|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1408-1734 |
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: 649.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1408 YGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGTYVIVVNCSEGLDYKSMGRMYSG 1487
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1488 LAQTGAWGCFDEFNRINIEVLSVVAQQILSILSALTANLTRFYFEGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFR 1567
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1568 PIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLTDEEVLL 1647
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1648 LSMRDMNIAKLTSVDVPLFNAIVQDLFPNIELPVIDYGKLRDTIEQEIREMGLQITPFTLTKVLQLYETKNSRHSTMIVG 1727
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 1958663403 1728 GTGSSKT 1734
Cdd:pfam12774 321 PTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
863-1271 |
6.76e-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: 529.91 E-value: 6.76e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 863 LQNLEKELDALQQVWEITRDWEESWNQWKTGCFLTLQTEAMESMAHGLFRRLTRLAKEYKDrnWEVIETTRAKIEQFKRT 942
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRD--WDVAEELKKKIDDFKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 943 MPLISDLRNPALRERHWDQVKEEIQREFDQESESFTLEQIVKLGMDQHVEKIAEISASATKELAIEVGLQNIAKTWDSTQ 1022
Cdd:pfam08393 79 LPLIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1023 LDIVPYKDKGHHRLRGTEEVFQALEDNQVALSTMKASRFVKAFEKDVDHWERCLSLILEVIEMVLTVQRQWMYLENIFLG 1102
Cdd:pfam08393 159 FELVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1103 EDIRKQLPNESALFDQVNNNWKGIMDRMNKDNNALRSTHYPGLLETLIEMNTILEDIQKSLDMYLETKRHMFPRFYFLSN 1182
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1183 DDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIQKvggsssKWEAVGMFSGDGEYIDFLHP-VLLEGAVESWLGDVERAMR 1261
Cdd:pfam08393 319 DELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE------NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMR 392
|
410
....*....|
gi 1958663403 1262 MTLRDLLRNC 1271
Cdd:pfam08393 393 ETLRDLLKEA 402
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
930-3751 |
1.23e-134 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 477.56 E-value: 1.23e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 930 ETTRA-KIEQFKRTMPLISDL-----RNPALRE---RHWDQV----KEEIQREF-DQESESFtleqivkLGMDQHVEKIA 995
Cdd:COG5245 480 EAGRFvKLCKIMRMFSFFNSLemfsrRTLANRMaivKYLSSVvrtgPLFLQRDFfGRMSELL-------MARDMFMEVDG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 996 EISASATKELA--IEVGLQNIAKTWDSTQLDivpykdkghhrlrgtEEVFQALEDNQVALSTMKASRFvkaFEKDVDhWE 1073
Cdd:COG5245 553 VLRLFFGGEWSgiVQLSGIRRAKRCVERQID---------------DEIREWCSSVLSDDFLEERAVR---VERGAD-GA 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1074 RCLSLILEvIEMVLTVQRQWMYLENiflgEDIRKQLPNESALFDQVNNNWKGIMDRMNKDNNALRSTHYPgLLETLIEMN 1153
Cdd:COG5245 614 RRLRASSG-SPVLRRLDEYLMMMSL----EDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFY 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1154 TILEDIQKSLDMYLETKRHMFPRFyfLSNDDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIqkvggSSSKWEAVGMFSGD 1233
Cdd:COG5245 688 KEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEEMKTV-----FSSRIQKKEPFSLD 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1234 GE-YIDFLHpvLLEGA-VESWLGDVERAMRMTLRDllrncrmALKKFLNKRDkwvkdwaGQMVITASQIQ--------WT 1303
Cdd:COG5245 761 SEaYVGFFR--LYEKSiVIRGINRSMGRVLSQYLE-------SVQEALEIED-------GSFFVSRHRVRdgglekgrGC 824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1304 ADVTKCLMTAKERSDKKILKVMKkkqvSILNKYSEAIRGnltkimrlKIVALVTIEIHARDVLEKLYKGGLMDVNAFDWL 1383
Cdd:COG5245 825 DAWENCFDPPLSEYFRILEKIFP----SEEGYFFDEVLK--------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSV 892
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1384 SQLRFYwEKDVDDCIIRQTNTQFQYGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSpkgpAGTGKTETVKDLGKAL 1463
Cdd:COG5245 893 SISELP-QGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGK 967
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1464 GTYVivvncsEGLDYKSmgRMYSGLAQTGAWGcFDEFNRINIEVLSVVA--QQILSILSALTANLTRFYFEGFeinLVWS 1541
Cdd:COG5245 968 GRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVVEHGL---KSPS 1035
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1542 CGIFITMNPgyagRTELPENLKSMFRPIAMVVPDSTlIAEIIlfgegfgncKILAKKVYTLYSLAVQQLSRQDHYDFglR 1621
Cdd:COG5245 1036 TPVEMIINE----RNIVLEIGRRALDMFLSNIPFGA-IKSRR---------ESLDREIGAFNNEVDGIAREEDELMF--Y 1099
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1622 ALTSLLRyagKKRRLQPDLTDEEVLLLSmrdmnIAKLTSVDVPLFNAIvqDLFPNIELPVIdygklRDTIEQEIREMGlQ 1701
Cdd:COG5245 1100 PMFKSLK---AKHRMLEEKTEYLNKILS-----ITGLPLISDTLRERI--DTLDAEWDSFC-----RISESLKKYESQ-Q 1163
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1702 ITPFTLTKVLQLYETKNSRHSTMIVGGTGSSKTTSWrilqaslTSLCragepnfnivkEFPLNPKALSLGELYGEYDLNT 1781
Cdd:COG5245 1164 VSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHY-------TDAC-----------DYLWHVKSPYVKKKYFDADMEL 1225
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1782 NEWTDGILSSVMRAACADEKpdeKWILFDGpvdtlWIESMNSVMDDNKVLTLINGERIAMpeqvsllfeVENLAvASPAT 1861
Cdd:COG5245 1226 RQFFLMFNREDMEARLADSK---MEYEVER-----YVEKTKAEVSSLKLELSSVGEGQVV---------VSNLG-SIGDK 1287
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1862 VSRCGMVYtDYVDLGWTPYVQSWLEKRPKAEIEPLQRMFE--------------KFINKILTFKKDnCNELVPVTEYSGI 1927
Cdd:COG5245 1288 VGRCLVEY-DSISRLSTKGVFLDELGDTKRYLDECLDFFScfeevqkeidelsmVFCADALRFSAD-LYHIVKERRFSGV 1365
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1928 ISLCKLYTVLATPENGVNpADTENHAFMVEMTFVFSMIWSVCASVDEDgRKKIDSYLREIEGSFPNKDTVYEYY------ 2001
Cdd:COG5245 1366 LAGSDASESLGGKSIELA-AILEHKDLIVEMKRGINDVLKLRIFGDKC-RESTPRFYLISDGDLIKDLNERSDYeemlim 1443
