|
Name |
Accession |
Description |
Interval |
E-value |
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
286-838 |
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: 652.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 286 LGKIEDCMKVWIKQTEQVLAENNQLLKEaddvGPRAELEHWKKRLSKFNYLLEQLKSPDVKAVLAVLAAAKSKLLKTWRE 365
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNP----GPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 366 MDIRITDATNEAKDNVKYLYTLEKCCDPLYS-SDPLSMMDAIPTLINAIKMIYSISHYYNTSEKITSLFVKVTNQIISAC 444
Cdd:pfam08385 77 LDTELTDALNEAKDNVKYLKTLERPFEDLEElTDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 445 KAYITNNGtasIWNQPQDVVEEKILSAIKLKQEYQLCFHKTKQKLKQNPNAKQFDFSEMYIFGKFETFHRRLAKIIDIFT 524
Cdd:pfam08385 157 KKYLSPEG---IFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWDFSERYIFGRFDAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 525 TLKTYSVLQDS------TIEG-LEDMATKYQGIVATIKKKEYNFLDQRKMDFDQDYEEFCKQTNDLHNELRKFMDVTFAK 597
Cdd:pfam08385 234 TIEQFSKLEKIggtkgpELEGvIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 598 IQNTNQALRMLKKFE-RLNIPNL--GIDDKYQLILENYGADIDMISKLYTKQKYDP-PLARNQPPIAGKILWARQLFHRI 673
Cdd:pfam08385 314 ARSTESAFKLLRIFEfLLERPIIrgALEEKYTDLLQMFKKELDAVKKIFDKQKYNPsPIAKNMPPVAGAIIWARQLFRRI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 674 QQPMQLFQQHPAVLSTAEAKPIIRSYNRMAKVLLEFEVLFHRAWLRQIEEIHVG-LEASLLVKAPGTGELF-VNFDPQIL 751
Cdd:pfam08385 394 QEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGnLKRPLLVRHPETGKLLsVNFDPQLL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 752 ILFRETECMAQMGLEVSPLATSLFQKRDRYKRNFSNMKMMLAEYQRVKSKIPAAIEQLIVPHLAKVDEALQPGLAALTWT 831
Cdd:pfam08385 474 ALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTWN 553
|
....*..
gi 1034644038 832 SLNIEAY 838
Cdd:pfam08385 554 SLGIDEY 560
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1978-2305 |
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: 596.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1978 YQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKG 2057
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2058 LAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINF 2137
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2138 RSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYKLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRANPMDTESTIV 2217
Cdd:pfam12774 160 RPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2218 MRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELEAAISRQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTL 2297
Cdd:pfam12774 240 LRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLV 319
|
....*...
gi 1034644038 2298 GPSGAGKT 2305
Cdd:pfam12774 320 GPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1438-1843 |
1.19e-147 |
|
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: 465.97 E-value: 1.19e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1438 LLEIKKQLNLLQKIYTLYNSVIETVNSYYDILWSEVNIEKINNELLEFQNRCRKLPRALKDWQAFLDLKKIIDDFSECCP 1517
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1518 LLEYMASKAMMERHWERITTLTGHSLDVGNESFKLRNIMEAPLLKYKEEIEDICISAVKERDIEQKLKQVINEWDNKTFT 1597
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1598 FGSFKTRGELLLRGdsTSEIIANMEDSLMLLGSLLSNRYNMPFKAQIQKWVQYLSNSTDIIESWMTVQNLWIYLEAVFVG 1677
Cdd:pfam08393 161 LVPYKDTGTFILKG--WDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1678 GDIAKQLPKEAKRFSNIDKSWVKIMTRAHEVPSVVQCCvGDETLGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVS 1757
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEAC-NIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1758 DPALLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiYDRILSISSQEGETIELDKP-VMAEGNVEVWLNSLLEESQSSL 1836
Cdd:pfam08393 318 NDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE--NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 1034644038 1837 HLVIRQA 1843
Cdd:pfam08393 396 RDLLKEA 402
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3610-3831 |
1.65e-115 |
|
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: 366.00 E-value: 1.65e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3610 SEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVG 3689
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3690 EELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMKGLEDQLLGRVIL 3769
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034644038 3770 TEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEV 3831
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1679-3887 |
4.20e-113 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 406.68 E-value: 4.20e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1679 DIAKQLPKEAKRFSNIDKSWVKIMTRahevpsVVQCCVGDETL----GQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFF 1754
Cdd:COG5245 639 DLMPLIPHAVHRKMSLVSGVRGIYKR------VVSGCEAINTIledvGDDLDLFYKEMDQVFMSIEKVLGLRWREVERAS 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1755 FVSDpaLLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiyDRILSISSQEGETIELDKPVMAEGNVEV--WLN----SL 1828
Cdd:COG5245 713 EVEE--LMDRVRELENRVYSYRFFVKKIAKEEMKTVFS---SRIQKKEPFSLDSEAYVGFFRLYEKSIVirGINrsmgRV 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1829 LEESQSSLhlvirQAAANIQETGFqlteFLSSFPAQVGLLGIQMiWTRDSEEALRNA------KFDKKIMQKTNQAFLEL 1902
Cdd:COG5245 788 LSQYLESV-----QEALEIEDGSF----FVSRHRVRDGGLEKGR-GCDAWENCFDPPlseyfrILEKIFPSEEGYFFDEV 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1903 LNtlidvttrdlsstervKYETLITIHVHQRDIFDDLCHMHIKSPMDFEWLKQCRFYFNEDsDKMMIHITDVAFIYQNEF 1982
Cdd:COG5245 858 LK----------------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLY-KRFIKVRSSYRSAEMFAK 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1983 LGCTDRLVITPLTDRCYITLAQALGMSMggapAGPAGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSG 2062
Cdd:COG5245 921 NTIPFFVFEHSMDTSQHQKLFEAVCDEV----CRFVDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEE 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2063 SWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEHKKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSV 2140
Cdd:COG5245 989 ERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMF 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2141 AMMVPDRQIIIRVKlascgfidnvVLARKFFTLYKLCEEQLSKQVHYDFglrnilsvlRTL-GAAKRANPMDTESTivmr 2219
