|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1800-2126 |
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: 652.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1800 YGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGIYVIVVNCSEGLDYKSMGRMYSG 1879
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1880 LAQSGAWGCFDEFNRINIEVLSVVAQQILSILSALTANLTRFYFEGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFR 1959
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1960 PIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLSDEEVLL 2039
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2040 LSMRDMNIAKLTSVDVPLFNAIVQDLFPNIELPVIDYGKLRDTIEQEIREMGLQITPFTLTKVLQLYETKNSRHSTMIVG 2119
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 124486773 2120 GTGSSKT 2126
Cdd:pfam12774 321 PTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1255-1663 |
2.87e-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: 531.06 E-value: 2.87e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1255 LQILEKELDALQQVWEITRDWEESWNQWKMGCFQTLQTEAMESMAHGLFRRLTRLAKEYKDrnWEIIETTRSKIEQFKRT 1334
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRD--WDVAEELKKKIDDFKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1335 MPLISDLRNPALRERHWDQVKEEVQREFDQESESFTLEQIVKLGMDQHVEKIAEISASATKELAIEVGLQNIAKTWDSTQ 1414
Cdd:pfam08393 79 LPLIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1415 LDIVPYKDKGHHRLRGTEEVFQALEDNQVALSTMKASRFVKAFEKDVDHWERCLSLILEVIEMVLTVQRQWMYLENIFLG 1494
Cdd:pfam08393 159 FELVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1495 EDIRKQLPNESALFDQVNNNWKAIMDRMNKDNNALRSTHYPGLLETLIEMNAILEDIQKSLDMYLETKRHIFPRFYFLSN 1574
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1575 DDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIQKvggsssKWEAVGMFSGDGEYIDFLHP-VLLEGPVESWLGDVERAMR 1653
Cdd:pfam08393 319 DELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE------NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMR 392
|
410
....*....|
gi 124486773 1654 MTLRDLLRNC 1663
Cdd:pfam08393 393 ETLRDLLKEA 402
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1327-4143 |
1.30e-134 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 477.56 E-value: 1.30e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1327 KIEQFKRTMPLISDL-----RNPALRE---RHWDQV----KEEVQREF-DQESESFtleqivkLGMDQHVEKIAEISASA 1393
Cdd:COG5245 486 KLCKIMRMFSFFNSLemfsrRTLANRMaivKYLSSVvrtgPLFLQRDFfGRMSELL-------MARDMFMEVDGVLRLFF 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1394 TKELA--IEVGLQNIAKTWDSTQLDivpykdkghhrlrgtEEVFQALEDNQVALSTMKASRFvkaFEKDVDhWERCLSLI 1471
Cdd:COG5245 559 GGEWSgiVQLSGIRRAKRCVERQID---------------DEIREWCSSVLSDDFLEERAVR---VERGAD-GARRLRAS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1472 LEvIEMVLTVQRQWMYLENiflgEDIRKQLPNESALFDQVNNNWKAIMDRMNKDNNALRSTHYPgLLETLIEMNAILEDI 1551
Cdd:COG5245 620 SG-SPVLRRLDEYLMMMSL----EDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQV 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1552 QKSLDMYLETKRHIFPRFyfLSNDDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIqkvggSSSKWEAVGMFSGDGEYIDF 1631
Cdd:COG5245 694 FMSIEKVLGLRWREVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEEMKTV-----FSSRIQKKEPFSLDSEAYVG 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1632 LHPVLLEGPVESWLGDVERAMRMTLRDllrncrvALKKFLNKRDkwvkdwaGQVVITASQIQ--------WTADVTKCLM 1703
Cdd:COG5245 767 FFRLYEKSIVIRGINRSMGRVLSQYLE-------SVQEALEIED-------GSFFVSRHRVRdgglekgrGCDAWENCFD 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1704 TAKERSDKKILKVMKkkqvSILNKYSEAIRGnltkimrlKIVALVTIEIHARDVLEKLYKSGLMDVSSFDWLSQLRFYwE 1783
Cdd:COG5245 833 PPLSEYFRILEKIFP----SEEGYFFDEVLK--------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-Q 899
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1784 KDVDDCIIRQTNTQFQYGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSpkgpAGTGKTETVKDLGKALGIYVivvn 1863
Cdd:COG5245 900 GLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY---- 971
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1864 csEGLDYKSmgRMYSGLAQSGAWGcFDEFNRINIEVLSVVA--QQILSILSALTANLTRFYFEGFeinLVWSCGIFITMN 1941
Cdd:COG5245 972 --DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVVEHGL---KSPSTPVEMIIN 1043
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1942 PgyagRTELPENLKSMFRPIAMVVPDSTlIAEIIlfgegfgncKILAKKVYTLYSLAVQQLSRQDHYDFglRALTSLLRy 2021
Cdd:COG5245 1044 E----RNIVLEIGRRALDMFLSNIPFGA-IKSRR---------ESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLK- 1106
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2022 agKKRRLQPDLSDEEVLLLSmrdmnIAKLTSVDVPLFNAIvqDLFPNIELPVIdygklRDTIEQEIREMGlQITPFTLTK 2101
Cdd:COG5245 1107 --AKHRMLEEKTEYLNKILS-----ITGLPLISDTLRERI--DTLDAEWDSFC-----RISESLKKYESQ-QVSGLDVAQ 1171
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2102 VLQLYETKNSRHSTMIVGGTGSSKTTSWKIlqasltslcragepnyniVREFPLNPKALSLGELYGEYDLNTNEWTDGIL 2181
Cdd:COG5245 1172 FVSFLRSVDTGAFHAEYFRVFLCKIKHYTD------------------ACDYLWHVKSPYVKKKYFDADMELRQFFLMFN 1233
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2182 SSVMRVACADEKpdeKWILFDGpvdtlWIESMNSVMDDNKVLTLINGERIAMpeqvsllfeVENLAvASPATVSRCGMVY 2261
Cdd:COG5245 1234 REDMEARLADSK---MEYEVER-----YVEKTKAEVSSLKLELSSVGEGQVV---------VSNLG-SIGDKVGRCLVEY 1295
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2262 TDYVDLGWKPYVQSWL--EKRPKTEVEPLQRMFE-----------KFINKILSFKKDnCNELVPVPEYSGIISLCKLYTV 2328
Cdd:COG5245 1296 DSISRLSTKGVFLDELgdTKRYLDECLDFFSCFEevqkeidelsmVFCADALRFSAD-LYHIVKERRFSGVLAGSDASES 1374
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2329 LATPENGVNpADAENYSFMVEMTFVFSMIWSVCASVDEDgRKKIDSYLREIEGSFPNKDTVYEYY---------VNPKMR 2399
Cdd:COG5245 1375 LGGKSIELA-AILEHKDLIVEMKRGINDVLKLRIFGDKC-RESTPRFYLISDGDLIKDLNERSDYeemlimmfnISAVIT 1452
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2400 TWTSFEEKLPKSWR--YPPNapfykIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSlpSSQWSVLV 2477
Cdd:COG5245 1453 NNGSIAGFELRGERvmLRKE-----VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS--ELITEVKY 1525
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2478 VNMSAQTTSNNVQSIIESRVEK-RTKGVYVPFGG---KSMITFMDDLNMPAKDMFGSQPPLELIR-LWIDYGFWYDrVKQ 2552
Cdd:COG5245 1526 FNFSTCTMTPSKLSVLERETEYyPNTGVVRLYPKpvvKDLVLFCDEINLPYGFEYYPPTVIVFLRpLVERQGFWSS-IAV 1604
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2553 SIKHIRDMFLMAAMGPPGG-GRTVISPRLQSRFNIINMTFPTESQIIRIFGTMINQKLQDFEEEVKPIGNVVTEATlDVY 2631
Cdd:COG5245 1605 SWVTICGIILYGACNPGTDeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASV-ELY 1683
