLDQRKMDFDQDYEEFCKQTNDLHNELRKFMDVTFAK 561
Cdd:pfam08385 234 TIEQFSKLEKIggtkgpELEGvIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 562 IQNTNQALRMLKKFE-RLNIPNL--GIDDKYQLILENYGADIDMISKLYTKQKYDP-PLARNQPPIAGKILWARQLFHRI 637
Cdd:pfam08385 314 ARSTESAFKLLRIFEfLLERPIIrgALEEKYTDLLQMFKKELDAVKKIFDKQKYNPsPIAKNMPPVAGAIIWARQLFRRI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 638 QQPMQLFQQHPAVLSTAEAKPIIRSYNRMAKVLLEFEVLFHRAWLRQIEEIHVG-LEASLLVKAPGTGELF-VNFDPQIL 715
Cdd:pfam08385 394 QEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGnLKRPLLVRHPETGKLLsVNFDPQLL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 716 ILFRETECMAQMGLEVSPLATSLFQKRDRYKRNFSNMKMMLAEYQRVKSKIPAAIEQLIVPHLAKVDEALQPGLAALTWT 795
Cdd:pfam08385 474 ALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTWN 553
|
....*..
gi 19115954 796 SLNIEAY 802
Cdd:pfam08385 554 SLGIDEY 560
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1942-2269 |
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 19115954 1942 YQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKG 2021
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2022 LAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINF 2101
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2102 RSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYKLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRANPMDTESTIV 2181
Cdd:pfam12774 160 RPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2182 MRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELEAAISRQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTL 2261
Cdd:pfam12774 240 LRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLV 319
|
....*...
gi 19115954 2262 GPSGAGKT 2269
Cdd:pfam12774 320 GPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1402-1807 |
6.24e-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: 6.24e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1402 LLEIKKQLNLLQKIYTLYNSVIETVNSYYDILWSEVNIEKINNELLEFQNRCRKLPRALKDWQAFLDLKKIIDDFSECCP 1481
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1482 LLEYMASKAMMERHWERITTLTGHSLDVGNESFKLRNIMEAPLLKYKEEIEDICISAVKERDIEQKLKQVINEWDNKTFT 1561
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1562 FGSFKTRGELLLRGdsTSEIIANMEDSLMLLGSLLSNRYNMPFKAQIQKWVQYLSNSTDIIESWMTVQNLWIYLEAVFVG 1641
Cdd:pfam08393 161 LVPYKDTGTFILKG--WDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1642 GDIAKQLPKEAKRFSNIDKSWVKIMTRAHEVPSVVQCCvGDETLGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVS 1721
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEAC-NIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1722 DPALLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiYDRILSISSQEGETIELDKP-VMAEGNVEVWLNSLLEESQSSL 1800
Cdd:pfam08393 318 NDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE--NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 19115954 1801 HLVIRQA 1807
Cdd:pfam08393 396 RDLLKEA 402
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4329-4621 |
8.81e-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: 8.81e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4329 AKDVLDTILGIQPKDTSG--GGDETREAVVARLADDMLEKLPPDYvPFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSL 4406
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGggGGGSSREEIVLELAKDILEKLPEPF-DIEEAEEKYPVGYEDPLNTVLLQEIERFNKLLKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4407 VRSTLTELKLAIDGTIIMSENLRDALDCMFDARIPAWWKKASWISS-TLGFWFTELIERNSQFTSWVF-NGRPHCFWMTG 4484
Cdd:pfam18199 83 IRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLkPLGSWIRDLLERLKQLQDWLDdEGPPKVFWLSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4485 FFNPQGFLTAMRQEITRANKgWALDNMVLCNEVTKWM-KDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFEL 4563
Cdd:pfam18199 163 FFFPQAFLTAVLQNYARKNG-WPIDKLSFDFEVTKKVsPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFSP 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4564 MPVIRIYAENNTL--RDPRFYSCPIYKKPVRTDLNYIAAVDLRTAQTPEHWVLRGVALLC 4621
Cdd:pfam18199 242 LPVIHLKPVESDKkkLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1643-4285 |
1.83e-124 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 444.43 E-value: 1.83e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1643 DIAKQLPKEAKRFSNIDKSWVKIMTRahevpsVVQCCVGDETL----GQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFF 1718