Cdd:COG5245 1060 LSNIPFGAIKSRRE----------SLDREIGAFNNEVDGIAREEDELMF---------YPMfKSLKAKHRMLEEKT---- 1116
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2220 vlrdMNLSKLIdedEPLFLSLIEDLFPNI--LLDKAGYPELEAAISRQVEEAGLINHPPWKlKVIQLFETQRVRHGMMTL 2297
Cdd:COG5245 1117 ----EYLNKIL---SITGLPLISDTLRERidTLDAEWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGAFHAEY 1188
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2298 GPSGAGKTTCIHTLMRAMTDCGKPHREMRMnpkaitapqmfgrLDvATNDWTdGIFSTLWRKTLRAK-KGEHIWIILDGp 2376
Cdd:COG5245 1189 FRVFLCKIKHYTDACDYLWHVKSPYVKKKY-------------FD-ADMELR-QFFLMFNREDMEARlADSKMEYEVER- 1252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2377 vdaiWIENLNSVLDDNKTLTLANGDRipmapncKIIFEphNIDnASPATVSRNGMVFMSSSILDWSPILEGFL------- 2449
Cdd:COG5245 1253 ----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgdtkryl 1318
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2450 -KKRSPQEAEILRQLYTESF-----PDLYRFCIQ-----------NLEYKMEVLEAfVITQSINMLQGLiplKEQGGEVs 2512
Cdd:COG5245 1319 dECLDFFSCFEEVQKEIDELsmvfcADALRFSADlyhivkerrfsGVLAGSDASES-LGGKSIELAAIL---EHKDLIV- 1393
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2513 qaHLGRLFVFALLWSAGAALELDGRRRLELWLR---SRPTGTLELPPPAGPGDTAFDYYVAPDGTWTHWNTRTQEYLYPS 2589
Cdd:COG5245 1394 --EMKRGINDVLKLRIFGDKCRESTPRFYLISDgdlIKDLNERSDYEEMLIMMFNISAVITNNGSIAGFELRGERVMLRK 1471
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2590 DttpeygsILVPNVDNVRTDFLIQTIAKQGKAVLLIGEQGTAKTVIIKG-FMSKYDPEchmIKSLNFS-SATTPLM---F 2664
Cdd:COG5245 1472 E-------VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPsLRSELITE---VKYFNFStCTMTPSKlsvL 1541
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2665 QRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPIINEWGDQVTNEIVRQLMEQNGFYN-LEKpgEFTSIVDIqFLAAMI 2743
Cdd:COG5245 1542 ERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGAC 1618
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2744 HPGG--GRNDIPQRLKRQFSIFNCTLPSEASVDKIFGVIGVGHYCTQRGFSEEVRDSVTKLVPLTRRLWQMTKikmlpTP 2821
Cdd:COG5245 1619 NPGTdeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTK-----FF 1693
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2822 AKFHYVFNLRDLSRVWQGMLNTTSEVIKEPN-DLLKLWKHECKRVIADRFTVSSDVTWFDKALVSLVEEEFGE------- 2893
Cdd:COG5245 1694 LQMNYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREmiaghig 1773
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2894 EKKLLVDcgiDTYFVDFlrdapeaagetsEEADAETPKIYepiesfshLKERLNMFlqlYNESIRgagMDMVFFADAMVH 2973
Cdd:COG5245 1774 EAEITFS---MILFFGM------------ACLLKKDLAVF--------VEEVRKIF---GSSHLD---VEAVAYKDALLH 1824
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2974 LVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNE 3053
Cdd:COG5245 1825 ILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESI 1904
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3054 IKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfPRCLPTNENLHDYFMSRVRQNLHIVL-CFSPVGEKFR 3132
Cdd:COG5245 1905 PVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVL 1983
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3133 NRALkFPALISGCTIDWFSRWPKDALVAVSEHFLT-SYDIDCSLEIKKEVVQCMGS-FQDGVAEKCVDYFQR-FRRSTHV 3209
Cdd:COG5245 1984 AGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVETlSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIE 2062
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3210 --TPKSYLSFIQG---YKFIYGEKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMK 3284
Cdd:COG5245 2063 gsLGESKIKFIGGlkvYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGE 2142
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3285 AQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMD--CV 3362
Cdd:COG5245 2143 RLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCD 2222
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3363 LLLFQRKVsavkidleksctmpsWQESLKLMTAGNFLQNLQQFPKDT-INEEVIEFL-SPYFEMPDYNIETAKR---VCG 3437
Cdd:COG5245 2223 LLGFEAKI---------------WFGEQQSLRRDDFIRIIGKYPDEIeFDLEARRFReARECSDPSFTGSILNRaskACG 2287
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3438 NvagLCSWTKAMASFFSINKEVLPLKANLVVQENRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAER 3517
Cdd:COG5245 2288 P---LKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDT 2364
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3518 CRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKRLVGDVLLATAFLSYSGPFNQEFRDLLLNDwRKEMKARKIPFGKNL 3597
Cdd:COG5245 2365 VHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIR 2443
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3598 NLSEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSL 3677
Cdd:COG5245 2444 RRQFITEGVQKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQAR 2523
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3678 SLGRPLLIEDvGEELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMK 3757
Cdd:COG5245 2524 REGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVL 2602
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3758 GLEDQLLGRVILTEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEVTQKLEI 3837
Cdd:COG5245 2603 GCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESE 2682
|
2250 2260 2270 2280 2290
....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3838 SAETEVQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLF 3887
Cdd:COG5245 2683 SMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEF 2732
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2962-3222 |
7.31e-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: 319.94 E-value: 7.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2962 MDMVFFADAMVHLVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQ 3041
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3042 GKGITFIFTDNEIKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfpRCLPTNENLHDYFMSRVRQNLHIV 3121
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQ--NIEDSREAVYNYFVKRCRNNLHIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3122 LCFSPVGEKFRNRALKFPALISGCTIDWFSRWPKDALVAVSEHFLTsyDIDCSLEIKKEVVQCMGSFQDGVAEKCVDYFQ 3201
Cdd:pfam12780 159 LCMSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLE--DIEIPEELKSNVVKVFVYVHSSVEDMSKKFYE 236
|
250 260
....*....|....*....|.