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2632 NTVVQRFlPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTK-ASITRLWIHECFRVFSDRLVDTADMEAFMGILSDKLGT 2710
Cdd:COG5245 1684 LSSKDKT-KFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPdVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLR 1762
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2711 FF-DLTFHHLcpNKRPPIFGDFLKEPKVYEDLVDLTVLktaMETALNEYNLSPSVVPMqlVLFREAIEHITRIVRVIGQP 2789
Cdd:COG5245 1763 AIrEMIAGHI--GEAEITFSMILFFGMACLLKKDLAVF---VEEVRKIFGSSHLDVEA--VAYKDALLHILRSRRGLLVV 1835
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2790 RGNMLLVGIGGSGRQSLARLASSICDYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVELQTTSFLFVDTQIADESFLEDIN 2869
Cdd:COG5245 1836 GGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFN 1915
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2870 NILSSGEVPNLYKSDEFEEIQNHIIDQARAEQIP-ESSDSLFAYLIERVRNNLHIVLCL-SPVGDPFRNWIRqYPALVNC 2947
Cdd:COG5245 1916 PLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEkDTEATLTRVFLVYMEENLPVVFSAcCSQDTSVLAGIR-SPALKNR 1994
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2948 TTINWFSEWPREALLEVAEKYI-----------IGVDLGTQE--NIHRKVAQIFVTMHWSVaqYSQKMLLELrryNYVTP 3014
Cdd:COG5245 1995 CFIDFKKLWDTEEMSQYANSVEtlsrdggrvffINGELGVGKgaLISEVFGDDAVVIEGRG--FEISMIEGS---LGESK 2069
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3015 TNYLELVSGYKKLLGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQ 3094
Cdd:COG5245 2070 IKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVK 2149
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3095 QKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPT 3174
Cdd:COG5245 2150 SVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAK 2229
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3175 -WAEAKRQLGEQNFIKSLINFDKD-NISDKVLKKIGA-YCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPK 3251
Cdd:COG5245 2230 iWFGEQQSLRRDDFIRIIGKYPDEiEFDLEARRFREArECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPL 2309
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3252 RIRMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEET 3331
Cdd:COG5245 2310 REEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGV 2389
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3332 VQGLEEDLGYLVGDCLIAAAFLSYMGPFLTNYRDEIINQIWIRKIRELQVPCSPRFA-IDNFLTNPTKVRDWNIQglpSD 3410
Cdd:COG5245 2390 FSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGMSFIRISKEFRDKEIRRRQfITEGVQKIEDFKEEACS---TD 2466
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3411 AFSTENGIIVTRGNRWALMIDPQGQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQnVQEYLDPTLNPVL 3490
Cdd:COG5245 2467 YGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIG-DAEALDEEIGRLI 2545
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3491 NKSVARIGGRMLIRIGDKEVEYNPNFR-FYLTTKLSNPHYNPEtSAKTTIVNFAVKEQGLEAQLLGIVVRKERPELEEQK 3569
Cdd:COG5245 2546 KEEFKSNLSEVKVMINPPEIVRSTVEAvFWLSEGRSGDMGSIE-WKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHE 2624
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3570 DSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEVTEQLETSETTEINIDLAREAYRPCAQRA 3649
Cdd:COG5245 2625 KALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRL 2704
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3650 SVLFFVLNDMGRIDPMYQFSldayIGLFILSIDKSHRSNKLE-DRIEYLNDYHTYAVYrYTCRTLFErHKLLFSFHMCAK 3728
Cdd:COG5245 2705 ESIRVEIAMFDEKALMYNKS----ICELSSEFEKWRRMKSKYlCAIRYMLMSSEWILD-HEDRSGFI-HRLDVSFLLRTK 2778
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3729 IletsgklnmdeynfFLRGGVVLDREGQMDNPCTSWLADAYWDNITELDKLTNFhglMNSFEQYPRDWHLWYTNSSpeka 3808
Cdd:COG5245 2779 R--------------FVSTLLEDKNYRQVLSSCSLYGNDVISHSCDRFDRDVYR---ALKHQMDNRTHSTILTSNS---- 2837
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3809 mlpgewenACNEMQRMLIVRSLRQ-DRVAFcvtsfivSNLGSRFieppvlnMKSVMEDSTPRSPLVFILSPGVDptsaLL 3887
Cdd:COG5245 2838 --------KTNPYKEYTYNDSWAEaFEVED-------SGDLYKF-------EEGLLELIVGHAPLIYAHKKSLE----NE 2891
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3888 QLAEHTGMAHRfhaLSLGQGQAPIAARllregvnQGHWVFLANCHLSLSWMPN-LDKLVEQLQVEDPHPSF-RLWLSSSP 3965
Cdd:COG5245 2892 RNVDRLGSKEN---EVYAVLNSLFSRK-------EKSWFEVYNISLSFGWFKRyVEDVVYPIKASRVCGKVkNMWTSMVD 2961
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3966 HPDFPISILQASIKMTTEPPKGLKANMTRLYQLMteaQFTHCSKPAKYKKLLFALCFFHSILLERKKFLQLGWNIIYGFN 4045
Cdd:COG5245 2962 ADMLPIQLLIAIDSFVSSTYPETGCGYADLVEID---RYPFDYTLVIACDDAFYLSWEHAAVASVISAGPKENNEEIYFG 3038
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 4046 DSDFEVSENLLS--LYLDEYEETPWDALKYLIAGVNYGGHVTDDWDRRLLTTYINDYFCDLSLTTPFYRLSVLDT---YY 4120
Cdd:COG5245 3039 DKDFEFKTHLLKniLFLNHLNARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGAHETSSQILASVPGGDPelvKF 3118
|
2890 2900
....*....|....*....|...
gi 124486773 4121 IPKDGSLASYKEYISMLPSMDPP 4143
Cdd:COG5245 3119 HMEEMCRSSAFGVIGQLPDLALC 3141
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4158-4458 |
4.38e-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: 4.38e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 4158 ITEARTLFETLLSLQPQITPTRVGG-QSREEKVLELAADVKQKIPEMIDYE-GTRKLLALDPSPLNVVLLQEIQRYNKLM 4235
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGgSSREEIVLELAKDILEKLPEPFDIEeAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 4236 KTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLWGKV-YPSQKPLASWTRDLAVRVEQFETWASRARPPVLFWL 4314
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKsYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 4315 SGFTFPTGFLTAVLQSAARQNNISVDSLSWEFIV-STVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVC 4393
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVtKKVSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486773 4394 LMPTIHFRPAE-SRKKSAKGMYSCPCYYYPNRAGSTdrasFVIGIDLRSGsMTSDHWIKRGTALLM 4458
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 ... |
2767-3027 |
4.26e-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: 400.83 E-value: 4.26e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2767 MQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICDYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVE 2846
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2847 LQTTSFLFVDTQIADESFLEDINNILSSGEVPNLYKSDEFEEIQNHIIDQARAEQIPESSDSLFAYLIERVRNNLHIVLC 2926
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2927 LSPVGDPFRNWIRQYPALVNCTTINWFSEWPREALLEVAEKYIigVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLEL 3006
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFL--EDIEIPEELKSNVVKVFVYVHSSVEDMSKKFYEEL 238
|
250 260
....*....|....*....|.
