|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
466-792 |
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: 630.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 466 YFYEYLGNSPRLVITPLTDRCYITLTQSLHLTMSGAPAGPAGTGKTETTKDLGRALGMMVYVFNCSEQMDYRSIGNIYKG 545
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 546 LVQTGAWGCFDEFNRIAVEVLSVVAVQVKMIHDAIRNGRKRFVFLGETIPLKPSVGIFITLNPGYAGRTELPENLKALFR 625
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 626 PCAMVAPDTELICEIMLVAEGFVDARSLARKFISLYTLCEELLSKQDHYDWGLRAIKSVLVVAGSLKRGDKNRPEDQVLM 705
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 706 RALRDFNMPKIVTDDVPVFLGLVSDLFPALDVPRQRKPHFEQMVKQSTLELRLQPEESFILKVVQLEELLAVRHSVFVVG 785
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 1039739712 786 NAGTGKS 792
Cdd:pfam12774 321 PTGSGKT 327
|
|
| MT super family |
cl37598 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
1699-2043 |
5.51e-171 |
|
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.
The actual alignment was detected with superfamily member pfam12777:
Pssm-ID: 463699 [Multi-domain] Cd Length: 344 Bit Score: 530.03 E-value: 5.51e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1699 EHLGNGIQKLQTTASQVGNLKSRLASQEAELQLRNLDAEALITKIGLQTEKVSREKAIADAEERKVAAIQTEASQKQREC 1778
Cdd:pfam12777 1 ERLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1779 EADLLKAEPALVAAKDALNTLNRVNLTELKTFPNPPNAVTNVTAAVMVLLAPRGRVPKDRSWKAAKIFMGKVDDFLQALI 1858
Cdd:pfam12777 81 EEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGGKIPKDKSWKAAKIMMAKVDGFLDSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1859 NYDKEHIPENCLKVVnEQYLKDPEFNPNLIRTKSFAAAGLCAWVINIIRFYEVYCDVEPKRQALAQTNLDLAAATEKLEA 1938
Cdd:pfam12777 161 KFDKEHIHEACLKAF-KPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1939 VRRKLVDLDHNLSRLTASFEKATAEKVRCQEEVNQTNKTIDLANKLVSELESEKIRWGQSIKSFETQEKTLCGDVLLTAA 2018
Cdd:pfam12777 240 IKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISA 319
|
330 340
....*....|....*....|....*
gi 1039739712 2019 FVSYIGSFTRQYRQELVDCKWIPFL 2043
Cdd:pfam12777 320 FISYLGFFTKKYRNELLDKFWIPYI 344
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
3-332 |
1.04e-129 |
|
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: 414.35 E-value: 1.04e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 3 TSLRAIAELQNPALRDRHWQQLMKAIGVRF-SINDSTTLSDLLAVQLHRVEDDVRDIVDQAVKELGTEKVITDVSHTWEA 81
Cdd:pfam08393 77 KSLPLIEDLRNPALRERHWKQLSEILGFDFdPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 82 LEFSYEAHHRTGTPLLKSDEQLFETLEHNQVQLQSLLQSKYVEYFIEQVLSWQNKLNVADAVIFTWMQVQRTWSHLESIF 161
Cdd:pfam08393 157 MEFELVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 162 VcSEDIRVQLVEDARRFDKVDAEFKELMFETAKVKNVLEATCRPHLYEKLKDFQHRLSLCEKALAEYLETKRVTFPRFYF 241
Cdd:pfam08393 237 S-SEDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYF 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 242 ISSADLLDILSKGAQPKQVTHHLVKLFDSISDLQFEDNLDVsthkaVGMFSKEKEYVPF-QAGCECIGHVESWLLQLEQT 320
Cdd:pfam08393 316 LSNDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDENKEI-----TGMISKEGEVVPFsKPPVEAKGNVEEWLNELEEE 390
|
330
....*....|..
gi 1039739712 321 MKDTVRLAITEA 332
Cdd:pfam08393 391 MRETLRDLLKEA 402
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
2780-3075 |
4.00e-123 |
|
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: 390.83 E-value: 4.00e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2780 TVTSNTLFRTLLEMQPRNAVSQEELGQSTEDKVKNILDDILERLPEEFNMAEIMQKNP--NRSPYVLVCFQECERMNVLI 2857
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGGSSREEIVLELAKDILEKLPEPFDIEEAEEKYPvgYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2858 REIRVSLQHLDLGLKGELTLSPDVETQLSALSYDRVPDTWNKLAYPSTYGLAQWFNDLLLRCRELDTWTQDLTLPAVVWL 2937
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2938 SGFFNPQSFLTAIMQTMARKNEWPLDRMCLTIDVTKK-TKEDYGHPPREGAYLHGLHLEGARWDIQSGALVDARLKELTS 3016
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKvSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039739712 3017 MMPVIFAKAVPVDRQEIKHA-YECPVYKTKARG-PTYVWTFRLRSKDRIAKWVLAGVALLL 3075
Cdd:pfam18199 241 PLPVIHLKPVESDKKKLDENtYECPVYKTSERHsTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DYN1 super family |
cl34955 |
Dynein, heavy chain [Cytoskeleton]; |
154-2727 |
4.28e-120 |
|
Dynein, heavy chain [Cytoskeleton];
The actual alignment was detected with superfamily member COG5245:
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 428.64 E-value: 4.28e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 154 WSHLESIFVCSEDIRVQLVEDARRFDKVDAEFKELMFETAKVKNVLEATCRPhLYEKLKDFQHRLSLCEKALAEYLETKR 233
Cdd:COG5245 627 RLDEYLMMMSLEDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQVFMSIEKVLGLRW 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 234 VTFPRFyfISSADLLDILSKGAQPKQVTHHLVKLFDSI-SDLQFEDNLdvsthKAVGMFSKEKE-YVPFQAGCECIgHVE 311
Cdd:COG5245 706 REVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEeMKTVFSSRI-----QKKEPFSLDSEaYVGFFRLYEKS-IVI 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 312 SWLLQLEQTMKDTVRLAITEAItayEEKPRELWIFDFPAQVALTGSQIWwtTDVgiafsrLEEGYETALKDFHKkqisQL 391
Cdd:COG5245 778 RGINRSMGRVLSQYLESVQEAL---EIEDGSFFVSRHRVRDGGLEKGRG--CDA------WENCFDPPLSEYFR----IL 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 392 NTLITLLLGELSPGDRQKVMTICTIDVHARDVVAKLISQKVVSPHAFTWLSqLRHEWEDSRKHCVVNICDAHFQYFYEYL 471
Cdd:COG5245 843 EKIFPSEEGYFFDEVLKRLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVS-ISELPQGLYKRFIKVRSSYRSAEMFAKN 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 472 GNSPRLVITPLTDRCYITLTQSLHLTMSGApagpAGTGKTETTKDLGRALGMMVyvfncsEQMDYRSigNIYKGLVQTGA 551
Cdd:COG5245 922 TIPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEE 989
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 552 WGcFDEFNRIAvEVLSVVAVQVKMIHDAIRNGRKRFVFLGETIPLKPSVGIFITLNPgyagRTELPENLKALFRPCAMVA 631
Cdd:COG5245 990 RG-TEESALLD-EISRTILVDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNI 1063
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 632 PdteliceimlvaEGFVDAR--SLARKFISLYTLCEELLSKQDHYDWglRAIKSVLVVAGSLKRgDKNRPEDQVLmralR 709
Cdd:COG5245 1064 P------------FGAIKSRreSLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRMLE-EKTEYLNKIL----S 1124
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 710 DFNMPKIvtDDVPVFLglvSDLFPALDVPRQRKPHFEQMVKQSTLELRLQPEESFILKVVQLEELLAVrhsvfvVGNAGT 789
