|
Name |
Accession |
Description |
Interval |
E-value |
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
170-722 |
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: 654.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 170 LGKIEDCMKVWIKQTEQVLAENNQLLKEaddvGPRAELEHWKKRLSKFNYLLEQLKSPDVKAVLAVLAAAKSKLLKTWRE 249
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNP----GPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 250 MDIRITDATNEAKDNVKYLYTLEKCCDPLYS-SDPLSMMDAIPTLINAIKMIYSISHYYNTSEKITSLFVKVTNQIISAC 328
Cdd:pfam08385 77 LDTELTDALNEAKDNVKYLKTLERPFEDLEElTDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 329 KAYITNNGtasIWNQPQDVVEEKILSAIKLKQEYQLCFHKTKQKLKQNPNAKQFDFSEMYIFGKFETFHRRLAKIIDIFT 408
Cdd:pfam08385 157 KKYLSPEG---IFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWDFSERYIFGRFDAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 409 TLKTYSVLQDS------TIEG-LEDMATKYQGIVATIKKKEYNFLDQRKMDFDQDYEEFCKQTNDLHNELRKFMDVTFAK 481
Cdd:pfam08385 234 TIEQFSKLEKIggtkgpELEGvIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 482 IQNTNQALRMLKKFE-RLNIPNL--GIDDKYQLILENYGADIDMISKLYTKQKYDP-PLARNQPPIAGKILWARQLFHRI 557
Cdd:pfam08385 314 ARSTESAFKLLRIFEfLLERPIIrgALEEKYTDLLQMFKKELDAVKKIFDKQKYNPsPIAKNMPPVAGAIIWARQLFRRI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 558 QQPMQLFQQHPAVLSTAEAKPIIRSYNRMAKVLLEFEVLFHRAWLRQIEEIHVG-LEASLLVKAPGTGELF-VNFDPQIL 635
Cdd:pfam08385 394 QEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGnLKRPLLVRHPETGKLLsVNFDPQLL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 636 ILFRETECMAQMGLEVSPLATSLFQKRDRYKRNFSNMKMMLAEYQRVKSKIPAAIEQLIVPHLAKVDEALQPGLAALTWT 715
Cdd:pfam08385 474 ALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTWN 553
|
....*..
gi 2462601185 716 SLNIEAY 722
Cdd:pfam08385 554 SLGIDEY 560
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1862-2189 |
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 2462601185 1862 YQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKG 1941
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1942 LAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINF 2021
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2022 RSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYKLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRANPMDTESTIV 2101
Cdd:pfam12774 160 RPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2102 MRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELEAAISRQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTL 2181
Cdd:pfam12774 240 LRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLV 319
|
....*...
gi 2462601185 2182 GPSGAGKT 2189
Cdd:pfam12774 320 GPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1322-1727 |
6.00e-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: 6.00e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1322 LLEIKKQLNLLQKIYTLYNSVIETVNSYYDILWSEVNIEKINNELLEFQNRCRKLPRALKDWQAFLDLKKIIDDFSECCP 1401
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1402 LLEYMASKAMMERHWERITTLTGHSLDVGNESFKLRNIMEAPLLKYKEEIEDICISAVKERDIEQKLKQVINEWDNKTFT 1481
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1482 FGSFKTRGELLLRGdsTSEIIANMEDSLMLLGSLLSNRYNMPFKAQIQKWVQYLSNSTDIIESWMTVQNLWIYLEAVFVG 1561
Cdd:pfam08393 161 LVPYKDTGTFILKG--WDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1562 GDIAKQLPKEAKRFSNIDKSWVKIMTRAHEVPSVVQCCvGDETLGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVS 1641
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEAC-NIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1642 DPALLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiYDRILSISSQEGETIELDKP-VMAEGNVEVWLNSLLEESQSSL 1720
Cdd:pfam08393 318 NDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE--NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 2462601185 1721 HLVIRQA 1727
Cdd:pfam08393 396 RDLLKEA 402
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4249-4541 |
8.82e-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: 8.82e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 4249 AKDVLDTILGIQPKDTSG--GGDETREAVVARLADDMLEKLPPDYvPFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSL 4326
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGggGGGSSREEIVLELAKDILEKLPEPF-DIEEAEEKYPVGYEDPLNTVLLQEIERFNKLLKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 4327 VRSTLTELKLAIDGTIIMSENLRDALDCMFDARIPAWWKKASWISS-TLGFWFTELIERNSQFTSWVF-NGRPHCFWMTG 4404
Cdd:pfam18199 83 IRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLkPLGSWIRDLLERLKQLQDWLDdEGPPKVFWLSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 4405 FFNPQGFLTAMRQEITRANKgWALDNMVLCNEVTKWM-KDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFEL 4483
Cdd:pfam18199 163 FFFPQAFLTAVLQNYARKNG-WPIDKLSFDFEVTKKVsPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFSP 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 4484 MPVIRIYAENNTL--RDPRFYSCPIYKKPVRTDLNYIAAVDLRTAQTPEHWVLRGVALLC 4541
Cdd:pfam18199 242 LPVIHLKPVESDKkkLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1563-4205 |
4.66e-124 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 443.27 E-value: 4.66e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1563 DIAKQLPKEAKRFSNIDKSWVKIMTRahevpsVVQCCVGDETL----GQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFF 1638
Cdd:COG5245 639 DLMPLIPHAVHRKMSLVSGVRGIYKR------VVSGCEAINTIledvGDDLDLFYKEMDQVFMSIEKVLGLRWREVERAS 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1639 FVSDpaLLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiyDRILSISSQEGETIELDKPVMAEGNVEV--WLN----SL 1712
Cdd:COG5245 713 EVEE--LMDRVRELENRVYSYRFFVKKIAKEEMKTVFS---SRIQKKEPFSLDSEAYVGFFRLYEKSIVirGINrsmgRV 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1713 LEESQSSLhlvirQAAANIQETGFqlteFLSSFPAQVGLLGIQMiWTRDSEEALRNA------KFDKKIMQKTNQAFLEL 1786
