|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1785-2111 |
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: 652.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1785 YGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGIYVIVVNCSEGLDYKSMGRMYSG 1864
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1865 LAQSGAWGCFDEFNRINIEVLSVVAQQILSILSALTANLTRFYFEGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFR 1944
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1945 PIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLSDEEVLL 2024
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2025 LSMRDMNIAKLTSVDVPLFNAIVQDLFPNIELPVIDYGKLRDTIEQEIREMGLQITPFTLTKVLQLYETKNSRHSTMIVG 2104
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 1720366517 2105 GTGSSKT 2111
Cdd:pfam12774 321 PTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1240-1648 |
5.96e-170 |
|
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: 530.29 E-value: 5.96e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1240 LQILEKELDALQQVWEITRDWEESWNQWKMGCFQTLQTEAMESMAHGLFRRLTRLAKEYKDrnWEIIETTRSKIEQFKRT 1319
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRD--WDVAEELKKKIDDFKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1320 MPLISDLRNPALRERHWDQVKEEVQREFDQESESFTLEQIVKLGMDQHVEKIAEISASATKELAIEVGLQNIAKTWDSTQ 1399
Cdd:pfam08393 79 LPLIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1400 LDIVPYKDKGHHRLRGTEEVFQALEDNQVALSTMKASRFVKAFEKDVDHWERCLSLILEVIEMVLTVQRQWMYLENIFLG 1479
Cdd:pfam08393 159 FELVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1480 EDIRKQLPNESALFDQVNNNWKAIMDRMNKDNNALRSTHYPGLLETLIEMNAILEDIQKSLDMYLETKRHIFPRFYFLSN 1559
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1560 DDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIQKvggsssKWEAVGMFSGDGEYIDFLHP-VLLEGPVESWLGDVERAMR 1638
Cdd:pfam08393 319 DELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE------NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMR 392
|
410
....*....|
gi 1720366517 1639 MTLRDLLRNC 1648
Cdd:pfam08393 393 ETLRDLLKEA 402
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
180-737 |
1.11e-155 |
|
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: 495.94 E-value: 1.11e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 180 VQRLETSMIHWTRQIKEVLSAQESvetGENLGPLEEIEFWHNRCMDLSSISKQLVKKGVKHIESILFLAKSSYLTPFRKL 259
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQ---GRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 260 AQQIQDGSRQAQSNLTFLSILREPYQELAFMK-PKDISEKLPKLISLIRIIWVNSPHYNTRERLTALFRKMSNEIIRLCC 338
Cdd:pfam08385 78 DTELTDALNEAKDNVKYLKTLERPFEDLEELTdPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQCK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 339 HSISLDRIFEGYVNSSKEDLEGCISCCQAWKEHYLRAVQ-MHTQFSNRGWVLDQTSIFAQVDAFVQRCKDLIEVCECQYH 417
Cdd:pfam08385 158 KYLSPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREkLEESPRERPWDFSERYIFGRFDAFLERLEKILELFETIEQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 418 FARWEDGKqgplpcffGAQGPQITRNLLEIEDIFHKNLQTLRAVRGGILDVKNTSWHEDYNKFRGGIKDLEVMTQNLITS 497
Cdd:pfam08385 238 FSKLEKIG--------GTKGPELEGVIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 498 AFELVRDVEHGVLLLDTFHRLATREAIMRTYEKKAVDLYMLFNSELALVNRELNKKW---PYLEPYMTQYSGQAHWVRIL 574
Cdd:pfam08385 310 AFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQKynpSPIAKNMPPVAGAIIWARQL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 575 RRRIDRVMNCLSGAHFLPHIGTGEESIHTYQQMAQAIDEMVRKTFQEWTATLDKDCIRRLDMSLLRISQEKVGMLDVNFD 654
Cdd:pfam08385 390 FRRIQEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGNLKRPLLVRHPETGKLLSVNFD 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 655 KTLLILFAEIDYWERLLFETPHYVMNVAERAEDLRILRENLLLVARDYNRIIAMLSPDEQALFKERIRFLDKKIHPGLKK 734
Cdd:pfam08385 470 PQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTT 549
|
...
gi 1720366517 735 LNW 737
Cdd:pfam08385 550 LTW 552
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1312-4128 |
4.80e-134 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 476.02 E-value: 4.80e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1312 KIEQFKRTMPLISDL-----RNPALRE---RHWDQV----KEEVQREF-DQESESFtleqivkLGMDQHVEKIAEISASA 1378
Cdd:COG5245 486 KLCKIMRMFSFFNSLemfsrRTLANRMaivKYLSSVvrtgPLFLQRDFfGRMSELL-------MARDMFMEVDGVLRLFF 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1379 TKELA--IEVGLQNIAKTWDSTQLDivpykdkghhrlrgtEEVFQALEDNQVALSTMKASRFvkaFEKDVDhWERCLSLI 1456
Cdd:COG5245 559 GGEWSgiVQLSGIRRAKRCVERQID---------------DEIREWCSSVLSDDFLEERAVR---VERGAD-GARRLRAS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1457 LEvIEMVLTVQRQWMYLENiflgEDIRKQLPNESALFDQVNNNWKAIMDRMNKDNNALRSTHYPgLLETLIEMNAILEDI 1536
Cdd:COG5245 620 SG-SPVLRRLDEYLMMMSL----EDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQV 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1537 QKSLDMYLETKRHIFPRFyfLSNDDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIqkvggSSSKWEAVGMFSGDGEYIDF 1616
Cdd:COG5245 694 FMSIEKVLGLRWREVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEEMKTV-----FSSRIQKKEPFSLDSEAYVG 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1617 LHPVLLEGPVESWLGDVERAMRMTLRDllrncrvALKKFLNKRDkwvkdwaGQVVITASQIQ--------WTADVTKCLM 1688
Cdd:COG5245 767 FFRLYEKSIVIRGINRSMGRVLSQYLE-------SVQEALEIED-------GSFFVSRHRVRdgglekgrGCDAWENCFD 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1689 TAKERSDKKILKVMKkkqvSILNKYSEAIRGnltkimrlKIVALVTIEIHARDVLEKLYKSGLMDVSSFDWLSQLRFYwE 1768
Cdd:COG5245 833 PPLSEYFRILEKIFP----SEEGYFFDEVLK--------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-Q 899
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1769 KDVDDCIIRQTNTQFQYGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSpkgpAGTGKTETVKDLGKALGIYVivvn 1848
Cdd:COG5245 900 GLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY---- 971
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1849 csEGLDYKSmgRMYSGLAQSGAWGcFDEFNRINIEVLSVVA--QQILSILSALTANLTRFYFEGFeinLVWSCGIFITMN 1926
Cdd:COG5245 972 --DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVVEHGL---KSPSTPVEMIIN 1043
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1927 PgyagRTELPENLKSMFRPIAMVVPDSTlIAEIIlfgegfgncKILAKKVYTLYSLAVQQLSRQDHYDFglRALTSLLRy 2006
Cdd:COG5245 1044 E----RNIVLEIGRRALDMFLSNIPFGA-IKSRR---------ESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLK- 1106
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2007 agKKRRLQPDLSDEEVLLLSmrdmnIAKLTSVDVPLFNAIvqDLFPNIELPVIdygklRDTIEQEIREMGlQITPFTLTK 2086
Cdd:COG5245 1107 --AKHRMLEEKTEYLNKILS-----ITGLPLISDTLRERI--DTLDAEWDSFC-----RISESLKKYESQ-QVSGLDVAQ 1171