Cdd:COG5245 1125 ITGLPLI--SDTLRER---IDTLDAEWDSFCRISESLKKYESQQVSGLDVAQFVSFLRSVDTGAFHAE------YFRVFL 1193
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 790 GKSKILRTL-------NRTYVnmkqkpvwsdlnpkavtTDELFgfihHATREWKdGLFSSILREQANLT-HDGPTWIVLD 861
Cdd:COG5245 1194 CKIKHYTDAcdylwhvKSPYV-----------------KKKYF----DADMELR-QFFLMFNREDMEARlADSKMEYEVE 1251
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 862 GdidplWIESLNTVMDDNKVLTLASNERvalkpsmRLLFEThhlRTATPATVSRAGILY----------VNPQDLG-WNP 930
Cdd:COG5245 1252 R-----YVEKTKAEVSSLKLELSSVGEG-------QVVVSN---LGSIGDKVGRCLVEYdsisrlstkgVFLDELGdTKR 1316
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 931 YVASWIDRRRHQSEKANLTILFDK-YIPVCLE---------KLRTSFKAITSVPES-SLVQTICTLLECLLTPENIppDS 999
Cdd:COG5245 1317 YLDECLDFFSCFEEVQKEIDELSMvFCADALRfsadlyhivKERRFSGVLAGSDASeSLGGKSIELAAILEHKDLI--VE 1394
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1000 PKETYEVYFAFACvwtFGGTLLRDQLSDYQ---ADFSrwwhKEMKAVKFPSQGTIFDYYLDHKTKKFLPwtdkVPQFSMD 1076
Cdd:COG5245 1395 MKRGINDVLKLRI---FGDKCRESTPRFYLisdGDLI----KDLNERSDYEEMLIMMFNISAVITNNGS----IAGFELR 1463
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1077 ADAPL--KTVLVHTPETTRLRYFTELLLCKGKPIMLVGNAGVGKTVFLSNTLASlSENYIVSCVPFNYYTTSAALQRILE 1154
Cdd:COG5245 1464 GERVMlrKEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS-ELITEVKYFNFSTCTMTPSKLSVLE 1542
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1155 KPLEKKagRNYG-----PKGN-KKLVYFIDDLNMPEVDLYGTIQPHALLRQHIDY-GHWYDRHKiMLKEIRNCQYVACMN 1227
Cdd:COG5245 1543 RETEYY--PNTGvvrlyPKPVvKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERqGFWSSIAV-SWVTICGIILYGACN 1619
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1228 P--MVGSFTVNPRLQRHfTVFAF-NFPSLDALTTIYgqifSFYLQQQAFC-PSVLRAGPSLIQATIAFHQMMAESFvPTA 1303
Cdd:COG5245 1620 PgtDEGRVKYYERFIRK-PVFVFcCYPELASLRNIY----EAVLMGSYLCfDEFNRLSEETMSASVELYLSSKDKT-KFF 1693
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1304 IKFHYNFNLRDLSNIFQGIL-FASPECLKSLEDLARLWLHETSRVYGDRLIDTNDFDLFQRKMLETAHKYFKGVDANALL 1382
Cdd:COG5245 1694 LQMNYGYKPRELTRSLRAIFgYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIG 1773
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1383 RQPLVYCHFASGGedpcyMPVKDWEGLKAVLMEMVDNYNELHSAMHLVLFEDAMQHVCRISRILRIPQGHALLIGVGGSG 1462
Cdd:COG5245 1774 EAEITFSMILFFG-----MACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRG 1848
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1463 KQSLSRLAAYICSLEVFQITLTEGYGAQELRVDLANLYVRTGAKNMPTVFLLTDAHVLDESFLVLINDLLASGDIPDLFS 1542
Cdd:COG5245 1849 ACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFS 1928
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1543 DEDMDKIISGIRNEVRGLGL-VDSRENCWAFFLARVRQQLKMVFCFSPVGHTLRVRARKFPAIVNCTAIDWFHEWPQEAL 1621
Cdd:COG5245 1929 GNERIRIPENLRFVFESTSLeKDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGIRSPALKNRCFIDFKKLWDTEEM 2008
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1622 VSVSRRFI-EEIEGIEPQH--------KDSISLFMAHVHTSVKEVSAWYYQNERRYNYTTPRSFLEQISLFKSLLKKKRE 1692
Cdd:COG5245 2009 SQYANSVEtLSRDGGRVFFingelgvgKGALISEVFGDDAVVIEGRGFEISMIEGSLGESKIKFIGGLKVYDARCVIYIE 2088
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1693 EVKQKQEHLGNGIQKLQTTASQVGNLKSRLASQEAELQLRNLDAEALITKIgLQTEKVSREKAIADAEERKVAAIQTEAS 1772
Cdd:COG5245 2089 ELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGT-PGERLEREVKSVFVEAPRDMLFLLEEEV 2167
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1773 QKQRECEADLLK-AEPALVAAKDALNTLNRVNLTELKTFPNPPNAVTNVTAAVMVLLaprGRVPKDrsWKAAKIFMgKVD 1851
Cdd:COG5245 2168 RKRKGSVMKFKSsKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLL---GFEAKI--WFGEQQSL-RRD 2241
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1852 DFLQALINYDKE-HIPENCLKVVNEQYLKDPEFNPNLIRTKSFAAAGLCAWVINIIRFYEVYCDVEPKRQALAQTNLDLA 1930
Cdd:COG5245 2242 DFIRIIGKYPDEiEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAF 2321
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1931 AATEKLEAVRRKLVDLDHNLSRLTASFEKATAEKVRCQEEVNQTNKTIDLANKLVSELESEKIRWGQSIKSFETQEKTLC 2010
Cdd:COG5245 2322 LVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELD 2401
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2011 GDVLLTAAFVSYIGSFTRQYRQ-ELVDCKwiPFLQQKVSIP-------IAEGLDLIamlTDDATIATWNNEGLPSDRMST 2082
Cdd:COG5245 2402 GDGHPSSCLHPYIGTLGFLCRAiEFGMSF--IRISKEFRDKeirrrqfITEGVQKI---EDFKEEACSTDYGLENSRIRK 2476
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2083 ENATILthcerwPLMIDPQQQGIKWIKNKYGPdlKVTHLG---QKGFLNTIETALAFGDVILIENlKETVDPVLGPLLGR 2159
Cdd:COG5245 2477 DLQDLT------AVLNDPSSKIVTSQRQMYDE--KKAILGsfrEMEFAFGLSQARREGSDKIIGD-AEALDEEIGRLIKE 2547
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2160 NTTKKGKFIR--IGDKECEFNKNFRLILHTKLANPHYKPELQAQTTLLNFTVTEDGLEGQLLAEVVSIERPDLERLKLVL 2237
Cdd:COG5245 2548 EFKSNLSEVKvmINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKAL 2627
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2238 TKQQNDFKIELRQLEDDLLLRLSAAEGSFLDDTDLVERLETTKATAAEIEHKVTEARENERKINETRECYRPVAARASLL 2317
Cdd:COG5245 2628 NALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESI 2707
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2318 YFVISDLRRINPVYQFSLKAFNTLFHRaieqadkVEDTQERICALIESITHATFLYasqaLFERDKLTFLSQMAFQAVAL 2397
Cdd:COG5245 2708 RVEIAMFDEKALMYNKSICELSSEFEK-------WRRMKSKYLCAIRYMLMSSEWI----LDHEDRSGFIHRLDVSFLLR 2776
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2398 MEEFRGLDRDVEGSAKQWRKWV----ESECPEKEKLPQE----WKKKSLIQKLIILRAVRPDRMTYALRNFVEEKLGAKY 2469
Cdd:COG5245 2777 TKRFVSTLLEDKNYRQVLSSCSlygnDVISHSCDRFDRDvyraLKHQMDNRTHSTILTSNSKTNPYKEYTYNDSWAEAFE 2856
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2470 VERT--RLDLGKAFEESSPST-PVFFILSPGVDALKDLEVLG--KRLGFTIDSGKFHNVSlgqgqelvaemamekaaagG 2544
Cdd:COG5245 2857 VEDSgdLYKFEEGLLELIVGHaPLIYAHKKSLENERNVDRLGskENEVYAVLNSLFSRKE-------------------K 2917
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2545 HWVILQNVHLVAKWlgtLEKLLEKFSQGS-----HRDYRVFLSAETVPSQhepiIPQGLLENSIKITNEPPTGMLANLhA 2619
Cdd:COG5245 2918 SWFEVYNISLSFGW---FKRYVEDVVYPIkasrvCGKVKNMWTSMVDADM----LPIQLLIAIDSFVSSTYPETGCGY-A 2989
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2620 ALYNFDQ---DTLEMCSKDqefksILFSLCYFHACVAGRLRFGPQGWSRSYPFSPGDLTICTNILYNYLEANP--NVPWE 2694
Cdd:COG5245 2990 DLVEIDRypfDYTLVIACD-----DAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNILFLNHlnARKWG 3064
|
2650 2660 2670
....*....|....*....|....*....|....*..