Cdd:COG5245 788 LSQYLESV-----QEALEIEDGSF----FVSRHRVRDGGLEKGR-GCDAWENCFDPPlseyfrILEKIFPSEEGYFFDEV 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1787 LNtlidvttrdlsstervKYETLITIHVHQRDIFDDLCHMHIKSPMDFEWLKQCRFYFNEDsDKMMIHITDVAFIYQNEF 1866
Cdd:COG5245 858 LK----------------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLY-KRFIKVRSSYRSAEMFAK 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1867 LGCTDRLVITPLTDRCYITLAQALGMSMggapAGPAGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSG 1946
Cdd:COG5245 921 NTIPFFVFEHSMDTSQHQKLFEAVCDEV----CRFVDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEE 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1947 SWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEHKKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSV 2024
Cdd:COG5245 989 ERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMF 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2025 AMMVPDRQIIIRVKlascgfidnvVLARKFFTLYKLCEEQLSKQVHYDFglrnilsvlRTL-GAAKRANPMDTESTivmr 2103
Cdd:COG5245 1060 LSNIPFGAIKSRRE----------SLDREIGAFNNEVDGIAREEDELMF---------YPMfKSLKAKHRMLEEKT---- 1116
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2104 vlrdMNLSKLIdedEPLFLSLIEDLFPNI--LLDKAGYPELEAAISRQVEEAGLINHPPWKlKVIQLFETQRVRHGMMTL 2181
Cdd:COG5245 1117 ----EYLNKIL---SITGLPLISDTLRERidTLDAEWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGAFHAEY 1188
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2182 GPSGAGKTTCIHTLMRAMTDCGKPHREMRMnpkaitapqmfgrLDvATNDWTdGIFSTLWRKTLRAK-KGEHIWIILDGp 2260
Cdd:COG5245 1189 FRVFLCKIKHYTDACDYLWHVKSPYVKKKY-------------FD-ADMELR-QFFLMFNREDMEARlADSKMEYEVER- 1252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2261 vdaiWIENLNSVLDDNKTLTLANGDRipmapncKIIFEphNIDnASPATVSRNGMVFMSSSILDWSPILEGFL------- 2333
Cdd:COG5245 1253 ----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgdtkryl 1318
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2334 -KKRSPQEAEILRQLYTESF-----PDLYRFCIQ-----------NLEYKMEVLEAfVITQSINMLQGLiplKEQGGEVs 2396
Cdd:COG5245 1319 dECLDFFSCFEEVQKEIDELsmvfcADALRFSADlyhivkerrfsGVLAGSDASES-LGGKSIELAAIL---EHKDLIV- 1393
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2397 qaHLGRLFVFALLWSAGAALELDGRRRLELWLR---SRPTGTLELPPPAGPGDTAFDYYVAPDGTWTHWNTRTQEYLYPS 2473
Cdd:COG5245 1394 --EMKRGINDVLKLRIFGDKCRESTPRFYLISDgdlIKDLNERSDYEEMLIMMFNISAVITNNGSIAGFELRGERVMLRK 1471
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2474 DttpeygsILVPNVDNVRTDFLIQTIAKQGKAVLLIGEQGTAKTVIIKG-FMSKYDPEchmIKSLNFS-SATTPLM---F 2548
Cdd:COG5245 1472 E-------VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPsLRSELITE---VKYFNFStCTMTPSKlsvL 1541
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2549 QRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPIINEWGDQVTNEIVRQLMEQNGFYN-LEKpgEFTSIVDIqFLAAMI 2627
Cdd:COG5245 1542 ERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGAC 1618
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2628 HPGG--GRNDIPQRLKRQFSIFNCTLPSEASVDKIFGVIGVGHYCTQRGFSEEVRDSVTKLVPLTRRLWQMTKikmlpTP 2705
Cdd:COG5245 1619 NPGTdeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTK-----FF 1693
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2706 AKFHYVFNLRDLSRVWQGMLNTTSEVIKEPN-DLLKLWKHECKRVIADRFTVSSDVTWFDKALVSLVEEEFGE------- 2777
Cdd:COG5245 1694 LQMNYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREmiaghig 1773
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2778 EKKLFVDcgiDTYFVDFlrdapeaagetsEEADAETPKIYepiesfshLKERLNMFlqlYNESIRgagMDMVFFADAMVH 2857
Cdd:COG5245 1774 EAEITFS---MILFFGM------------ACLLKKDLAVF--------VEEVRKIF---GSSHLD---VEAVAYKDALLH 1824
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2858 LVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNE 2937
Cdd:COG5245 1825 ILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESI 1904
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2938 IKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfPRCLPTNENLHDYFMSRVRQNLHIVL-CFSPVGEKFR 3016
Cdd:COG5245 1905 PVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVL 1983
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3017 NRALkFPALISGCTIDWFSRWPKDALVAVSEHFLT-SYDIDCSLEIKKEVVQCMGS-FQDGVAEKCVDYFQR-FRRSTHV 3093
Cdd:COG5245 1984 AGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVETlSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIE 2062
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3094 --TPKSYLSFIQG---YKFIYGEKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMK 3168
Cdd:COG5245 2063 gsLGESKIKFIGGlkvYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGE 2142
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3169 AQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMD--CV 3246
Cdd:COG5245 2143 RLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCD 2222
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3247 LLLFQRKVsavkidleksctmpsWQESLKLMTAGNFLQNLQQFPKDT-INEEVIEFL-SPYFEMPDYNIETAKR---VCG 3321
Cdd:COG5245 2223 LLGFEAKI---------------WFGEQQSLRRDDFIRIIGKYPDEIeFDLEARRFReARECSDPSFTGSILNRaskACG 2287
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3322 NvagLCSWTKAMASFFSINKEVLPLKANLVVQENRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAER 3401
Cdd:COG5245 2288 P---LKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDT 2364
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3402 CRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKRLVGDVLLATAFLSYSGPFNQEFRDLLLNDwRKEMKARKIPFGKNL 3481
Cdd:COG5245 2365 VHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIR 2443
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3482 NLSEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSL 3561
Cdd:COG5245 2444 RRQFITEGVQKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQAR 2523