gi 1034644038 3202 RFRRSTHVTPKSYLSFIQGYK 3222
Cdd:pfam12780 237 ELKRKNYVTPKSYLELLRLYK 257
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
3215-3336 |
2.66e-06 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 50.34 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3215 LSFIQGYKFIYGEKHVEvRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQA-----AE 3289
Cdd:PRK07352 29 LAIVIGLLYYFGRGFLG-KILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAiraeiEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034644038 3290 KVKAEVQKVKDRAQAIVDSiSKDKAIAEEKLEAAKPALEEAEAALQT 3336
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 ... |
3244-3333 |
5.43e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3244 EKLKEASESVAALSKELEAKEKELQVANDKADmvlKEVTMKAQAAEKVKAEVQKVKDRAQAivdsisKDKAIAEEKLeAA 3323
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEA------KAKAEAEAKA-KA 191
|
90
....*....|
gi 1034644038 3324 KPALEEAEAA 3333
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 ... |
3233-3335 |
9.68e-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: 42.04 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3233 RTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKE-----VTMKAQAAEKVKAEVQKVKDRAQAIVD 3307
Cdd:cd06503 26 KALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEAERILEQAKAEIE 105
|
90 100
....*....|....*....|....*...
gi 1034644038 3308 SiSKDKAIAEEKLEAAKPALEEAEAALQ 3335
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 ... |
286-838 |
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: 652.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 286 LGKIEDCMKVWIKQTEQVLAENNQLLKEaddvGPRAELEHWKKRLSKFNYLLEQLKSPDVKAVLAVLAAAKSKLLKTWRE 365
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQGRNP----GPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 366 MDIRITDATNEAKDNVKYLYTLEKCCDPLYS-SDPLSMMDAIPTLINAIKMIYSISHYYNTSEKITSLFVKVTNQIISAC 444
Cdd:pfam08385 77 LDTELTDALNEAKDNVKYLKTLERPFEDLEElTDPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 445 KAYITNNGtasIWNQPQDVVEEKILSAIKLKQEYQLCFHKTKQKLKQNPNAKQFDFSEMYIFGKFETFHRRLAKIIDIFT 524
Cdd:pfam08385 157 KKYLSPEG---IFDGDVEEALEKLQECIELLEAWKEEYKKTREKLEESPRERPWDFSERYIFGRFDAFLERLEKILELFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 525 TLKTYSVLQDS------TIEG-LEDMATKYQGIVATIKKKEYNFLDQRKMDFDQDYEEFCKQTNDLHNELRKFMDVTFAK 597
Cdd:pfam08385 234 TIEQFSKLEKIggtkgpELEGvIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 598 IQNTNQALRMLKKFE-RLNIPNL--GIDDKYQLILENYGADIDMISKLYTKQKYDP-PLARNQPPIAGKILWARQLFHRI 673
Cdd:pfam08385 314 ARSTESAFKLLRIFEfLLERPIIrgALEEKYTDLLQMFKKELDAVKKIFDKQKYNPsPIAKNMPPVAGAIIWARQLFRRI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 674 QQPMQLFQQHPAVLSTAEAKPIIRSYNRMAKVLLEFEVLFHRAWLRQIEEIHVG-LEASLLVKAPGTGELF-VNFDPQIL 751
Cdd:pfam08385 394 QEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGnLKRPLLVRHPETGKLLsVNFDPQLL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 752 ILFRETECMAQMGLEVSPLATSLFQKRDRYKRNFSNMKMMLAEYQRVKSKIPAAIEQLIVPHLAKVDEALQPGLAALTWT 831
Cdd:pfam08385 474 ALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTWN 553
|
....*..
gi 1034644038 832 SLNIEAY 838
Cdd:pfam08385 554 SLGIDEY 560
|
|
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1978-2305 |
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: 596.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1978 YQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKG 2057
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2058 LAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFtDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINF 2137
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVF-EGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2138 RSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYKLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRANPMDTESTIV 2217
Cdd:pfam12774 160 RPVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2218 MRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELEAAISRQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTL 2297
Cdd:pfam12774 240 LRALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLV 319
|
....*...