gi 1039739712 2695 DLRYLFGEIMYGGHITDAWD----RKLCRVYLEEFMN 2727
Cdd:COG5245 3065 NNRDLIFTIVYGKKHSLMEDskvvDKYCRGYGAHETS 3101
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
466-792 |
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: 630.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 466 YFYEYLGNSPRLVITPLTDRCYITLTQSLHLTMSGAPAGPAGTGKTETTKDLGRALGMMVYVFNCSEQMDYRSIGNIYKG 545
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 546 LVQTGAWGCFDEFNRIAVEVLSVVAVQVKMIHDAIRNGRKRFVFLGETIPLKPSVGIFITLNPGYAGRTELPENLKALFR 625
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 626 PCAMVAPDTELICEIMLVAEGFVDARSLARKFISLYTLCEELLSKQDHYDWGLRAIKSVLVVAGSLKRGDKNRPEDQVLM 705
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 706 RALRDFNMPKIVTDDVPVFLGLVSDLFPALDVPRQRKPHFEQMVKQSTLELRLQPEESFILKVVQLEELLAVRHSVFVVG 785
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 1039739712 786 NAGTGKS 792
Cdd:pfam12774 321 PTGSGKT 327
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
1699-2043 |
5.51e-171 |
|
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: 530.03 E-value: 5.51e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1699 EHLGNGIQKLQTTASQVGNLKSRLASQEAELQLRNLDAEALITKIGLQTEKVSREKAIADAEERKVAAIQTEASQKQREC 1778
Cdd:pfam12777 1 ERLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1779 EADLLKAEPALVAAKDALNTLNRVNLTELKTFPNPPNAVTNVTAAVMVLLAPRGRVPKDRSWKAAKIFMGKVDDFLQALI 1858
Cdd:pfam12777 81 EEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGGKIPKDKSWKAAKIMMAKVDGFLDSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1859 NYDKEHIPENCLKVVnEQYLKDPEFNPNLIRTKSFAAAGLCAWVINIIRFYEVYCDVEPKRQALAQTNLDLAAATEKLEA 1938
Cdd:pfam12777 161 KFDKEHIHEACLKAF-KPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1939 VRRKLVDLDHNLSRLTASFEKATAEKVRCQEEVNQTNKTIDLANKLVSELESEKIRWGQSIKSFETQEKTLCGDVLLTAA 2018
Cdd:pfam12777 240 IKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISA 319
|
330 340
....*....|....*....|....*
gi 1039739712 2019 FVSYIGSFTRQYRQELVDCKWIPFL 2043
Cdd:pfam12777 320 FISYLGFFTKKYRNELLDKFWIPYI 344
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
3-332 |
1.04e-129 |
|
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: 414.35 E-value: 1.04e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 3 TSLRAIAELQNPALRDRHWQQLMKAIGVRF-SINDSTTLSDLLAVQLHRVEDDVRDIVDQAVKELGTEKVITDVSHTWEA 81
Cdd:pfam08393 77 KSLPLIEDLRNPALRERHWKQLSEILGFDFdPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 82 LEFSYEAHHRTGTPLLKSDEQLFETLEHNQVQLQSLLQSKYVEYFIEQVLSWQNKLNVADAVIFTWMQVQRTWSHLESIF 161
Cdd:pfam08393 157 MEFELVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 162 VcSEDIRVQLVEDARRFDKVDAEFKELMFETAKVKNVLEATCRPHLYEKLKDFQHRLSLCEKALAEYLETKRVTFPRFYF 241
Cdd:pfam08393 237 S-SEDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYF 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 242 ISSADLLDILSKGAQPKQVTHHLVKLFDSISDLQFEDNLDVsthkaVGMFSKEKEYVPF-QAGCECIGHVESWLLQLEQT 320
Cdd:pfam08393 316 LSNDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDENKEI-----TGMISKEGEVVPFsKPPVEAKGNVEEWLNELEEE 390
|
330
....*....|..
gi 1039739712 321 MKDTVRLAITEA 332
Cdd:pfam08393 391 MRETLRDLLKEA 402
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
2780-3075 |
4.00e-123 |
|
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: 390.83 E-value: 4.00e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2780 TVTSNTLFRTLLEMQPRNAVSQEELGQSTEDKVKNILDDILERLPEEFNMAEIMQKNP--NRSPYVLVCFQECERMNVLI 2857
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGGSSREEIVLELAKDILEKLPEPFDIEEAEEKYPvgYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2858 REIRVSLQHLDLGLKGELTLSPDVETQLSALSYDRVPDTWNKLAYPSTYGLAQWFNDLLLRCRELDTWTQDLTLPAVVWL 2937
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2938 SGFFNPQSFLTAIMQTMARKNEWPLDRMCLTIDVTKK-TKEDYGHPPREGAYLHGLHLEGARWDIQSGALVDARLKELTS 3016
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKvSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039739712 3017 MMPVIFAKAVPVDRQEIKHA-YECPVYKTKARG-PTYVWTFRLRSKDRIAKWVLAGVALLL 3075
Cdd:pfam18199 241 PLPVIHLKPVESDKKKLDENtYECPVYKTSERHsTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
154-2727 |
4.28e-120 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 428.64 E-value: 4.28e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 154 WSHLESIFVCSEDIRVQLVEDARRFDKVDAEFKELMFETAKVKNVLEATCRPhLYEKLKDFQHRLSLCEKALAEYLETKR 233
Cdd:COG5245 627 RLDEYLMMMSLEDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQVFMSIEKVLGLRW 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 234 VTFPRFyfISSADLLDILSKGAQPKQVTHHLVKLFDSI-SDLQFEDNLdvsthKAVGMFSKEKE-YVPFQAGCECIgHVE 311
Cdd:COG5245 706 REVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEeMKTVFSSRI-----QKKEPFSLDSEaYVGFFRLYEKS-IVI 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 312 SWLLQLEQTMKDTVRLAITEAItayEEKPRELWIFDFPAQVALTGSQIWwtTDVgiafsrLEEGYETALKDFHKkqisQL 391
Cdd:COG5245 778 RGINRSMGRVLSQYLESVQEAL---EIEDGSFFVSRHRVRDGGLEKGRG--CDA------WENCFDPPLSEYFR----IL 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 392 NTLITLLLGELSPGDRQKVMTICTIDVHARDVVAKLISQKVVSPHAFTWLSqLRHEWEDSRKHCVVNICDAHFQYFYEYL 471
Cdd:COG5245 843 EKIFPSEEGYFFDEVLKRLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVS-ISELPQGLYKRFIKVRSSYRSAEMFAKN 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 472 GNSPRLVITPLTDRCYITLTQSLHLTMSGApagpAGTGKTETTKDLGRALGMMVyvfncsEQMDYRSigNIYKGLVQTGA 551
Cdd:COG5245 922 TIPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEE 989
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 552 WGcFDEFNRIAvEVLSVVAVQVKMIHDAIRNGRKRFVFLGETIPLKPSVGIFITLNPgyagRTELPENLKALFRPCAMVA 631
Cdd:COG5245 990 RG-TEESALLD-EISRTILVDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNI 1063
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 632 PdteliceimlvaEGFVDAR--SLARKFISLYTLCEELLSKQDHYDWglRAIKSVLVVAGSLKRgDKNRPEDQVLmralR 709
Cdd:COG5245 1064 P------------FGAIKSRreSLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRMLE-EKTEYLNKIL----S 1124
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 710 DFNMPKIvtDDVPVFLglvSDLFPALDVPRQRKPHFEQMVKQSTLELRLQPEESFILKVVQLEELLAVrhsvfvVGNAGT 789
Cdd:COG5245 1125 ITGLPLI--SDTLRER---IDTLDAEWDSFCRISESLKKYESQQVSGLDVAQFVSFLRSVDTGAFHAE------YFRVFL 1193