Cdd:COG5245 639 DLMPLIPHAVHRKMSLVSGVRGIYKR------VVSGCEAINTIledvGDDLDLFYKEMDQVFMSIEKVLGLRWREVERAS 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1719 FVSDpaLLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiyDRILSISSQEGETIELDKPVMAEGNVEV--WLN----SL 1792
Cdd:COG5245 713 EVEE--LMDRVRELENRVYSYRFFVKKIAKEEMKTVFS---SRIQKKEPFSLDSEAYVGFFRLYEKSIVirGINrsmgRV 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1793 LEESQSSLhlvirQAAANIQETGFqlteFLSSFPAQVGLLGIQMiWTRDSEEALRNA------KFDKKIMQKTNQAFLEL 1866
Cdd:COG5245 788 LSQYLESV-----QEALEIEDGSF----FVSRHRVRDGGLEKGR-GCDAWENCFDPPlseyfrILEKIFPSEEGYFFDEV 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1867 LNtlidvttrdlsstervKYETLITIHVHQRDIFDDLCHMHIKSPMDFEWLKQCRFYFNEDsDKMMIHITDVAFIYQNEF 1946
Cdd:COG5245 858 LK----------------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLY-KRFIKVRSSYRSAEMFAK 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 1947 LGCTDRLVITPLTDRCYITLAQALGMSMggapAGPAGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSG 2026
Cdd:COG5245 921 NTIPFFVFEHSMDTSQHQKLFEAVCDEV----CRFVDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEE 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2027 SWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEHKKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSV 2104
Cdd:COG5245 989 ERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMF 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2105 AMMVPDRQIIIRVKlascgfidnvVLARKFFTLYKLCEEQLSKQVHYDFglrnilsvlRTL-GAAKRANPMDTESTivmr 2183
Cdd:COG5245 1060 LSNIPFGAIKSRRE----------SLDREIGAFNNEVDGIAREEDELMF---------YPMfKSLKAKHRMLEEKT---- 1116
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2184 vlrdMNLSKLIdedEPLFLSLIEDLFPNI--LLDKAGYPELEAAISRQVEEAGLINHPPWKlKVIQLFETQRVRHGMMTL 2261
Cdd:COG5245 1117 ----EYLNKIL---SITGLPLISDTLRERidTLDAEWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGAFHAEY 1188
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2262 GPSGAGKTTCIHTLMRAMTDCGKPHREMRMnpkaitapqmfgrLDvATNDWTdGIFSTLWRKTLRAK-KGEHIWIILDGp 2340
Cdd:COG5245 1189 FRVFLCKIKHYTDACDYLWHVKSPYVKKKY-------------FD-ADMELR-QFFLMFNREDMEARlADSKMEYEVER- 1252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2341 vdaiWIENLNSVLDDNKTLTLANGDRipmapncKIIFEphNIDnASPATVSRNGMVFMSSSILDWSPILEGFL------- 2413
Cdd:COG5245 1253 ----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgdtkryl 1318
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2414 -KKRSPQEAEILRQLYTESF-----PDLYRFCIQ-----------NLEYKMEVLEAfVITQSINMLQGLiplKEQGGEVs 2476
Cdd:COG5245 1319 dECLDFFSCFEEVQKEIDELsmvfcADALRFSADlyhivkerrfsGVLAGSDASES-LGGKSIELAAIL---EHKDLIV- 1393
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2477 qaHLGRLFVFALLWSAGAALELDGRRRLELWLR---SRPTGTLELPPPAGPGDTAFDYYVAPDGTWTHWNTRTQEYLYPS 2553
Cdd:COG5245 1394 --EMKRGINDVLKLRIFGDKCRESTPRFYLISDgdlIKDLNERSDYEEMLIMMFNISAVITNNGSIAGFELRGERVMLRK 1471
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2554 DttpeygsILVPNVDNVRTDFLIQTIAKQGKAVLLIGEQGTAKTVIIKG-FMSKYDPEchmIKSLNFS-SATTPLM---F 2628
Cdd:COG5245 1472 E-------VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPsLRSELITE---VKYFNFStCTMTPSKlsvL 1541
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2629 QRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPIINEWGDQVTNEIVRQLMEQNGFYN-LEKpgEFTSIVDIqFLAAMI 2707
Cdd:COG5245 1542 ERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGAC 1618
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2708 HPGG--GRNDIPQRLKRQFSIFNCTLPSEASVDKIFGVIGVGHYCTQRGFSEEVRDSVTKLVPLTRRLWQMTKikmlpTP 2785
Cdd:COG5245 1619 NPGTdeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTK-----FF 1693
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2786 AKFHYVFNLRDLSRVWQGMLNTTSEVIKEPN-DLLKLWKHECKRVIADRFTVSSDVTWFDKALVSLVEEEFGE------- 2857
Cdd:COG5245 1694 LQMNYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREmiaghig 1773
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2858 EKKLLVDcgiDTYFVDFlrdapeaagetsEEADAETPKIYepiesfshLKERLNMFlqlYNESIRgagMDMVFFADAMVH 2937
Cdd:COG5245 1774 EAEITFS---MILFFGM------------ACLLKKDLAVF--------VEEVRKIF---GSSHLD---VEAVAYKDALLH 1824