gi 1034644038 2298 GPSGAGKT 2305
Cdd:pfam12774 320 GPTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1438-1843 |
1.19e-147 |
|
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: 465.97 E-value: 1.19e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1438 LLEIKKQLNLLQKIYTLYNSVIETVNSYYDILWSEVNIEKINNELLEFQNRCRKLPRALKDWQAFLDLKKIIDDFSECCP 1517
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRDWDVAEELKKKIDDFKKSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1518 LLEYMASKAMMERHWERITTLTGHSLDVGNESFKLRNIMEAPLLKYKEEIEDICISAVKERDIEQKLKQVINEWDNKTFT 1597
Cdd:pfam08393 81 LIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTMEFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1598 FGSFKTRGELLLRGdsTSEIIANMEDSLMLLGSLLSNRYNMPFKAQIQKWVQYLSNSTDIIESWMTVQNLWIYLEAVFVG 1677
Cdd:pfam08393 161 LVPYKDTGTFILKG--WDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1678 GDIAKQLPKEAKRFSNIDKSWVKIMTRAHEVPSVVQCCvGDETLGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVS 1757
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEAC-NIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1758 DPALLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiYDRILSISSQEGETIELDKP-VMAEGNVEVWLNSLLEESQSSL 1836
Cdd:pfam08393 318 NDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE--NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMRETL 395
|
....*..
gi 1034644038 1837 HLVIRQA 1843
Cdd:pfam08393 396 RDLLKEA 402
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3610-3831 |
1.65e-115 |
|
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: 366.00 E-value: 1.65e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3610 SEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSLSLGRPLLIEDVG 3689
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3690 EELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMKGLEDQLLGRVIL 3769
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034644038 3770 TEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEV 3831
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1679-3887 |
4.20e-113 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 406.68 E-value: 4.20e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1679 DIAKQLPKEAKRFSNIDKSWVKIMTRahevpsVVQCCVGDETL----GQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFF 1754
Cdd:COG5245 639 DLMPLIPHAVHRKMSLVSGVRGIYKR------VVSGCEAINTIledvGDDLDLFYKEMDQVFMSIEKVLGLRWREVERAS 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1755 FVSDpaLLEILGQASDSHTIQAHLLNVFDNIKSVKFHEkiyDRILSISSQEGETIELDKPVMAEGNVEV--WLN----SL 1828
Cdd:COG5245 713 EVEE--LMDRVRELENRVYSYRFFVKKIAKEEMKTVFS---SRIQKKEPFSLDSEAYVGFFRLYEKSIVirGINrsmgRV 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1829 LEESQSSLhlvirQAAANIQETGFqlteFLSSFPAQVGLLGIQMiWTRDSEEALRNA------KFDKKIMQKTNQAFLEL 1902
Cdd:COG5245 788 LSQYLESV-----QEALEIEDGSF----FVSRHRVRDGGLEKGR-GCDAWENCFDPPlseyfrILEKIFPSEEGYFFDEV 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1903 LNtlidvttrdlsstervKYETLITIHVHQRDIFDDLCHMHIKSPMDFEWLKQCRFYFNEDsDKMMIHITDVAFIYQNEF 1982
Cdd:COG5245 858 LK----------------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELPQGLY-KRFIKVRSSYRSAEMFAK 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 1983 LGCTDRLVITPLTDRCYITLAQALGMSMggapAGPAGTGKTETTKDMGRCLGKYVvvfncsDQMDFRGlgRIFKGLAQSG 2062
Cdd:COG5245 921 NTIPFFVFEHSMDTSQHQKLFEAVCDEV----CRFVDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEE 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2063 SWGcFDEFNRIDLPVLSVAA--QQISIILTCKKEHKKSFIftdgDNVTMNPEFGLFLTMNPgyagRQELPENLKINFRSV 2140
Cdd:COG5245 989 ERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVV----EHGLKSPSTPVEMIINE----RNIVLEIGRRALDMF 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2141 AMMVPDRQIIIRVKlascgfidnvVLARKFFTLYKLCEEQLSKQVHYDFglrnilsvlRTL-GAAKRANPMDTESTivmr 2219
Cdd:COG5245 1060 LSNIPFGAIKSRRE----------SLDREIGAFNNEVDGIAREEDELMF---------YPMfKSLKAKHRMLEEKT---- 1116
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2220 vlrdMNLSKLIdedEPLFLSLIEDLFPNI--LLDKAGYPELEAAISRQVEEAGLINHPPWKlKVIQLFETQRVRHGMMTL 2297
Cdd:COG5245 1117 ----EYLNKIL---SITGLPLISDTLRERidTLDAEWDSFCRISESLKKYESQQVSGLDVA-QFVSFLRSVDTGAFHAEY 1188
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2298 GPSGAGKTTCIHTLMRAMTDCGKPHREMRMnpkaitapqmfgrLDvATNDWTdGIFSTLWRKTLRAK-KGEHIWIILDGp 2376
Cdd:COG5245 1189 FRVFLCKIKHYTDACDYLWHVKSPYVKKKY-------------FD-ADMELR-QFFLMFNREDMEARlADSKMEYEVER- 1252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2377 vdaiWIENLNSVLDDNKTLTLANGDRipmapncKIIFEphNIDnASPATVSRNGMVFMSSSILDWSPILEGFL------- 2449
Cdd:COG5245 1253 ----YVEKTKAEVSSLKLELSSVGEG-------QVVVS--NLG-SIGDKVGRCLVEYDSISRLSTKGVFLDELgdtkryl 1318
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2450 -KKRSPQEAEILRQLYTESF-----PDLYRFCIQ-----------NLEYKMEVLEAfVITQSINMLQGLiplKEQGGEVs 2512
Cdd:COG5245 1319 dECLDFFSCFEEVQKEIDELsmvfcADALRFSADlyhivkerrfsGVLAGSDASES-LGGKSIELAAIL---EHKDLIV- 1393
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2513 qaHLGRLFVFALLWSAGAALELDGRRRLELWLR---SRPTGTLELPPPAGPGDTAFDYYVAPDGTWTHWNTRTQEYLYPS 2589