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3562 SLGRPLLIEDvGEELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMK 3641
Cdd:COG5245 2524 REGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVL 2602
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3642 GLEDQLLGRVILTEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEVTQKLEI 3721
Cdd:COG5245 2603 GCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESE 2682
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3722 SAETEVQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLFDlsLARSVKSpitskRIANIIEHMTYEVYK 3801
Cdd:COG5245 2683 SMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFE--KWRRMKS-----KYLCAIRYMLMSSEW 2755
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3802 YaargLYEEhkflFTLLLTLKIDIQRN-RVKHEEFLTLIKGGASLDLKACppkpskwilDITWLNLVELSKLRQFSDVLD 3880
Cdd:COG5245 2756 I----LDHE----DRSGFIHRLDVSFLlRTKRFVSTLLEDKNYRQVLSSC---------SLYGNDVISHSCDRFDRDVYR 2818
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3881 QISRNEKMWKIWFDKenpeeeplpnAYDKSLDCFRRLLLIRSWcpdrtiaqARKYIVDSMGEKYaegvilDLEK-TWEES 3959
Cdd:COG5245 2819 ALKHQMDNRTHSTIL----------TSNSKTNPYKEYTYNDSW--------AEAFEVEDSGDLY------KFEEgLLELI 2874
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3960 DPRTPLICLLsMGSDPTDSIIalgKRLKIETRyvsmgqgqEVHARKLLQQTMANGGWALLQNCHLGLDFMDELMDIIIE- 4038
Cdd:COG5245 2875 VGHAPLIYAH-KKSLENERNV---DRLGSKEN--------EVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYVEDVVYp 2942
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 4039 ---TELVHDAFRLWMTTEAHKQFPITLLQMSIKFANDPPQGLRAGLKrtysgvsqDLLdvssGSQWKPMLYA-------- 4107
Cdd:COG5245 2943 ikaSRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYA--------DLV----EIDRYPFDYTlviacdda 3010
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 4108 --VAFLHSTVQERRKFGALGWNIPYEFNQADFNATVQFIQNHLdDMDVKKGVSWTTIRYMIGEIQYGGR--------VTD 4177
Cdd:COG5245 3011 fyLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNIL-FLNHLNARKWGNNRDLIFTIVYGKKhslmedskVVD 3089
|
2730 2740
....*....|....*....|....*...
gi 2462601185 4178 DYDKRLLNTFAKVWFSENMFGPDFSFYQ 4205
Cdd:COG5245 3090 KYCRGYGAHETSSQILASVPGGDPELVK 3117
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3494-3715 |
5.61e-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: 5.61e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3494 SEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVG 3573
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3574 EELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMKGLEDQLLGRVIL 3653
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462601185 3654 TEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEV 3715
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
3099-3220 |
1.55e-06 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 51.49 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3099 LSFIQGYKFIYGEKHVEvRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQA-----AE 3173
Cdd:PRK07352 29 LAIVIGLLYYFGRGFLG-KILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAiraeiEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462601185 3174 KVKAEVQKVKDRAQAIVDSiSKDKAIAEEKLEAAKPALEEAEAALQT 3220
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 ... |
3128-3217 |
3.17e-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: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3128 EKLKEASESVAALSKELEAKEKELQVANDKADmvlKEVTMKAQAAEKVKAEVQKVKDRAQAivdsisKDKAIAEEKLeAA 3207
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEA------KAKAEAEAKA-KA 191
|
90
....*....|
gi 2462601185 3208 KPALEEAEAA 3217
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 ... |
3117-3219 |
5.57e-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: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3117 RTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKE-----VTMKAQAAEKVKAEVQKVKDRAQAIVD 3191
Cdd:cd06503 26 KALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEAERILEQAKAEIE 105
|
90 100
....*....|....*....|....*...
gi 2462601185 3192 SiSKDKAIAEEKLEAAKPALEEAEAALQ 3219
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 ... |
170-722 |
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: 654.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 170 LGKIEDCMKVWIKQTEQVLAENNQLLKEaddvGPRAELEHWKKRLSKFNYLLEQLKSPDVKAVLAVLAAAKSKLLKTWRE 249
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNP----GPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 250 MDIRITDATNEAKDNVKYLYTLEKCCDPLYS-SDPLSMMDAIPTLINAIKMIYSISHYYNTSEKITSLFVKVTNQIISAC 328
Cdd:pfam08385 77 LDTELTDALNEAKDNVKYLKTLERPFEDLEElTDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 329 KAYITNNGtasIWNQPQDVVEEKILSAIKLKQEYQLCFHKTKQKLKQNPNAKQFDFSEMYIFGKFETFHRRLAKIIDIFT 408
Cdd:pfam08385 157 KKYLSPEG---IFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWDFSERYIFGRFDAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 409 TLKTYSVLQDS------TIEG-LEDMATKYQGIVATIKKKEYNFLDQRKMDFDQDYEEFCKQTNDLHNELRKFMDVTFAK 481
Cdd:pfam08385 234 TIEQFSKLEKIggtkgpELEGvIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 482 IQNTNQALRMLKKFE-RLNIPNL--GIDDKYQLILENYGADIDMISKLYTKQKYDP-PLARNQPPIAGKILWARQLFHRI 557
Cdd:pfam08385 314 ARSTESAFKLLRIFEfLLERPIIrgALEEKYTDLLQMFKKELDAVKKIFDKQKYNPsPIAKNMPPVAGAIIWARQLFRRI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 558 QQPMQLFQQHPAVLSTAEAKPIIRSYNRMAKVLLEFEVLFHRAWLRQIEEIHVG-LEASLLVKAPGTGELF-VNFDPQIL 635
Cdd:pfam08385 394 QEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGnLKRPLLVRHPETGKLLsVNFDPQLL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 636 ILFRETECMAQMGLEVSPLATSLFQKRDRYKRNFSNMKMMLAEYQRVKSKIPAAIEQLIVPHLAKVDEALQPGLAALTWT 715
Cdd:pfam08385 474 ALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTWN 553
|
....*..