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2938 LVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNE 3017
Cdd:COG5245 1825 ILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESI 1904
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3018 IKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfPRCLPTNENLHDYFMSRVRQNLHIVL-CFSPVGEKFR 3096
Cdd:COG5245 1905 PVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVL 1983
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3097 NRALkFPALISGCTIDWFSRWPKDALVAVSEHFLT-SYDIDCSLEIKKEVVQCMGS-FQDGVAEKCVDYFQR-FRRSTHV 3173
Cdd:COG5245 1984 AGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVETlSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIE 2062
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3174 --TPKSYLSFIQG---YKFIYGEKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMK 3248
Cdd:COG5245 2063 gsLGESKIKFIGGlkvYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGE 2142
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3249 AQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMD--CV 3326
Cdd:COG5245 2143 RLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCD 2222
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3327 LLLFQRKVsavkidleksctmpsWQESLKLMTAGNFLQNLQQFPKDT-INEEVIEFL-SPYFEMPDYNIETAKR---VCG 3401
Cdd:COG5245 2223 LLGFEAKI---------------WFGEQQSLRRDDFIRIIGKYPDEIeFDLEARRFReARECSDPSFTGSILNRaskACG 2287
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3402 NvagLCSWTKAMASFFSINKEVLPLKANLVVQENRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAER 3481
Cdd:COG5245 2288 P---LKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDT 2364
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3482 CRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKRLVGDVLLATAFLSYSGPFNQEFRDLLLNDwRKEMKARKIPFGKNL 3561
Cdd:COG5245 2365 VHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIR 2443
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3562 NLSEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSL 3641
Cdd:COG5245 2444 RRQFITEGVQKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQAR 2523
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3642 SLGRPLLIEDvGEELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMK 3721
Cdd:COG5245 2524 REGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVL 2602
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3722 GLEDQLLGRVILTEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEVTQKLEI 3801
Cdd:COG5245 2603 GCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESE 2682
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3802 SAETEVQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLFDlsLARSVKSpitskRIANIIEHMTYEVYK 3881
Cdd:COG5245 2683 SMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFE--KWRRMKS-----KYLCAIRYMLMSSEW 2755
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3882 YaargLYEEhkflFTLLLTLKIDIQRN-RVKHEEFLTLIKGGASLDLKACppkpskwilDITWLNLVELSKLRQFSDVLD 3960
Cdd:COG5245 2756 I----LDHE----DRSGFIHRLDVSFLlRTKRFVSTLLEDKNYRQVLSSC---------SLYGNDVISHSCDRFDRDVYR 2818
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3961 QISRNEKMWKIWFDKenpeeeplpnAYDKSLDCFRRLLLIRSWcpdrtiaqARKYIVDSMGEKYaegvilDLEK-TWEES 4039
Cdd:COG5245 2819 ALKHQMDNRTHSTIL----------TSNSKTNPYKEYTYNDSW--------AEAFEVEDSGDLY------KFEEgLLELI 2874
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4040 DPRTPLICLLsMGSDPTDSIIalgKRLKIETRyvsmgqgqEVHARKLLQQTMANGGWALLQNCHLGLDFMDELMDIIIE- 4118
Cdd:COG5245 2875 VGHAPLIYAH-KKSLENERNV---DRLGSKEN--------EVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYVEDVVYp 2942
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4119 ---TELVHDAFRLWMTTEAHKQFPITLLQMSIKFANDPPQGLRAGLKrtysgvsqDLLdvssGSQWKPMLYA-------- 4187
Cdd:COG5245 2943 ikaSRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYA--------DLV----EIDRYPFDYTlviacdda 3010
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4188 --VAFLHSTVQERRKFGALGWNIPYEFNQADFNATVQFIQNHLdDMDVKKGVSWTTIRYMIGEIQYGGR--------VTD 4257
Cdd:COG5245 3011 fyLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNIL-FLNHLNARKWGNNRDLIFTIVYGKKhslmedskVVD 3089
|
2730 2740
....*....|....*....|....*...