Cdd:COG5245 1394 --EMKRGINDVLKLRIFGDKCRESTPRFYLISDgdlIKDLNERSDYEEMLIMMFNISAVITNNGSIAGFELRGERVMLRK 1471
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2590 DttpeygsILVPNVDNVRTDFLIQTIAKQGKAVLLIGEQGTAKTVIIKG-FMSKYDPEchmIKSLNFS-SATTPLM---F 2664
Cdd:COG5245 1472 E-------VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPsLRSELITE---VKYFNFStCTMTPSKlsvL 1541
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2665 QRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPIINEWGDQVTNEIVRQLMEQNGFYN-LEKpgEFTSIVDIqFLAAMI 2743
Cdd:COG5245 1542 ERETEYYPNTGVVRLYPKPVVKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERQGFWSsIAV--SWVTICGI-ILYGAC 1618
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2744 HPGG--GRNDIPQRLKRQFSIFNCTLPSEASVDKIFGVIGVGHYCTQRGFSEEVRDSVTKLVPLTRRLWQMTKikmlpTP 2821
Cdd:COG5245 1619 NPGTdeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASVELYLSSKDKTK-----FF 1693
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2822 AKFHYVFNLRDLSRVWQGMLNTTSEVIKEPN-DLLKLWKHECKRVIADRFTVSSDVTWFDKALVSLVEEEFGE------- 2893
Cdd:COG5245 1694 LQMNYGYKPRELTRSLRAIFGYAETRIDTPDvSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREmiaghig 1773
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2894 EKKLLVDcgiDTYFVDFlrdapeaagetsEEADAETPKIYepiesfshLKERLNMFlqlYNESIRgagMDMVFFADAMVH 2973
Cdd:COG5245 1774 EAEITFS---MILFFGM------------ACLLKKDLAVF--------VEEVRKIF---GSSHLD---VEAVAYKDALLH 1824
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2974 LVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNE 3053
Cdd:COG5245 1825 ILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESI 1904
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3054 IKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfPRCLPTNENLHDYFMSRVRQNLHIVL-CFSPVGEKFR 3132
Cdd:COG5245 1905 PVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFEST-SLEKDTEATLTRVFLVYMEENLPVVFsACCSQDTSVL 1983
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3133 NRALkFPALISGCTIDWFSRWPKDALVAVSEHFLT-SYDIDCSLEIKKEVVQCMGS-FQDGVAEKCVDYFQR-FRRSTHV 3209
Cdd:COG5245 1984 AGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVETlSRDGGRVFFINGELGVGKGAlISEVFGDDAVVIEGRgFEISMIE 2062
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3210 --TPKSYLSFIQG---YKFIYGEKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMK 3284
Cdd:COG5245 2063 gsLGESKIKFIGGlkvYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGE 2142
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3285 AQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMD--CV 3362
Cdd:COG5245 2143 RLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEdvCD 2222
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3363 LLLFQRKVsavkidleksctmpsWQESLKLMTAGNFLQNLQQFPKDT-INEEVIEFL-SPYFEMPDYNIETAKR---VCG 3437
Cdd:COG5245 2223 LLGFEAKI---------------WFGEQQSLRRDDFIRIIGKYPDEIeFDLEARRFReARECSDPSFTGSILNRaskACG 2287
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3438 NvagLCSWTKAMASFFSINKEVLPLKANLVVQENRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAER 3517
Cdd:COG5245 2288 P---LKRWLVRECNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDT 2364
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3518 CRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKRLVGDVLLATAFLSYSGPFNQEFRDLLLNDwRKEMKARKIPFGKNL 3597
Cdd:COG5245 2365 VHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGM-SFIRISKEFRDKEIR 2443
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3598 NLSEMLIDAPTISEWNLQGLPNDDLSIQNGIIVTKASRYPLLIDPQTQGKIWIKNKESRNELQITSLNHKYFRNHLEDSL 3677
Cdd:COG5245 2444 RRQFITEGVQKIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQAR 2523
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3678 SLGRPLLIEDvGEELDPALDNVLERNFIKTGSTFKVKVGDKEVDVLDGFRLYITTKLPNPAYTPEISARTSIIDFTVTMK 3757
Cdd:COG5245 2524 REGSDKIIGD-AEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVL 2602
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3758 GLEDQLLGRVILTEKQELEKERTHLMEDVTANKRRMKELEDNLLYRLTSTQGSLVEDESLIVVLSNTKRTAEEVTQKLEI 3837
Cdd:COG5245 2603 GCETEIPDALEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESE 2682
|
2250 2260 2270 2280 2290
....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3838 SAETEVQINSAREEYRPVATRGSILYFLITEMRLVNEMYQTSLRQFLGLF 3887
Cdd:COG5245 2683 SMEIEDRIDALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEF 2732
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2962-3222 |
7.31e-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: 319.94 E-value: 7.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2962 MDMVFFADAMVHLVKISRVIRTPQGNALLVGVGGSGKQSLTRLASFIAGYVSFQITLTRSYNTSNLMEDLKVLYRTAGQQ 3041
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3042 GKGITFIFTDNEIKDESFLEYMNNVLSSGEVSNLFARDEIDEINSDLASVMKKEfpRCLPTNENLHDYFMSRVRQNLHIV 3121
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQ--NIEDSREAVYNYFVKRCRNNLHIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3122 LCFSPVGEKFRNRALKFPALISGCTIDWFSRWPKDALVAVSEHFLTsyDIDCSLEIKKEVVQCMGSFQDGVAEKCVDYFQ 3201
Cdd:pfam12780 159 LCMSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLE--DIEIPEELKSNVVKVFVYVHSSVEDMSKKFYE 236
|
250 260
....*....|....*....|.