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2087 VLQLYETKNSRHSTMIVGGTGSSKTTSWKIlqasltslcragepnyniVREFPLNPKALSLGELYGEYDLNTNEWTDGIL 2166
Cdd:COG5245 1172 FVSFLRSVDTGAFHAEYFRVFLCKIKHYTD------------------ACDYLWHVKSPYVKKKYFDADMELRQFFLMFN 1233
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2167 SSVMRVACADEKpdeKWILFDGpvdtlWIESMNSVMDDNKVLTLINGERIAMpeqvsllfeVENLAvASPATVSRCGMVY 2246
Cdd:COG5245 1234 REDMEARLADSK---MEYEVER-----YVEKTKAEVSSLKLELSSVGEGQVV---------VSNLG-SIGDKVGRCLVEY 1295
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2247 TDYVDLGWKPYVQSWL--EKRPKTEVEPLQRMFEK-----------FINKILSFKKDnCNELVPVPEYSGIISLCKLYTV 2313
Cdd:COG5245 1296 DSISRLSTKGVFLDELgdTKRYLDECLDFFSCFEEvqkeidelsmvFCADALRFSAD-LYHIVKERRFSGVLAGSDASES 1374
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2314 LATPENGVNpADAENYSFMVEMTFVFSMIWSVCASVDEDgRKKIDSYLREIEGSFPNKDTVYEYY---------VNPKMR 2384
Cdd:COG5245 1375 LGGKSIELA-AILEHKDLIVEMKRGINDVLKLRIFGDKC-RESTPRFYLISDGDLIKDLNERSDYeemlimmfnISAVIT 1452
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2385 TWTSFEEKLPKSWR--YPPNapfykIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSlpSSQWSVLV 2462
Cdd:COG5245 1453 NNGSIAGFELRGERvmLRKE-----VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS--ELITEVKY 1525
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2463 VNMSAQTTSNNVQSIIESRVEK-RTKGVYVPFGG---KSMITFMDDLNMPAKDMFGSQPPLELIR-LWIDYGFWYDrVKQ 2537
Cdd:COG5245 1526 FNFSTCTMTPSKLSVLERETEYyPNTGVVRLYPKpvvKDLVLFCDEINLPYGFEYYPPTVIVFLRpLVERQGFWSS-IAV 1604
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2538 SIKHIRDMFLMAAMGPPGG-GRTVISPRLQSRFNIINMTFPTESQIIRIFGTMINQKLQDFEEEVKPIGNVVTEATlDVY 2616
Cdd:COG5245 1605 SWVTICGIILYGACNPGTDeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASV-ELY 1683
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2617 NTVVQRFlPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTK-ASITRLWIHECFRVFSDRLVDTADMEAFMGILSDKLGT 2695
Cdd:COG5245 1684 LSSKDKT-KFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPdVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLR 1762
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2696 FF-DLTFHHLcpNKRPPIFGDFLKEPKVYEDLVDLTVLktaMETALNEYNLSPSVVPMqlVLFREAIEHITRIVRVIGQP 2774
Cdd:COG5245 1763 AIrEMIAGHI--GEAEITFSMILFFGMACLLKKDLAVF---VEEVRKIFGSSHLDVEA--VAYKDALLHILRSRRGLLVV 1835
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2775 RGNMLLVGIGGSGRQSLARLASSICDYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVELQTTSFLFVDTQIADESFLEDIN 2854
Cdd:COG5245 1836 GGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFN 1915
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2855 NILSSGEVPNLYKSDEFEEIQNHIIDQARAEQIP-ESSDSLFAYLIERVRNNLHIVLCL-SPVGDPFRNWIRqYPALVNC 2932
Cdd:COG5245 1916 PLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEkDTEATLTRVFLVYMEENLPVVFSAcCSQDTSVLAGIR-SPALKNR 1994
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2933 TTINWFSEWPREALLEVAEKYI-----------IGVDLGTQE--NIHRKVAQIFVTMHWSVaqYSQKMLLELrryNYVTP 2999
Cdd:COG5245 1995 CFIDFKKLWDTEEMSQYANSVEtlsrdggrvffINGELGVGKgaLISEVFGDDAVVIEGRG--FEISMIEGS---LGESK 2069
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3000 TNYLELVSGYKKLLGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQ 3079
Cdd:COG5245 2070 IKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVK 2149
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3080 QKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPT 3159
Cdd:COG5245 2150 SVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAK 2229
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3160 -WAEAKRQLGEQNFIKSLINFDKD-NISDKVLKKIGA-YCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPK 3236
Cdd:COG5245 2230 iWFGEQQSLRRDDFIRIIGKYPDEiEFDLEARRFREArECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPL 2309
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3237 RIRMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEET 3316
Cdd:COG5245 2310 REEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGV 2389
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3317 VQGLEEDLGYLVGDCLIAAAFLSYMGPFLTNYRDEIINQIWIRKIRELQVPCSPRFA-IDNFLTNPTKVRDWNIQglpSD 3395
Cdd:COG5245 2390 FSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGMSFIRISKEFRDKEIRRRQfITEGVQKIEDFKEEACS---TD 2466
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3396 AFSTENGIIVTRGNRWALMIDPQGQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQnVQEYLDPTLNPVL 3475
Cdd:COG5245 2467 YGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIG-DAEALDEEIGRLI 2545
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3476 NKSVARIGGRMLIRIGDKEVEYNPNFR-FYLTTKLSNPHYNPEtSAKTTIVNFAVKEQGLEAQLLGIVVRKERPELEEQK 3554
Cdd:COG5245 2546 KEEFKSNLSEVKVMINPPEIVRSTVEAvFWLSEGRSGDMGSIE-WKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHE 2624
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3555 DSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEVTEQLETSETTEINIDLAREAYRPCAQRA 3634
Cdd:COG5245 2625 KALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRL 2704
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3635 SVLFFVLNDMGRIDPMYQFSldayIGLFILSIDKSHRSNKLE-DRIEYLNDYHTYAVYrYTCRTLFErHKLLFSFHMCAK 3713
Cdd:COG5245 2705 ESIRVEIAMFDEKALMYNKS----ICELSSEFEKWRRMKSKYlCAIRYMLMSSEWILD-HEDRSGFI-HRLDVSFLLRTK 2778
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3714 IletsgklnmdeynfFLRGGVVLDREGQMDNPCTSWLADAYWDNITELDKLTNFhglMNSFEQYPRDWHLWYTNSSpeka 3793
Cdd:COG5245 2779 R--------------FVSTLLEDKNYRQVLSSCSLYGNDVISHSCDRFDRDVYR---ALKHQMDNRTHSTILTSNS---- 2837
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3794 mlpgewenACNEMQRMLIVRSLRQ-DRVAFcvtsfivSNLGSRFieppvlnMKSVMEDSTPRSPLVFILSPGVDptsaLL 3872
Cdd:COG5245 2838 --------KTNPYKEYTYNDSWAEaFEVED-------SGDLYKF-------EEGLLELIVGHAPLIYAHKKSLE----NE 2891
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3873 QLAEHTGMAHRfhaLSLGQGQAPIAARllregvnQGHWVFLANCHLSLSWMPN-LDKLVEQLQVEDPHPSF-RLWLSSSP 3950
Cdd:COG5245 2892 RNVDRLGSKEN---EVYAVLNSLFSRK-------EKSWFEVYNISLSFGWFKRyVEDVVYPIKASRVCGKVkNMWTSMVD 2961
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3951 HPDFPISILQASIKMTTEPPKGLKANMTRLYQLMteaQFTHCSKPAKYKKLLFALCFFHSILLERKKFLQLGWNIIYGFN 4030
Cdd:COG5245 2962 ADMLPIQLLIAIDSFVSSTYPETGCGYADLVEID---RYPFDYTLVIACDDAFYLSWEHAAVASVISAGPKENNEEIYFG 3038
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 4031 DSDFEVSENLLS--LYLDEYEETPWDALKYLIAGVNYGGHVTDDWDRRLLTTYINDYFC--DLSLTTPFYRLS-VLDTYY 4105
Cdd:COG5245 3039 DKDFEFKTHLLKniLFLNHLNARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGAheTSSQILASVPGGdPELVKF 3118
|
2890 2900
....*....|....*....|...