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 790 GKSKILRTL-------NRTYVnmkqkpvwsdlnpkavtTDELFgfihHATREWKdGLFSSILREQANLT-HDGPTWIVLD 861
Cdd:COG5245 1194 CKIKHYTDAcdylwhvKSPYV-----------------KKKYF----DADMELR-QFFLMFNREDMEARlADSKMEYEVE 1251
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 862 GdidplWIESLNTVMDDNKVLTLASNERvalkpsmRLLFEThhlRTATPATVSRAGILY----------VNPQDLG-WNP 930
Cdd:COG5245 1252 R-----YVEKTKAEVSSLKLELSSVGEG-------QVVVSN---LGSIGDKVGRCLVEYdsisrlstkgVFLDELGdTKR 1316
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 931 YVASWIDRRRHQSEKANLTILFDK-YIPVCLE---------KLRTSFKAITSVPES-SLVQTICTLLECLLTPENIppDS 999
Cdd:COG5245 1317 YLDECLDFFSCFEEVQKEIDELSMvFCADALRfsadlyhivKERRFSGVLAGSDASeSLGGKSIELAAILEHKDLI--VE 1394
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1000 PKETYEVYFAFACvwtFGGTLLRDQLSDYQ---ADFSrwwhKEMKAVKFPSQGTIFDYYLDHKTKKFLPwtdkVPQFSMD 1076
Cdd:COG5245 1395 MKRGINDVLKLRI---FGDKCRESTPRFYLisdGDLI----KDLNERSDYEEMLIMMFNISAVITNNGS----IAGFELR 1463
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1077 ADAPL--KTVLVHTPETTRLRYFTELLLCKGKPIMLVGNAGVGKTVFLSNTLASlSENYIVSCVPFNYYTTSAALQRILE 1154
Cdd:COG5245 1464 GERVMlrKEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS-ELITEVKYFNFSTCTMTPSKLSVLE 1542
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1155 KPLEKKagRNYG-----PKGN-KKLVYFIDDLNMPEVDLYGTIQPHALLRQHIDY-GHWYDRHKiMLKEIRNCQYVACMN 1227
Cdd:COG5245 1543 RETEYY--PNTGvvrlyPKPVvKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERqGFWSSIAV-SWVTICGIILYGACN 1619
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1228 P--MVGSFTVNPRLQRHfTVFAF-NFPSLDALTTIYgqifSFYLQQQAFC-PSVLRAGPSLIQATIAFHQMMAESFvPTA 1303
Cdd:COG5245 1620 PgtDEGRVKYYERFIRK-PVFVFcCYPELASLRNIY----EAVLMGSYLCfDEFNRLSEETMSASVELYLSSKDKT-KFF 1693
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1304 IKFHYNFNLRDLSNIFQGIL-FASPECLKSLEDLARLWLHETSRVYGDRLIDTNDFDLFQRKMLETAHKYFKGVDANALL 1382
Cdd:COG5245 1694 LQMNYGYKPRELTRSLRAIFgYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIG 1773
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1383 RQPLVYCHFASGGedpcyMPVKDWEGLKAVLMEMVDNYNELHSAMHLVLFEDAMQHVCRISRILRIPQGHALLIGVGGSG 1462
Cdd:COG5245 1774 EAEITFSMILFFG-----MACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRG 1848
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1463 KQSLSRLAAYICSLEVFQITLTEGYGAQELRVDLANLYVRTGAKNMPTVFLLTDAHVLDESFLVLINDLLASGDIPDLFS 1542
Cdd:COG5245 1849 ACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFS 1928
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1543 DEDMDKIISGIRNEVRGLGL-VDSRENCWAFFLARVRQQLKMVFCFSPVGHTLRVRARKFPAIVNCTAIDWFHEWPQEAL 1621
Cdd:COG5245 1929 GNERIRIPENLRFVFESTSLeKDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGIRSPALKNRCFIDFKKLWDTEEM 2008
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1622 VSVSRRFI-EEIEGIEPQH--------KDSISLFMAHVHTSVKEVSAWYYQNERRYNYTTPRSFLEQISLFKSLLKKKRE 1692
Cdd:COG5245 2009 SQYANSVEtLSRDGGRVFFingelgvgKGALISEVFGDDAVVIEGRGFEISMIEGSLGESKIKFIGGLKVYDARCVIYIE 2088
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1693 EVKQKQEHLGNGIQKLQTTASQVGNLKSRLASQEAELQLRNLDAEALITKIgLQTEKVSREKAIADAEERKVAAIQTEAS 1772
Cdd:COG5245 2089 ELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGT-PGERLEREVKSVFVEAPRDMLFLLEEEV 2167
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1773 QKQRECEADLLK-AEPALVAAKDALNTLNRVNLTELKTFPNPPNAVTNVTAAVMVLLaprGRVPKDrsWKAAKIFMgKVD 1851
Cdd:COG5245 2168 RKRKGSVMKFKSsKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLL---GFEAKI--WFGEQQSL-RRD 2241
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1852 DFLQALINYDKE-HIPENCLKVVNEQYLKDPEFNPNLIRTKSFAAAGLCAWVINIIRFYEVYCDVEPKRQALAQTNLDLA 1930
Cdd:COG5245 2242 DFIRIIGKYPDEiEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAF 2321
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1931 AATEKLEAVRRKLVDLDHNLSRLTASFEKATAEKVRCQEEVNQTNKTIDLANKLVSELESEKIRWGQSIKSFETQEKTLC 2010
Cdd:COG5245 2322 LVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELD 2401
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2011 GDVLLTAAFVSYIGSFTRQYRQ-ELVDCKwiPFLQQKVSIP-------IAEGLDLIamlTDDATIATWNNEGLPSDRMST 2082
Cdd:COG5245 2402 GDGHPSSCLHPYIGTLGFLCRAiEFGMSF--IRISKEFRDKeirrrqfITEGVQKI---EDFKEEACSTDYGLENSRIRK 2476
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2083 ENATILthcerwPLMIDPQQQGIKWIKNKYGPdlKVTHLG---QKGFLNTIETALAFGDVILIENlKETVDPVLGPLLGR 2159
Cdd:COG5245 2477 DLQDLT------AVLNDPSSKIVTSQRQMYDE--KKAILGsfrEMEFAFGLSQARREGSDKIIGD-AEALDEEIGRLIKE 2547
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2160 NTTKKGKFIR--IGDKECEFNKNFRLILHTKLANPHYKPELQAQTTLLNFTVTEDGLEGQLLAEVVSIERPDLERLKLVL 2237
Cdd:COG5245 2548 EFKSNLSEVKvmINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKAL 2627
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2238 TKQQNDFKIELRQLEDDLLLRLSAAEGSFLDDTDLVERLETTKATAAEIEHKVTEARENERKINETRECYRPVAARASLL 2317
Cdd:COG5245 2628 NALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESI 2707
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2318 YFVISDLRRINPVYQFSLKAFNTLFHRaieqadkVEDTQERICALIESITHATFLYasqaLFERDKLTFLSQMAFQAVAL 2397
Cdd:COG5245 2708 RVEIAMFDEKALMYNKSICELSSEFEK-------WRRMKSKYLCAIRYMLMSSEWI----LDHEDRSGFIHRLDVSFLLR 2776
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2398 MEEFRGLDRDVEGSAKQWRKWV----ESECPEKEKLPQE----WKKKSLIQKLIILRAVRPDRMTYALRNFVEEKLGAKY 2469
Cdd:COG5245 2777 TKRFVSTLLEDKNYRQVLSSCSlygnDVISHSCDRFDRDvyraLKHQMDNRTHSTILTSNSKTNPYKEYTYNDSWAEAFE 2856
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2470 VERT--RLDLGKAFEESSPST-PVFFILSPGVDALKDLEVLG--KRLGFTIDSGKFHNVSlgqgqelvaemamekaaagG 2544
Cdd:COG5245 2857 VEDSgdLYKFEEGLLELIVGHaPLIYAHKKSLENERNVDRLGskENEVYAVLNSLFSRKE-------------------K 2917
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2545 HWVILQNVHLVAKWlgtLEKLLEKFSQGS-----HRDYRVFLSAETVPSQhepiIPQGLLENSIKITNEPPTGMLANLhA 2619
Cdd:COG5245 2918 SWFEVYNISLSFGW---FKRYVEDVVYPIkasrvCGKVKNMWTSMVDADM----LPIQLLIAIDSFVSSTYPETGCGY-A 2989
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2620 ALYNFDQ---DTLEMCSKDqefksILFSLCYFHACVAGRLRFGPQGWSRSYPFSPGDLTICTNILYNYLEANP--NVPWE 2694
Cdd:COG5245 2990 DLVEIDRypfDYTLVIACD-----DAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNILFLNHlnARKWG 3064
|
2650 2660 2670
....*....|....*....|....*....|....*..