gi 19115954 4258 DYDKRLLNTFAKVWFSENMFGPDFSFYQ 4285
Cdd:COG5245 3090 KYCRGYGAHETSSQILASVPGGDPELVK 3117
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3574-3795 |
5.88e-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: 5.88e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3574 SEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVG 3653
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3654 EELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMKGLEDQLLGRVIL 3733
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115954 3734 TEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEV 3795
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 ... |
2926-3186 |
5.15e-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: 5.15e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2926 MDMVFFADAMVHLVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQ 3005
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3006 GKGITFIFTDNEIKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfpRCLPTNENLHDYFMSRVRQNLHIV 3085
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQ--NIEDSREAVYNYFVKRCRNNLHIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3086 LCFSPVGEKFRNRALKFPALISGCTIDWFSRWPKDALVAVSEHFLTsyDIDCSLEIKKEVVQCMGSFQDGVAEKCVDYFQ 3165
Cdd:pfam12780 159 LCMSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLE--DIEIPEELKSNVVKVFVYVHSSVEDMSKKFYE 236
|
250 260
....*....|....*....|.
gi 19115954 3166 RFRRSTHVTPKSYLSFIQGYK 3186
Cdd:pfam12780 237 ELKRKNYVTPKSYLELLRLYK 257
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2551-2732 |
8.09e-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: 284.67 E-value: 8.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2551 YPSDTtpEYGSILVPNVDNVRTDFLIQTIAKQGKAVLLIGEQGTAKTVIIKGFMSKYDPECHMIKSLNFSSATTPLMFQR 2630
Cdd:pfam12775 1 IPPDV--PFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2631 TIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPIINEWGDQVTNEIVRQLMEQNGFYNLEKPgEFTSIVDIQFLAAMIHPG 2710
Cdd:pfam12775 79 IIESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKL-TFKEIVDVQFVAAMGPPG 157
|
170 180
....*....|....*....|..
gi 19115954 2711 GGRNDIPQRLKRQFSIFNCTLP 2732
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 ... |
4181-4320 |
6.05e-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: 246.21 E-value: 6.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4181 WKPMLYAVAFLHSTVQERRKFGALGWNIPYEFNQADFNATVQFIQNHLDdmDVKKGVSWTTIRYMIGEIQYGGRVTDDYD 4260
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLD--EYDEKIPWDALRYLIGEINYGGRVTDDWD 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115954 4261 KRLLNTFAKVWFSENMFGPDFSFYQG-YNIPKCSTVDNYLQYIQSLPAYDSPEVFGLHPNA 4320
Cdd:pfam18198 79 RRLLNTYLEEFFNPEVLEEDFKFSPSlYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
4040-4149 |
1.37e-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: 1.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 4040 DPRTPLICLLSMGSDPTDSIIALGKRLKIETRY--VSMGQGQEVHARKLLQQTMANGGWALLQNCHLGLDFMDELMDII- 4116
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGFGGKLhsISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILe 80
|
90 100 110
....*....|....*....|....*....|....