gi 1720366517 4106 IPKDGSLASYKEYISMLPSMDPP 4128
Cdd:COG5245 3119 HMEEMCRSSAFGVIGQLPDLALC 3141
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4143-4443 |
4.58e-128 |
|
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: 405.47 E-value: 4.58e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 4143 ITEARTLFETLLSLQPQITPTRVGG-QSREEKVLELAADVKQKIPEMIDYE-GTRKLLALDPSPLNVVLLQEIQRYNKLM 4220
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGgSSREEIVLELAKDILEKLPEPFDIEeAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 4221 KTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLWGKV-YPSQKPLASWTRDLAVRVEQFETWASRARPPVLFWL 4299
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKsYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 4300 SGFTFPTGFLTAVLQSAARQNNISVDSLSWEFIV-STVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVC 4378
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVtKKVSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366517 4379 LMPTIHFRPAE-SRKKSAKGMYSCPCYYYPNRAGSTdrasFVIGIDLRSGsMTSDHWIKRGTALLM 4443
Cdd:pfam18199 241 PLPVIHLKPVEsDKKKLDENTYECPVYKTSERHSTN----FVFSVDLPTD-KPPDHWILRGVALLL 301
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2752-3012 |
9.39e-127 |
|
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: 400.06 E-value: 9.39e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2752 MQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICDYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVE 2831
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2832 LQTTSFLFVDTQIADESFLEDINNILSSGEVPNLYKSDEFEEIQNHIIDQARAEQIPESSDSLFAYLIERVRNNLHIVLC 2911
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2912 LSPVGDPFRNWIRQYPALVNCTTINWFSEWPREALLEVAEKYIigVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLEL 2991
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFL--EDIEIPEELKSNVVKVFVYVHSSVEDMSKKFYEEL 238
|
250 260
....*....|....*....|.
gi 1720366517 2992 RRYNYVTPTNYLELVSGYKKL 3012
Cdd:pfam12780 239 KRKNYVTPKSYLELLRLYKNL 259
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2430-2572 |
1.09e-08 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 57.16 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2430 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPfgGKSMITFMDDLNMPA 2509
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK--AKPGVLFIDEIDSLS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366517 2510 KDMFGSQppLELIRLWIDYGFWYDRVKqsikhirdmFLMAAMGPPGGGrtvISPRLQSRFNII 2572
Cdd:cd00009 98 RGAQNAL--LRVLETLNDLRIDRENVR---------VIGATNRPLLGD---LDRALYDRLDIR 146
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3033-3324 |
1.93e-06 |
|
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: 54.30 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3033 KIDETREKVEVMSLELEDAKKkVAEFQKQCEEY-LVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEA 3111
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAER-YQALLKEKREYeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3112 LPALEEAMRALESLN-------KKDIGEIKsygrppAQVEivmQAVMILRGNEptwAEAKRQLGEQNFIKSLINFDKDNI 3184
Cdd:TIGR02169 271 EQLLEELNKKIKDLGeeeqlrvKEKIGELE------AEIA---SLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3185 sDKVLKKIGAYCAQpdfqpdiigRVSLAAKslcmwvramelygrlyrvVEPKRIRMNAAMAQLQEKQAALAEAQEKLREV 3264
Cdd:TIGR02169 339 -EELEREIEEERKR---------RDKLTEE------------------YAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3265 AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 3324
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2990-3134 |
8.37e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2990 ELRRYNYVTPTNYLELVSGYKKLLGE---KRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL 3066
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366517 3067 VIIVQQKREADEQQKAVtansekiaiEEVKcqaLADNAQKDLEEALPALEEAMRALESLNKKDIGEIK 3134
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKA---------EEAK---KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2430-2488 |
3.30e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 3.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366517 2430 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKG 2488
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG 61
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1785-2111 |
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: 652.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1785 YGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGIYVIVVNCSEGLDYKSMGRMYSG 1864
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1865 LAQSGAWGCFDEFNRINIEVLSVVAQQILSILSALTANLTRFYFEGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFR 1944
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1945 PIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLSDEEVLL 2024
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2025 LSMRDMNIAKLTSVDVPLFNAIVQDLFPNIELPVIDYGKLRDTIEQEIREMGLQITPFTLTKVLQLYETKNSRHSTMIVG 2104
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 1720366517 2105 GTGSSKT 2111
Cdd:pfam12774 321 PTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1240-1648 |
5.96e-170 |
|
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: 530.29 E-value: 5.96e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1240 LQILEKELDALQQVWEITRDWEESWNQWKMGCFQTLQTEAMESMAHGLFRRLTRLAKEYKDrnWEIIETTRSKIEQFKRT 1319
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRD--WDVAEELKKKIDDFKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1320 MPLISDLRNPALRERHWDQVKEEVQREFDQESESFTLEQIVKLGMDQHVEKIAEISASATKELAIEVGLQNIAKTWDSTQ 1399
Cdd:pfam08393 79 LPLIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1400 LDIVPYKDKGHHRLRGTEEVFQALEDNQVALSTMKASRFVKAFEKDVDHWERCLSLILEVIEMVLTVQRQWMYLENIFLG 1479
Cdd:pfam08393 159 FELVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1480 EDIRKQLPNESALFDQVNNNWKAIMDRMNKDNNALRSTHYPGLLETLIEMNAILEDIQKSLDMYLETKRHIFPRFYFLSN 1559
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1560 DDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIQKvggsssKWEAVGMFSGDGEYIDFLHP-VLLEGPVESWLGDVERAMR 1638
Cdd:pfam08393 319 DELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE------NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMR 392
|
410
....*....|
gi 1720366517 1639 MTLRDLLRNC 1648
Cdd:pfam08393 393 ETLRDLLKEA 402
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
180-737 |
1.11e-155 |
|
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: 495.94 E-value: 1.11e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 180 VQRLETSMIHWTRQIKEVLSAQESvetGENLGPLEEIEFWHNRCMDLSSISKQLVKKGVKHIESILFLAKSSYLTPFRKL 259
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQ---GRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 260 AQQIQDGSRQAQSNLTFLSILREPYQELAFMK-PKDISEKLPKLISLIRIIWVNSPHYNTRERLTALFRKMSNEIIRLCC 338
Cdd:pfam08385 78 DTELTDALNEAKDNVKYLKTLERPFEDLEELTdPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQCK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 339 HSISLDRIFEGYVNSSKEDLEGCISCCQAWKEHYLRAVQ-MHTQFSNRGWVLDQTSIFAQVDAFVQRCKDLIEVCECQYH 417
Cdd:pfam08385 158 KYLSPEGIFDGDVEEALEKLQECIELLEAWKEEYKKTREkLEESPRERPWDFSERYIFGRFDAFLERLEKILELFETIEQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 418 FARWEDGKqgplpcffGAQGPQITRNLLEIEDIFHKNLQTLRAVRGGILDVKNTSWHEDYNKFRGGIKDLEVMTQNLITS 497
Cdd:pfam08385 238 FSKLEKIG--------GTKGPELEGVIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 498 AFELVRDVEHGVLLLDTFHRLATREAIMRTYEKKAVDLYMLFNSELALVNRELNKKW---PYLEPYMTQYSGQAHWVRIL 574
Cdd:pfam08385 310 AFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQKynpSPIAKNMPPVAGAIIWARQL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 575 RRRIDRVMNCLSGAHFLPHIGTGEESIHTYQQMAQAIDEMVRKTFQEWTATLDKDCIRRLDMSLLRISQEKVGMLDVNFD 654
Cdd:pfam08385 390 FRRIQEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGNLKRPLLVRHPETGKLLSVNFD 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 655 KTLLILFAEIDYWERLLFETPHYVMNVAERAEDLRILRENLLLVARDYNRIIAMLSPDEQALFKERIRFLDKKIHPGLKK 734
Cdd:pfam08385 470 PQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTT 549
|
...