gi 1039739712 2695 DLRYLFGEIMYGGHITDAWD----RKLCRVYLEEFMN 2727
Cdd:COG5245 3065 NNRDLIFTIVYGKKHSLMEDskvvDKYCRGYGAHETS 3101
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
2068-2286 |
8.34e-112 |
|
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: 354.83 E-value: 8.34e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2068 ATWNNEGLPSDRMSTENATILTHCERWPLMIDPQQQGIKWIKNKYGP-DLKVTHLGQKGFLNTIETALAFGDVILIENLK 2146
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDnGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2147 ETVDPVLGPLLGRNTTKKG--KFIRIGDKECEFNKNFRLILHTKLANPHYKPELQAQTTLLNFTVTEDGLEGQLLAEVVS 2224
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGgrKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039739712 2225 IERPDLERLKLVLTKQQNDFKIELRQLEDDLLLRLSAAEGSFLDDTDLVERLETTKATAAEI 2286
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1677-1801 |
2.58e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1677 LEQISLFKSLLKKKREEVKQKQEHLGNGIQKLQTTASQVGNLKSRLASQEAELQLRNLDAEALITKIGLQTEKVSREKAI 1756
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1039739712 1757 ADAEERKVAAIQTEASQKQRECEADLLKAEPALVAAKDALNTLNR 1801
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1706-1800 |
7.77e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 44.72 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1706 QKLQTTASQVGNLKSRLASQEAEL-QLRNLDAEALITKIGLQTEKVSREKAIADAEErKVAAIQTEASQKQ----RECEA 1780
Cdd:TIGR04320 247 TPIPNPPNSLAALQAKLATAQADLaAAQTALNTAQAALTSAQTAYAAAQAALATAQK-ELANAQAQALQTAqnnlATAQA 325
|
90 100
....*....|....*....|
gi 1039739712 1781 DLLKAEPALVAAKDALNTLN 1800
Cdd:TIGR04320 326 ALANAEARLAKAKEALANLN 345
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
466-792 |
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: 630.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 466 YFYEYLGNSPRLVITPLTDRCYITLTQSLHLTMSGAPAGPAGTGKTETTKDLGRALGMMVYVFNCSEQMDYRSIGNIYKG 545
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 546 LVQTGAWGCFDEFNRIAVEVLSVVAVQVKMIHDAIRNGRKRFVFLGETIPLKPSVGIFITLNPGYAGRTELPENLKALFR 625
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 626 PCAMVAPDTELICEIMLVAEGFVDARSLARKFISLYTLCEELLSKQDHYDWGLRAIKSVLVVAGSLKRGDKNRPEDQVLM 705
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 706 RALRDFNMPKIVTDDVPVFLGLVSDLFPALDVPRQRKPHFEQMVKQSTLELRLQPEESFILKVVQLEELLAVRHSVFVVG 785
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 1039739712 786 NAGTGKS 792
Cdd:pfam12774 321 PTGSGKT 327
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
1699-2043 |
5.51e-171 |
|
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: 530.03 E-value: 5.51e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1699 EHLGNGIQKLQTTASQVGNLKSRLASQEAELQLRNLDAEALITKIGLQTEKVSREKAIADAEERKVAAIQTEASQKQREC 1778
Cdd:pfam12777 1 ERLENGLLKLHSTAAQVDDLKAKLAAQEAELKQKNEDADKLIQVVGIEADKVSKEKAIADEEEQKVAVIMKEVKEKQKAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1779 EADLLKAEPALVAAKDALNTLNRVNLTELKTFPNPPNAVTNVTAAVMVLLAPRGRVPKDRSWKAAKIFMGKVDDFLQALI 1858
Cdd:pfam12777 81 EEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILMAPGGKIPKDKSWKAAKIMMAKVDGFLDSLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1859 NYDKEHIPENCLKVVnEQYLKDPEFNPNLIRTKSFAAAGLCAWVINIIRFYEVYCDVEPKRQALAQTNLDLAAATEKLEA 1938
Cdd:pfam12777 161 KFDKEHIHEACLKAF-KPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQEKLAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1939 VRRKLVDLDHNLSRLTASFEKATAEKVRCQEEVNQTNKTIDLANKLVSELESEKIRWGQSIKSFETQEKTLCGDVLLTAA 2018
Cdd:pfam12777 240 IKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDILLISA 319
|
330 340
....*....|....*....|....*
gi 1039739712 2019 FVSYIGSFTRQYRQELVDCKWIPFL 2043
Cdd:pfam12777 320 FISYLGFFTKKYRNELLDKFWIPYI 344
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
3-332 |
1.04e-129 |
|
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: 414.35 E-value: 1.04e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 3 TSLRAIAELQNPALRDRHWQQLMKAIGVRF-SINDSTTLSDLLAVQLHRVEDDVRDIVDQAVKELGTEKVITDVSHTWEA 81
Cdd:pfam08393 77 KSLPLIEDLRNPALRERHWKQLSEILGFDFdPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 82 LEFSYEAHHRTGTPLLKSDEQLFETLEHNQVQLQSLLQSKYVEYFIEQVLSWQNKLNVADAVIFTWMQVQRTWSHLESIF 161
Cdd:pfam08393 157 MEFELVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 162 VcSEDIRVQLVEDARRFDKVDAEFKELMFETAKVKNVLEATCRPHLYEKLKDFQHRLSLCEKALAEYLETKRVTFPRFYF 241
Cdd:pfam08393 237 S-SEDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYF 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 242 ISSADLLDILSKGAQPKQVTHHLVKLFDSISDLQFEDNLDVsthkaVGMFSKEKEYVPF-QAGCECIGHVESWLLQLEQT 320
Cdd:pfam08393 316 LSNDELLEILSQTKDPTRVQPHLKKCFEGIASLEFDENKEI-----TGMISKEGEVVPFsKPPVEAKGNVEEWLNELEEE 390
|
330
....*....|..