gi 2462601185 716 SLNIEAY 722
Cdd:pfam08385 554 SLGIDEY 560
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1862-2189 |
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 2462601185 1862 YQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKG 1941
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1942 LAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINF 2021
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2022 RSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYKLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRANPMDTESTIV 2101
Cdd:pfam12774 160 RPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2102 MRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELEAAISRQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTL 2181
Cdd:pfam12774 240 LRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLV 319
|
....*...
gi 2462601185 2182 GPSGAGKT 2189
Cdd:pfam12774 320 GPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1322-1727 |
6.00e-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: 6.00e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1322 LLEIKKQLNLLQKIYTLYNSVIETVNSYYDILWSEVNIEKINNELLEFQNRCRKLPRALKDWQAFLDLKKIIDDFSECCP 1401
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1402 LLEYMASKAMMERHWERITTLTGHSLDVGNESFKLRNIMEAPLLKYKEEIEDICISAVKERDIEQKLKQVINEWDNKTFT 1481
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1482 FGSFKTRGELLLRGdsTSEIIANMEDSLMLLGSLLSNRYNMPFKAQIQKWVQYLSNSTDIIESWMTVQNLWIYLEAVFVG 1561
Cdd:pfam08393 161 LVPYKDTGTFILKG--WDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1562 GDIAKQLPKEAKRFSNIDKSWVKIMTRAHEVPSVVQCCvGDETLGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVS 1641
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEAC-NIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1642 DPALLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiYDRILSISSQEGETIELDKP-VMAEGNVEVWLNSLLEESQSSL 1720
Cdd:pfam08393 318 NDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE--NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 2462601185 1721 HLVIRQA 1727
Cdd:pfam08393 396 RDLLKEA 402
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4249-4541 |
8.82e-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: 8.82e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 4249 AKDVLDTILGIQPKDTSG--GGDETREAVVARLADDMLEKLPPDYvPFEVKERLQKMGPFQPMNIFLRQEIDRMQRVLSL 4326
Cdd:pfam18199 4 TNELLSTLLSLQPRSDSGggGGGSSREEIVLELAKDILEKLPEPF-DIEEAEEKYPVGYEDPLNTVLLQEIERFNKLLKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 4327 VRSTLTELKLAIDGTIIMSENLRDALDCMFDARIPAWWKKASWISS-TLGFWFTELIERNSQFTSWVF-NGRPHCFWMTG 4404
Cdd:pfam18199 83 IRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLkPLGSWIRDLLERLKQLQDWLDdEGPPKVFWLSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 4405 FFNPQGFLTAMRQEITRANKgWALDNMVLCNEVTKWM-KDDISAPPTEGVYVYGLYLEGAGWDKRNMKLIESKPKVLFEL 4483
Cdd:pfam18199 163 FFFPQAFLTAVLQNYARKNG-WPIDKLSFDFEVTKKVsPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFSP 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 4484 MPVIRIYAENNTL--RDPRFYSCPIYKKPVRTDLNYIAAVDLRTAQTPEHWVLRGVALLC 4541
Cdd:pfam18199 242 LPVIHLKPVESDKkkLDENTYECPVYKTSERHSTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1563-4205 |
4.66e-124 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 443.27 E-value: 4.66e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1563 DIAKQLPKEAKRFSNIDKSWVKIMTRahevpsVVQCCVGDETL----GQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFF 1638
Cdd:COG5245 639 DLMPLIPHAVHRKMSLVSGVRGIYKR------VVSGCEAINTIledvGDDLDLFYKEMDQVFMSIEKVLGLRWREVERAS 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1639 FVSDpaLLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiyDRILSISSQEGETIELDKPVMAEGNVEV--WLN----SL 1712
Cdd:COG5245 713 EVEE--LMDRVRELENRVYSYRFFVKKIAKEEMKTVFS---SRIQKKEPFSLDSEAYVGFFRLYEKSIVirGINrsmgRV 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1713 LEESQSSLhlvirQAAANIQETGFqlteFLSSFPAQVGLLGIQMiWTRDSEEALRNA------KFDKKIMQKTNQAFLEL 1786
Cdd:COG5245 788 LSQYLESV-----QEALEIEDGSF----FVSRHRVRDGGLEKGR-GCDAWENCFDPPlseyfrILEKIFPSEEGYFFDEV 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1787 LNtlidvttrdlsstervKYETLITIHVHQRDIFDDLCHMHIKSPMDFEWLKQCRFYFNEDsDKMMIHITDVAFIYQNEF 1866
Cdd:COG5245 858 LK----------------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLY-KRFIKVRSSYRSAEMFAK 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1867 LGCTDRLVITPLTDRCYITLAQALGMSMggapAGPAGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSG 1946
Cdd:COG5245 921 NTIPFFVFEHSMDTSQHQKLFEAVCDEV----CRFVDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEE 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 1947 SWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEHKKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSV 2024
Cdd:COG5245 989 ERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMF 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2025 AMMVPDRQIIIRVKlascgfidnvVLARKFFTLYKLCEEQLSKQVHYDFglrnilsvlRTL-GAAKRANPMDTESTivmr 2103
Cdd:COG5245 1060 LSNIPFGAIKSRRE----------SLDREIGAFNNEVDGIAREEDELMF---------YPMfKSLKAKHRMLEEKT---- 1116
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2104 vlrdMNLSKLIdedEPLFLSLIEDLFPNI--LLDKAGYPELEAAISRQVEEAGLINHPPWKlKVIQLFETQRVRHGMMTL 2181
Cdd:COG5245 1117 ----EYLNKIL---SITGLPLISDTLRERidTLDAEWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGAFHAEY 1188
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2182 GPSGAGKTTCIHTLMRAMTDCGKPHREMRMnpkaitapqmfgrLDvATNDWTdGIFSTLWRKTLRAK-KGEHIWIILDGp 2260
Cdd:COG5245 1189 FRVFLCKIKHYTDACDYLWHVKSPYVKKKY-------------FD-ADMELR-QFFLMFNREDMEARlADSKMEYEVER- 1252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2261 vdaiWIENLNSVLDDNKTLTLANGDRipmapncKIIFEphNIDnASPATVSRNGMVFMSSSILDWSPILEGFL------- 2333
Cdd:COG5245 1253 ----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgdtkryl 1318