gi 1720366517 735 LNW 737
Cdd:pfam08385 550 LTW 552
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1312-4128 |
4.80e-134 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 476.02 E-value: 4.80e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1312 KIEQFKRTMPLISDL-----RNPALRE---RHWDQV----KEEVQREF-DQESESFtleqivkLGMDQHVEKIAEISASA 1378
Cdd:COG5245 486 KLCKIMRMFSFFNSLemfsrRTLANRMaivKYLSSVvrtgPLFLQRDFfGRMSELL-------MARDMFMEVDGVLRLFF 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1379 TKELA--IEVGLQNIAKTWDSTQLDivpykdkghhrlrgtEEVFQALEDNQVALSTMKASRFvkaFEKDVDhWERCLSLI 1456
Cdd:COG5245 559 GGEWSgiVQLSGIRRAKRCVERQID---------------DEIREWCSSVLSDDFLEERAVR---VERGAD-GARRLRAS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1457 LEvIEMVLTVQRQWMYLENiflgEDIRKQLPNESALFDQVNNNWKAIMDRMNKDNNALRSTHYPgLLETLIEMNAILEDI 1536
Cdd:COG5245 620 SG-SPVLRRLDEYLMMMSL----EDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQV 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1537 QKSLDMYLETKRHIFPRFyfLSNDDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIqkvggSSSKWEAVGMFSGDGEYIDF 1616
Cdd:COG5245 694 FMSIEKVLGLRWREVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEEMKTV-----FSSRIQKKEPFSLDSEAYVG 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1617 LHPVLLEGPVESWLGDVERAMRMTLRDllrncrvALKKFLNKRDkwvkdwaGQVVITASQIQ--------WTADVTKCLM 1688
Cdd:COG5245 767 FFRLYEKSIVIRGINRSMGRVLSQYLE-------SVQEALEIED-------GSFFVSRHRVRdgglekgrGCDAWENCFD 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1689 TAKERSDKKILKVMKkkqvSILNKYSEAIRGnltkimrlKIVALVTIEIHARDVLEKLYKSGLMDVSSFDWLSQLRFYwE 1768
Cdd:COG5245 833 PPLSEYFRILEKIFP----SEEGYFFDEVLK--------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-Q 899
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1769 KDVDDCIIRQTNTQFQYGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSpkgpAGTGKTETVKDLGKALGIYVivvn 1848
Cdd:COG5245 900 GLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY---- 971
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1849 csEGLDYKSmgRMYSGLAQSGAWGcFDEFNRINIEVLSVVA--QQILSILSALTANLTRFYFEGFeinLVWSCGIFITMN 1926
Cdd:COG5245 972 --DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVVEHGL---KSPSTPVEMIIN 1043
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1927 PgyagRTELPENLKSMFRPIAMVVPDSTlIAEIIlfgegfgncKILAKKVYTLYSLAVQQLSRQDHYDFglRALTSLLRy 2006
Cdd:COG5245 1044 E----RNIVLEIGRRALDMFLSNIPFGA-IKSRR---------ESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLK- 1106
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2007 agKKRRLQPDLSDEEVLLLSmrdmnIAKLTSVDVPLFNAIvqDLFPNIELPVIdygklRDTIEQEIREMGlQITPFTLTK 2086
Cdd:COG5245 1107 --AKHRMLEEKTEYLNKILS-----ITGLPLISDTLRERI--DTLDAEWDSFC-----RISESLKKYESQ-QVSGLDVAQ 1171
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2087 VLQLYETKNSRHSTMIVGGTGSSKTTSWKIlqasltslcragepnyniVREFPLNPKALSLGELYGEYDLNTNEWTDGIL 2166
Cdd:COG5245 1172 FVSFLRSVDTGAFHAEYFRVFLCKIKHYTD------------------ACDYLWHVKSPYVKKKYFDADMELRQFFLMFN 1233
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2167 SSVMRVACADEKpdeKWILFDGpvdtlWIESMNSVMDDNKVLTLINGERIAMpeqvsllfeVENLAvASPATVSRCGMVY 2246
Cdd:COG5245 1234 REDMEARLADSK---MEYEVER-----YVEKTKAEVSSLKLELSSVGEGQVV---------VSNLG-SIGDKVGRCLVEY 1295
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2247 TDYVDLGWKPYVQSWL--EKRPKTEVEPLQRMFEK-----------FINKILSFKKDnCNELVPVPEYSGIISLCKLYTV 2313
Cdd:COG5245 1296 DSISRLSTKGVFLDELgdTKRYLDECLDFFSCFEEvqkeidelsmvFCADALRFSAD-LYHIVKERRFSGVLAGSDASES 1374
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2314 LATPENGVNpADAENYSFMVEMTFVFSMIWSVCASVDEDgRKKIDSYLREIEGSFPNKDTVYEYY---------VNPKMR 2384
Cdd:COG5245 1375 LGGKSIELA-AILEHKDLIVEMKRGINDVLKLRIFGDKC-RESTPRFYLISDGDLIKDLNERSDYeemlimmfnISAVIT 1452
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2385 TWTSFEEKLPKSWR--YPPNapfykIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSlpSSQWSVLV 2462
Cdd:COG5245 1453 NNGSIAGFELRGERvmLRKE-----VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS--ELITEVKY 1525
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2463 VNMSAQTTSNNVQSIIESRVEK-RTKGVYVPFGG---KSMITFMDDLNMPAKDMFGSQPPLELIR-LWIDYGFWYDrVKQ 2537
Cdd:COG5245 1526 FNFSTCTMTPSKLSVLERETEYyPNTGVVRLYPKpvvKDLVLFCDEINLPYGFEYYPPTVIVFLRpLVERQGFWSS-IAV 1604
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2538 SIKHIRDMFLMAAMGPPGG-GRTVISPRLQSRFNIINMTFPTESQIIRIFGTMINQKLQDFEEEVKPIGNVVTEATlDVY 2616
Cdd:COG5245 1605 SWVTICGIILYGACNPGTDeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASV-ELY 1683
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2617 NTVVQRFlPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTK-ASITRLWIHECFRVFSDRLVDTADMEAFMGILSDKLGT 2695
Cdd:COG5245 1684 LSSKDKT-KFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPdVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLR 1762
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2696 FF-DLTFHHLcpNKRPPIFGDFLKEPKVYEDLVDLTVLktaMETALNEYNLSPSVVPMqlVLFREAIEHITRIVRVIGQP 2774
Cdd:COG5245 1763 AIrEMIAGHI--GEAEITFSMILFFGMACLLKKDLAVF---VEEVRKIFGSSHLDVEA--VAYKDALLHILRSRRGLLVV 1835
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2775 RGNMLLVGIGGSGRQSLARLASSICDYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVELQTTSFLFVDTQIADESFLEDIN 2854
Cdd:COG5245 1836 GGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFN 1915
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2855 NILSSGEVPNLYKSDEFEEIQNHIIDQARAEQIP-ESSDSLFAYLIERVRNNLHIVLCL-SPVGDPFRNWIRqYPALVNC 2932
Cdd:COG5245 1916 PLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEkDTEATLTRVFLVYMEENLPVVFSAcCSQDTSVLAGIR-SPALKNR 1994
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2933 TTINWFSEWPREALLEVAEKYI-----------IGVDLGTQE--NIHRKVAQIFVTMHWSVaqYSQKMLLELrryNYVTP 2999
Cdd:COG5245 1995 CFIDFKKLWDTEEMSQYANSVEtlsrdggrvffINGELGVGKgaLISEVFGDDAVVIEGRG--FEISMIEGS---LGESK 2069
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3000 TNYLELVSGYKKLLGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQ 3079
Cdd:COG5245 2070 IKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVK 2149
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3080 QKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPT 3159
Cdd:COG5245 2150 SVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAK 2229
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3160 -WAEAKRQLGEQNFIKSLINFDKD-NISDKVLKKIGA-YCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPK 3236
Cdd:COG5245 2230 iWFGEQQSLRRDDFIRIIGKYPDEiEFDLEARRFREArECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPL 2309
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3237 RIRMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEET 3316
Cdd:COG5245 2310 REEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGV 2389
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3317 VQGLEEDLGYLVGDCLIAAAFLSYMGPFLTNYRDEIINQIWIRKIRELQVPCSPRFA-IDNFLTNPTKVRDWNIQglpSD 3395
Cdd:COG5245 2390 FSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGMSFIRISKEFRDKEIRRRQfITEGVQKIEDFKEEACS---TD 2466
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3396 AFSTENGIIVTRGNRWALMIDPQGQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQnVQEYLDPTLNPVL 3475
Cdd:COG5245 2467 YGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIG-DAEALDEEIGRLI 2545
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3476 NKSVARIGGRMLIRIGDKEVEYNPNFR-FYLTTKLSNPHYNPEtSAKTTIVNFAVKEQGLEAQLLGIVVRKERPELEEQK 3554
Cdd:COG5245 2546 KEEFKSNLSEVKVMINPPEIVRSTVEAvFWLSEGRSGDMGSIE-WKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHE 2624