gi 1034644038 3202 RFRRSTHVTPKSYLSFIQGYK 3222
Cdd:pfam12780 237 ELKRKNYVTPKSYLELLRLYK 257
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2587-2768 |
4.46e-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: 285.44 E-value: 4.46e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2587 YPSDTtpEYGSILVPNVDNVRTDFLIQTIAKQGKAVLLIGEQGTAKTVIIKGFMSKYDPECHMIKSLNFSSATTPLMFQR 2666
Cdd:pfam12775 1 IPPDV--PFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2667 TIESYVDKRMGTTYGPPAGKKMTVFIDDVNMPIINEWGDQVTNEIVRQLMEQNGFYNLEKPgEFTSIVDIQFLAAMIHPG 2746
Cdd:pfam12775 79 IIESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKL-TFKEIVDVQFVAAMGPPG 157
|
170 180
....*....|....*....|..
gi 1034644038 2747 GGRNDIPQRLKRQFSIFNCTLP 2768
Cdd:pfam12775 158 GGRNDITPRLLRHFNVFNITFP 179
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
3238-3583 |
1.71e-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: 1.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3238 RMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAE 3317
Cdd:pfam12777 2 RLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKACE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3318 EKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPHLIMRIMDCVLLLFqrkVSAVKIDLEKsctmpSWQESlKLMTA-- 3395
Cdd:pfam12777 82 EDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILM---APGGKIPKDK-----SWKAA-KIMMAkv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3396 GNFLQNLQQFPKDTINEEVIEFLSPYFEMPDYNIETAKRVCGNVAGLCSWTKAMASFFSINKEVLPlKANLVVQENRHLL 3475
Cdd:pfam12777 153 DGFLDSLIKFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAP-KRQALEEANADLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3476 AMQD-LQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAERCRHKMQTASTLISGLAGEKERWTEQSQEFAAQTKRLV 3554
Cdd:pfam12777 232 AAQEkLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLC 311
|
330 340 350
....*....|....*....|....*....|
gi 1034644038 3555 GDVLLATAFLSYSGPFNQEFRDLLLND-WR 3583
Cdd:pfam12777 312 GDILLISAFISYLGFFTKKYRNELLDKfWI 341
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2460-2579 |
2.17e-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: 95.43 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2460 LRQLYTESFPDLYRFCIQNLEYKMEVLEAFVITQSINMLQGLIP-------LKEQGGEVSQAHLGRLFVFALLWSAGAAL 2532
Cdd:pfam17852 1 LEPLFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDevleyngVHPLSPDKLKEYLEKLFLFALVWSIGGTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1034644038 2533 ELDGRRRLELWLRSRPTGtLELPPPagPGDTAFDYYV-APDGTWTHWN 2579
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. |
2802-2891 |
2.40e-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: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2802 LVPLTRRLWQMTKIKMLPTPAKFHYVFNLRDLSRVWQGMLNTTSEVIKEPNDLLKLWKHECKRVIADRFTVSSDVTWFDK 2881
Cdd:pfam17857 1 LIAAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDK 80
|
90
....*....|
gi 1034644038 2882 ALVSLVEEEF 2891
Cdd:pfam17857 81 IQMASLKKFF 90
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2293-2428 |
1.73e-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: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2293 GMMTLGPSGAGKTTCIHTLMRAMTDCGKphrEMRMNPKAITAPQMFGRLDVATND--WTDGIFstlwrkTLRAKKGehiW 2370
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPV---FYVQLTRDTTEEDLFGRRNIDPGGasWVDGPL------VRAAREG---E 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034644038 2371 IILDGPVDAI---WIENLNSVLDDNKTLTLANGDRIPMAPNC-KIIFEPHNID----NASPATVSR 2428
Cdd:pfam07728 69 IAVLDEINRAnpdVLNSLLSLLDERRLLLPDGGELVKAAPDGfRLIATMNPLDrglnELSPALRSR 134
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3232-3353 |
1.12e-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: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3232 VRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVandkadmvlkevtmKAQAAEKVKAEVQKVKDRAQAIVDSISK 3311
Cdd:COG3883 124 LSKIADADADLLEELKADKAELEAKKAELEAKLAELEA--------------LKAELEAAKAELEAQQAEQEALLAQLSA 189
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1034644038 3312 DKAIAEEKLEAAKPALEEAEAALQTIRPSDIATVRTLGRPPH 3353
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
3215-3336 |
2.66e-06 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 50.34 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3215 LSFIQGYKFIYGEKHVEvRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQA-----AE 3289
Cdd:PRK07352 29 LAIVIGLLYYFGRGFLG-KILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAiraeiEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034644038 3290 KVKAEVQKVKDRAQAIVDSiSKDKAIAEEKLEAAKPALEEAEAALQT 3336
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 ... |
3244-3333 |
5.43e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3244 EKLKEASESVAALSKELEAKEKELQVANDKADmvlKEVTMKAQAAEKVKAEVQKVKDRAQAivdsisKDKAIAEEKLeAA 3323
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEA------KAKAEAEAKA-KA 191
|
90
....*....|
gi 1034644038 3324 KPALEEAEAA 3333
Cdd:TIGR02794 192 EEAKAKAEAA 201
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3476-3549 |
2.16e-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: 2.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034644038 3476 AMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLEDAERcrhKMQTASTLISGLAGEKERWTEQSQEFAAQ 3549
Cdd:COG3883 134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3245-3333 |
2.70e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3245 KLKEASES--VAALSK--ELEAKEKELQVANDKADMVLKEvtmKAQAAEKVKAEV---QKVKDRAQAIVDSISKDKAIAE 3317
Cdd:PRK09510 146 KAKAEAEAkrAAAAAKkaAAEAKKKAEAEAAKKAAAEAKK---KAEAEAAAKAAAeakKKAEAEAKKKAAAEAKKKAAAE 222
|
90
....*....|....*.