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2334 -KKRSPQEAEILRQLYTESF-----PDLYRFCIQ-----------NLEYKMEVLEAfVITQSINMLQGLiplKEQGGEVs 2396
Cdd:COG5245 1319 dECLDFFSCFEEVQKEIDELsmvfcADALRFSADlyhivkerrfsGVLAGSDASES-LGGKSIELAAIL---EHKDLIV- 1393
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2397 qaHLGRLFVFALLWSAGAALELDGRRRLELWLR---SRPTGTLELPPPAGPGDTAFDYYVAPDGTWTHWNTRTQEYLYPS 2473
Cdd:COG5245 1394 --EMKRGINDVLKLRIFGDKCRESTPRFYLISDgdlIKDLNERSDYEEMLIMMFNISAVITNNGSIAGFELRGERVMLRK 1471
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2474 DttpeygsILVPNVDNVRTDFLIQTIAKQGKAVLLIGEQGTAKTVIIKG-FMSKYDPEchmIKSLNFS-SATTPLM---F 2548
Cdd:COG5245 1472 E-------VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPsLRSELITE---VKYFNFStCTMTPSKlsvL 1541
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2549 QRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPIINEWGDQVTNEIVRQLMEQNGFYN-LEKpgEFTSIVDIqFLAAMI 2627
Cdd:COG5245 1542 ERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGAC 1618
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2628 HPGG--GRNDIPQRLKRQFSIFNCTLPSEASVDKIFGVIGVGHYCTQRGFSEEVRDSVTKLVPLTRRLWQMTKikmlpTP 2705
Cdd:COG5245 1619 NPGTdeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTK-----FF 1693
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2706 AKFHYVFNLRDLSRVWQGMLNTTSEVIKEPN-DLLKLWKHECKRVIADRFTVSSDVTWFDKALVSLVEEEFGE------- 2777
Cdd:COG5245 1694 LQMNYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREmiaghig 1773
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2778 EKKLFVDcgiDTYFVDFlrdapeaagetsEEADAETPKIYepiesfshLKERLNMFlqlYNESIRgagMDMVFFADAMVH 2857
Cdd:COG5245 1774 EAEITFS---MILFFGM------------ACLLKKDLAVF--------VEEVRKIF---GSSHLD---VEAVAYKDALLH 1824
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2858 LVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNE 2937
Cdd:COG5245 1825 ILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESI 1904
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2938 IKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfPRCLPTNENLHDYFMSRVRQNLHIVL-CFSPVGEKFR 3016
Cdd:COG5245 1905 PVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVL 1983
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3017 NRALkFPALISGCTIDWFSRWPKDALVAVSEHFLT-SYDIDCSLEIKKEVVQCMGS-FQDGVAEKCVDYFQR-FRRSTHV 3093
Cdd:COG5245 1984 AGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVETlSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIE 2062
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3094 --TPKSYLSFIQG---YKFIYGEKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMK 3168
Cdd:COG5245 2063 gsLGESKIKFIGGlkvYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGE 2142
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3169 AQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMD--CV 3246
Cdd:COG5245 2143 RLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCD 2222
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3247 LLLFQRKVsavkidleksctmpsWQESLKLMTAGNFLQNLQQFPKDT-INEEVIEFL-SPYFEMPDYNIETAKR---VCG 3321
Cdd:COG5245 2223 LLGFEAKI---------------WFGEQQSLRRDDFIRIIGKYPDEIeFDLEARRFReARECSDPSFTGSILNRaskACG 2287
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3322 NvagLCSWTKAMASFFSINKEVLPLKANLVVQENRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAER 3401
Cdd:COG5245 2288 P---LKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDT 2364
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3402 CRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKRLVGDVLLATAFLSYSGPFNQEFRDLLLNDwRKEMKARKIPFGKNL 3481
Cdd:COG5245 2365 VHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIR 2443
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3482 NLSEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSL 3561
Cdd:COG5245 2444 RRQFITEGVQKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQAR 2523
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3562 SLGRPLLIEDvGEELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMK 3641
Cdd:COG5245 2524 REGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVL 2602
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3642 GLEDQLLGRVILTEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEVTQKLEI 3721
Cdd:COG5245 2603 GCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESE 2682
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3722 SAETEVQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLFDlsLARSVKSpitskRIANIIEHMTYEVYK 3801
Cdd:COG5245 2683 SMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFE--KWRRMKS-----KYLCAIRYMLMSSEW 2755
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3802 YaargLYEEhkflFTLLLTLKIDIQRN-RVKHEEFLTLIKGGASLDLKACppkpskwilDITWLNLVELSKLRQFSDVLD 3880
Cdd:COG5245 2756 I----LDHE----DRSGFIHRLDVSFLlRTKRFVSTLLEDKNYRQVLSSC---------SLYGNDVISHSCDRFDRDVYR 2818
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3881 QISRNEKMWKIWFDKenpeeeplpnAYDKSLDCFRRLLLIRSWcpdrtiaqARKYIVDSMGEKYaegvilDLEK-TWEES 3959
Cdd:COG5245 2819 ALKHQMDNRTHSTIL----------TSNSKTNPYKEYTYNDSW--------AEAFEVEDSGDLY------KFEEgLLELI 2874
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3960 DPRTPLICLLsMGSDPTDSIIalgKRLKIETRyvsmgqgqEVHARKLLQQTMANGGWALLQNCHLGLDFMDELMDIIIE- 4038
Cdd:COG5245 2875 VGHAPLIYAH-KKSLENERNV---DRLGSKEN--------EVYAVLNSLFSRKEKSWFEVYNISLSFGWFKRYVEDVVYp 2942
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 4039 ---TELVHDAFRLWMTTEAHKQFPITLLQMSIKFANDPPQGLRAGLKrtysgvsqDLLdvssGSQWKPMLYA-------- 4107
Cdd:COG5245 2943 ikaSRVCGKVKNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYA--------DLV----EIDRYPFDYTlviacdda 3010
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 4108 --VAFLHSTVQERRKFGALGWNIPYEFNQADFNATVQFIQNHLdDMDVKKGVSWTTIRYMIGEIQYGGR--------VTD 4177
Cdd:COG5245 3011 fyLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNIL-FLNHLNARKWGNNRDLIFTIVYGKKhslmedskVVD 3089
|
2730 2740
....*....|....*....|....*...