gi 19115954 4117 -IETELVHDAFRLWMTTEAHKQFPITLLQMSIKF 4149
Cdd:pfam03028 81 eLPEETLHPDFRLWLTSEPSPKFPISILQNSIKI 114
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
3202-3547 |
2.01e-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: 2.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3202 RMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAE 3281
Cdd:pfam12777 2 RLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3282 EKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMDCVLLLFqrkVSAVKIDLEKsctmpSWQESlKLMTA-- 3359
Cdd:pfam12777 82 EDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILM---APGGKIPKDK-----SWKAA-KIMMAkv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3360 GNFLQNLQQFPKDTINEEVIEFLSPYFEMPDYNIETAKRVCGNVAGLCSWTKAMASFFSINKEVLPlKANLVVQENRHLL 3439
Cdd:pfam12777 153 DGFLDSLIKFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAP-KRQALEEANADLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3440 AMQD-LQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAERCRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKRLV 3518
Cdd:pfam12777 232 AAQEkLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLC 311
|
330 340 350
....*....|....*....|....*....|
gi 19115954 3519 GDVLLATAFLSYSGPFNQEFRDLLLND-WR 3547
Cdd:pfam12777 312 GDILLISAFISYLGFFTKKYRNELLDKfWI 341
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2424-2543 |
4.17e-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: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2424 LRQLYTESFPDLYRFCIQNLEYKMEVLEAFVITQSINMLQGLIP-------LKEQGGEVSQAHLGRLFVFALLWSAGAAL 2496
Cdd:pfam17852 1 LEPLFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDevleyngVHPLSPDKLKEYLEKLFLFALVWSIGGTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 19115954 2497 ELDGRRRLELWLRSRPTGtLELPPPagPGDTAFDYYV-APDGTWTHWN 2543
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. |
2766-2855 |
2.62e-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: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2766 LVPLTRRLWQMTKIKMLPTPAKFHYVFNLRDLSRVWQGMLNTTSEVIKEPNDLLKLWKHECKRVIADRFTVSSDVTWFDK 2845
Cdd:pfam17857 1 LIAAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDK 80
|
90
....*....|
gi 19115954 2846 ALVSLVEEEF 2855
Cdd:pfam17857 81 IQMASLKKFF 90
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2257-2392 |
2.02e-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: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2257 GMMTLGPSGAGKTTCIHTLMRAMTDCGKphrEMRMNPKAITAPQMFGRLDVATND--WTDGIFstlwrkTLRAKKGehiW 2334
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPV---FYVQLTRDTTEEDLFGRRNIDPGGasWVDGPL------VRAAREG---E 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115954 2335 IILDGPVDAI---WIENLNSVLDDNKTLTLANGDRIPMAPNC-KIIFEPHNID----NASPATVSR 2392
Cdd:pfam07728 69 IAVLDEINRAnpdVLNSLLSLLDERRLLLPDGGELVKAAPDGfRLIATMNPLDrglnELSPALRSR 134
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3196-3317 |
1.29e-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: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3196 VRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVandkadmvlkevtmKAQAAEKVKAEVQKVKDRAQAIVDSISK 3275
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEA--------------LKAELEAAKAELEAQQAEQEALLAQLSA 189
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 19115954 3276 DKAIAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPH 3317
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
3179-3300 |
1.87e-06 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 51.11 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3179 LSFIQGYKFIYGEKHVEvRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQA-----AE 3253
Cdd:PRK07352 29 LAIVIGLLYYFGRGFLG-KILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAiraeiEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 19115954 3254 KVKAEVQKVKDRAQAIVDSiSKDKAIAEEKLEAAKPALEEAEAALQT 3300
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 ... |
3208-3297 |
3.22e-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: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3208 EKLKEASESVAALSKELEAKEKELQVANDKADmvlKEVTMKAQAAEKVKAEVQKVKDRAQAivdsisKDKAIAEEKLeAA 3287
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEA------KAKAEAEAKA-KA 191
|
90
....*....|
gi 19115954 3288 KPALEEAEAA 3297
Cdd:TIGR02794 192 EEAKAKAEAA 201
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3209-3296 |
1.90e-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: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3209 KLKEAsesvAALSKELEAKEKELQVANDKADMVLK----EVTMKAQAAEKVKAEVQKVKDRAqaivdsiSKDKAIAE--E 3282
Cdd:TIGR02794 143 KAKEE----AAKQAEEEAKAKAAAEAKKKAEEAKKkaeaEAKAKAEAEAKAKAEEAKAKAEA-------AKAKAAAEaaA 211
|
90
....*....|....