gi 124486773 3007 RRYNYVTPTNYLELVSGYKKL 3027
Cdd:pfam12780 239 KRKNYVTPKSYLELLRLYKNL 259
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
277-752 |
1.50e-117 |
|
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: 386.16 E-value: 1.50e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 277 VQRLETSMIHWTRQIKEVLSAQESvetGENLGPLEEIEFWHNRCMDLSSISKQLVKKGVKHIESILFLAKSSYLTPFRKL 356
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQ---GRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 357 AQQIQDGSRQAQSNLTFLSILREPYQELAFMK-PKDISEKLPKLISLIRIIWVNSPHYNTRERLTALFRKVC-------- 427
Cdd:pfam08385 78 DTELTDALNEAKDNVKYLKTLERPFEDLEELTdPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISnqlieqck 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 428 ---------------------ECQYHFARWED------------GKQGP------------------------------- 443
Cdd:pfam08385 158 kylspegifdgdveealeklqECIELLEAWKEeykktrekleesPRERPwdfseryifgrfdaflerlekilelfetieq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 444 ---LPCFFGAQGPQITRNLLEIEDIFHKNLQTLRAVRGGILDVKNTSWHEDYNKFRGGIKDLEVMTQNLITSAFELVRDV 520
Cdd:pfam08385 238 fskLEKIGGTKGPELEGVIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDDARST 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 521 EHGVLLLDTFHRLATREAIMRTYEKKAVDLYMLFNSELALVNRELNKKW---PYLEPYMTQYSGQAHWVRILRRRIDRVM 597
Cdd:pfam08385 318 ESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQKynpSPIAKNMPPVAGAIIWARQLFRRIQEPM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 598 NCLSGAHFLPHIGTGEESIHTYQQMAQAIDEMVRKTFQEWTATLDKDCIRRLDMSLLRISQEKVGMLDVNFDKTLLILFA 677
Cdd:pfam08385 398 KRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGNLKRPLLVRHPETGKLLSVNFDPQLLALLR 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486773 678 EIDYWERLLFETPHYVMNVAERAEDLRILRENLLLVARDYNRIIAMLSPDEQALFKERIRFLDKKIHPGLKKLNW 752
Cdd:pfam08385 478 EVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTW 552
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2445-2587 |
1.10e-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: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2445 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPfgGKSMITFMDDLNMPA 2524
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK--AKPGVLFIDEIDSLS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486773 2525 KDMFGSQppLELIRLWIDYGFWYDRVKqsikhirdmFLMAAMGPPGGGrtvISPRLQSRFNII 2587
Cdd:cd00009 98 RGAQNAL--LRVLETLNDLRIDRENVR---------VIGATNRPLLGD---LDRALYDRLDIR 146
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3048-3339 |
1.94e-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: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3048 KIDETREKVEVMSLELEDAKKkVAEFQKQCEEY-LVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEA 3126
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAER-YQALLKEKREYeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3127 LPALEEAMRALESLN-------KKDIGEIKsygrppAQVEivmQAVMILRGNEptwAEAKRQLGEQNFIKSLINFDKDNI 3199
Cdd:TIGR02169 271 EQLLEELNKKIKDLGeeeqlrvKEKIGELE------AEIA---SLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3200 sDKVLKKIGAYCAQpdfqpdiigRVSLAAKslcmwvramelygrlyrvVEPKRIRMNAAMAQLQEKQAALAEAQEKLREV 3279
Cdd:TIGR02169 339 -EELEREIEEERKR---------RDKLTEE------------------YAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3280 AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 3339
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3005-3149 |
8.40e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3005 ELRRYNYVTPTNYLELVSGYKKLLGE---KRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL 3081
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486773 3082 VIIVQQKREADEQQKAVtansekiaiEEVKcqaLADNAQKDLEEALPALEEAMRALESLNKKDIGEIK 3149
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKA---------EEAK---KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2445-2503 |
3.35e-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: 3.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 124486773 2445 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKG 2503
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 ... |
1800-2126 |
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: 652.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1800 YGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGIYVIVVNCSEGLDYKSMGRMYSG 1879
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1880 LAQSGAWGCFDEFNRINIEVLSVVAQQILSILSALTANLTRFYFEGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFR 1959
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1960 PIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLSDEEVLL 2039
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2040 LSMRDMNIAKLTSVDVPLFNAIVQDLFPNIELPVIDYGKLRDTIEQEIREMGLQITPFTLTKVLQLYETKNSRHSTMIVG 2119
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 124486773 2120 GTGSSKT 2126
Cdd:pfam12774 321 PTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
1255-1663 |
2.87e-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: 531.06 E-value: 2.87e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1255 LQILEKELDALQQVWEITRDWEESWNQWKMGCFQTLQTEAMESMAHGLFRRLTRLAKEYKDrnWEIIETTRSKIEQFKRT 1334
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRD--WDVAEELKKKIDDFKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1335 MPLISDLRNPALRERHWDQVKEEVQREFDQESESFTLEQIVKLGMDQHVEKIAEISASATKELAIEVGLQNIAKTWDSTQ 1414
Cdd:pfam08393 79 LPLIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1415 LDIVPYKDKGHHRLRGTEEVFQALEDNQVALSTMKASRFVKAFEKDVDHWERCLSLILEVIEMVLTVQRQWMYLENIFLG 1494
Cdd:pfam08393 159 FELVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1495 EDIRKQLPNESALFDQVNNNWKAIMDRMNKDNNALRSTHYPGLLETLIEMNAILEDIQKSLDMYLETKRHIFPRFYFLSN 1574
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1575 DDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIQKvggsssKWEAVGMFSGDGEYIDFLHP-VLLEGPVESWLGDVERAMR 1653
Cdd:pfam08393 319 DELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE------NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMR 392
|
410
....*....|
gi 124486773 1654 MTLRDLLRNC 1663
Cdd:pfam08393 393 ETLRDLLKEA 402
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1327-4143 |
1.30e-134 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 477.56 E-value: 1.30e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1327 KIEQFKRTMPLISDL-----RNPALRE---RHWDQV----KEEVQREF-DQESESFtleqivkLGMDQHVEKIAEISASA 1393
Cdd:COG5245 486 KLCKIMRMFSFFNSLemfsrRTLANRMaivKYLSSVvrtgPLFLQRDFfGRMSELL-------MARDMFMEVDGVLRLFF 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1394 TKELA--IEVGLQNIAKTWDSTQLDivpykdkghhrlrgtEEVFQALEDNQVALSTMKASRFvkaFEKDVDhWERCLSLI 1471
Cdd:COG5245 559 GGEWSgiVQLSGIRRAKRCVERQID---------------DEIREWCSSVLSDDFLEERAVR---VERGAD-GARRLRAS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1472 LEvIEMVLTVQRQWMYLENiflgEDIRKQLPNESALFDQVNNNWKAIMDRMNKDNNALRSTHYPgLLETLIEMNAILEDI 1551
Cdd:COG5245 620 SG-SPVLRRLDEYLMMMSL----EDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFYKEMDQV 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1552 QKSLDMYLETKRHIFPRFyfLSNDDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIqkvggSSSKWEAVGMFSGDGEYIDF 1631
Cdd:COG5245 694 FMSIEKVLGLRWREVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEEMKTV-----FSSRIQKKEPFSLDSEAYVG 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1632 LHPVLLEGPVESWLGDVERAMRMTLRDllrncrvALKKFLNKRDkwvkdwaGQVVITASQIQ--------WTADVTKCLM 1703
Cdd:COG5245 767 FFRLYEKSIVIRGINRSMGRVLSQYLE-------SVQEALEIED-------GSFFVSRHRVRdgglekgrGCDAWENCFD 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1704 TAKERSDKKILKVMKkkqvSILNKYSEAIRGnltkimrlKIVALVTIEIHARDVLEKLYKSGLMDVSSFDWLSQLRFYwE 1783