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2002 ---VNPKMRTWSSFEEQLPKSWR--YPPNapfykIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSl 2076
Cdd:COG5245 1444 mfnISAVITNNGSIAGFELRGERvmLRKE-----VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS- 1517
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2077 pSSQWSVLVVNMSAQTTSNNVQSIIESRVEK-RTKGVYVPFGG---KSMITFMDDLNMPAKDMFGSQPPLELIR-LWIDY 2151
Cdd:COG5245 1518 -ELITEVKYFNFSTCTMTPSKLSVLERETEYyPNTGVVRLYPKpvvKDLVLFCDEINLPYGFEYYPPTVIVFLRpLVERQ 1596
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2152 GFWYDrVKQTIKHIRDMFLMAAMGPPGG-GRTVISPRLQSRFNIINMTFPTESQIIRIFGTMINQKLQDFEEEVKPIGNV 2230
Cdd:COG5245 1597 GFWSS-IAVSWVTICGIILYGACNPGTDeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEET 1675
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2231 VTEATlDVYNTVVQRFlPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTK-ASITRLWIHECFRVFSDRLVDTTDMEAFI 2309
Cdd:COG5245 1676 MSASV-ELYLSSKDKT-KFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPdVSLIIDWYCEAIREKIDRLVQQKESSTSR 1753
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2310 GILSDKLGTFFdltfhhlcpnkRPPIFGDFLKEPKVYEDLVDLS---VLKTAMETALNEY--NLSPSVVQMQLVLFREAI 2384
Cdd:COG5245 1754 QDLYDFGLRAI-----------REMIAGHIGEAEITFSMILFFGmacLLKKDLAVFVEEVrkIFGSSHLDVEAVAYKDAL 1822
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2385 EHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICEYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVELQATSFLFVD 2464
Cdd:COG5245 1823 LHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFE 1902
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2465 TQIADESFLEDINNILSSGEVPNLYKADEFEEIQNQIIDQARAEQIS-ESSDSLFAYLIERVRNNLHIVLCL-SPVGDPF 2542
Cdd:COG5245 1903 SIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEkDTEATLTRVFLVYMEENLPVVFSAcCSQDTSV 1982
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2543 RNWIRqYPALVNCTTINWFSEWPREALLEVAEKYL-----------VGVDLGTQE--NIHRKVAQIFVTMHWSVaqYSQK 2609
Cdd:COG5245 1983 LAGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVEtlsrdggrvffINGELGVGKgaLISEVFGDDAVVIEGRG--FEIS 2059
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2610 MLLELrrhNYVTPTNYLELVSGYKKLLGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL 2689
Cdd:COG5245 2060 MIEGS---LGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDAL 2136
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2690 VIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIV 2769
Cdd:COG5245 2137 SGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIE 2216
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2770 MQAVMILRGNEPT-WAEAKRQLGEQNFIKSLI-YFDKDNISDKVLKKIGA-YCAQPDFQPDIIGRVSLAAKSLCMWVRAM 2846
Cdd:COG5245 2217 MEDVCDLLGFEAKiWFGEQQSLRRDDFIRIIGkYPDEIEFDLEARRFREArECSDPSFTGSILNRASKACGPLKRWLVRE 2296
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2847 ELYGRLYRVVEPKRIRMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLV 2926
Cdd:COG5245 2297 CNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVS 2376
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2927 SGLAGEKARWEETVQGLEEDLGYLVGDCLIAAAFLSYMGPflTNYRDEIVNQIWIKKIWELQVPCSpRFAIDNFLTN-PT 3005
Cdd:COG5245 2377 EILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGT--LGFLCRAIEFGMSFIRISKEFRDK-EIRRRQFITEgVQ 2453
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3006 KVRDWNIQGLPSDSFSTENGIIVTRGNRWALMIDPQAQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQn 3085
Cdd:COG5245 2454 KIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIG- 2532
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3086 VQEYLDPSLNPVLNKSVARIGGRMLMRIADKEVEYNPNFR-FYLTTKLSNPHYSPEtSAKTTIVNFAVKEQGLEAQLLGI 3164
Cdd:COG5245 2533 DAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAvFWLSEGRSGDMGSIE-WKQLIQVMFVSKVLGCETEIPDA 2611
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3165 VVRKERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEVTEQLETSETTEINID 3244
Cdd:COG5245 2612 LEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRID 2691
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3245 LAREAYRPCAQRASVLFFVLNDMGRIDPMYQFSLDAYISLF-ILSIDKSHRSNKLEDRIEYLNDYhtyavyrytcrtLFE 3323
Cdd:COG5245 2692 ALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFeKWRRMKSKYLCAIRYMLMSSEWI------------LDH 2759
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3324 RHKLLFSFhmcakILETSGKLNMDEynfFLRGGVVLDREGQMDNPCTSWLADAYWDNITELDKLTNFhglMNSFEQYPRD 3403
Cdd:COG5245 2760 EDRSGFIH-----RLDVSFLLRTKR---FVSTLLEDKNYRQVLSSCSLYGNDVISHSCDRFDRDVYR---ALKHQMDNRT 2828
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3404 wHLWYTNSNpekamlpgeweNACNEMQRMLIVRSLRQ-DRVAFcvtsfivSNLGSRFieppvlnMKLVMEDSTPRSPLVF 3482
Cdd:COG5245 2829 -HSTILTSN-----------SKTNPYKEYTYNDSWAEaFEVED-------SGDLYKF-------EEGLLELIVGHAPLIY 2882
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3483 ILSPGVDptsaLLQLAEHTGMAHRfhaLSLGQGQAPIAARllregvnQGHWVFLANCHLSLSWMPN-LDKLVEQLQVEDP 3561
Cdd:COG5245 2883 AHKKSLE----NERNVDRLGSKEN---EVYAVLNSLFSRK-------EKSWFEVYNISLSFGWFKRyVEDVVYPIKASRV 2948
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3562 HPSF-RLWLSSSPHPDFPISILQASIKMTTEPPKGLKANMTRLYqlmtEAQFThcskPTKYK-----KLLFALCFFHSIL 3635
Cdd:COG5245 2949 CGKVkNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLV----EIDRY----PFDYTlviacDDAFYLSWEHAAV 3020
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3636 LERKKFLQLGWNIIYGFNDSDFEVSENLLS--LYLDEYEETPWDALKYLIAGVNYGGHVTDDWDRRLLTTYINDYFC--D 3711
Cdd:COG5245 3021 ASVISAGPKENNEEIYFGDKDFEFKTHLLKniLFLNHLNARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGAheT 3100
|
2890 2900 2910 2920
....*....|....*....|....*....|....*....|.