gi 19115954 3283 KLEAAKPALEEAEA 3296
Cdd:TIGR02794 212 KAEAEAAAAAAAEA 225
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3440-3513 |
2.49e-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: 2.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115954 3440 AMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAERcrhKMQTASTLISGLAGEKERWTEQSQEFAAQ 3513
Cdd:COG3883 134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3209-3297 |
2.74e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3209 KLKEASES--VAALSK--ELEAKEKELQVANDKADMVLKEvtmKAQAAEKVKAEV---QKVKDRAQAIVDSISKDKAIAE 3281
Cdd:PRK09510 146 KAKAEAEAkrAAAAAKkaAAEAKKKAEAEAAKKAAAEAKK---KAEAEAAAKAAAeakKKAEAEAKKKAAAEAKKKAAAE 222
|
90
....*....|....*.
gi 19115954 3282 EKLEAAKPALEEAEAA 3297
Cdd:PRK09510 223 AKAAAAKAAAEAKAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3191-3524 |
3.88e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3191 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRaqaiV 3270
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----I 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3271 DSISKDKAIAEEKLEAAKPALEEAEAALQTIRpSDIATVRTlgrpphLIMRIMDCVLLL------FQRKVSAVKIDL-EK 3343
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAE-AEIEELEA------QIEQLKEELKALrealdeLRAELTLLNEEAaNL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3344 SCTMPSWQESLKLmtAGNFLQNLQQFPKDtiNEEVIEFLSPYFEMPDYNIETAKRvcgnvaGLCSWTKAMASFFSINKEV 3423
Cdd:TIGR02168 823 RERLESLERRIAA--TERRLEDLEEQIEE--LSEDIESLAAEIEELEELIEELES------ELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3424 LPLKANLVVQENRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQ-AMTEKQTLLEDAERcrhKMQTASTLISGLAGEKER 3502
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVrIDNLQERLSEEYSL---TLEEAEALENKIEDDEEE 969
|
330 340
....*....|....*....|..
gi 19115954 3503 WTEQSQEFAAQTKRLvGDVLLA 3524
Cdd:TIGR02168 970 ARRRLKRLENKIKEL-GPVNLA 990
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3209-3297 |
6.12e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.57 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3209 KLKEASESVAALSKEL--EAKEKELQVANDKAD---MVLKEVTMKAQAAEKVKAEVQ---KVKDRAQAIVDSISKDKAIA 3280
Cdd:PRK09510 118 KQAEEAAKQAALKQKQaeEAAAKAAAAAKAKAEaeaKRAAAAAKKAAAEAKKKAEAEaakKAAAEAKKKAEAEAAAKAAA 197
|
90
....*....|....*..
gi 19115954 3281 EEKLEAAKPALEEAEAA 3297
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAE 214
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
3197-3299 |
6.43e-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: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3197 RTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKE-----VTMKAQAAEKVKAEVQKVKDRAQAIVD 3271
Cdd:cd06503 26 KALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEAERILEQAKAEIE 105
|
90 100
....*....|....*....|....*...
gi 19115954 3272 SiSKDKAIAEEKLEAAKPALEEAEAALQ 3299
Cdd:cd06503 106 Q-EKEKALAELRKEVADLAVEAAEKILG 132
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3191-3298 |
9.50e-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: 44.15 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3191 EKHVEVRTLANRmntgLEKLKEASESVA------ALSKELEAKEKELQVANDKadmvLKEVTMKAQAAEKVKAEVQKVKD 3264
Cdd:COG1579 63 RLELEIEEVEAR----IKKYEEQLGNVRnnkeyeALQKEIESLKRRISDLEDE----ILELMERIEELEEELAELEAELA 134
|
90 100 110
....*....|....*....|....*....|....
gi 19115954 3265 RAQAIVDSISKDKAIAEEKLEAAKPALEEAEAAL 3298
Cdd:COG1579 135 ELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3195-3300 |
1.28e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3195 EVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSIS 3274
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100
....*....|....*....|....*.