Cdd:COG5245 833 PPLSEYFRILEKIFP----SEEGYFFDEVLK--------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSVSISELP-Q 899
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1784 KDVDDCIIRQTNTQFQYGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSpkgpAGTGKTETVKDLGKALGIYVivvn 1863
Cdd:COG5245 900 GLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGKGRIY---- 971
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1864 csEGLDYKSmgRMYSGLAQSGAWGcFDEFNRINIEVLSVVA--QQILSILSALTANLTRFYFEGFeinLVWSCGIFITMN 1941
Cdd:COG5245 972 --DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVVEHGL---KSPSTPVEMIIN 1043
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1942 PgyagRTELPENLKSMFRPIAMVVPDSTlIAEIIlfgegfgncKILAKKVYTLYSLAVQQLSRQDHYDFglRALTSLLRy 2021
Cdd:COG5245 1044 E----RNIVLEIGRRALDMFLSNIPFGA-IKSRR---------ESLDREIGAFNNEVDGIAREEDELMF--YPMFKSLK- 1106
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2022 agKKRRLQPDLSDEEVLLLSmrdmnIAKLTSVDVPLFNAIvqDLFPNIELPVIdygklRDTIEQEIREMGlQITPFTLTK 2101
Cdd:COG5245 1107 --AKHRMLEEKTEYLNKILS-----ITGLPLISDTLRERI--DTLDAEWDSFC-----RISESLKKYESQ-QVSGLDVAQ 1171
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2102 VLQLYETKNSRHSTMIVGGTGSSKTTSWKIlqasltslcragepnyniVREFPLNPKALSLGELYGEYDLNTNEWTDGIL 2181
Cdd:COG5245 1172 FVSFLRSVDTGAFHAEYFRVFLCKIKHYTD------------------ACDYLWHVKSPYVKKKYFDADMELRQFFLMFN 1233
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2182 SSVMRVACADEKpdeKWILFDGpvdtlWIESMNSVMDDNKVLTLINGERIAMpeqvsllfeVENLAvASPATVSRCGMVY 2261
Cdd:COG5245 1234 REDMEARLADSK---MEYEVER-----YVEKTKAEVSSLKLELSSVGEGQVV---------VSNLG-SIGDKVGRCLVEY 1295
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2262 TDYVDLGWKPYVQSWL--EKRPKTEVEPLQRMFE-----------KFINKILSFKKDnCNELVPVPEYSGIISLCKLYTV 2328
Cdd:COG5245 1296 DSISRLSTKGVFLDELgdTKRYLDECLDFFSCFEevqkeidelsmVFCADALRFSAD-LYHIVKERRFSGVLAGSDASES 1374
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2329 LATPENGVNpADAENYSFMVEMTFVFSMIWSVCASVDEDgRKKIDSYLREIEGSFPNKDTVYEYY---------VNPKMR 2399
Cdd:COG5245 1375 LGGKSIELA-AILEHKDLIVEMKRGINDVLKLRIFGDKC-RESTPRFYLISDGDLIKDLNERSDYeemlimmfnISAVIT 1452
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2400 TWTSFEEKLPKSWR--YPPNapfykIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSlpSSQWSVLV 2477
Cdd:COG5245 1453 NNGSIAGFELRGERvmLRKE-----VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS--ELITEVKY 1525
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2478 VNMSAQTTSNNVQSIIESRVEK-RTKGVYVPFGG---KSMITFMDDLNMPAKDMFGSQPPLELIR-LWIDYGFWYDrVKQ 2552
Cdd:COG5245 1526 FNFSTCTMTPSKLSVLERETEYyPNTGVVRLYPKpvvKDLVLFCDEINLPYGFEYYPPTVIVFLRpLVERQGFWSS-IAV 1604
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2553 SIKHIRDMFLMAAMGPPGG-GRTVISPRLQSRFNIINMTFPTESQIIRIFGTMINQKLQDFEEEVKPIGNVVTEATlDVY 2631
Cdd:COG5245 1605 SWVTICGIILYGACNPGTDeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEETMSASV-ELY 1683
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2632 NTVVQRFlPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTK-ASITRLWIHECFRVFSDRLVDTADMEAFMGILSDKLGT 2710
Cdd:COG5245 1684 LSSKDKT-KFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPdVSLIIDWYCEAIREKIDRLVQQKESSTSRQDLYDFGLR 1762
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2711 FF-DLTFHHLcpNKRPPIFGDFLKEPKVYEDLVDLTVLktaMETALNEYNLSPSVVPMqlVLFREAIEHITRIVRVIGQP 2789
Cdd:COG5245 1763 AIrEMIAGHI--GEAEITFSMILFFGMACLLKKDLAVF---VEEVRKIFGSSHLDVEA--VAYKDALLHILRSRRGLLVV 1835
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2790 RGNMLLVGIGGSGRQSLARLASSICDYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVELQTTSFLFVDTQIADESFLEDIN 2869
Cdd:COG5245 1836 GGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFESIPVESSFLEDFN 1915
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2870 NILSSGEVPNLYKSDEFEEIQNHIIDQARAEQIP-ESSDSLFAYLIERVRNNLHIVLCL-SPVGDPFRNWIRqYPALVNC 2947
Cdd:COG5245 1916 PLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEkDTEATLTRVFLVYMEENLPVVFSAcCSQDTSVLAGIR-SPALKNR 1994
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2948 TTINWFSEWPREALLEVAEKYI-----------IGVDLGTQE--NIHRKVAQIFVTMHWSVaqYSQKMLLELrryNYVTP 3014
Cdd:COG5245 1995 CFIDFKKLWDTEEMSQYANSVEtlsrdggrvffINGELGVGKgaLISEVFGDDAVVIEGRG--FEISMIEGS---LGESK 2069
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3015 TNYLELVSGYKKLLGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQ 3094
Cdd:COG5245 2070 IKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDALSGTPGERLEREVK 2149
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3095 QKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPT 3174
Cdd:COG5245 2150 SVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIEMEDVCDLLGFEAK 2229
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3175 -WAEAKRQLGEQNFIKSLINFDKD-NISDKVLKKIGA-YCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPK 3251
Cdd:COG5245 2230 iWFGEQQSLRRDDFIRIIGKYPDEiEFDLEARRFREArECSDPSFTGSILNRASKACGPLKRWLVRECNRSKVLEVKIPL 2309
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3252 RIRMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEET 3331
Cdd:COG5245 2310 REEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVSEILINEDSEWGGV 2389
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3332 VQGLEEDLGYLVGDCLIAAAFLSYMGPFLTNYRDEIINQIWIRKIRELQVPCSPRFA-IDNFLTNPTKVRDWNIQglpSD 3410
Cdd:COG5245 2390 FSEVPKLMVELDGDGHPSSCLHPYIGTLGFLCRAIEFGMSFIRISKEFRDKEIRRRQfITEGVQKIEDFKEEACS---TD 2466
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3411 AFSTENGIIVTRGNRWALMIDPQGQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQnVQEYLDPTLNPVL 3490
Cdd:COG5245 2467 YGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIG-DAEALDEEIGRLI 2545
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3491 NKSVARIGGRMLIRIGDKEVEYNPNFR-FYLTTKLSNPHYNPEtSAKTTIVNFAVKEQGLEAQLLGIVVRKERPELEEQK 3569
Cdd:COG5245 2546 KEEFKSNLSEVKVMINPPEIVRSTVEAvFWLSEGRSGDMGSIE-WKQLIQVMFVSKVLGCETEIPDALEKLVSGPLFVHE 2624
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3570 DSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEVTEQLETSETTEINIDLAREAYRPCAQRA 3649
Cdd:COG5245 2625 KALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRIDALKSEYNASVKRL 2704
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3650 SVLFFVLNDMGRIDPMYQFSldayIGLFILSIDKSHRSNKLE-DRIEYLNDYHTYAVYrYTCRTLFErHKLLFSFHMCAK 3728
Cdd:COG5245 2705 ESIRVEIAMFDEKALMYNKS----ICELSSEFEKWRRMKSKYlCAIRYMLMSSEWILD-HEDRSGFI-HRLDVSFLLRTK 2778
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3729 IletsgklnmdeynfFLRGGVVLDREGQMDNPCTSWLADAYWDNITELDKLTNFhglMNSFEQYPRDWHLWYTNSSpeka 3808
Cdd:COG5245 2779 R--------------FVSTLLEDKNYRQVLSSCSLYGNDVISHSCDRFDRDVYR---ALKHQMDNRTHSTILTSNS---- 2837
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3809 mlpgewenACNEMQRMLIVRSLRQ-DRVAFcvtsfivSNLGSRFieppvlnMKSVMEDSTPRSPLVFILSPGVDptsaLL 3887
Cdd:COG5245 2838 --------KTNPYKEYTYNDSWAEaFEVED-------SGDLYKF-------EEGLLELIVGHAPLIYAHKKSLE----NE 2891
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3888 QLAEHTGMAHRfhaLSLGQGQAPIAARllregvnQGHWVFLANCHLSLSWMPN-LDKLVEQLQVEDPHPSF-RLWLSSSP 3965
Cdd:COG5245 2892 RNVDRLGSKEN---EVYAVLNSLFSRK-------EKSWFEVYNISLSFGWFKRyVEDVVYPIKASRVCGKVkNMWTSMVD 2961
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3966 HPDFPISILQASIKMTTEPPKGLKANMTRLYQLMteaQFTHCSKPAKYKKLLFALCFFHSILLERKKFLQLGWNIIYGFN 4045
Cdd:COG5245 2962 ADMLPIQLLIAIDSFVSSTYPETGCGYADLVEID---RYPFDYTLVIACDDAFYLSWEHAAVASVISAGPKENNEEIYFG 3038
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 4046 DSDFEVSENLLS--LYLDEYEETPWDALKYLIAGVNYGGHVTDDWDRRLLTTYINDYFCDLSLTTPFYRLSVLDT---YY 4120
Cdd:COG5245 3039 DKDFEFKTHLLKniLFLNHLNARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGAHETSSQILASVPGGDPelvKF 3118
|
2890 2900
....*....|....*....|...