gi 1958663403 3712 LSLTTPSYRLS-VLDTYYIPKDGSLASYKEYISLLPSMDPP 3751
Cdd:COG5245 3101 SSQILASVPGGdPELVKFHMEEMCRSSAFGVIGQLPDLALC 3141
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
3766-4066 |
2.86e-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: 405.85 E-value: 2.86e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3766 ITEARTLFETLLSLQPQITPTRIGG-QSREEKVLELAADVKQKIPEMIDYE-GTRKLLALDPSPLNVVLLQEIQRYNKLM 3843
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGgSSREEIVLELAKDILEKLPEPFDIEeAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3844 KTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLWGKV-YPSQKPLASWTRDLAVRVEQFETWANRAHPPVLFWL 3922
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKsYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3923 SGFTFPTGFLTAVLQSAARQNNISVDSLSWEFIV-STVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVC 4001
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVtKKVSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663403 4002 LMPTIHFRPAE-SRKKSAKGMYSCPCYYYPNRAGSadraSFVIGIDLRSGaMTSDHWIKRGTALLM 4066
Cdd:pfam18199 241 PLPVIHLKPVEsDKKKLDENTYECPVYKTSERHST----NFVFSVDLPTD-KPPDHWILRGVALLL 301
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2375-2635 |
4.61e-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: 4.61e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2375 MQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICEYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVE 2454
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2455 LQATSFLFVDTQIADESFLEDINNILSSGEVPNLYKADEFEEIQNQIIDQARAEQISESSDSLFAYLIERVRNNLHIVLC 2534
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2535 LSPVGDPFRNWIRQYPALVNCTTINWFSEWPREALLEVAEKYLvgVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLEL 2614
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFL--EDIEIPEELKSNVVKVFVYVHSSVEDMSKKFYEEL 238
|
250 260
....*....|....*....|.
gi 1958663403 2615 RRHNYVTPTNYLELVSGYKKL 2635
Cdd:pfam12780 239 KRKNYVTPKSYLELLRLYKNL 259
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
1-360 |
2.88e-85 |
|
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: 292.56 E-value: 2.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1 MHTQFSNRGWVLDQTSIFAQVDAFVQRCKDLIEVCDCQYHFARwldgtqgpLPCFFGAQGPQITRNLLEIEDIFHKNLQT 80
Cdd:pfam08385 198 LEESPRERPWDFSERYIFGRFDAFLERLEKILELFETIEQFSK--------LEKIGGTKGPELEGVIEEILEEFQEAYKV 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 81 LRAVRGGILDVKNTSWHEDYNKFRAGIKDLEVMTQNLITSAFELVRDVEHGVLLLDTFHRLANREAIMRTYEKKAVDLYM 160
Cdd:pfam08385 270 FKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQ 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 161 LFNSELALVNRELNKKW---PYLEPYMAQYSGQAHWVRILRRRIDRVMNCLSGAHFLPHIGTGEETVHTYQQMVQAIDEL 237
Cdd:pfam08385 350 MFKKELDAVKKIFDKQKynpSPIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEY 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 238 VRKTFQEWTATLDKDCIRRLDMPLLRISQEKAGMLDVNFDKTLLILFVEIDYWERLLFETPHYVMNVADRAEDLRILREN 317
Cdd:pfam08385 430 ERLIYEAWLKEVEEASEGNLKRPLLVRHPETGKLLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAES 509
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958663403 318 LLLVARDYNRIIAMLSPDEQALFKERIRFLDKKIHPGLKKLNW 360
Cdd:pfam08385 510 LELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTW 552
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2053-2195 |
1.04e-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: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2053 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPfgGKSMITFMDDLNMPA 2132
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK--AKPGVLFIDEIDSLS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958663403 2133 KDMFGSQppLELIRLWIDYGFWYDRVKqtikhirdmFLMAAMGPPGGGrtvISPRLQSRFNII 2195
Cdd:cd00009 98 RGAQNAL--LRVLETLNDLRIDRENVR---------VIGATNRPLLGD---LDRALYDRLDIR 146
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2656-2947 |
7.67e-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: 52.38 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2656 KIDETREKVEVMSLELEDAKKkVAEFQKQCEEY-LVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEA 2734
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAER-YQALLKEKREYeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2735 LPALEEAMRALESLN-------KKDIGEIKsygrppAQVEivmQAVMILRGNEptwAEAKRQLGEQNFIKSLIYFDKDNI 2807
Cdd:TIGR02169 271 EQLLEELNKKIKDLGeeeqlrvKEKIGELE------AEIA---SLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2808 sDKVLKKIGAYCAQpdfqpdiigRVSLAAKslcmwvramelygrlyrvVEPKRIRMNAAIAQLQEKQAALAEAQEKLREV 2887
Cdd:TIGR02169 339 -EELEREIEEERKR---------RDKLTEE------------------YAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2888 AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 2947
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2613-2757 |
9.73e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2613 ELRRHNYVTPTNYLELVSGYKKLLGE---KRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL 2689
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958663403 2690 VIIVQQKREADEQQKAVtansekiaiEEVKcqaLADNAQKDLEEALPALEEAMRALESLNKKDIGEIK 2757
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKA---------EEAK---KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2053-2111 |
3.08e-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: 3.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663403 2053 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKG 2111
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 ... |
1408-1734 |