gi 2462601185 4178 DYDKRLLNTFAKVWFSENMFGPDFSFYQ 4205
Cdd:COG5245 3090 KYCRGYGAHETSSQILASVPGGDPELVK 3117
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3494-3715 |
5.61e-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: 5.61e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3494 SEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVG 3573
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3574 EELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMKGLEDQLLGRVIL 3653
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462601185 3654 TEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEV 3715
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 ... |
2846-3106 |
4.68e-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: 320.71 E-value: 4.68e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2846 MDMVFFADAMVHLVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQ 2925
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2926 GKGITFIFTDNEIKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfpRCLPTNENLHDYFMSRVRQNLHIV 3005
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQ--NIEDSREAVYNYFVKRCRNNLHIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3006 LCFSPVGEKFRNRALKFPALISGCTIDWFSRWPKDALVAVSEHFLTsyDIDCSLEIKKEVVQCMGSFQDGVAEKCVDYFQ 3085
Cdd:pfam12780 159 LCMSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLE--DIEIPEELKSNVVKVFVYVHSSVEDMSKKFYE 236
|
250 260
....*....|....*....|.
gi 2462601185 3086 RFRRSTHVTPKSYLSFIQGYK 3106
Cdd:pfam12780 237 ELKRKNYVTPKSYLELLRLYK 257
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2471-2652 |
9.28e-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: 9.28e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2471 YPSDTtpEYGSILVPNVDNVRTDFLIQTIAKQGKAVLLIGEQGTAKTVIIKGFMSKYDPECHMIKSLNFSSATTPLMFQR 2550
Cdd:pfam12775 1 IPPDV--PFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2551 TIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPIINEWGDQVTNEIVRQLMEQNGFYNLEKPgEFTSIVDIQFLAAMIHPG 2630
Cdd:pfam12775 79 IIESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKL-TFKEIVDVQFVAAMGPPG 157
|
170 180
....*....|....*....|..
gi 2462601185 2631 GGRNDIPQRLKRQFSIFNCTLP 2652
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 ... |
4101-4240 |
6.49e-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: 6.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 4101 WKPMLYAVAFLHSTVQERRKFGALGWNIPYEFNQADFNATVQFIQNHLDdmDVKKGVSWTTIRYMIGEIQYGGRVTDDYD 4180
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLD--EYDEKIPWDALRYLIGEINYGGRVTDDWD 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462601185 4181 KRLLNTFAKVWFSENMFGPDFSFYQG-YNIPKCSTVDNYLQYIQSLPAYDSPEVFGLHPNA 4240
Cdd:pfam18198 79 RRLLNTYLEEFFNPEVLEEDFKFSPSlYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
3960-4069 |
1.34e-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: 1.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3960 DPRTPLICLLSMGSDPTDSIIALGKRLKIETRY--VSMGQGQEVHARKLLQQTMANGGWALLQNCHLGLDFMDELMDII- 4036
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGFGGKLhsISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILe 80
|
90 100 110
....*....|....*....|....*....|....