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3555 DSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEVTEQLETSETTEINIDLAREAYRPCAQRA 3634
Cdd:COG5245 2625 KALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRL 2704
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3635 SVLFFVLNDMGRIDPMYQFSldayIGLFILSIDKSHRSNKLE-DRIEYLNDYHTYAVYrYTCRTLFErHKLLFSFHMCAK 3713
Cdd:COG5245 2705 ESIRVEIAMFDEKALMYNKS----ICELSSEFEKWRRMKSKYlCAIRYMLMSSEWILD-HEDRSGFI-HRLDVSFLLRTK 2778
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3714 IletsgklnmdeynfFLRGGVVLDREGQMDNPCTSWLADAYWDNITELDKLTNFhglMNSFEQYPRDWHLWYTNSSpeka 3793
Cdd:COG5245 2779 R--------------FVSTLLEDKNYRQVLSSCSLYGNDVISHSCDRFDRDVYR---ALKHQMDNRTHSTILTSNS---- 2837
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3794 mlpgewenACNEMQRMLIVRSLRQ-DRVAFcvtsfivSNLGSRFieppvlnMKSVMEDSTPRSPLVFILSPGVDptsaLL 3872
Cdd:COG5245 2838 --------KTNPYKEYTYNDSWAEaFEVED-------SGDLYKF-------EEGLLELIVGHAPLIYAHKKSLE----NE 2891
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3873 QLAEHTGMAHRfhaLSLGQGQAPIAARllregvnQGHWVFLANCHLSLSWMPN-LDKLVEQLQVEDPHPSF-RLWLSSSP 3950
Cdd:COG5245 2892 RNVDRLGSKEN---EVYAVLNSLFSRK-------EKSWFEVYNISLSFGWFKRyVEDVVYPIKASRVCGKVkNMWTSMVD 2961
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3951 HPDFPISILQASIKMTTEPPKGLKANMTRLYQLMteaQFTHCSKPAKYKKLLFALCFFHSILLERKKFLQLGWNIIYGFN 4030
Cdd:COG5245 2962 ADMLPIQLLIAIDSFVSSTYPETGCGYADLVEID---RYPFDYTLVIACDDAFYLSWEHAAVASVISAGPKENNEEIYFG 3038
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 4031 DSDFEVSENLLS--LYLDEYEETPWDALKYLIAGVNYGGHVTDDWDRRLLTTYINDYFC--DLSLTTPFYRLS-VLDTYY 4105
Cdd:COG5245 3039 DKDFEFKTHLLKniLFLNHLNARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGAheTSSQILASVPGGdPELVKF 3118
|
2890 2900
....*....|....*....|...
gi 1720366517 4106 IPKDGSLASYKEYISMLPSMDPP 4128
Cdd:COG5245 3119 HMEEMCRSSAFGVIGQLPDLALC 3141
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4143-4443 |
4.58e-128 |
|
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: 405.47 E-value: 4.58e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 4143 ITEARTLFETLLSLQPQITPTRVGG-QSREEKVLELAADVKQKIPEMIDYE-GTRKLLALDPSPLNVVLLQEIQRYNKLM 4220
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGgSSREEIVLELAKDILEKLPEPFDIEeAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 4221 KTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLWGKV-YPSQKPLASWTRDLAVRVEQFETWASRARPPVLFWL 4299
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKsYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 4300 SGFTFPTGFLTAVLQSAARQNNISVDSLSWEFIV-STVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVC 4378
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVtKKVSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366517 4379 LMPTIHFRPAE-SRKKSAKGMYSCPCYYYPNRAGSTdrasFVIGIDLRSGsMTSDHWIKRGTALLM 4443
Cdd:pfam18199 241 PLPVIHLKPVEsDKKKLDENTYECPVYKTSERHSTN----FVFSVDLPTD-KPPDHWILRGVALLL 301
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2752-3012 |
9.39e-127 |
|
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: 400.06 E-value: 9.39e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2752 MQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICDYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVE 2831
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2832 LQTTSFLFVDTQIADESFLEDINNILSSGEVPNLYKSDEFEEIQNHIIDQARAEQIPESSDSLFAYLIERVRNNLHIVLC 2911
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2912 LSPVGDPFRNWIRQYPALVNCTTINWFSEWPREALLEVAEKYIigVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLEL 2991
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFL--EDIEIPEELKSNVVKVFVYVHSSVEDMSKKFYEEL 238
|
250 260
....*....|....*....|.
gi 1720366517 2992 RRYNYVTPTNYLELVSGYKKL 3012
Cdd:pfam12780 239 KRKNYVTPKSYLELLRLYKNL 259
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3385-3606 |
5.95e-125 |
|
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: 392.96 E-value: 5.95e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3385 RDWNIQGLPSDAFSTENGIIVTRGNRWALMIDPQGQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQNVQ 3464
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3465 EYLDPTLNPVLNKSVARIGGRMLIRIGDKEVEYNPNFRFYLTTKLSNPHYNPETSAKTTIVNFAVKEQGLEAQLLGIVVR 3544
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366517 3545 KERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEV 3606
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2399-2577 |
1.48e-103 |
|
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: 329.74 E-value: 1.48e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2399 YPPNAPFYKIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSII 2478
Cdd:pfam12775 1 IPPDVPFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQDII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2479 ESRVEKRTKGVYVPFGGKSMITFMDDLNMPAKDMFGSQPPLELIRLWIDYGFWYDRVKQSIKHIRDMFLMAAMGPPGGGR 2558
Cdd:pfam12775 81 ESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPGGGR 160
|
170
....*....|....*....
gi 1720366517 2559 TVISPRLQSRFNIINMTFP 2577
Cdd:pfam12775 161 NDITPRLLRHFNVFNITFP 179
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
3998-4137 |
3.50e-73 |
|
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: 241.20 E-value: 3.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3998 YKKLLFALCFFHSILLERKKFLQLGWNIIYGFNDSDFEVSENLLSLYLDEY-EETPWDALKYLIAGVNYGGHVTDDWDRR 4076
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYdEKIPWDALRYLIGEINYGGRVTDDWDRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366517 4077 LLTTYINDYFCDlSLTTPFYRLSVlDTYYIPKDGSLASYKEYISMLPSMDPPEAFGQHPNA 4137
Cdd:pfam18198 81 LLNTYLEEFFNP-EVLEEDFKFSP-SLYYIPPDGDLEDYLEYIESLPLVDSPEVFGLHPNA 139
|
|
| Dynein_heavy |
pfam03028 |
Dynein heavy chain region D6 P-loop domain; This family represents the C-terminal region of ... |
3852-3966 |
1.70e-63 |
|
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: 212.30 E-value: 1.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3852 TPRSPLVFILSPGVDPTSALLQLAEHTGMAHRFHALSLGQGQAPIAARLLREGVNQGHWVFLANCHLSLSWMPNLDKLVE 3931
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGFGGKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILE 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1720366517 3932 QLQVEDPHPSFRLWLSSSPHPDFPISILQASIKMT 3966
Cdd:pfam03028 81 ELPEETLHPDFRLWLTSEPSPKFPISILQNSIKIT 115
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
3026-3358 |
3.07e-57 |
|
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: 203.77 E-value: 3.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3026 KLRTGLFKIDETREKVEvmsleleDAKKKVA----EFQKQCE--EYLVIIVQQKREADEQQKAVTANSE-KIAIEEVKCQ 3098
Cdd:pfam12777 2 RLENGLLKLHSTAAQVD-------DLKAKLAaqeaELKQKNEdaDKLIQVVGIEADKVSKEKAIADEEEqKVAVIMKEVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3099 ALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMIL---RGNEP---TWAEAKRQLGE-QN 3171
Cdd:pfam12777 75 EKQKACEEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILmapGGKIPkdkSWKAAKIMMAKvDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3172 FIKSLINFDKDNISDKVLKKIGAYCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRIRMNAAMAQLQEKQ 3251
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3252 AALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDC 3331
Cdd:pfam12777 235 EKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDI 314
|
330 340
....*....|....*....|....*..