gi 1034644038 3318 EKLEAAKPALEEAEAA 3333
Cdd:PRK09510 223 AKAAAAKAAAEAKAAA 238
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3245-3332 |
3.48e-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: 45.99 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3245 KLKEAsesvAALSKELEAKEKELQVANDKADMVLK----EVTMKAQAAEKVKAEVQKVKDRAqaivdsiSKDKAIAE--E 3318
Cdd:TIGR02794 143 KAKEE----AAKQAEEEAKAKAAAEAKKKAEEAKKkaeaEAKAKAEAEAKAKAEEAKAKAEA-------AKAKAAAEaaA 211
|
90
....*....|....
gi 1034644038 3319 KLEAAKPALEEAEA 3332
Cdd:TIGR02794 212 KAEAEAAAAAAAEA 225
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3245-3333 |
5.93e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.57 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3245 KLKEASESVAALSKEL--EAKEKELQVANDKAD---MVLKEVTMKAQAAEKVKAEVQ---KVKDRAQAIVDSISKDKAIA 3316
Cdd:PRK09510 118 KQAEEAAKQAALKQKQaeEAAAKAAAAAKAKAEaeaKRAAAAAKKAAAEAKKKAEAEaakKAAAEAKKKAEAEAAAKAAA 197
|
90
....*....|....*..
gi 1034644038 3317 EEKLEAAKPALEEAEAA 3333
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAE 214
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3227-3560 |
7.73e-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: 45.82 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3227 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRaqaiV 3306
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----I 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3307 DSISKDKAIAEEKLEAAKPALEEAEAALQTIRpSDIATVRTlgrpphLIMRIMDCVLLL------FQRKVSAVKIDL-EK 3379
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAE-AEIEELEA------QIEQLKEELKALrealdeLRAELTLLNEEAaNL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3380 SCTMPSWQESLKLmtAGNFLQNLQQFPKDtiNEEVIEFLSPYFEMPDYNIETAKRvcgnvaGLCSWTKAMASFFSINKEV 3459
Cdd:TIGR02168 823 RERLESLERRIAA--TERRLEDLEEQIEE--LSEDIESLAAEIEELEELIEELES------ELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3460 LPLKANLVVQENRHLLAMQDLQKAQAELDDKQAELDVVQAEYEQ-AMTEKQTLLEDAERcrhKMQTASTLISGLAGEKER 3538
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVrIDNLQERLSEEYSL---TLEEAEALENKIEDDEEE 969
|
330 340
....*....|....*....|..
gi 1034644038 3539 WTEQSQEFAAQTKRLvGDVLLA 3560
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 ... |
3233-3335 |
9.68e-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: 42.04 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3233 RTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKE-----VTMKAQAAEKVKAEVQKVKDRAQAIVD 3307
Cdd:cd06503 26 KALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEAERILEQAKAEIE 105
|
90 100
....*....|....*....|....*...
gi 1034644038 3308 SiSKDKAIAEEKLEAAKPALEEAEAALQ 3335
Cdd:cd06503 106 Q-EKEKALAELRKEVADLAVEAAEKILG 132
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2622-2760 |
1.13e-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: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 2622 VLLIGEQGTAKTVIIKGFMSKYDP-ECHMIkslNFSSATTP--LMFQRTIESYVDKRMGTTYGPPAGKKMTVFIDDVNMP 2698
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNrPVFYV---QLTRDTTEedLFGRRNIDPGGASWVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034644038 2699 ---IINEWgDQVTNEIVRQLMEqNGFYNLEKPGEFtsivdiQFLAAMIHPGGGRNDIPQRLKRQF 2760
Cdd:pfam07728 79 npdVLNSL-LSLLDERRLLLPD-GGELVKAAPDGF------RLIATMNPLDRGLNELSPALRSRF 135
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3243-3332 |
1.47e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.03 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3243 LEKLKEASES----VAALSKELEAKEKELQVANDKADmvlKEVTMKAQAAEKVKAEVQ---KVKDRAQAIVDSISKDKAI 3315
Cdd:PRK09510 128 ALKQKQAEEAaakaAAAAKAKAEAEAKRAAAAAKKAA---AEAKKKAEAEAAKKAAAEakkKAEAEAAAKAAAEAKKKAE 204
|
90
....*....|....*..
gi 1034644038 3316 AEEKLEAAKPALEEAEA 3332
Cdd:PRK09510 205 AEAKKKAAAEAKKKAAA 221
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3227-3334 |
1.58e-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: 43.37 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3227 EKHVEVRTLANRmntgLEKLKEASESVA------ALSKELEAKEKELQVANDKadmvLKEVTMKAQAAEKVKAEVQKVKD 3300
Cdd:COG1579 63 RLELEIEEVEAR----IKKYEEQLGNVRnnkeyeALQKEIESLKRRISDLEDE----ILELMERIEELEEELAELEAELA 134
|
90 100 110
....*....|....*....|....*....|....