gi 2462601185 4037 -IETELVHDAFRLWMTTEAHKQFPITLLQMSIKF 4069
Cdd:pfam03028 81 eLPEETLHPDFRLWLTSEPSPKFPISILQNSIKI 114
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
3122-3467 |
1.98e-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: 1.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3122 RMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAE 3201
Cdd:pfam12777 2 RLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3202 EKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMDCVLLLFqrkVSAVKIDLEKsctmpSWQESlKLMTA-- 3279
Cdd:pfam12777 82 EDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILM---APGGKIPKDK-----SWKAA-KIMMAkv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3280 GNFLQNLQQFPKDTINEEVIEFLSPYFEMPDYNIETAKRVCGNVAGLCSWTKAMASFFSINKEVLPlKANLVVQENRHLL 3359
Cdd:pfam12777 153 DGFLDSLIKFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAP-KRQALEEANADLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3360 AMQD-LQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAERCRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKRLV 3438
Cdd:pfam12777 232 AAQEkLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLC 311
|
330 340 350
....*....|....*....|....*....|
gi 2462601185 3439 GDVLLATAFLSYSGPFNQEFRDLLLND-WR 3467
Cdd:pfam12777 312 GDILLISAFISYLGFFTKKYRNELLDKfWI 341
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2344-2463 |
4.39e-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: 4.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2344 LRQLYTESFPDLYRFCIQNLEYKMEVLEAFVITQSINMLQGLIP-------LKEQGGEVSQAHLGRLFVFALLWSAGAAL 2416
Cdd:pfam17852 1 LEPLFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDevleyngVHPLSPDKLKEYLEKLFLFALVWSIGGTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2462601185 2417 ELDGRRRLELWLRSRPTGtLELPPPagPGDTAFDYYV-APDGTWTHWN 2463
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. |
2686-2775 |
2.55e-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: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2686 LVPLTRRLWQMTKIKMLPTPAKFHYVFNLRDLSRVWQGMLNTTSEVIKEPNDLLKLWKHECKRVIADRFTVSSDVTWFDK 2765
Cdd:pfam17857 1 LIAAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDK 80
|
90
....*....|
gi 2462601185 2766 ALVSLVEEEF 2775
Cdd:pfam17857 81 IQMASLKKFF 90
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2177-2312 |
1.99e-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: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2177 GMMTLGPSGAGKTTCIHTLMRAMTDCGKphrEMRMNPKAITAPQMFGRLDVATND--WTDGIFstlwrkTLRAKKGehiW 2254
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPV---FYVQLTRDTTEEDLFGRRNIDPGGasWVDGPL------VRAAREG---E 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462601185 2255 IILDGPVDAI---WIENLNSVLDDNKTLTLANGDRIPMAPNC-KIIFEPHNID----NASPATVSR 2312
Cdd:pfam07728 69 IAVLDEINRAnpdVLNSLLSLLDERRLLLPDGGELVKAAPDGfRLIATMNPLDrglnELSPALRSR 134
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3116-3237 |
1.27e-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: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3116 VRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVandkadmvlkevtmKAQAAEKVKAEVQKVKDRAQAIVDSISK 3195
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEA--------------LKAELEAAKAELEAQQAEQEALLAQLSA 189
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462601185 3196 DKAIAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPH 3237
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
3099-3220 |
1.55e-06 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 51.49 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3099 LSFIQGYKFIYGEKHVEvRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQA-----AE 3173
Cdd:PRK07352 29 LAIVIGLLYYFGRGFLG-KILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAiraeiEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462601185 3174 KVKAEVQKVKDRAQAIVDSiSKDKAIAEEKLEAAKPALEEAEAALQT 3220
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 ... |
3128-3217 |
3.17e-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: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3128 EKLKEASESVAALSKELEAKEKELQVANDKADmvlKEVTMKAQAAEKVKAEVQKVKDRAQAivdsisKDKAIAEEKLeAA 3207
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEA------KAKAEAEAKA-KA 191
|
90
....*....|
gi 2462601185 3208 KPALEEAEAA 3217
Cdd:TIGR02794 192 EEAKAKAEAA 201
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3129-3216 |
1.86e-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: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3129 KLKEAsesvAALSKELEAKEKELQVANDKADMVLK----EVTMKAQAAEKVKAEVQKVKDRAqaivdsiSKDKAIAE--E 3202
Cdd:TIGR02794 143 KAKEE----AAKQAEEEAKAKAAAEAKKKAEEAKKkaeaEAKAKAEAEAKAKAEEAKAKAEA-------AKAKAAAEaaA 211
|
90
....*....|....
gi 2462601185 3203 KLEAAKPALEEAEA 3216
Cdd:TIGR02794 212 KAEAEAAAAAAAEA 225
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3360-3433 |
2.45e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 2.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462601185 3360 AMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAERcrhKMQTASTLISGLAGEKERWTEQSQEFAAQ 3433
Cdd:COG3883 134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3129-3217 |
2.69e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3129 KLKEASES--VAALSK--ELEAKEKELQVANDKADMVLKEvtmKAQAAEKVKAEV---QKVKDRAQAIVDSISKDKAIAE 3201
Cdd:PRK09510 146 KAKAEAEAkrAAAAAKkaAAEAKKKAEAEAAKKAAAEAKK---KAEAEAAAKAAAeakKKAEAEAKKKAAAEAKKKAAAE 222
|
90
....*....|....*.
gi 2462601185 3202 EKLEAAKPALEEAEAA 3217
Cdd:PRK09510 223 AKAAAAKAAAEAKAAA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3111-3444 |
3.56e-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: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3111 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRaqaiV 3190
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----I 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3191 DSISKDKAIAEEKLEAAKPALEEAEAALQTIRpSDIATVRTlgrpphLIMRIMDCVLLL------FQRKVSAVKIDL-EK 3263
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAE-AEIEELEA------QIEQLKEELKALrealdeLRAELTLLNEEAaNL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3264 SCTMPSWQESLKLmtAGNFLQNLQQFPKDtiNEEVIEFLSPYFEMPDYNIETAKRvcgnvaGLCSWTKAMASFFSINKEV 3343
Cdd:TIGR02168 823 RERLESLERRIAA--TERRLEDLEEQIEE--LSEDIESLAAEIEELEELIEELES------ELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3344 LPLKANLVVQENRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQ-AMTEKQTLLEDAERcrhKMQTASTLISGLAGEKER 3422
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVrIDNLQERLSEEYSL---TLEEAEALENKIEDDEEE 969
|
330 340
....*....|....*....|..
gi 2462601185 3423 WTEQSQEFAAQTKRLvGDVLLA 3444
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 ... |
3117-3219 |
5.57e-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: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3117 RTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKE-----VTMKAQAAEKVKAEVQKVKDRAQAIVD 3191
Cdd:cd06503 26 KALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEAERILEQAKAEIE 105
|
90 100
....*....|....*....|....*...