gi 1039739712 321 MKDTVRLAITEA 332
Cdd:pfam08393 391 MRETLRDLLKEA 402
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
2780-3075 |
4.00e-123 |
|
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: 390.83 E-value: 4.00e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2780 TVTSNTLFRTLLEMQPRNAVSQEELGQSTEDKVKNILDDILERLPEEFNMAEIMQKNP--NRSPYVLVCFQECERMNVLI 2857
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGGSSREEIVLELAKDILEKLPEPFDIEEAEEKYPvgYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2858 REIRVSLQHLDLGLKGELTLSPDVETQLSALSYDRVPDTWNKLAYPSTYGLAQWFNDLLLRCRELDTWTQDLTLPAVVWL 2937
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKSYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2938 SGFFNPQSFLTAIMQTMARKNEWPLDRMCLTIDVTKK-TKEDYGHPPREGAYLHGLHLEGARWDIQSGALVDARLKELTS 3016
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVTKKvSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039739712 3017 MMPVIFAKAVPVDRQEIKHA-YECPVYKTKARG-PTYVWTFRLRSKDRIAKWVLAGVALLL 3075
Cdd:pfam18199 241 PLPVIHLKPVESDKKKLDENtYECPVYKTSERHsTNFVFSVDLPTDKPPDHWILRGVALLL 301
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
154-2727 |
4.28e-120 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 428.64 E-value: 4.28e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 154 WSHLESIFVCSEDIRVQLVEDARRFDKVDAEFKELMFETAKVKNVLEATCRPhLYEKLKDFQHRLSLCEKALAEYLETKR 233
Cdd:COG5245 627 RLDEYLMMMSLEDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQVFMSIEKVLGLRW 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 234 VTFPRFyfISSADLLDILSKGAQPKQVTHHLVKLFDSI-SDLQFEDNLdvsthKAVGMFSKEKE-YVPFQAGCECIgHVE 311
Cdd:COG5245 706 REVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEeMKTVFSSRI-----QKKEPFSLDSEaYVGFFRLYEKS-IVI 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 312 SWLLQLEQTMKDTVRLAITEAItayEEKPRELWIFDFPAQVALTGSQIWwtTDVgiafsrLEEGYETALKDFHKkqisQL 391
Cdd:COG5245 778 RGINRSMGRVLSQYLESVQEAL---EIEDGSFFVSRHRVRDGGLEKGRG--CDA------WENCFDPPLSEYFR----IL 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 392 NTLITLLLGELSPGDRQKVMTICTIDVHARDVVAKLISQKVVSPHAFTWLSqLRHEWEDSRKHCVVNICDAHFQYFYEYL 471
Cdd:COG5245 843 EKIFPSEEGYFFDEVLKRLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVS-ISELPQGLYKRFIKVRSSYRSAEMFAKN 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 472 GNSPRLVITPLTDRCYITLTQSLHLTMSGApagpAGTGKTETTKDLGRALGMMVyvfncsEQMDYRSigNIYKGLVQTGA 551
Cdd:COG5245 922 TIPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY------DGTEPRS--RIEAGPICEEE 989
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 552 WGcFDEFNRIAvEVLSVVAVQVKMIHDAIRNGRKRFVFLGETIPLKPSVGIFITLNPgyagRTELPENLKALFRPCAMVA 631
Cdd:COG5245 990 RG-TEESALLD-EISRTILVDEYLNSDEFRMLEELNSAVVEHGLKSPSTPVEMIINE----RNIVLEIGRRALDMFLSNI 1063
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 632 PdteliceimlvaEGFVDAR--SLARKFISLYTLCEELLSKQDHYDWglRAIKSVLVVAGSLKRgDKNRPEDQVLmralR 709
Cdd:COG5245 1064 P------------FGAIKSRreSLDREIGAFNNEVDGIAREEDELMF--YPMFKSLKAKHRMLE-EKTEYLNKIL----S 1124
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 710 DFNMPKIvtDDVPVFLglvSDLFPALDVPRQRKPHFEQMVKQSTLELRLQPEESFILKVVQLEELLAVrhsvfvVGNAGT 789
Cdd:COG5245 1125 ITGLPLI--SDTLRER---IDTLDAEWDSFCRISESLKKYESQQVSGLDVAQFVSFLRSVDTGAFHAE------YFRVFL 1193
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 790 GKSKILRTL-------NRTYVnmkqkpvwsdlnpkavtTDELFgfihHATREWKdGLFSSILREQANLT-HDGPTWIVLD 861
Cdd:COG5245 1194 CKIKHYTDAcdylwhvKSPYV-----------------KKKYF----DADMELR-QFFLMFNREDMEARlADSKMEYEVE 1251
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 862 GdidplWIESLNTVMDDNKVLTLASNERvalkpsmRLLFEThhlRTATPATVSRAGILY----------VNPQDLG-WNP 930
Cdd:COG5245 1252 R-----YVEKTKAEVSSLKLELSSVGEG-------QVVVSN---LGSIGDKVGRCLVEYdsisrlstkgVFLDELGdTKR 1316
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 931 YVASWIDRRRHQSEKANLTILFDK-YIPVCLE---------KLRTSFKAITSVPES-SLVQTICTLLECLLTPENIppDS 999
Cdd:COG5245 1317 YLDECLDFFSCFEEVQKEIDELSMvFCADALRfsadlyhivKERRFSGVLAGSDASeSLGGKSIELAAILEHKDLI--VE 1394
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1000 PKETYEVYFAFACvwtFGGTLLRDQLSDYQ---ADFSrwwhKEMKAVKFPSQGTIFDYYLDHKTKKFLPwtdkVPQFSMD 1076
Cdd:COG5245 1395 MKRGINDVLKLRI---FGDKCRESTPRFYLisdGDLI----KDLNERSDYEEMLIMMFNISAVITNNGS----IAGFELR 1463
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1077 ADAPL--KTVLVHTPETTRLRYFTELLLCKGKPIMLVGNAGVGKTVFLSNTLASlSENYIVSCVPFNYYTTSAALQRILE 1154
Cdd:COG5245 1464 GERVMlrKEVVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS-ELITEVKYFNFSTCTMTPSKLSVLE 1542
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1155 KPLEKKagRNYG-----PKGN-KKLVYFIDDLNMPEVDLYGTIQPHALLRQHIDY-GHWYDRHKiMLKEIRNCQYVACMN 1227
Cdd:COG5245 1543 RETEYY--PNTGvvrlyPKPVvKDLVLFCDEINLPYGFEYYPPTVIVFLRPLVERqGFWSSIAV-SWVTICGIILYGACN 1619
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1228 P--MVGSFTVNPRLQRHfTVFAF-NFPSLDALTTIYgqifSFYLQQQAFC-PSVLRAGPSLIQATIAFHQMMAESFvPTA 1303
Cdd:COG5245 1620 PgtDEGRVKYYERFIRK-PVFVFcCYPELASLRNIY----EAVLMGSYLCfDEFNRLSEETMSASVELYLSSKDKT-KFF 1693
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1304 IKFHYNFNLRDLSNIFQGIL-FASPECLKSLEDLARLWLHETSRVYGDRLIDTNDFDLFQRKMLETAHKYFKGVDANALL 1382
Cdd:COG5245 1694 LQMNYGYKPRELTRSLRAIFgYAETRIDTPDVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLRAIREMIAGHIG 1773
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1383 RQPLVYCHFASGGedpcyMPVKDWEGLKAVLMEMVDNYNELHSAMHLVLFEDAMQHVCRISRILRIPQGHALLIGVGGSG 1462
Cdd:COG5245 1774 EAEITFSMILFFG-----MACLLKKDLAVFVEEVRKIFGSSHLDVEAVAYKDALLHILRSRRGLLVVGGHGVLKGVLIRG 1848
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1463 KQSLSRLAAYICSLEVFQITLTEGYGAQELRVDLANLYVRTGAKNMPTVFLLTDAHVLDESFLVLINDLLASGDIPDLFS 1542
Cdd:COG5245 1849 ACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFNPLLDNNRFLCLFS 1928
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1543 DEDMDKIISGIRNEVRGLGL-VDSRENCWAFFLARVRQQLKMVFCFSPVGHTLRVRARKFPAIVNCTAIDWFHEWPQEAL 1621
Cdd:COG5245 1929 GNERIRIPENLRFVFESTSLeKDTEATLTRVFLVYMEENLPVVFSACCSQDTSVLAGIRSPALKNRCFIDFKKLWDTEEM 2008