gi 124486773 4121 IPKDGSLASYKEYISMLPSMDPP 4143
Cdd:COG5245 3119 HMEEMCRSSAFGVIGQLPDLALC 3141
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
4158-4458 |
4.38e-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: 4.38e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 4158 ITEARTLFETLLSLQPQITPTRVGG-QSREEKVLELAADVKQKIPEMIDYE-GTRKLLALDPSPLNVVLLQEIQRYNKLM 4235
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGgSSREEIVLELAKDILEKLPEPFDIEeAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 4236 KTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLWGKV-YPSQKPLASWTRDLAVRVEQFETWASRARPPVLFWL 4314
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKsYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 4315 SGFTFPTGFLTAVLQSAARQNNISVDSLSWEFIV-STVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVC 4393
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVtKKVSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486773 4394 LMPTIHFRPAE-SRKKSAKGMYSCPCYYYPNRAGSTdrasFVIGIDLRSGsMTSDHWIKRGTALLM 4458
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 ... |
2767-3027 |
4.26e-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: 400.83 E-value: 4.26e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2767 MQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICDYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVE 2846
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2847 LQTTSFLFVDTQIADESFLEDINNILSSGEVPNLYKSDEFEEIQNHIIDQARAEQIPESSDSLFAYLIERVRNNLHIVLC 2926
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2927 LSPVGDPFRNWIRQYPALVNCTTINWFSEWPREALLEVAEKYIigVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLEL 3006
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFL--EDIEIPEELKSNVVKVFVYVHSSVEDMSKKFYEEL 238
|
250 260
....*....|....*....|.
gi 124486773 3007 RRYNYVTPTNYLELVSGYKKL 3027
Cdd:pfam12780 239 KRKNYVTPKSYLELLRLYKNL 259
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3400-3621 |
5.97e-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: 5.97e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3400 RDWNIQGLPSDAFSTENGIIVTRGNRWALMIDPQGQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQNVQ 3479
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3480 EYLDPTLNPVLNKSVARIGGRMLIRIGDKEVEYNPNFRFYLTTKLSNPHYNPETSAKTTIVNFAVKEQGLEAQLLGIVVR 3559
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486773 3560 KERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEV 3621
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
277-752 |
1.50e-117 |
|
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: 386.16 E-value: 1.50e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 277 VQRLETSMIHWTRQIKEVLSAQESvetGENLGPLEEIEFWHNRCMDLSSISKQLVKKGVKHIESILFLAKSSYLTPFRKL 356
Cdd:pfam08385 1 LHALESVVIKWTKQIQDVLKEDSQ---GRNPGPLAEIEFWKSREANLSSIYEQLKSPEVKKVLEILEAAKSSYLPAFKAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 357 AQQIQDGSRQAQSNLTFLSILREPYQELAFMK-PKDISEKLPKLISLIRIIWVNSPHYNTRERLTALFRKVC-------- 427
Cdd:pfam08385 78 DTELTDALNEAKDNVKYLKTLERPFEDLEELTdPPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISnqlieqck 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 428 ---------------------ECQYHFARWED------------GKQGP------------------------------- 443
Cdd:pfam08385 158 kylspegifdgdveealeklqECIELLEAWKEeykktrekleesPRERPwdfseryifgrfdaflerlekilelfetieq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 444 ---LPCFFGAQGPQITRNLLEIEDIFHKNLQTLRAVRGGILDVKNTSWHEDYNKFRGGIKDLEVMTQNLITSAFELVRDV 520
Cdd:pfam08385 238 fskLEKIGGTKGPELEGVIEEILEEFQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDDARST 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 521 EHGVLLLDTFHRLATREAIMRTYEKKAVDLYMLFNSELALVNRELNKKW---PYLEPYMTQYSGQAHWVRILRRRIDRVM 597
Cdd:pfam08385 318 ESAFKLLRIFEFLLERPIIRGALEEKYTDLLQMFKKELDAVKKIFDKQKynpSPIAKNMPPVAGAIIWARQLFRRIQEPM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 598 NCLSGAHFLPHIGTGEESIHTYQQMAQAIDEMVRKTFQEWTATLDKDCIRRLDMSLLRISQEKVGMLDVNFDKTLLILFA 677
Cdd:pfam08385 398 KRFKEELGLLKHAEGKKVIKKYNELAKKLDEYERLIYEAWLKEVEEASEGNLKRPLLVRHPETGKLLSVNFDPQLLALLR 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486773 678 EIDYWERLLFETPHYVMNVAERAEDLRILRENLLLVARDYNRIIAMLSPDEQALFKERIRFLDKKIHPGLKKLNW 752
Cdd:pfam08385 478 EVKYLQKLGFEIPESALNIALKEERLRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTW 552
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2414-2592 |
1.40e-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: 330.12 E-value: 1.40e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2414 YPPNAPFYKIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSII 2493
Cdd:pfam12775 1 IPPDVPFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQDII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2494 ESRVEKRTKGVYVPFGGKSMITFMDDLNMPAKDMFGSQPPLELIRLWIDYGFWYDRVKQSIKHIRDMFLMAAMGPPGGGR 2573
Cdd:pfam12775 81 ESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPGGGR 160
|
170
....*....|....*....
gi 124486773 2574 TVISPRLQSRFNIINMTFP 2592
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 ... |
4013-4152 |
2.89e-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: 241.59 E-value: 2.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 4013 YKKLLFALCFFHSILLERKKFLQLGWNIIYGFNDSDFEVSENLLSLYLDEY-EETPWDALKYLIAGVNYGGHVTDDWDRR 4091
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYdEKIPWDALRYLIGEINYGGRVTDDWDRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486773 4092 LLTTYINDYFCDlSLTTPFYRLSVlDTYYIPKDGSLASYKEYISMLPSMDPPEAFGQHPNA 4152
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 ... |
3867-3981 |
1.81e-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: 1.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3867 TPRSPLVFILSPGVDPTSALLQLAEHTGMAHRFHALSLGQGQAPIAARLLREGVNQGHWVFLANCHLSLSWMPNLDKLVE 3946
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGFGGKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILE 80
|
90 100 110
....*....|....*....|....*....|....*
gi 124486773 3947 QLQVEDPHPSFRLWLSSSPHPDFPISILQASIKMT 3981
Cdd:pfam03028 81 ELPEETLHPDFRLWLTSEPSPKFPISILQNSIKIT 115
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
3041-3373 |
3.08e-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: 3.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3041 KLRTGLFKIDETREKVEvmsleleDAKKKVA----EFQKQCE--EYLVIIVQQKREADEQQKAVTANSE-KIAIEEVKCQ 3113
Cdd:pfam12777 2 RLENGLLKLHSTAAQVD-------DLKAKLAaqeaELKQKNEdaDKLIQVVGIEADKVSKEKAIADEEEqKVAVIMKEVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3114 ALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMIL---RGNEP---TWAEAKRQLGE-QN 3186
Cdd:pfam12777 75 EKQKACEEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILmapGGKIPkdkSWKAAKIMMAKvDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3187 FIKSLINFDKDNISDKVLKKIGAYCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRIRMNAAMAQLQEKQ 3266
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3267 AALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDC 3346
Cdd:pfam12777 235 EKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDI 314
|
330 340
....*....|....*....|....*..