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: 649.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1408 YGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGTYVIVVNCSEGLDYKSMGRMYSG 1487
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1488 LAQTGAWGCFDEFNRINIEVLSVVAQQILSILSALTANLTRFYFEGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFR 1567
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1568 PIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLTDEEVLL 1647
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1648 LSMRDMNIAKLTSVDVPLFNAIVQDLFPNIELPVIDYGKLRDTIEQEIREMGLQITPFTLTKVLQLYETKNSRHSTMIVG 1727
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 1958663403 1728 GTGSSKT 1734
Cdd:pfam12774 321 PTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
863-1271 |
6.76e-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: 529.91 E-value: 6.76e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 863 LQNLEKELDALQQVWEITRDWEESWNQWKTGCFLTLQTEAMESMAHGLFRRLTRLAKEYKDrnWEVIETTRAKIEQFKRT 942
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRD--WDVAEELKKKIDDFKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 943 MPLISDLRNPALRERHWDQVKEEIQREFDQESESFTLEQIVKLGMDQHVEKIAEISASATKELAIEVGLQNIAKTWDSTQ 1022
Cdd:pfam08393 79 LPLIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1023 LDIVPYKDKGHHRLRGTEEVFQALEDNQVALSTMKASRFVKAFEKDVDHWERCLSLILEVIEMVLTVQRQWMYLENIFLG 1102
Cdd:pfam08393 159 FELVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1103 EDIRKQLPNESALFDQVNNNWKGIMDRMNKDNNALRSTHYPGLLETLIEMNTILEDIQKSLDMYLETKRHMFPRFYFLSN 1182
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1183 DDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIQKvggsssKWEAVGMFSGDGEYIDFLHP-VLLEGAVESWLGDVERAMR 1261
Cdd:pfam08393 319 DELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE------NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMR 392
|
410
....*....|
gi 1958663403 1262 MTLRDLLRNC 1271
Cdd:pfam08393 393 ETLRDLLKEA 402
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
930-3751 |
1.23e-134 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 477.56 E-value: 1.23e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 930 ETTRA-KIEQFKRTMPLISDL-----RNPALRE---RHWDQV----KEEIQREF-DQESESFtleqivkLGMDQHVEKIA 995
Cdd:COG5245 480 EAGRFvKLCKIMRMFSFFNSLemfsrRTLANRMaivKYLSSVvrtgPLFLQRDFfGRMSELL-------MARDMFMEVDG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 996 EISASATKELA--IEVGLQNIAKTWDSTQLDivpykdkghhrlrgtEEVFQALEDNQVALSTMKASRFvkaFEKDVDhWE 1073
Cdd:COG5245 553 VLRLFFGGEWSgiVQLSGIRRAKRCVERQID---------------DEIREWCSSVLSDDFLEERAVR---VERGAD-GA 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1074 RCLSLILEvIEMVLTVQRQWMYLENiflgEDIRKQLPNESALFDQVNNNWKGIMDRMNKDNNALRSTHYPgLLETLIEMN 1153
Cdd:COG5245 614 RRLRASSG-SPVLRRLDEYLMMMSL----EDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFY 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1154 TILEDIQKSLDMYLETKRHMFPRFyfLSNDDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIqkvggSSSKWEAVGMFSGD 1233
Cdd:COG5245 688 KEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEEMKTV-----FSSRIQKKEPFSLD 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1234 GE-YIDFLHpvLLEGA-VESWLGDVERAMRMTLRDllrncrmALKKFLNKRDkwvkdwaGQMVITASQIQ--------WT 1303
Cdd:COG5245 761 SEaYVGFFR--LYEKSiVIRGINRSMGRVLSQYLE-------SVQEALEIED-------GSFFVSRHRVRdgglekgrGC 824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1304 ADVTKCLMTAKERSDKKILKVMKkkqvSILNKYSEAIRGnltkimrlKIVALVTIEIHARDVLEKLYKGGLMDVNAFDWL 1383
Cdd:COG5245 825 DAWENCFDPPLSEYFRILEKIFP----SEEGYFFDEVLK--------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSV 892
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1384 SQLRFYwEKDVDDCIIRQTNTQFQYGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSpkgpAGTGKTETVKDLGKAL 1463
Cdd:COG5245 893 SISELP-QGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGK 967
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1464 GTYVivvncsEGLDYKSmgRMYSGLAQTGAWGcFDEFNRINIEVLSVVA--QQILSILSALTANLTRFYFEGFeinLVWS 1541
Cdd:COG5245 968 GRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVVEHGL---KSPS 1035
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1542 CGIFITMNPgyagRTELPENLKSMFRPIAMVVPDSTlIAEIIlfgegfgncKILAKKVYTLYSLAVQQLSRQDHYDFglR 1621
Cdd:COG5245 1036 TPVEMIINE----RNIVLEIGRRALDMFLSNIPFGA-IKSRR---------ESLDREIGAFNNEVDGIAREEDELMF--Y 1099
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1622 ALTSLLRyagKKRRLQPDLTDEEVLLLSmrdmnIAKLTSVDVPLFNAIvqDLFPNIELPVIdygklRDTIEQEIREMGlQ 1701
Cdd:COG5245 1100 PMFKSLK---AKHRMLEEKTEYLNKILS-----ITGLPLISDTLRERI--DTLDAEWDSFC-----RISESLKKYESQ-Q 1163
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1702 ITPFTLTKVLQLYETKNSRHSTMIVGGTGSSKTTSWrilqaslTSLCragepnfnivkEFPLNPKALSLGELYGEYDLNT 1781
Cdd:COG5245 1164 VSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHY-------TDAC-----------DYLWHVKSPYVKKKYFDADMEL 1225
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1782 NEWTDGILSSVMRAACADEKpdeKWILFDGpvdtlWIESMNSVMDDNKVLTLINGERIAMpeqvsllfeVENLAvASPAT 1861
Cdd:COG5245 1226 RQFFLMFNREDMEARLADSK---MEYEVER-----YVEKTKAEVSSLKLELSSVGEGQVV---------VSNLG-SIGDK 1287
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1862 VSRCGMVYtDYVDLGWTPYVQSWLEKRPKAEIEPLQRMFE--------------KFINKILTFKKDnCNELVPVTEYSGI 1927
Cdd:COG5245 1288 VGRCLVEY-DSISRLSTKGVFLDELGDTKRYLDECLDFFScfeevqkeidelsmVFCADALRFSAD-LYHIVKERRFSGV 1365
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1928 ISLCKLYTVLATPENGVNpADTENHAFMVEMTFVFSMIWSVCASVDEDgRKKIDSYLREIEGSFPNKDTVYEYY------ 2001
Cdd:COG5245 1366 LAGSDASESLGGKSIELA-AILEHKDLIVEMKRGINDVLKLRIFGDKC-RESTPRFYLISDGDLIKDLNERSDYeemlim 1443