gi 1034644038 3301 RAQAIVDSISKDKAIAEEKLEAAKPALEEAEAAL 3334
Cdd:COG1579 135 ELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
3244-3333 |
1.82e-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: 44.25 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3244 EKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISKDKAIAEEKLEAA 3323
Cdd:pfam05701 370 AKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAI 449
|
90
....*....|
gi 1034644038 3324 KpALEEAEAA 3333
Cdd:pfam05701 450 K-ALQESESS 458
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3243-3562 |
2.58e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3243 LEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVT-MKAQAAEKVKAEVQKVKDRAQAIVDSISKdkaiAEEKLE 3321
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEE----AQEELE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3322 AAKPALEEAEAALQTIRPSD--------------IATVRTLGRPPHLIMRIMDCVLLLFQRKVSAVKIDLEKSCTMPswQ 3387
Cdd:COG4717 224 ELEEELEQLENELEAAALEErlkearlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL--G 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3388 ESLKLMTAGNFLQNLQQfpkdtinEEVIEFLSPYFEMPDYNIETAKRVCGNVAglcSWTKAMASFFSINKEvlpLKANLV 3467
Cdd:COG4717 302 KEAEELQALPALEELEE-------EELEELLAALGLPPDLSPEELLELLDRIE---ELQELLREAEELEEE---LQLEEL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3468 VQENRHLLAMQD---------LQKAQAELDDKQAELDVVQAEYEQAMTEKQTLLE--DAERCRHKMQTASTLISGLAGEK 3536
Cdd:COG4717 369 EQEIAALLAEAGvedeeelraALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEEL 448
|
330 340
....*....|....*....|....*.
gi 1034644038 3537 ERWTEQSQEFAAQTKRLVGDVLLATA 3562
Cdd:COG4717 449 EELREELAELEAELEQLEEDGELAEL 474
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3231-3336 |
3.07e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3231 EVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSIS 3310
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100
....*....|....*....|....*.
gi 1034644038 3311 KDKAiAEEKLEAAKPALEEAEAALQT 3336
Cdd:COG4372 119 ELQK-ERQDLEQQRKQLEAQIAELQS 143
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
3230-3337 |
4.25e-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: 42.01 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3230 VEVRTLANRMNTGLEKLKEASESVA-ALSKELEAKEKELQVANDkadmVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDS 3308
Cdd:pfam06008 151 KAAQDLLSRIQTWFQSPQEENKALAnALRDSLAEYEAKLSDLRE----LLREAAAKTRDANRLNLANQANLREFQRKKEE 226
|
90 100
....*....|....*....|....*....
gi 1034644038 3309 ISKDKAIAEEKLEAAKPALEEAEAALQTI 3337
Cdd:pfam06008 227 VSEQKNQLEETLKTARDSLDAANLLLQEI 255
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3227-3336 |
4.76e-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: 43.12 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3227 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKadmvLKEVTMKAQAAEKVKAEVQKVKDRAQAIV 3306
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK----LEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110
....*....|....*....|....*....|
gi 1034644038 3307 DSISKDKAIAEEKLEAAKPALEEAEAALQT 3336
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEE 327
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3248-3338 |
5.03e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3248 EASESVAALSKELEAKEKELQVANDKADMVLKEvtmkaqaAEKVKAEVQKVKDRAQAIVDS-ISKDKAIAEEKLEAAKpa 3326
Cdd:PRK00409 513 EDKEKLNELIASLEELERELEQKAEEAEALLKE-------AEKLKEELEEKKEKLQEEEDKlLEEAEKEAQQAIKEAK-- 583
|
90
....*....|..
gi 1034644038 3327 lEEAEAALQTIR 3338
Cdd:PRK00409 584 -KEADEIIKELR 594
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
3233-3335 |
5.57e-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: 40.16 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3233 RTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVT-----MKAQAAEKVKAEVQKVKDRAQAIVD 3307
Cdd:COG0711 27 KALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARkeaeaIAEEAKAEAEAEAERIIAQAEAEIE 106
|
90 100
....*....|....*....|....*...
gi 1034644038 3308 SIsKDKAIAEEKLEAAKPALEEAEAALQ 3335
Cdd:COG0711 107 QE-RAKALAELRAEVADLAVAIAEKILG 133
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3231-3333 |
6.90e-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: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3231 EVRTLANRMNTgLEKLKEASES---VAALSKELEAKEKELQvANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVD 3307
Cdd:COG4913 639 ELDALQERREA-LQRLAEYSWDeidVASAEREIAELEAELE-RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIG 716
|
90 100
....*....|....*....|....*.
gi 1034644038 3308 SISKDKAIAEEKLEAAKPALEEAEAA 3333
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEDL 742
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3231-3334 |
8.15e-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: 42.36 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3231 EVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKdraqaivdsis 3310
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE----------- 764
|
90 100
....*....|....*....|....
gi 1034644038 3311 KDKAIAEEKLEAAKPALEEAEAAL 3334
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARL 788
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3227-3338 |
8.41e-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: 41.06 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3227 EKHVEVRTLANRMNTGLEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDR--AQA 3304
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEA 93
|
90 100 110
....*....|....*....|....*....|....*..
gi 1034644038 3305 I---VDSISKDKAIAEEKLEAAKPALEEAEAALQTIR 3338
Cdd:COG1579 94 LqkeIESLKRRISDLEDEILELMERIEELEEELAELE 130
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3243-3347 |
9.82e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644038 3243 LEKLKEASESVAALSKELEAKEKELQVANDKADMVLKEVTMKAQAAEKVKAEVQKVKDRAQAIVDSISK-DKAIAEEKLE 3321
Cdd:COG4913 677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFA 756
|
90 100
....*....|....*....|....*.
gi 1034644038 3322 AAkpALEEAEAALQTIRPSDIATVRT 3347
Cdd:COG4913 757 AA--LGDAVERELRENLEERIDALRA 780
|
|
| |