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1622 VSVSRRFI-EEIEGIEPQH--------KDSISLFMAHVHTSVKEVSAWYYQNERRYNYTTPRSFLEQISLFKSLLKKKRE 1692
Cdd:COG5245 2009 SQYANSVEtLSRDGGRVFFingelgvgKGALISEVFGDDAVVIEGRGFEISMIEGSLGESKIKFIGGLKVYDARCVIYIE 2088
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1693 EVKQKQEHLGNGIQKLQTTASQVGNLKSRLASQEAELQLRNLDAEALITKIgLQTEKVSREKAIADAEERKVAAIQTEAS 1772
Cdd:COG5245 2089 ELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGT-PGERLEREVKSVFVEAPRDMLFLLEEEV 2167
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1773 QKQRECEADLLK-AEPALVAAKDALNTLNRVNLTELKTFPNPPNAVTNVTAAVMVLLaprGRVPKDrsWKAAKIFMgKVD 1851
Cdd:COG5245 2168 RKRKGSVMKFKSsKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLL---GFEAKI--WFGEQQSL-RRD 2241
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1852 DFLQALINYDKE-HIPENCLKVVNEQYLKDPEFNPNLIRTKSFAAAGLCAWVINIIRFYEVYCDVEPKRQALAQTNLDLA 1930
Cdd:COG5245 2242 DFIRIIGKYPDEiEFDLEARRFREARECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPLREEEKRIDGEAF 2321
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1931 AATEKLEAVRRKLVDLDHNLSRLTASFEKATAEKVRCQEEVNQTNKTIDLANKLVSELESEKIRWGQSIKSFETQEKTLC 2010
Cdd:COG5245 2322 LVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGVFSEVPKLMVELD 2401
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2011 GDVLLTAAFVSYIGSFTRQYRQ-ELVDCKwiPFLQQKVSIP-------IAEGLDLIamlTDDATIATWNNEGLPSDRMST 2082
Cdd:COG5245 2402 GDGHPSSCLHPYIGTLGFLCRAiEFGMSF--IRISKEFRDKeirrrqfITEGVQKI---EDFKEEACSTDYGLENSRIRK 2476
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2083 ENATILthcerwPLMIDPQQQGIKWIKNKYGPdlKVTHLG---QKGFLNTIETALAFGDVILIENlKETVDPVLGPLLGR 2159
Cdd:COG5245 2477 DLQDLT------AVLNDPSSKIVTSQRQMYDE--KKAILGsfrEMEFAFGLSQARREGSDKIIGD-AEALDEEIGRLIKE 2547
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2160 NTTKKGKFIR--IGDKECEFNKNFRLILHTKLANPHYKPELQAQTTLLNFTVTEDGLEGQLLAEVVSIERPDLERLKLVL 2237
Cdd:COG5245 2548 EFKSNLSEVKvmINPPEIVRSTVEAVFWLSEGRSGDMGSIEWKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHEKAL 2627
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2238 TKQQNDFKIELRQLEDDLLLRLSAAEGSFLDDTDLVERLETTKATAAEIEHKVTEARENERKINETRECYRPVAARASLL 2317
Cdd:COG5245 2628 NALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRLESI 2707
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2318 YFVISDLRRINPVYQFSLKAFNTLFHRaieqadkVEDTQERICALIESITHATFLYasqaLFERDKLTFLSQMAFQAVAL 2397
Cdd:COG5245 2708 RVEIAMFDEKALMYNKSICELSSEFEK-------WRRMKSKYLCAIRYMLMSSEWI----LDHEDRSGFIHRLDVSFLLR 2776
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2398 MEEFRGLDRDVEGSAKQWRKWV----ESECPEKEKLPQE----WKKKSLIQKLIILRAVRPDRMTYALRNFVEEKLGAKY 2469
Cdd:COG5245 2777 TKRFVSTLLEDKNYRQVLSSCSlygnDVISHSCDRFDRDvyraLKHQMDNRTHSTILTSNSKTNPYKEYTYNDSWAEAFE 2856
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2470 VERT--RLDLGKAFEESSPST-PVFFILSPGVDALKDLEVLG--KRLGFTIDSGKFHNVSlgqgqelvaemamekaaagG 2544
Cdd:COG5245 2857 VEDSgdLYKFEEGLLELIVGHaPLIYAHKKSLENERNVDRLGskENEVYAVLNSLFSRKE-------------------K 2917
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2545 HWVILQNVHLVAKWlgtLEKLLEKFSQGS-----HRDYRVFLSAETVPSQhepiIPQGLLENSIKITNEPPTGMLANLhA 2619
Cdd:COG5245 2918 SWFEVYNISLSFGW---FKRYVEDVVYPIkasrvCGKVKNMWTSMVDADM----LPIQLLIAIDSFVSSTYPETGCGY-A 2989
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2620 ALYNFDQ---DTLEMCSKDqefksILFSLCYFHACVAGRLRFGPQGWSRSYPFSPGDLTICTNILYNYLEANP--NVPWE 2694
Cdd:COG5245 2990 DLVEIDRypfDYTLVIACD-----DAFYLSWEHAAVASVISAGPKENNEEIYFGDKDFEFKTHLLKNILFLNHlnARKWG 3064
|
2650 2660 2670
....*....|....*....|....*....|....*..
gi 1039739712 2695 DLRYLFGEIMYGGHITDAWD----RKLCRVYLEEFMN 2727
Cdd:COG5245 3065 NNRDLIFTIVYGKKHSLMEDskvvDKYCRGYGAHETS 3101
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
2068-2286 |
8.34e-112 |
|
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: 354.83 E-value: 8.34e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2068 ATWNNEGLPSDRMSTENATILTHCERWPLMIDPQQQGIKWIKNKYGP-DLKVTHLGQKGFLNTIETALAFGDVILIENLK 2146
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDnGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2147 ETVDPVLGPLLGRNTTKKG--KFIRIGDKECEFNKNFRLILHTKLANPHYKPELQAQTTLLNFTVTEDGLEGQLLAEVVS 2224
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGgrKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039739712 2225 IERPDLERLKLVLTKQQNDFKIELRQLEDDLLLRLSAAEGSFLDDTDLVERLETTKATAAEI 2286
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 ... |
1427-1686 |
6.44e-110 |
|
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: 351.14 E-value: 6.44e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1427 MHLVLFEDAMQHVCRISRILRIPQGHALLIGVGGSGKQSLSRLAAYICSLEVFQITLTEGYGAQELRVDLANLYVRTGAK 1506
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1507 NMPTVFLLTDAHVLDESFLVLINDLLASGDIPDLFSDEDMDKIISGIRNEVRGLGLVDSRENCWAFFLARVRQQLKMVFC 1586
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1587 FSPVGHTLRVRARKFPAIVNCTAIDWFHEWPQEALVSVSRRFIEEIEGIEpQHKDSISLFMAHVHTSVKEVSAWYYQNER 1666
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFLEDIEIPE-ELKSNVVKVFVYVHSSVEDMSKKFYEELK 239
|
250 260
....*....|....*....|
gi 1039739712 1667 RYNYTTPRSFLEQISLFKSL 1686
Cdd:pfam12780 240 RKNYVTPKSYLELLRLYKNL 259
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
1076-1251 |
2.89e-87 |
|
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).
Pssm-ID: 463698 [Multi-domain] Cd Length: 179 Bit Score: 282.74 E-value: 2.89e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1076 DADAPLKTVLVHTPETTRLRYFTELLLCKGKPIMLVGNAGVGKTVFLSNTLASLS-ENYIVSCVPFNYYTTSAALQRILE 1154
Cdd:pfam12775 2 PPDVPFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDkEKYLPLFINFSAQTTSNQTQDIIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1155 KPLEKKAGRNYGPKGNKKLVYFIDDLNMPEVDLYGTIQPHALLRQHIDYGHWYDRHKIMLKEIRNCQYVACMNPMVGS-F 1233
Cdd:pfam12775 82 SKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPGGGrN 161
|
170
....*....|....*...