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2002 ---VNPKMRTWSSFEEQLPKSWR--YPPNapfykIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSl 2076
Cdd:COG5245 1444 mfnISAVITNNGSIAGFELRGERvmLRKE-----VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS- 1517
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2077 pSSQWSVLVVNMSAQTTSNNVQSIIESRVEK-RTKGVYVPFGG---KSMITFMDDLNMPAKDMFGSQPPLELIR-LWIDY 2151
Cdd:COG5245 1518 -ELITEVKYFNFSTCTMTPSKLSVLERETEYyPNTGVVRLYPKpvvKDLVLFCDEINLPYGFEYYPPTVIVFLRpLVERQ 1596
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2152 GFWYDrVKQTIKHIRDMFLMAAMGPPGG-GRTVISPRLQSRFNIINMTFPTESQIIRIFGTMINQKLQDFEEEVKPIGNV 2230
Cdd:COG5245 1597 GFWSS-IAVSWVTICGIILYGACNPGTDeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEET 1675
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2231 VTEATlDVYNTVVQRFlPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTK-ASITRLWIHECFRVFSDRLVDTTDMEAFI 2309
Cdd:COG5245 1676 MSASV-ELYLSSKDKT-KFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPdVSLIIDWYCEAIREKIDRLVQQKESSTSR 1753
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2310 GILSDKLGTFFdltfhhlcpnkRPPIFGDFLKEPKVYEDLVDLS---VLKTAMETALNEY--NLSPSVVQMQLVLFREAI 2384
Cdd:COG5245 1754 QDLYDFGLRAI-----------REMIAGHIGEAEITFSMILFFGmacLLKKDLAVFVEEVrkIFGSSHLDVEAVAYKDAL 1822
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2385 EHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICEYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVELQATSFLFVD 2464
Cdd:COG5245 1823 LHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFE 1902
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2465 TQIADESFLEDINNILSSGEVPNLYKADEFEEIQNQIIDQARAEQIS-ESSDSLFAYLIERVRNNLHIVLCL-SPVGDPF 2542
Cdd:COG5245 1903 SIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEkDTEATLTRVFLVYMEENLPVVFSAcCSQDTSV 1982
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2543 RNWIRqYPALVNCTTINWFSEWPREALLEVAEKYL-----------VGVDLGTQE--NIHRKVAQIFVTMHWSVaqYSQK 2609
Cdd:COG5245 1983 LAGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVEtlsrdggrvffINGELGVGKgaLISEVFGDDAVVIEGRG--FEIS 2059
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2610 MLLELrrhNYVTPTNYLELVSGYKKLLGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL 2689
Cdd:COG5245 2060 MIEGS---LGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDAL 2136
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2690 VIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIV 2769
Cdd:COG5245 2137 SGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIE 2216
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2770 MQAVMILRGNEPT-WAEAKRQLGEQNFIKSLI-YFDKDNISDKVLKKIGA-YCAQPDFQPDIIGRVSLAAKSLCMWVRAM 2846
Cdd:COG5245 2217 MEDVCDLLGFEAKiWFGEQQSLRRDDFIRIIGkYPDEIEFDLEARRFREArECSDPSFTGSILNRASKACGPLKRWLVRE 2296
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2847 ELYGRLYRVVEPKRIRMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLV 2926
Cdd:COG5245 2297 CNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVS 2376
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2927 SGLAGEKARWEETVQGLEEDLGYLVGDCLIAAAFLSYMGPflTNYRDEIVNQIWIKKIWELQVPCSpRFAIDNFLTN-PT 3005
Cdd:COG5245 2377 EILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGT--LGFLCRAIEFGMSFIRISKEFRDK-EIRRRQFITEgVQ 2453
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3006 KVRDWNIQGLPSDSFSTENGIIVTRGNRWALMIDPQAQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQn 3085
Cdd:COG5245 2454 KIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIG- 2532
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3086 VQEYLDPSLNPVLNKSVARIGGRMLMRIADKEVEYNPNFR-FYLTTKLSNPHYSPEtSAKTTIVNFAVKEQGLEAQLLGI 3164
Cdd:COG5245 2533 DAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAvFWLSEGRSGDMGSIE-WKQLIQVMFVSKVLGCETEIPDA 2611
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3165 VVRKERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEVTEQLETSETTEINID 3244
Cdd:COG5245 2612 LEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRID 2691
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3245 LAREAYRPCAQRASVLFFVLNDMGRIDPMYQFSLDAYISLF-ILSIDKSHRSNKLEDRIEYLNDYhtyavyrytcrtLFE 3323
Cdd:COG5245 2692 ALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFeKWRRMKSKYLCAIRYMLMSSEWI------------LDH 2759
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3324 RHKLLFSFhmcakILETSGKLNMDEynfFLRGGVVLDREGQMDNPCTSWLADAYWDNITELDKLTNFhglMNSFEQYPRD 3403
Cdd:COG5245 2760 EDRSGFIH-----RLDVSFLLRTKR---FVSTLLEDKNYRQVLSSCSLYGNDVISHSCDRFDRDVYR---ALKHQMDNRT 2828
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3404 wHLWYTNSNpekamlpgeweNACNEMQRMLIVRSLRQ-DRVAFcvtsfivSNLGSRFieppvlnMKLVMEDSTPRSPLVF 3482
Cdd:COG5245 2829 -HSTILTSN-----------SKTNPYKEYTYNDSWAEaFEVED-------SGDLYKF-------EEGLLELIVGHAPLIY 2882
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3483 ILSPGVDptsaLLQLAEHTGMAHRfhaLSLGQGQAPIAARllregvnQGHWVFLANCHLSLSWMPN-LDKLVEQLQVEDP 3561
Cdd:COG5245 2883 AHKKSLE----NERNVDRLGSKEN---EVYAVLNSLFSRK-------EKSWFEVYNISLSFGWFKRyVEDVVYPIKASRV 2948
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3562 HPSF-RLWLSSSPHPDFPISILQASIKMTTEPPKGLKANMTRLYqlmtEAQFThcskPTKYK-----KLLFALCFFHSIL 3635
Cdd:COG5245 2949 CGKVkNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLV----EIDRY----PFDYTlviacDDAFYLSWEHAAV 3020
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3636 LERKKFLQLGWNIIYGFNDSDFEVSENLLS--LYLDEYEETPWDALKYLIAGVNYGGHVTDDWDRRLLTTYINDYFC--D 3711
Cdd:COG5245 3021 ASVISAGPKENNEEIYFGDKDFEFKTHLLKniLFLNHLNARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGAheT 3100
|
2890 2900 2910 2920
....*....|....*....|....*....|....*....|.