gi 1720366517 3332 LIAAAFLSYMGPFLTNYRDEIINQIWI 3358
Cdd:pfam12777 315 LLISAFISYLGFFTKKYRNELLDKFWI 341
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2273-2391 |
3.28e-31 |
|
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: 120.85 E-value: 3.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2273 LQRMFEKFINKILSFKKDNCNELVPVPEYSGIISLCKLYTVLATP---ENGVNPADAENYSFMVEMTFVFSMIWSVCASV 2349
Cdd:pfam17852 1 LEPLFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDEvleYNGVHPLSPDKLKEYLEKLFLFALVWSIGGTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1720366517 2350 DEDGRKKIDSYLREIEGS----FPNKDTVYEYYVNPKMRTWTSFEE 2391
Cdd:pfam17852 81 DEDSRKKFDEFLRELFSGldlpPPEKGTVYDYFVDLEKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2431-2569 |
5.54e-25 |
|
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: 103.14 E-value: 5.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2431 PVLLVGPVGTGKTSIAQSVLQSLpsSQWSVLVVNMSAQTTSNNVQSIIESRVE--KRTKGVYVPFGGKSMITFMDDLNMP 2508
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL--SNRPVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366517 2509 AKDMFGSQ-PPLELIRLWIDYGFWYDRVKQSikhirDMFLMAAMGPPGGGRTVISPRLQSRF 2569
Cdd:pfam07728 79 NPDVLNSLlSLLDERRLLLPDGGELVKAAPD-----GFRLIATMNPLDRGLNELSPALRSRF 135
|
|
| AAA_lid_1 |
pfam17857 |
AAA+ lid domain; This domain represents the AAA lid domain from dynein heavy chain D3. |
2610-2698 |
7.14e-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: 78.82 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2610 EATLDVYNTVVQRFLPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTKASITRLWIHECFRVFSDRLVDTADMEAFMGIL 2689
Cdd:pfam17857 3 AAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDKIQ 82
|
....*....
gi 1720366517 2690 SDKLGTFFD 2698
Cdd:pfam17857 83 MASLKKFFD 91
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2430-2572 |
1.09e-08 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 57.16 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2430 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPfgGKSMITFMDDLNMPA 2509
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK--AKPGVLFIDEIDSLS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366517 2510 KDMFGSQppLELIRLWIDYGFWYDRVKqsikhirdmFLMAAMGPPGGGrtvISPRLQSRFNII 2572
Cdd:cd00009 98 RGAQNAL--LRVLETLNDLRIDRENVR---------VIGATNRPLLGD---LDRALYDRLDIR 146
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2958-3291 |
7.94e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.50 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2958 DLGTQ-ENihRKVAQIFVTMHwsvaqySQKMLLELRRYNYVTPTNYLELvsgykkllgEKRQELLDQANKLRTGLFKIDE 3036
Cdd:pfam05483 475 DLKTElEK--EKLKNIELTAH------CDKLLLENKELTQEASDMTLEL---------KKHQEDIINCKKQEERMLKQIE 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3037 TREKVEV-MSLELEDAKKkvaEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIAIEEVKCqalaDNAQKDLEEALPAL 3115
Cdd:pfam05483 538 NLEEKEMnLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC----NNLKKQIENKNKNI 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3116 EEAMRALESLNKKDIGEIKsygrppaQVEIVMQAVMILrgnEPTWAEAKRQLGE--QNFIKSLinFDKDNISDKVLKKIG 3193
Cdd:pfam05483 611 EELHQENKALKKKGSAENK-------QLNAYEIKVNKL---ELELASAKQKFEEiiDNYQKEI--EDKKISEEKLLEEVE 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3194 AYCAQPD----FQPDIIGRVSlaaKSLCMWVRAMELYGRLY-RVVEPKRIRMNAAMAQLQEKQAALAEAQEKLREVAEKL 3268
Cdd:pfam05483 679 KAKAIADeavkLQKEIDKRCQ---HKIAEMVALMEKHKHQYdKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAEL 755
|
330 340
....*....|....*....|...
gi 1720366517 3269 EMLKKQYDEKLAQKEELRKKSEE 3291
Cdd:pfam05483 756 LSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3033-3324 |
1.93e-06 |
|
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: 54.30 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3033 KIDETREKVEVMSLELEDAKKkVAEFQKQCEEY-LVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEA 3111
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAER-YQALLKEKREYeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3112 LPALEEAMRALESLN-------KKDIGEIKsygrppAQVEivmQAVMILRGNEptwAEAKRQLGEQNFIKSLINFDKDNI 3184
Cdd:TIGR02169 271 EQLLEELNKKIKDLGeeeqlrvKEKIGELE------AEIA---SLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3185 sDKVLKKIGAYCAQpdfqpdiigRVSLAAKslcmwvramelygrlyrvVEPKRIRMNAAMAQLQEKQAALAEAQEKLREV 3264
Cdd:TIGR02169 339 -EELEREIEEERKR---------RDKLTEE------------------YAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3265 AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 3324
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2990-3134 |
8.37e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 2990 ELRRYNYVTPTNYLELVSGYKKLLGE---KRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL 3066
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366517 3067 VIIVQQKREADEQQKAVtansekiaiEEVKcqaLADNAQKDLEEALPALEEAMRALESLNKKDIGEIK 3134
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKA---------EEAK---KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1822-1943 |
1.62e-05 |
|
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: 47.29 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1822 KGPAGTGKTETVKDLGKALGIY-VIVVNCSE---------GLDYKSMG--RMYSGL---AQSGAWGCFDEFNRINIEVLS 1886
Cdd:pfam07728 5 VGPPGTGKTELAERLAAALSNRpVFYVQLTRdtteedlfgRRNIDPGGasWVDGPLvraAREGEIAVLDEINRANPDVLN 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366517 1887 VVaqqiLSILSA----LTANLTRFYFEGFEINLVwscgifITMNPGYAGRTELPENLKSMF 1943
Cdd:pfam07728 85 SL----LSLLDErrllLPDGGELVKAAPDGFRLI------ATMNPLDRGLNELSPALRSRF 135
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3034-3298 |
2.00e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3034 IDETREKVEVMSLELEDAKKKVAEFQKQCE--EYLVII------VQQKREADEQ---QKAVTANSEKIAIEEVKCQA--L 3100
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLEraEDLVEAedrierLEERREDLEEliaERRETIEEKRERAEELRERAaeL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3101 ADNAQKDLEEALPALEEAMRALESLNK--KDIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAKRQLGEQNfiksliN 3178
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAElnSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELN------D 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3179 FDKDNISDKVLKKigaycaqpdfqpdiigrVSLAAKslcmwvramelygrlyrvVEPKRIrmNAAMAQLQEKQAALAEAQ 3258
Cdd:PRK02224 624 ERRERLAEKRERK-----------------RELEAE------------------FDEARI--EEAREDKERAEEYLEQVE 666
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1720366517 3259 EKLREVAEKLEMLKKQ---YDEKLAQKEELRKKSEEMELKLER 3298
Cdd:PRK02224 667 EKLDELREERDDLQAEigaVENELEELEELRERREALENRVEA 709
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3013-3327 |
2.14e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3013 LGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL--VIIVQQKREADEQQKAVTANSEKI 3090
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrLEELEERHELYEEAKAKKEELERL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3091 AiEEVKCQALaDNAQKDLEEALPALEEAMRALESLNKKdIGEIKSygrppaQVEIVMQAVMILRGNEPTWAEAKRQLGEQ 3170
Cdd:PRK03918 378 K-KRLTGLTP-EKLEKELEELEKAKEEIEEEISKITAR-IGELKK------EIKELKKAIEELKKAKGKCPVCGRELTEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3171 nfikslinfDKDNISDKVLKKIGaycaqpDFQPDIIgrvSLAAKSLCMWVRAMELYGRLYRvvEPKRIRMNAAMAQLQEK 3250
Cdd:PRK03918 449 ---------HRKELLEEYTAELK------RIEKELK---EIEEKERKLRKELRELEKVLKK--ESELIKLKELAEQLKEL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3251 QAALAEAQ-EKLREVAEKLEMLKKQYD----------EKLAQKEELRKKSEEMELKLERAGMLVSGLAGE-KARWEETVQ 3318
Cdd:PRK03918 509 EEKLKKYNlEELEKKAEEYEKLKEKLIklkgeikslkKELEKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVE 588
|
....*....