gi 124486773 3347 LIAAAFLSYMGPFLTNYRDEIINQIWI 3373
Cdd:pfam12777 315 LLISAFISYLGFFTKKYRNELLDKFWI 341
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
2288-2406 |
2.56e-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: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2288 LQRMFEKFINKILSFKKDNCNELVPVPEYSGIISLCKLYTVLATP---ENGVNPADAENYSFMVEMTFVFSMIWSVCASV 2364
Cdd:pfam17852 1 LEPLFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDEvleYNGVHPLSPDKLKEYLEKLFLFALVWSIGGTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 124486773 2365 DEDGRKKIDSYLREIEGS----FPNKDTVYEYYVNPKMRTWTSFEE 2406
Cdd:pfam17852 81 DEDSRKKFDEFLRELFSGldlpPPEKGTVYDYFVDLEKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2446-2584 |
5.56e-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: 5.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2446 PVLLVGPVGTGKTSIAQSVLQSLpsSQWSVLVVNMSAQTTSNNVQSIIESRVE--KRTKGVYVPFGGKSMITFMDDLNMP 2523
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL--SNRPVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486773 2524 AKDMFGSQ-PPLELIRLWIDYGFWYDRVKQSikhirDMFLMAAMGPPGGGRTVISPRLQSRF 2584
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. |
2625-2713 |
6.96e-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: 6.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2625 EATLDVYNTVVQRFLPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTKASITRLWIHECFRVFSDRLVDTADMEAFMGIL 2704
Cdd:pfam17857 3 AAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDKIQ 82
|
....*....
gi 124486773 2705 SDKLGTFFD 2713
Cdd:pfam17857 83 MASLKKFFD 91
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2445-2587 |
1.10e-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: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2445 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPfgGKSMITFMDDLNMPA 2524
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK--AKPGVLFIDEIDSLS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486773 2525 KDMFGSQppLELIRLWIDYGFWYDRVKqsikhirdmFLMAAMGPPGGGrtvISPRLQSRFNII 2587
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 ... |
2973-3306 |
8.04e-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: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 2973 DLGTQ-ENihRKVAQIFVTMHwsvaqySQKMLLELRRYNYVTPTNYLELvsgykkllgEKRQELLDQANKLRTGLFKIDE 3051
Cdd:pfam05483 475 DLKTElEK--EKLKNIELTAH------CDKLLLENKELTQEASDMTLEL---------KKHQEDIINCKKQEERMLKQIE 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3052 TREKVEV-MSLELEDAKKkvaEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIAIEEVKCqalaDNAQKDLEEALPAL 3130
Cdd:pfam05483 538 NLEEKEMnLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC----NNLKKQIENKNKNI 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3131 EEAMRALESLNKKDIGEIKsygrppaQVEIVMQAVMILrgnEPTWAEAKRQLGE--QNFIKSLInfDKDNISDKVLKKIG 3208
Cdd:pfam05483 611 EELHQENKALKKKGSAENK-------QLNAYEIKVNKL---ELELASAKQKFEEiiDNYQKEIE--DKKISEEKLLEEVE 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3209 AYCAQPD----FQPDIIGRVSlaaKSLCMWVRAMELYGRLY-RVVEPKRIRMNAAMAQLQEKQAALAEAQEKLREVAEKL 3283
Cdd:pfam05483 679 KAKAIADeavkLQKEIDKRCQ---HKIAEMVALMEKHKHQYdKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAEL 755
|
330 340
....*....|....*....|...
gi 124486773 3284 EMLKKQYDEKLAQKEELRKKSEE 3306
Cdd:pfam05483 756 LSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3048-3339 |
1.94e-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: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3048 KIDETREKVEVMSLELEDAKKkVAEFQKQCEEY-LVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEA 3126
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAER-YQALLKEKREYeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3127 LPALEEAMRALESLN-------KKDIGEIKsygrppAQVEivmQAVMILRGNEptwAEAKRQLGEQNFIKSLINFDKDNI 3199
Cdd:TIGR02169 271 EQLLEELNKKIKDLGeeeqlrvKEKIGELE------AEIA---SLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3200 sDKVLKKIGAYCAQpdfqpdiigRVSLAAKslcmwvramelygrlyrvVEPKRIRMNAAMAQLQEKQAALAEAQEKLREV 3279
Cdd:TIGR02169 339 -EELEREIEEERKR---------RDKLTEE------------------YAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3280 AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 3339
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3005-3149 |
8.40e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3005 ELRRYNYVTPTNYLELVSGYKKLLGE---KRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL 3081
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486773 3082 VIIVQQKREADEQQKAVtansekiaiEEVKcqaLADNAQKDLEEALPALEEAMRALESLNKKDIGEIK 3149
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 ... |
1837-1958 |
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 124486773 1837 KGPAGTGKTETVKDLGKALGIY-VIVVNCSE---------GLDYKSMG--RMYSGL---AQSGAWGCFDEFNRINIEVLS 1901
Cdd:pfam07728 5 VGPPGTGKTELAERLAAALSNRpVFYVQLTRdtteedlfgRRNIDPGGasWVDGPLvraAREGEIAVLDEINRANPDVLN 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486773 1902 VVaqqiLSILSA----LTANLTRFYFEGFEINLVwscgifITMNPGYAGRTELPENLKSMF 1958
Cdd:pfam07728 85 SL----LSLLDErrllLPDGGELVKAAPDGFRLI------ATMNPLDRGLNELSPALRSRF 135
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3049-3313 |
2.11e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3049 IDETREKVEVMSLELEDAKKKVAEFQKQCE--EYLVII------VQQKREADEQ---QKAVTANSEKIAIEEVKCQA--L 3115
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLEraEDLVEAedrierLEERREDLEEliaERRETIEEKRERAEELRERAaeL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3116 ADNAQKDLEEALPALEEAMRALESLNK--KDIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAKRQLGEQNfiksliN 3193
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAElnSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELN------D 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3194 FDKDNISDKVLKKigaycaqpdfqpdiigrVSLAAKslcmwvramelygrlyrvVEPKRIrmNAAMAQLQEKQAALAEAQ 3273
Cdd:PRK02224 624 ERRERLAEKRERK-----------------RELEAE------------------FDEARI--EEAREDKERAEEYLEQVE 666
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 124486773 3274 EKLREVAEKLEMLKKQ---YDEKLAQKEELRKKSEEMELKLER 3313
Cdd:PRK02224 667 EKLDELREERDDLQAEigaVENELEELEELRERREALENRVEA 709
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3028-3342 |
2.15e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3028 LGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL--VIIVQQKREADEQQKAVTANSEKI 3105
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrLEELEERHELYEEAKAKKEELERL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3106 AiEEVKCQALaDNAQKDLEEALPALEEAMRALESLNKKdIGEIKSygrppaQVEIVMQAVMILRGNEPTWAEAKRQLGEQ 3185
Cdd:PRK03918 378 K-KRLTGLTP-EKLEKELEELEKAKEEIEEEISKITAR-IGELKK------EIKELKKAIEELKKAKGKCPVCGRELTEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3186 nfikslinfDKDNISDKVLKKIGaycaqpDFQPDIIgrvSLAAKSLCMWVRAMELYGRLYRvvEPKRIRMNAAMAQLQEK 3265
Cdd:PRK03918 449 ---------HRKELLEEYTAELK------RIEKELK---EIEEKERKLRKELRELEKVLKK--ESELIKLKELAEQLKEL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3266 QAALAEAQ-EKLREVAEKLEMLKKQYD----------EKLAQKEELRKKSEEMELKLERAGMLVSGLAGE-KARWEETVQ 3333
Cdd:PRK03918 509 EEKLKKYNlEELEKKAEEYEKLKEKLIklkgeikslkKELEKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVE 588
|
....*....