gi 1958663403 3712 LSLTTPSYRLS-VLDTYYIPKDGSLASYKEYISLLPSMDPP 3751
Cdd:COG5245 3101 SSQILASVPGGdPELVKFHMEEMCRSSAFGVIGQLPDLALC 3141
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
3766-4066 |
2.86e-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: 405.85 E-value: 2.86e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3766 ITEARTLFETLLSLQPQITPTRIGG-QSREEKVLELAADVKQKIPEMIDYE-GTRKLLALDPSPLNVVLLQEIQRYNKLM 3843
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGgSSREEIVLELAKDILEKLPEPFDIEeAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3844 KTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLWGKV-YPSQKPLASWTRDLAVRVEQFETWANRAHPPVLFWL 3922
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKsYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3923 SGFTFPTGFLTAVLQSAARQNNISVDSLSWEFIV-STVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVC 4001
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVtKKVSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663403 4002 LMPTIHFRPAE-SRKKSAKGMYSCPCYYYPNRAGSadraSFVIGIDLRSGaMTSDHWIKRGTALLM 4066
Cdd:pfam18199 241 PLPVIHLKPVEsDKKKLDENTYECPVYKTSERHST----NFVFSVDLPTD-KPPDHWILRGVALLL 301
|
|
| AAA_8 |
pfam12780 |
P-loop containing dynein motor region D4; The 380 kDa motor unit of dynein belongs to the AAA ... |
2375-2635 |
4.61e-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: 4.61e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2375 MQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICEYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVE 2454
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2455 LQATSFLFVDTQIADESFLEDINNILSSGEVPNLYKADEFEEIQNQIIDQARAEQISESSDSLFAYLIERVRNNLHIVLC 2534
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2535 LSPVGDPFRNWIRQYPALVNCTTINWFSEWPREALLEVAEKYLvgVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLEL 2614
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFL--EDIEIPEELKSNVVKVFVYVHSSVEDMSKKFYEEL 238
|
250 260
....*....|....*....|.
gi 1958663403 2615 RRHNYVTPTNYLELVSGYKKL 2635
Cdd:pfam12780 239 KRKNYVTPKSYLELLRLYKNL 259
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3008-3229 |
2.76e-123 |
|
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: 388.34 E-value: 2.76e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3008 RDWNIQGLPSDSFSTENGIIVTRGNRWALMIDPQAQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQNVQ 3087
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3088 EYLDPSLNPVLNKSVARIGGRMLMRIADKEVEYNPNFRFYLTTKLSNPHYSPETSAKTTIVNFAVKEQGLEAQLLGIVVR 3167
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958663403 3168 KERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEV 3229
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2022-2200 |
9.09e-104 |
|
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: 330.51 E-value: 9.09e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2022 YPPNAPFYKIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSII 2101
Cdd:pfam12775 1 IPPDVPFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQDII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2102 ESRVEKRTKGVYVPFGGKSMITFMDDLNMPAKDMFGSQPPLELIRLWIDYGFWYDRVKQTIKHIRDMFLMAAMGPPGGGR 2181
Cdd:pfam12775 81 ESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPGGGR 160
|
170
....*....|....*....