gi 2462601185 3192 SiSKDKAIAEEKLEAAKPALEEAEAALQ 3219
Cdd:cd06503 106 Q-EKEKALAELRKEVADLAVEAAEKILG 132
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3129-3217 |
6.01e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.57 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3129 KLKEASESVAALSKEL--EAKEKELQVANDKAD---MVLKEVTMKAQAAEKVKAEVQ---KVKDRAQAIVDSISKDKAIA 3200
Cdd:PRK09510 118 KQAEEAAKQAALKQKQaeEAAAKAAAAAKAKAEaeaKRAAAAAKKAAAEAKKKAEAEaakKAAAEAKKKAEAEAAAKAAA 197
|
90
....*....|....*..
gi 2462601185 3201 EEKLEAAKPALEEAEAA 3217
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAE 214
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3111-3218 |
7.93e-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: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3111 EKHVEVRTLANRmntgLEKLKEASESVA------ALSKELEAKEKELQVANDKadmvLKEVTMKAQAAEKVKAEVQKVKD 3184
Cdd:COG1579 63 RLELEIEEVEAR----IKKYEEQLGNVRnnkeyeALQKEIESLKRRISDLEDE----ILELMERIEELEEELAELEAELA 134
|
90 100 110
....*....|....*....|....*....|....
gi 2462601185 3185 RAQAIVDSISKDKAIAEEKLEAAKPALEEAEAAL 3218
Cdd:COG1579 135 ELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3115-3220 |
1.09e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3115 EVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSIS 3194
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100
....*....|....*....|....*.
gi 2462601185 3195 KDKAiAEEKLEAAKPALEEAEAALQT 3220
Cdd:COG4372 119 ELQK-ERQDLEQQRKQLEAQIAELQS 143
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
3128-3217 |
1.26e-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: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3128 EKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAA 3207
Cdd:pfam05701 370 AKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAI 449
|
90
....*....|
gi 2462601185 3208 KpALEEAEAA 3217
Cdd:pfam05701 450 K-ALQESESS 458
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2506-2644 |
1.29e-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: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 2506 VLLIGEQGTAKTVIIKGFMSKYDP-ECHMIkslNFSSATTP--LMFQRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMP 2582
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNrPVFYV---QLTRDTTEedLFGRRNIDPGGASWVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462601185 2583 ---IINEWgDQVTNEIVRQLMEqNGFYNLEKPGEFtsivdiQFLAAMIHPGGGRNDIPQRLKRQF 2644
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 ... |
3114-3221 |
2.62e-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: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3114 VEVRTLANRMNTGLEKLKEASESVA-ALSKELEAKEKELQVANDkadmVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDS 3192
Cdd:pfam06008 151 KAAQDLLSRIQTWFQSPQEENKALAnALRDSLAEYEAKLSDLRE----LLREAAAKTRDANRLNLANQANLREFQRKKEE 226
|
90 100
....*....|....*....|....*....
gi 2462601185 3193 ISKDKAIAEEKLEAAKPALEEAEAALQTI 3221
Cdd:pfam06008 227 VSEQKNQLEETLKTARDSLDAANLLLQEI 255
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
3105-3219 |
3.00e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.31 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3105 YKFIYgeKHVeVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVT-----MKAQAAEKVKAEV 3179
Cdd:COG0711 18 KKFAW--PPI-LKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARkeaeaIAEEAKAEAEAEA 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462601185 3180 QKVKDRAQAIVDSIsKDKAIAEEKLEAAKPALEEAEAALQ 3219
Cdd:COG0711 95 ERIIAQAEAEIEQE-RAKALAELRAEVADLAVAIAEKILG 133
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3111-3220 |
3.61e-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: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3111 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKadmvLKEVTMKAQAAEKVKAEVQKVKDRAQAIV 3190
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK----LEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110
....*....|....*....|....*....|
gi 2462601185 3191 DSISKDKAIAEEKLEAAKPALEEAEAALQT 3220
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEE 327
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3132-3222 |
4.18e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3132 EASESVAALSKELEAKEKELQVANDKADMVLKEvtmkaqaAEKVKAEVQKVKDRAQAIVDS-ISKDKAIAEEKLEAAKpa 3210
Cdd:PRK00409 513 EDKEKLNELIASLEELERELEQKAEEAEALLKE-------AEKLKEELEEKKEKLQEEEDKlLEEAEKEAQQAIKEAK-- 583
|
90
....*....|..
gi 2462601185 3211 lEEAEAALQTIR 3222
Cdd:PRK00409 584 -KEADEIIKELR 594
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3111-3222 |
5.06e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3111 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDR--AQA 3188
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEA 93
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462601185 3189 I---VDSISKDKAIAEEKLEAAKPALEEAEAALQTIR 3222
Cdd:COG1579 94 LqkeIESLKRRISDLEDEILELMERIEELEEELAELE 130
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3115-3217 |
5.78e-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: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3115 EVRTLANRMNTgLEKLKEASES---VAALSKELEAKEKELQvANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVD 3191
Cdd:COG4913 639 ELDALQERREA-LQRLAEYSWDeidVASAEREIAELEAELE-RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIG 716
|
90 100
....*....|....*....|....*.
gi 2462601185 3192 SISKDKAIAEEKLEAAKPALEEAEAA 3217
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEDL 742
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3115-3218 |
5.92e-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: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3115 EVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKdraqaivdsis 3194
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE----------- 764
|
90 100
....*....|....*....|....
gi 2462601185 3195 KDKAIAEEKLEAAKPALEEAEAAL 3218
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARL 788
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3127-3231 |
8.23e-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: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462601185 3127 LEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISK-DKAIAEEKLE 3205
Cdd:COG4913 677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFA 756
|
90 100
....*....|....*....|....*.
gi 2462601185 3206 AAkpALEEAEAALQTIRPSDIATVRT 3231
Cdd:COG4913 757 AA--LGDAVERELRENLEERIDALRA 780
|
|
| |