gi 124486773 3334 GLEEDLGYL 3342
Cdd:PRK03918 589 ELEERLKEL 597
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
3033-3143 |
5.43e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3033 QELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIaieeVKC 3112
Cdd:COG1340 146 EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEI----VEA 221
|
90 100 110
....*....|....*....|....*....|.
gi 124486773 3113 QALADNAQKDLEEALPALEEAMRALESLNKK 3143
Cdd:COG1340 222 QEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3030-3136 |
5.96e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3030 EKRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQ-KREADEQQKAVTANSEKIAiE 3108
Cdd:PRK09510 91 ELQQKQAAEQERLK----QLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAaKAKAEAEAKRAAAAAKKAA-A 165
|
90 100
....*....|....*....|....*...
gi 124486773 3109 EVKCQALADNAQKDLEEALPALEEAMRA 3136
Cdd:PRK09510 166 EAKKKAEAEAAKKAAAEAKKKAEAEAAA 193
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3028-3321 |
7.12e-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: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3028 LGEKRQELLDQANKLRTGLF----KIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVII---VQQKREADEQQKAVTA 3100
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEeltaELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrlEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3101 NSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKdigeiksygrppaqveivmqavmiLRGNEPTWAEAKR 3180
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE------------------------LEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3181 QLGEQNfiKSLINFDKDniSDKVLKKIGAycaqpdfqpdIIGRVSLAAKSLCMWVRAMElygRLYRVVE-----PKRIRM 3255
Cdd:TIGR02168 373 RLEELE--EQLETLRSK--VAQLELQIAS----------LNNEIERLEARLERLEDRRE---RLQQEIEellkkLEEAEL 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486773 3256 NAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKlaqKEELRKKSEEMELKLERAGMLVSGL 3321
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEA---EQALDAAERELAQLQARLDSLERLQ 498
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3254-3312 |
8.23e-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: 8.23e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486773 3254 RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLA----QKEELRKKSEEMELKLE 3312
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAeleaELEELEAEREELAAKIP 173
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3048-3333 |
8.34e-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: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3048 KIDETREKVEVMSLELEDAKKKVAEFQKQceeylviIVQQKREADEQQKAVTANSEKIaieevkcqalaDNAQKDLEEAL 3127
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAE-------LEELNEEYNELQAELEALQAEI-----------DKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3128 PALEEAMRALeslnKKDIGEIKSYGRPPAQVEIVMQAvmilrgneptwaeakrqlgeqnfikslinfdkDNISDkVLKKI 3207
Cdd:COG3883 79 AEIEERREEL----GERARALYRSGGSVSYLDVLLGS--------------------------------ESFSD-FLDRL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3208 GAYCAQPDFQPDIIGRVslaakslcmwvramelygrlyrvvepkrirmNAAMAQLQEKQAALAEAQEKLREVAEKLEMLK 3287
Cdd:COG3883 122 SALSKIADADADLLEEL-------------------------------KADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 124486773 3288 KQYDEKLAQKEELRK--KSEEMELKLERAGMLVSGLAGEKARWEETVQ 3333
Cdd:COG3883 171 AELEAQQAEQEALLAqlSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3018-3348 |
8.43e-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: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3018 LELVSGYKKLLGEKRQELLDQANKLRTglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL-VIIVQQKREADEQQK 3096
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEA---ELEELRLELEELELELEEAQAEEYELLAELARLEqDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3097 AVTANSEKIAIEEV--KCQALADNAQKDLEEALPALEEAMRALESLNKkdigeiksygrppAQVEIVMQAVMILRGNEPT 3174
Cdd:COG1196 318 LEELEEELAELEEEleELEEELEELEEELEEAEEELEEAEAELAEAEE-------------ALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3175 WAEAKRQLGEQNFIKSLINFDKDNISDKVLKKIgaycaqpdfqpdiigrvslaakslcmwvRAMELYGRLYRVVEPKRIR 3254
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLE----------------------------RLEEELEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3255 MNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQG 3334
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
330
....*....|....
gi 124486773 3335 LEEDLGYLVGDCLI 3348
Cdd:COG1196 517 AGLRGLAGAVAVLI 530
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
3254-3314 |
1.02e-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: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486773 3254 RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYD---EKLA-QKEELRKKSEEMELKLERA 3314
Cdd:pfam18595 51 KLEEAKKKLKELRDALEEKEIELRELERREERLQRQLEnaqEKLErLREQAEEKREAAQARLEEL 115
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3087-3339 |
1.63e-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: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3087 QKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKkdigEIKSygrppAQVEIvmqavm 3166
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----EIAE-----AEAEI------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3167 ilrgneptwAEAKRQLGEQnfIKSLinfdkdNISDKVLKKIGAYCAQPDFQpDIIGRVSLaakslcmwvramelygrLYR 3246
Cdd:COG3883 82 ---------EERREELGER--ARAL------YRSGGSVSYLDVLLGSESFS-DFLDRLSA-----------------LSK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3247 VVEpkriRMNAAMAQLQEKQAALAEAQEKLREVAEKLEmlkkqydeklAQKEELRKKSEEMELKLERAGMLVSGLAGEKA 3326
Cdd:COG3883 127 IAD----ADADLLEELKADKAELEAKKAELEAKLAELE----------ALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
250
....*....|...
gi 124486773 3327 RWEETVQGLEEDL 3339
Cdd:COG3883 193 AAEAQLAELEAEL 205
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3028-3339 |
2.02e-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: 47.74 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3028 LGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEyLVIIVQQKREADEQQKAVTANSEKIAI 3107
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGLSG 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3108 EEvkcQALAD--NAQKDLEEALP-ALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAKRQLGE 3184
Cdd:TIGR02168 521 IL---GVLSEliSVDEGYEAAIEaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3185 QNFIKSLINFDKdnisdkvlkkigaycAQPDFQPDIIGRVS--LAAKSLcmwVRAMELYGRL---YRVVEP--KRIRMNA 3257
Cdd:TIGR02168 598 EGFLGVAKDLVK---------------FDPKLRKALSYLLGgvLVVDDL---DNALELAKKLrpgYRIVTLdgDLVRPGG 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3258 AMAQLQEKQAALAEAQEK-LREVAEKLEMLKKQYDEKLAQKEELRKKSEEME-------LKLERAGMLVSGLAGEKARWE 3329
Cdd:TIGR02168 660 VITGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlrKELEELSRQISALRKDLARLE 739
|
330
....*....|
gi 124486773 3330 ETVQGLEEDL 3339
Cdd:TIGR02168 740 AEVEQLEERI 749
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3254-3339 |
2.63e-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: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3254 RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQ 3333
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
....*.
gi 124486773 3334 GLEEDL 3339
Cdd:COG1196 313 ELEERL 318
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2445-2503 |
3.35e-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: 3.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 124486773 2445 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKG 2503
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG 61
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3254-3339 |
4.13e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3254 RMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQ 3333
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
....*.
gi 124486773 3334 GLEEDL 3339
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 ... |
3254-3339 |
6.71e-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: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3254 RMNAAMAQLQEKQAALAEAQEKL-REV------AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAgmlvsglageKA 3326
Cdd:pfam07926 23 QLQKLQEDLEKQAEIAREAQQNYeRELvlhaedIKALQALREELNELKAEIAELKAEAESAKAELEES----------EE 92
|
90
....*....|...