gi 1958663403 2182 TVISPRLQSRFNIINMTFP 2200
Cdd:pfam12775 161 NDITPRLLRHFNVFNITFP 179
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
1-360 |
2.88e-85 |
|
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: 292.56 E-value: 2.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1 MHTQFSNRGWVLDQTSIFAQVDAFVQRCKDLIEVCDCQYHFARwldgtqgpLPCFFGAQGPQITRNLLEIEDIFHKNLQT 80
Cdd:pfam08385 198 LEESPRERPWDFSERYIFGRFDAFLERLEKILELFETIEQFSK--------LEKIGGTKGPELEGVIEEILEEFQEAYKV 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 81 LRAVRGGILDVKNTSWHEDYNKFRAGIKDLEVMTQNLITSAFELVRDVEHGVLLLDTFHRLANREAIMRTYEKKAVDLYM 160
Cdd:pfam08385 270 FKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEEKYTDLLQ 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 161 LFNSELALVNRELNKKW---PYLEPYMAQYSGQAHWVRILRRRIDRVMNCLSGAHFLPHIGTGEETVHTYQQMVQAIDEL 237
Cdd:pfam08385 350 MFKKELDAVKKIFDKQKynpSPIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLLKHAEGKKVIKKYNELAKKLDEY 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 238 VRKTFQEWTATLDKDCIRRLDMPLLRISQEKAGMLDVNFDKTLLILFVEIDYWERLLFETPHYVMNVADRAEDLRILREN 317
Cdd:pfam08385 430 ERLIYEAWLKEVEEASEGNLKRPLLVRHPETGKLLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEERLRPYAES 509
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958663403 318 LLLVARDYNRIIAMLSPDEQALFKERIRFLDKKIHPGLKKLNW 360
Cdd:pfam08385 510 LELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTW 552
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
3621-3760 |
7.80e-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: 240.05 E-value: 7.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3621 YKKLLFALCFFHSILLERKKFLQLGWNIIYGFNDSDFEVSENLLSLYLDEY-EETPWDALKYLIAGVNYGGHVTDDWDRR 3699
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYdEKIPWDALRYLIGEINYGGRVTDDWDRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958663403 3700 LLTTYINDYFCDlSLTTPSYRLSVlDTYYIPKDGSLASYKEYISLLPSMDPPEAFGQHPNA 3760
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 ... |
3475-3589 |
1.35e-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: 212.69 E-value: 1.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 3475 TPRSPLVFILSPGVDPTSALLQLAEHTGMAHRFHALSLGQGQAPIAARLLREGVNQGHWVFLANCHLSLSWMPNLDKLVE 3554
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGFGGKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILE 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1958663403 3555 QLQVEDPHPSFRLWLSSSPHPDFPISILQASIKMT 3589
Cdd:pfam03028 81 ELPEETLHPDFRLWLTSEPSPKFPISILQNSIKIT 115
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
2649-2984 |
3.47e-56 |
|
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: 200.68 E-value: 3.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2649 KLRTGLFKIDETREKVEvmsleleDAKKKVA----EFQKQCE--EYLVIIVQQKREADEQQKAVTANSE-KIAIEEVKCQ 2721
Cdd:pfam12777 2 RLENGLLKLHSTAAQVD-------DLKAKLAaqeaELKQKNEdaDKLIQVVGIEADKVSKEKAIADEEEqKVAVIMKEVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2722 ALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMIL---RGNEP---TWAEAKRQLGE-QN 2794
Cdd:pfam12777 75 EKQKACEEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILmapGGKIPkdkSWKAAKIMMAKvDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2795 FIKSLIYFDKDNISDKVLKKIGAYCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRIRMNAAIAQLQEKQ 2874
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2875 AALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDC 2954
Cdd:pfam12777 235 EKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDI 314
|
330 340 350
....*....|....*....|....*....|
gi 1958663403 2955 LIAAAFLSYMGPFLTNYRDEIVNQIWIKKI 2984
Cdd:pfam12777 315 LLISAFISYLGFFTKKYRNELLDKFWIPYI 344
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
1896-2014 |
5.37e-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: 120.08 E-value: 5.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1896 LQRMFEKFINKILTFKKDNCNELVPVTEYSGIISLCKLYTVLATP---ENGVNPADTENHAFMVEMTFVFSMIWSVCASV 1972
Cdd:pfam17852 1 LEPLFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDEvleYNGVHPLSPDKLKEYLEKLFLFALVWSIGGTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1958663403 1973 DEDGRKKIDSYLREIEGS----FPNKDTVYEYYVNPKMRTWSSFEE 2014
Cdd:pfam17852 81 DEDSRKKFDEFLRELFSGldlpPPEKGTVYDYFVDLEKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2054-2192 |
2.49e-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: 103.91 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2054 PVLLVGPVGTGKTSIAQSVLQSLpsSQWSVLVVNMSAQTTSNNVQSIIESRVE--KRTKGVYVPFGGKSMITFMDDLNMP 2131
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL--SNRPVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958663403 2132 AKDMFGSQ-PPLELIRLWIDYGFWYDRVKQTikhirDMFLMAAMGPPGGGRTVISPRLQSRF 2192
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. |
2233-2321 |
9.92e-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: 78.44 E-value: 9.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2233 EATLDVYNTVVQRFLPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTKASITRLWIHECFRVFSDRLVDTTDMEAFIGIL 2312
Cdd:pfam17857 3 AAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDKIQ 82
|
....*....
gi 1958663403 2313 SDKLGTFFD 2321
Cdd:pfam17857 83 MASLKKFFD 91
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2053-2195 |
1.04e-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: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2053 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPfgGKSMITFMDDLNMPA 2132
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK--AKPGVLFIDEIDSLS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958663403 2133 KDMFGSQppLELIRLWIDYGFWYDRVKqtikhirdmFLMAAMGPPGGGrtvISPRLQSRFNII 2195
Cdd:cd00009 98 RGAQNAL--LRVLETLNDLRIDRENVR---------VIGATNRPLLGD---LDRALYDRLDIR 146
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1724-1865 |
1.21e-07 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 53.45 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1724 MIVGGTGSSKTTSWRILqASLtsLCRAgepNFNIVkefpLNPKALSLGELYGEYDLNTN--EWTDGILssvMRAAcadek 1801
Cdd:pfam07728 3 LLVGPPGTGKTELAERL-AAA--LSNR---PVFYV----QLTRDTTEEDLFGRRNIDPGgaSWVDGPL---VRAA----- 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958663403 1802 pDEKWILFDGPVDTL---WIESMNSVMDDNKVLTLINGERI-AMPEQVSLLFEVENL----AVASPATVSRC 1865