gi 1039739712 1234 TVNPRLQRHFTVFAFNFP 1251
Cdd:pfam12775 162 DITPRLLRHFNVFNITFP 179
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
2638-2774 |
5.50e-65 |
|
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: 217.32 E-value: 5.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2638 FKSILFSLCYFHACVAGRLRFGPQGWSRSYPFSPGDLTICTNILYNYLEANP-NVPWEDLRYLFGEIMYGGHITDAWDRK 2716
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYDeKIPWDALRYLIGEINYGGRVTDDWDRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2717 LCRVYLEEFMNPSLIEDEVMLAPG-FAAPPYSDYSGYHQYIEdTLP-PESPALYGLHPNA 2774
Cdd:pfam18198 81 LLNTYLEEFFNPEVLEEDFKFSPSlYYIPPDGDLEDYLEYIE-SLPlVDSPEVFGLHPNA 139
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
2485-2606 |
1.45e-42 |
|
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: 152.21 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 2485 SPSTPVFFILSPGVDALKDLEVLGKRLGFTidsGKFHNVSLGQGQELVAEMAMEKAAAGGHWVILQNVHLVAKWLGTLEK 2564
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGFG---GKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1039739712 2565 LLEKF-SQGSHRDYRVFLSAEtvPSqhePIIPQGLLENSIKIT 2606
Cdd:pfam03028 78 ILEELpEETLHPDFRLWLTSE--PS---PKFPISILQNSIKIT 115
|
|
| AAA_lid_1 |
pfam17857 |
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3. |
1284-1373 |
9.95e-36 |
|
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: 131.98 E-value: 9.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1284 LIQATIAFHQMMAESFVPTAIKFHYNFNLRDLSNIFQGILFASPECLKSLEDLARLWLHETSRVYGDRLIDTNDFDLFQR 1363
Cdd:pfam17857 1 LIAAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDK 80
|
90
....*....|
gi 1039739712 1364 KMLETAHKYF 1373
Cdd:pfam17857 81 IQMASLKKFF 90
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
951-1068 |
1.66e-29 |
|
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: 115.46 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 951 LFDKYIPVCLEKLRTSFKAITSVPESSLVQTICTLLECLLTP-------ENIPPDSPKETYEVYFAFACVWTFGGTLLRD 1023
Cdd:pfam17852 4 LFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDEvleyngvHPLSPDKLKEYLEKLFLFALVWSIGGTLDED 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1039739712 1024 QlsdyQADFSRWWHKEMKAVKFP--SQGTIFDYYLDHKTKKFLPWTD 1068
Cdd:pfam17852 84 S----RKKFDEFLRELFSGLDLPppEKGTVYDYFVDLEKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
780-915 |
2.23e-11 |
|
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: 63.85 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 780 SVFVVGNAGTGKSKILRTLNRTYVNmkqKPVWSDLNPKAVTTDELFGFIHHATR--EWKDGLFSSILREqanlthdgpTW 857
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSN---RPVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAARE---------GE 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039739712 858 IVLDGDID---PLWIESLNTVMDDNKVLTLASNERVALKP-SMRLLFETHHLRT----ATPATVSR 915
Cdd:pfam07728 69 IAVLDEINranPDVLNSLLSLLDERRLLLPDGGELVKAAPdGFRLIATMNPLDRglneLSPALRSR 134
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1107-1243 |
8.66e-07 |
|
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: 50.75 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1107 PIMLVGNAGVGKTvFLSNTLASLSENYIVSCVPFNYYTTSAALQRILEkPLEKKAGRNYGP---KGNKKLVYFIDDLNMP 1183
Cdd:pfam07728 1 GVLLVGPPGTGKT-ELAERLAAALSNRPVFYVQLTRDTTEEDLFGRRN-IDPGGASWVDGPlvrAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039739712 1184 EVDLYGTIQPhaLL---RQHIDYGHWYDRHKimlKEIRNCqyVACMNP-MVGSFTVNPRLQRHF 1243
Cdd:pfam07728 79 NPDVLNSLLS--LLderRLLLPDGGELVKAA---PDGFRL--IATMNPlDRGLNELSPALRSRF 135
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1677-1801 |
2.58e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1677 LEQISLFKSLLKKKREEVKQKQEHLGNGIQKLQTTASQVGNLKSRLASQEAELQLRNLDAEALITKIGLQTEKVSREKAI 1756
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1039739712 1757 ADAEERKVAAIQTEASQKQRECEADLLKAEPALVAAKDALNTLNR 1801
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
1925-1989 |
5.70e-04 |
|
Laminin Domain II; 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: 368703 [Multi-domain] Cd Length: 138 Bit Score: 42.47 E-value: 5.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039739712 1925 TNLDLAAATEKLEAVRRKLVDLDHNLSRLTASFEKATAEKVRCQEEVNQTNKTIDLANKLVSELE 1989
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLE 65
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
1679-1809 |
6.26e-04 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 43.60 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1679 QISLFKSLLKKKREEVKQKQEHLGNG-IQKLQTTASQVGNLKSRLASQEAELQLRNLDAEALITKIGLQTE--------K 1749
Cdd:pfam14988 1 ENKFFLEYLAKKTEEKQKKIEKLWNQyVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQalrpfaklK 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1750 VSREKAIADAEERKvAAIQTEASQKQRECEADLLKAEPALvaaKDALNTLNRVNLTELKT 1809
Cdd:pfam14988 81 ESQEREIQDLEEEK-EKVRAETAEKDREAHLQFLKEKALL---EKQLQELRILELGERAT 136
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1706-1800 |
7.77e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 44.72 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1706 QKLQTTASQVGNLKSRLASQEAEL-QLRNLDAEALITKIGLQTEKVSREKAIADAEErKVAAIQTEASQKQ----RECEA 1780
Cdd:TIGR04320 247 TPIPNPPNSLAALQAKLATAQADLaAAQTALNTAQAALTSAQTAYAAAQAALATAQK-ELANAQAQALQTAqnnlATAQA 325
|
90 100
....*....|....*....|
gi 1039739712 1781 DLLKAEPALVAAKDALNTLN 1800
Cdd:TIGR04320 326 ALANAEARLAKAKEALANLN 345
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
504-624 |
1.05e-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: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 504 GPAGTGKTETTKDLGRAL-GMMVYVFNCSEQMDY------RSIGNIYKGLV--------QTGAWGCFDEFNRIAVEVLSV 568
Cdd:pfam07728 6 GPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEedlfgrRNIDPGGASWVdgplvraaREGEIAVLDEINRANPDVLNS 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039739712 569 VavqvkmiHDAIRNGRKRFVFLGETIPLKP-SVGIFITLNPGYAGRTELPENLKALF 624
Cdd:pfam07728 86 L-------LSLLDERRLLLPDGGELVKAAPdGFRLIATMNPLDRGLNELSPALRSRF 135
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1674-1808 |
4.24e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1674 RSFLEQISLFKSLLKKKREEVKQKQEHLGNGIQKLQTTasqvgnlKSRLASQEAELQLRNLDAEALITKIGLQTEKVSRE 1753
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQA-------RSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039739712 1754 KAIADAEERKVAAIQTE---ASQKQRECEADLLKAEPALVAAKDALNTLNRvNLTELK 1808
Cdd:COG4372 107 QEEAEELQEELEELQKErqdLEQQRKQLEAQIAELQSEIAEREEELKELEE-QLESLQ 163
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1919-2009 |
6.71e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1919 RQALAQTNLDLAAATEKLEAVRRKLVDLDHNLSRLTASFEKATAEKVRCQEEVNQTNKTIDLANKLVSELESEKIRWGQS 1998
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90
....*....|.
gi 1039739712 1999 IKSFETQEKTL 2009
Cdd:COG4372 131 RKQLEAQIAEL 141
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1678-1808 |
8.14e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1678 EQISLFKSLLKKKREEVKQKQEHLGNGIQKLQTTASQVGNLKSRLASQEAELQLRNLDAEALITKIGLQTEKVSREKAIA 1757
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1039739712 1758 DAEERKVAAIQTEASQKQREceadLLKAEPALVAAKDALNTLNRVNLTELK 1808
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEA----LLEAEAELAEAEEELEELAEELLEALR 393
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1919-2009 |
8.69e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039739712 1919 RQALAQTNLDLAAATEKLEAVRRKLVDLDHNLSRLTASFEKATAEKVRCQEEVNQTNKTIDLANKLVSELESEKIRWGQS 1998
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
90
....*....|.
gi 1039739712 1999 IKSFETQEKTL 2009
Cdd:COG4372 159 LESLQEELAAL 169
|
|
| |