gi 1720366517 3319 GLEEDLGYL 3327
Cdd:PRK03918 589 ELEERLKEL 597
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
3018-3128 |
5.41e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3018 QELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIaieeVKC 3097
Cdd:COG1340 146 EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEI----VEA 221
|
90 100 110
....*....|....*....|....*....|.
gi 1720366517 3098 QALADNAQKDLEEALPALEEAMRALESLNKK 3128
Cdd:COG1340 222 QEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3015-3121 |
5.94e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3015 EKRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQ-KREADEQQKAVTANSEKIAiE 3093
Cdd:PRK09510 91 ELQQKQAAEQERLK----QLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAaKAKAEAEAKRAAAAAKKAA-A 165
|
90 100
....*....|....*....|....*...
gi 1720366517 3094 EVKCQALADNAQKDLEEALPALEEAMRA 3121
Cdd:PRK09510 166 EAKKKAEAEAAKKAAAEAKKKAEAEAAA 193
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3013-3306 |
6.92e-05 |
|
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: 49.28 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3013 LGEKRQELLDQANKLRTGLF----KIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVII---VQQKREADEQQKAVTA 3085
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEeltaELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrlEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3086 NSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKdigeiksygrppaqveivmqavmiLRGNEPTWAEAKR 3165
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE------------------------LEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3166 QLGEQNfiKSLINFDKDniSDKVLKKIGAycaqpdfqpdIIGRVSLAAKSLCMWVRAMElygRLYRVVE-----PKRIRM 3240
Cdd:TIGR02168 373 RLEELE--EQLETLRSK--VAQLELQIAS----------LNNEIERLEARLERLEDRRE---RLQQEIEellkkLEEAEL 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366517 3241 NAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKlaqKEELRKKSEEMELKLERAGMLVSGL 3306
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEA---EQALDAAERELAQLQARLDSLERLQ 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3003-3333 |
7.92e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3003 LELVSGYKKLLGEKRQELLDQANKLRTglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL-VIIVQQKREADEQQK 3081
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEA---ELEELRLELEELELELEEAQAEEYELLAELARLEqDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3082 AVTANSEKIAIEEV--KCQALADNAQKDLEEALPALEEAMRALESLNKkdigeiksygrppAQVEIVMQAVMILRGNEPT 3159
Cdd:COG1196 318 LEELEEELAELEEEleELEEELEELEEELEEAEEELEEAEAELAEAEE-------------ALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3160 WAEAKRQLGEQNFIKSLINFDKDNISDKVLKKIgaycaqpdfqpdiigrvslaakslcmwvRAMELYGRLYRVVEPKRIR 3239
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLE----------------------------RLEEELEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3240 MNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQG 3319
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
330
....*....|....
gi 1720366517 3320 LEEDLGYLVGDCLI 3333
Cdd:COG1196 517 AGLRGLAGAVAVLI 530
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3239-3297 |
8.13e-05 |
|
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: 47.23 E-value: 8.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366517 3239 RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLA----QKEELRKKSEEMELKLE 3297
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAeleaELEELEAEREELAAKIP 173
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3033-3318 |
8.31e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3033 KIDETREKVEVMSLELEDAKKKVAEFQKQceeylviIVQQKREADEQQKAVTANSEKIaieevkcqalaDNAQKDLEEAL 3112
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAE-------LEELNEEYNELQAELEALQAEI-----------DKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3113 PALEEAMRALeslnKKDIGEIKSYGRPPAQVEIVMQAvmilrgneptwaeakrqlgeqnfikslinfdkDNISDkVLKKI 3192
Cdd:COG3883 79 AEIEERREEL----GERARALYRSGGSVSYLDVLLGS--------------------------------ESFSD-FLDRL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3193 GAYCAQPDFQPDIIGRVslaakslcmwvramelygrlyrvvepkrirmNAAMAQLQEKQAALAEAQEKLREVAEKLEMLK 3272
Cdd:COG3883 122 SALSKIADADADLLEEL-------------------------------KADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720366517 3273 KQYDEKLAQKEELRK--KSEEMELKLERAGMLVSGLAGEKARWEETVQ 3318
Cdd:COG3883 171 AELEAQQAEQEALLAqlSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
3239-3299 |
1.04e-04 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 44.50 E-value: 1.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366517 3239 RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYD---EKLA-QKEELRKKSEEMELKLERA 3299
Cdd:pfam18595 51 KLEEAKKKLKELRDALEEKEIELRELERREERLQRQLEnaqEKLErLREQAEEKREAAQARLEEL 115
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3072-3324 |
1.62e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3072 QKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKkdigEIKSygrppAQVEIvmqavm 3151
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----EIAE-----AEAEI------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3152 ilrgneptwAEAKRQLGEQnfIKSLinfdkdNISDKVLKKIGAYCAQPDFQpDIIGRVSLaakslcmwvramelygrLYR 3231
Cdd:COG3883 82 ---------EERREELGER--ARAL------YRSGGSVSYLDVLLGSESFS-DFLDRLSA-----------------LSK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3232 VVEpkriRMNAAMAQLQEKQAALAEAQEKLREVAEKLEmlkkqydeklAQKEELRKKSEEMELKLERAGMLVSGLAGEKA 3311
Cdd:COG3883 127 IAD----ADADLLEELKADKAELEAKKAELEAKLAELE----------ALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
250
....*....|...
gi 1720366517 3312 RWEETVQGLEEDL 3324
Cdd:COG3883 193 AAEAQLAELEAEL 205
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3013-3324 |
1.87e-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: 48.13 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3013 LGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEyLVIIVQQKREADEQQKAVTANSEKIAI 3092
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGLSG 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3093 EEvkcQALAD--NAQKDLEEALP-ALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAKRQLGE 3169
Cdd:TIGR02168 521 IL---GVLSEliSVDEGYEAAIEaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3170 QNFIKSLINFDKdnisdkvlkkigaycAQPDFQPDIIGRVS--LAAKSLcmwVRAMELYGRL---YRVVEP--KRIRMNA 3242
Cdd:TIGR02168 598 EGFLGVAKDLVK---------------FDPKLRKALSYLLGgvLVVDDL---DNALELAKKLrpgYRIVTLdgDLVRPGG 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3243 AMAQLQEKQAALAEAQEK-LREVAEKLEMLKKQYDEKLAQKEELRKKSEEME-------LKLERAGMLVSGLAGEKARWE 3314
Cdd:TIGR02168 660 VITGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlrKELEELSRQISALRKDLARLE 739
|
330
....*....|
gi 1720366517 3315 ETVQGLEEDL 3324
Cdd:TIGR02168 740 AEVEQLEERI 749
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3239-3324 |
2.60e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3239 RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQ 3318
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
....*.
gi 1720366517 3319 GLEEDL 3324
Cdd:COG1196 313 ELEERL 318
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2430-2488 |
3.30e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 3.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366517 2430 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKG 2488
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG 61
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3239-3324 |
3.94e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3239 RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQ 3318
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
....*.
gi 1720366517 3319 GLEEDL 3324
Cdd:COG4372 161 SLQEEL 166
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
3239-3324 |
6.62e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 42.63 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3239 RMNAAMAQLQEKQAALAEAQEKL-REV------AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAgmlvsglageKA 3311
Cdd:pfam07926 23 QLQKLQEDLEKQAEIAREAQQNYeRELvlhaedIKALQALREELNELKAEIAELKAEAESAKAELEES----------EE 92
|
90
....*....|...