gi 124486773 3327 RWEETVQGLEEDL 3339
Cdd:pfam07926 93 SWEEQKKELEKEL 105
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3025-3143 |
8.85e-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: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3025 KKLLGEKRQELLDQANKLRtglfKIDETREKV--EVMSLELEDAKKKVAEFQKQCEEylviivQQKREADEQQKAVTANS 3102
Cdd:TIGR02794 71 KKLEQQAEEAEKQRAAEQA----RQKELEQRAaaEKAAKQAEQAAKQAEEKQKQAEE------AKAKQAAEAKAKAEAEA 140
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 124486773 3103 EKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKK 3143
Cdd:TIGR02794 141 ERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA 181
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3260-3339 |
1.11e-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: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3260 AQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 3339
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
3026-3307 |
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 124486773 3026 KLLGEKRQELLDQANKLRTGLFkiDETREKVEVMSLELEDAKKKVAEFQKQCEEYL--VIIVQQKREADEQQKAVTANSE 3103
Cdd:COG5185 249 AQTSDKLEKLVEQNTDLRLEKL--GENAESSKRLNENANNLIKQFENTKEKIAEYTksIDIKKATESLEEQLAAAEAEQE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3104 KI-AIEEV-----KCQALADNAQKDLEEALPALEEAMRALE-----SLNKKDIGEIKSygrppaQVEIVMQAVMILRGNe 3172
Cdd:COG5185 327 LEeSKRETetgiqNLTAEIEQGQESLTENLEAIKEEIENIVgevelSKSSEELDSFKD------TIESTKESLDEIPQN- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3173 ptwAEAKRQLGEQNFIKSLINFDKDnisdkvLKKIGAYCAQPDFQPDIIGRVSLAAKSlcmwvramelygrlyRVVEPKR 3252
Cdd:COG5185 400 ---QRGYAQEILATLEDTLKAADRQ------IEELQRQIEQATSSNEEVSKLLNELIS---------------ELNKVMR 455
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124486773 3253 IRMNAAMAQLQEKQAALA-EAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEM 3307
Cdd:COG5185 456 EADEESQSRLEEAYDEINrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3260-3343 |
3.31e-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: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3260 AQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 3339
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
....
gi 124486773 3340 GYLV 3343
Cdd:TIGR02168 312 ANLE 315
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3252-3330 |
3.57e-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: 3.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486773 3252 RIRMNAAMAQLQEKQaaLAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAgmlvsglAGEKARWEE 3330
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 ... |
3033-3143 |
4.14e-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: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3033 QELLDQANKLRTGLfkidET-----REKVEVMSLELEDAKKKVAEFQKQCEEYlviiVQQKREADEQQKAVT-ANSE--- 3103
Cdd:pfam05622 310 QQLLEDANRRKNEL----ETqnrlaNQRILELQQQVEELQKALQEQGSKAEDS----SLLKQKLEEHLEKLHeAQSElqk 381
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 124486773 3104 -KIAIEEVKCQALADNAQK--DLEEALPALEEAMRALESLNKK 3143
Cdd:pfam05622 382 kKEQIEELEPKQDSNLAQKidELQEALRKKDEDMKAMEERYKK 424
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
3257-3324 |
4.17e-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: 43.09 E-value: 4.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486773 3257 AAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGE 3324
Cdd:pfam05701 121 AAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIE 188
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
1838-1923 |
4.56e-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: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 1838 GPAGTGKTETVKDLGKALGIYVIVVNCSEgLDYKSMGRMYSGL------AQSGAWGC--FDEFNRI-------NIEVLSV 1902
Cdd:pfam00004 5 GPPGTGKTTLAKAVAKELGAPFIEISGSE-LVSKYVGESEKRLrelfeaAKKLAPCVifIDEIDALagsrgsgGDSESRR 83
|
90 100
....*....|....*....|.
gi 124486773 1903 VAQQILSILSALTANLTRFYF 1923
Cdd:pfam00004 84 VVNQLLTELDGFTSSNSKVIV 104
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3248-3339 |
4.58e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3248 VEPKRIRMNAAMAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKAR 3327
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90
....*....|..
gi 124486773 3328 WEETVQGLEEDL 3339
Cdd:COG4372 134 LEAQIAELQSEI 145
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
3233-3315 |
4.82e-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: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3233 MWVRAMELY-GRLYRVVEPKRIRMNAAMAQLQEKQAALAEAQEKLREvaEKLE------MLKKQYDEK-LAQKEELRKK- 3303
Cdd:pfam15558 62 QWQAEKEQRkARLGREERRRADRREKQVIEKESRWREQAEDQENQRQ--EKLErarqeaEQRKQCQEQrLKEKEEELQAl 139
|
90
....*....|....*.
gi 124486773 3304 --SEEMEL--KLERAG 3315
Cdd:pfam15558 140 reQNSLQLqeRLEEAC 155
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
3019-3330 |
5.01e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3019 ELVSGYKKLLgEKRQELLDQANKLRTglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAV 3098
Cdd:COG1340 54 ELREEAQELR-EKRDELNEKVKELKE---ERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3099 -TANSEKIAIEEVKcqaladnaqkDLEEALPALEEAMRALESLnKKDIGEIKsygrppaqvEIVMQAvmilrgneptwae 3177
Cdd:COG1340 130 lSPEEEKELVEKIK----------ELEKELEKAKKALEKNEKL-KELRAELK---------ELRKEA------------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3178 akRQLGEQnfIKSLINfdkdnISDKVLKKIGAycaqpdfqpdiigrvslaakslcmwvramelygrLYRVVEPKRIRMNA 3257
Cdd:COG1340 177 --EEIHKK--IKELAE-----EAQELHEEMIE----------------------------------LYKEADELRKEADE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3258 AMAQLQEKQAALAE-------AQEKLREVAEKLEMLKKQYD--EKLAQKEELRKKSEEMELKLERagmlvsglaGEKARW 3328
Cdd:COG1340 214 LHKEIVEAQEKADElheeiieLQKELRELRKELKKLRKKQRalKREKEKEELEEKAEEIFEKLKK---------GEKLTT 284
|
..
gi 124486773 3329 EE 3330
Cdd:COG1340 285 EE 286
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3030-3351 |
6.10e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3030 EKRQELLDQANKLRTGLFKIDETREKVEvmslELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQ-QKAVTANSEKIAIE 3108
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLAEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3109 EVKcQALADNAQKDLEEALPALEEAMRALESLNKKD---------------IGEIKSYGRPPAQVEIVMQAVMILRGNEP 3173
Cdd:COG4717 212 EEE-LEEAQEELEELEEELEQLENELEAAALEERLKearlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLF 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3174 TWAEAKRQLGEQNFIKSLINFDKDNISDKVLKKI-GAYCAQPDFQPDIIGRVSLAAKSLC-MWVRAMELYGRLYRVVEPK 3251
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELlAALGLPPDLSPEELLELLDRIEELQeLLREAEELEEELQLEELEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3252 RIRMNAAMAQLQEKQA--ALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKS--EEMELKLERAGMLVSGLAGEKAR 3327
Cdd:COG4717 371 EIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEEELEE 450
|
330 340
....*....|....*....|....
gi 124486773 3328 WEETVQGLEEDLGYLVGDCLIAAA 3351
Cdd:COG4717 451 LREELAELEAELEQLEEDGELAEL 474
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
3259-3299 |
9.28e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 39.50 E-value: 9.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 124486773 3259 MAQLQEKQAA--LAEAQEKLREVAEKLEMLKKQYDEKLAQKEE 3299
Cdd:COG2882 13 LAEKEEDEAAreLGQAQQALEQAEEQLEQLEQYREEYEQRLQQ 55
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3261-3342 |
9.78e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486773 3261 QLQEKQAALAEAQEKLREVAEKLEMLKKQYDEklaqkEELRKKSEEMeLKLERAgmlVSGLAGEKARWEETVQGLEEDLG 3340
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSE-----EEYEELREEY-LELSRE---LAGLRAELEELEKRREEIKKTLE 697
|
..
gi 124486773 3341 YL 3342
Cdd:PRK03918 698 KL 699
|
|
| |