gi 19115954 3275 KDKAiAEEKLEAAKPALEEAEAALQT 3300
Cdd:COG4372 119 ELQK-ERQDLEQQRKQLEAQIAELQS 143
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2586-2724 |
1.32e-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: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 2586 VLLIGEQGTAKTVIIKGFMSKYDP-ECHMIkslNFSSATTP--LMFQRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMP 2662
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNrPVFYV---QLTRDTTEedLFGRRNIDPGGASWVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115954 2663 ---IINEWgDQVTNEIVRQLMEqNGFYNLEKPGEFtsivdiQFLAAMIHPGGGRNDIPQRLKRQF 2724
Cdd:pfam07728 79 npdVLNSL-LSLLDERRLLLPD-GGELVKAAPDGF------RLIATMNPLDRGLNELSPALRSRF 135
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
3208-3297 |
1.38e-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: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3208 EKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAA 3287
Cdd:pfam05701 370 AKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAI 449
|
90
....*....|
gi 19115954 3288 KpALEEAEAA 3297
Cdd:pfam05701 450 K-ALQESESS 458
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
3194-3301 |
2.89e-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: 42.78 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3194 VEVRTLANRMNTGLEKLKEASESVA-ALSKELEAKEKELQVANDkadmVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDS 3272
Cdd:pfam06008 151 KAAQDLLSRIQTWFQSPQEENKALAnALRDSLAEYEAKLSDLRE----LLREAAAKTRDANRLNLANQANLREFQRKKEE 226
|
90 100
....*....|....*....|....*....
gi 19115954 3273 ISKDKAIAEEKLEAAKPALEEAEAALQTI 3301
Cdd:pfam06008 227 VSEQKNQLEETLKTARDSLDAANLLLQEI 255
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
3185-3299 |
3.52e-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: 40.93 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3185 YKFIYgeKHVeVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVT-----MKAQAAEKVKAEV 3259
Cdd:COG0711 18 KKFAW--PPI-LKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARkeaeaIAEEAKAEAEAEA 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 19115954 3260 QKVKDRAQAIVDSIsKDKAIAEEKLEAAKPALEEAEAALQ 3299
Cdd:COG0711 95 ERIIAQAEAEIEQE-RAKALAELRAEVADLAVAIAEKILG 133
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3191-3300 |
3.99e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3191 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKadmvLKEVTMKAQAAEKVKAEVQKVKDRAQAIV 3270
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK----LEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110
....*....|....*....|....*....|
gi 19115954 3271 DSISKDKAIAEEKLEAAKPALEEAEAALQT 3300
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEE 327
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3212-3302 |
4.32e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3212 EASESVAALSKELEAKEKELQVANDKADMVLKEvtmkaqaAEKVKAEVQKVKDRAQAIVDS-ISKDKAIAEEKLEAAKpa 3290
Cdd:PRK00409 513 EDKEKLNELIASLEELERELEQKAEEAEALLKE-------AEKLKEELEEKKEKLQEEEDKlLEEAEKEAQQAIKEAK-- 583
|
90
....*....|..
gi 19115954 3291 lEEAEAALQTIR 3302
Cdd:PRK00409 584 -KEADEIIKELR 594
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3191-3302 |
5.59e-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: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3191 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDR--AQA 3268
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEA 93
|
90 100 110
....*....|....*....|....*....|....*..
gi 19115954 3269 I---VDSISKDKAIAEEKLEAAKPALEEAEAALQTIR 3302
Cdd:COG1579 94 LqkeIESLKRRISDLEDEILELMERIEELEEELAELE 130
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3195-3298 |
6.18e-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: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3195 EVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKdraqaivdsis 3274
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE----------- 764
|
90 100
....*....|....*....|....
gi 19115954 3275 KDKAIAEEKLEAAKPALEEAEAAL 3298
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARL 788
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3195-3297 |
6.51e-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: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3195 EVRTLANRMNTgLEKLKEASES---VAALSKELEAKEKELQvANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVD 3271
Cdd:COG4913 639 ELDALQERREA-LQRLAEYSWDeidVASAEREIAELEAELE-RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIG 716
|
90 100
....*....|....*....|....*.
gi 19115954 3272 SISKDKAIAEEKLEAAKPALEEAEAA 3297
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEDL 742
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3207-3311 |
8.89e-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: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115954 3207 LEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISK-DKAIAEEKLE 3285
Cdd:COG4913 677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFA 756
|
90 100
....*....|....*....|....*.
gi 19115954 3286 AAkpALEEAEAALQTIRPSDIATVRT 3311
Cdd:COG4913 757 AA--LGDAVERELRENLEERIDALRA 780
|
|
| |