gi 1720366517 3312 RWEETVQGLEEDL 3324
Cdd:pfam07926 93 SWEEQKKELEKEL 105
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3010-3128 |
8.82e-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: 44.84 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3010 KKLLGEKRQELLDQANKLRtglfKIDETREKV--EVMSLELEDAKKKVAEFQKQCEEylviivQQKREADEQQKAVTANS 3087
Cdd:TIGR02794 71 KKLEQQAEEAEKQRAAEQA----RQKELEQRAaaEKAAKQAEQAAKQAEEKQKQAEE------AKAKQAAEAKAKAEAEA 140
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1720366517 3088 EKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKK 3128
Cdd:TIGR02794 141 ERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA 181
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3245-3324 |
1.08e-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: 45.43 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3245 AQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 3324
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
3011-3292 |
1.24e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3011 KLLGEKRQELLDQANKLRTGLFkiDETREKVEVMSLELEDAKKKVAEFQKQCEEYL--VIIVQQKREADEQQKAVTANSE 3088
Cdd:COG5185 249 AQTSDKLEKLVEQNTDLRLEKL--GENAESSKRLNENANNLIKQFENTKEKIAEYTksIDIKKATESLEEQLAAAEAEQE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3089 KI-AIEEV-----KCQALADNAQKDLEEALPALEEAMRALE-----SLNKKDIGEIKSygrppaQVEIVMQAVMILRGNe 3157
Cdd:COG5185 327 LEeSKRETetgiqNLTAEIEQGQESLTENLEAIKEEIENIVgevelSKSSEELDSFKD------TIESTKESLDEIPQN- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3158 ptwAEAKRQLGEQNFIKSLINFDKDnisdkvLKKIGAYCAQPDFQPDIIGRVSLAAKSlcmwvramelygrlyRVVEPKR 3237
Cdd:COG5185 400 ---QRGYAQEILATLEDTLKAADRQ------IEELQRQIEQATSSNEEVSKLLNELIS---------------ELNKVMR 455
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366517 3238 IRMNAAMAQLQEKQAALA-EAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEM 3292
Cdd:COG5185 456 EADEESQSRLEEAYDEINrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3245-3328 |
3.24e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3245 AQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 3324
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
....
gi 1720366517 3325 GYLV 3328
Cdd:TIGR02168 312 ANLE 315
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
3242-3309 |
3.85e-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: 43.48 E-value: 3.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366517 3242 AAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGE 3309
Cdd:pfam05701 121 AAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIE 188
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3237-3315 |
3.91e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 3.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366517 3237 RIRMNAAMAQLQEKQaaLAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAgmlvsglAGEKARWEE 3315
Cdd:pfam13868 100 REQMDEIVERIQEED--QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEY-------LKEKAEREE 169
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
3018-3128 |
4.02e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.14 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3018 QELLDQANKLRTGLfkidET-----REKVEVMSLELEDAKKKVAEFQKQCEEYlviiVQQKREADEQQKAVT-ANSE--- 3088
Cdd:pfam05622 310 QQLLEDANRRKNEL----ETqnrlaNQRILELQQQVEELQKALQEQGSKAEDS----SLLKQKLEEHLEKLHeAQSElqk 381
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1720366517 3089 -KIAIEEVKCQALADNAQK--DLEEALPALEEAMRALESLNKK 3128
Cdd:pfam05622 382 kKEQIEELEPKQDSNLAQKidELQEALRKKDEDMKAMEERYKK 424
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1823-1908 |
4.37e-03 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 40.27 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 1823 GPAGTGKTETVKDLGKALGIYVIVVNCSEgLDYKSMGRMYSGL------AQSGAWGC--FDEFNRI-------NIEVLSV 1887
Cdd:pfam00004 5 GPPGTGKTTLAKAVAKELGAPFIEISGSE-LVSKYVGESEKRLrelfeaAKKLAPCVifIDEIDALagsrgsgGDSESRR 83
|
90 100
....*....|....*....|.
gi 1720366517 1888 VAQQILSILSALTANLTRFYF 1908
Cdd:pfam00004 84 VVNQLLTELDGFTSSNSKVIV 104
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3233-3324 |
4.41e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3233 VEPKRIRMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKAR 3312
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90
....*....|..
gi 1720366517 3313 WEETVQGLEEDL 3324
Cdd:COG4372 134 LEAQIAELQSEI 145
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
3004-3315 |
4.99e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3004 ELVSGYKKLLgEKRQELLDQANKLRTglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAV 3083
Cdd:COG1340 54 ELREEAQELR-EKRDELNEKVKELKE---ERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3084 -TANSEKIAIEEVKcqaladnaqkDLEEALPALEEAMRALESLnKKDIGEIKsygrppaqvEIVMQAvmilrgneptwae 3162
Cdd:COG1340 130 lSPEEEKELVEKIK----------ELEKELEKAKKALEKNEKL-KELRAELK---------ELRKEA------------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3163 akRQLGEQnfIKSLINfdkdnISDKVLKKIGAycaqpdfqpdiigrvslaakslcmwvramelygrLYRVVEPKRIRMNA 3242
Cdd:COG1340 177 --EEIHKK--IKELAE-----EAQELHEEMIE----------------------------------LYKEADELRKEADE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3243 AMAQLQEKQAALAE-------AQEKLREVAEKLEMLKKQYD--EKLAQKEELRKKSEEMELKLERagmlvsglaGEKARW 3313
Cdd:COG1340 214 LHKEIVEAQEKADElheeiieLQKELRELRKELKKLRKKQRalKREKEKEELEEKAEEIFEKLKK---------GEKLTT 284
|
..
gi 1720366517 3314 EE 3315
Cdd:COG1340 285 EE 286
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
3218-3300 |
5.02e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 42.72 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3218 MWVRAMELY-GRLYRVVEPKRIRMNAAMAQLQEKQAALAEAQEKLREvaEKLE------MLKKQYDEK-LAQKEELRKK- 3288
Cdd:pfam15558 62 QWQAEKEQRkARLGREERRRADRREKQVIEKESRWREQAEDQENQRQ--EKLErarqeaEQRKQCQEQrLKEKEEELQAl 139
|
90
....*....|....*.
gi 1720366517 3289 --SEEMEL--KLERAG 3300
Cdd:pfam15558 140 reQNSLQLqeRLEEAC 155
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3015-3336 |
5.93e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3015 EKRQELLDQANKLRTGLFKIDETREKVEvmslELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQ-QKAVTANSEKIAIE 3093
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLAEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3094 EVKcQALADNAQKDLEEALPALEEAMRALESLNKKD---------------IGEIKSYGRPPAQVEIVMQAVMILRGNEP 3158
Cdd:COG4717 212 EEE-LEEAQEELEELEEELEQLENELEAAALEERLKearlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLF 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3159 TWAEAKRQLGEQNFIKSLINFDKDNISDKVLKKI-GAYCAQPDFQPDIIGRVSLAAKSLC-MWVRAMELYGRLYRVVEPK 3236
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELlAALGLPPDLSPEELLELLDRIEELQeLLREAEELEEELQLEELEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3237 RIRMNAAMAQLQEKQA--ALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKS--EEMELKLERAGMLVSGLAGEKAR 3312
Cdd:COG4717 371 EIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEEELEE 450
|
330 340
....*....|....*....|....
gi 1720366517 3313 WEETVQGLEEDLGYLVGDCLIAAA 3336
Cdd:COG4717 451 LREELAELEAELEQLEEDGELAEL 474
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3246-3327 |
9.66e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366517 3246 QLQEKQAALAEAQEKLREVAEKLEMLKKQYDEklaqkEELRKKSEEMeLKLERAgmlVSGLAGEKARWEETVQGLEEDLG 3325
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSE-----EEYEELREEY-LELSRE---LAGLRAELEELEKRREEIKKTLE 697
|
..
gi 1720366517 3326 YL 3327
Cdd:PRK03918 698 KL 699
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
3244-3284 |
9.88e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 39.50 E-value: 9.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1720366517 3244 MAQLQEKQAA--LAEAQEKLREVAEKLEMLKKQYDEKLAQKEE 3284
Cdd:COG2882 13 LAEKEEDEAAreLGQAQQALEQAEEQLEQLEQYREEYEQRLQQ 55
|
|
| |