Cdd:pfam07728 65 -REGEIAVLDEINRAnpdVLNSLLSLLDERRLLLPDGGELVkAAPDGFRLIATMNPLdrglNELSPALRSRF 135
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2570-2914 |
4.35e-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: 56.27 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2570 LEVAEKYLVGVDLGTQENIHRKVAQIFVTMhwSVAQYSQKMLLELRRHNYVTPTNYLELVSGYKKLLGEKR---QELLDQ 2646
Cdd:pfam05483 434 LKGKEQELIFLLQAREKEIHDLEIQLTAIK--TSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKeltQEASDM 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2647 ANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKRE-----------ADEQQKAVTANSEKIAI 2715
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEvkckldkseenARSIEYEVLKKEKQMKI 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2716 EEVKCqalaDNAQKDLEEALPALEEAMRALESLNKKDIGEIKsygrppaQVEIVMQAVMILrgnEPTWAEAKRQLGE--Q 2793
Cdd:pfam05483 592 LENKC----NNLKKQIENKNKNIEELHQENKALKKKGSAENK-------QLNAYEIKVNKL---ELELASAKQKFEEiiD 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2794 NFIKSLIyfDKDNISDKVLKKIGAYCAQPD----FQPDIIGRVSlaaKSLCMWVRAMELYGRLY-RVVEPKRIRMNAAIA 2868
Cdd:pfam05483 658 NYQKEIE--DKKISEEKLLEEVEKAKAIADeavkLQKEIDKRCQ---HKIAEMVALMEKHKHQYdKIIEERDSELGLYKN 732
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958663403 2869 QLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEE 2914
Cdd:pfam05483 733 KEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1445-1566 |
2.22e-06 |
|
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: 49.98 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 1445 KGPAGTGKTETVKDLGKALGTY-VIVVNCSE---------GLDYKSMG--RMYSGL---AQTGAWGCFDEFNRINIEVLS 1509
Cdd:pfam07728 5 VGPPGTGKTELAERLAAALSNRpVFYVQLTRdtteedlfgRRNIDPGGasWVDGPLvraAREGEIAVLDEINRANPDVLN 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958663403 1510 VVaqqiLSILSA----LTANLTRFYFEGFEINLVwscgifITMNPGYAGRTELPENLKSMF 1566
Cdd:pfam07728 85 SL----LSLLDErrllLPDGGELVKAAPDGFRLI------ATMNPLDRGLNELSPALRSRF 135
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2656-2947 |
7.67e-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: 52.38 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2656 KIDETREKVEVMSLELEDAKKkVAEFQKQCEEY-LVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEA 2734
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAER-YQALLKEKREYeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2735 LPALEEAMRALESLN-------KKDIGEIKsygrppAQVEivmQAVMILRGNEptwAEAKRQLGEQNFIKSLIYFDKDNI 2807
Cdd:TIGR02169 271 EQLLEELNKKIKDLGeeeqlrvKEKIGELE------AEIA---SLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2808 sDKVLKKIGAYCAQpdfqpdiigRVSLAAKslcmwvramelygrlyrvVEPKRIRMNAAIAQLQEKQAALAEAQEKLREV 2887
Cdd:TIGR02169 339 -EELEREIEEERKR---------RDKLTEE------------------YAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2888 AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 2947
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2613-2757 |
9.73e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2613 ELRRHNYVTPTNYLELVSGYKKLLGE---KRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL 2689
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958663403 2690 VIIVQQKREADEQQKAVtansekiaiEEVKcqaLADNAQKDLEEALPALEEAMRALESLNKKDIGEIK 2757
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKA---------EEAK---KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2636-2950 |
1.69e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2636 LGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL--VIIVQQKREADEQQKAVTANSEKI 2713
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrLEELEERHELYEEAKAKKEELERL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2714 AiEEVKCQALaDNAQKDLEEALPALEEAMRALESLNKKdIGEIKSygrppaQVEIVMQAVMILRGNEPTWAEAKRQLGEQ 2793
Cdd:PRK03918 378 K-KRLTGLTP-EKLEKELEELEKAKEEIEEEISKITAR-IGELKK------EIKELKKAIEELKKAKGKCPVCGRELTEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2794 nfiksliyfDKDNISDKVLKKIGaycaqpDFQPDIIgrvSLAAKSLCMWVRAMELYGRLYRvvEPKRIRMNAAIAQLQEK 2873
Cdd:PRK03918 449 ---------HRKELLEEYTAELK------RIEKELK---EIEEKERKLRKELRELEKVLKK--ESELIKLKELAEQLKEL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2874 QAALAEAQ-EKLREVAEKLEMLKKQYD----------EKLAQKEELRKKSEEMELKLERAGMLVSGLAGE-KARWEETVQ 2941
Cdd:PRK03918 509 EEKLKKYNlEELEKKAEEYEKLKEKLIklkgeikslkKELEKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVE 588
|
....*....
gi 1958663403 2942 GLEEDLGYL 2950
Cdd:PRK03918 589 ELEERLKEL 597
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2657-2921 |
5.24e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2657 IDETREKVEVMSLELEDAKKKVAEFQKQCE--EYLVII------VQQKREADEQ---QKAVTANSEKIAIEEVKCQA--L 2723
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLEraEDLVEAedrierLEERREDLEEliaERRETIEEKRERAEELRERAaeL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2724 ADNAQKDLEEALPALEEAMRALESLNK--KDIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAKRQLGEQNfiksliy 2801
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAElnSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELN------- 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2802 fdkDNISDKvlkkigaycaqpdfqpdiigrvsLAAKSlcmwVRAMELYGRlyrvVEPKRIrmNAAIAQLQEKQAALAEAQ 2881
Cdd:PRK02224 623 ---DERRER-----------------------LAEKR----ERKRELEAE----FDEARI--EEAREDKERAEEYLEQVE 666
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958663403 2882 EKLREVAEKLEMLKKQ---YDEKLAQKEELRKKSEEMELKLER 2921
Cdd:PRK02224 667 EKLDELREERDDLQAEigaVENELEELEELRERREALENRVEA 709
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2638-2744 |
5.41e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2638 EKRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQ-KREADEQQKAVTANSEKIAiE 2716
Cdd:PRK09510 91 ELQQKQAAEQERLK----QLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAaKAKAEAEAKRAAAAAKKAA-A 165
|
90 100
....*....|....*....|....*...
gi 1958663403 2717 EVKCQALADNAQKDLEEALPALEEAMRA 2744
Cdd:PRK09510 166 EAKKKAEAEAAKKAAAEAKKKAEAEAAA 193
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2641-2751 |
5.69e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2641 QELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIaieeVKC 2720
Cdd:COG1340 146 EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEI----VEA 221
|
90 100 110
....*....|....*....|....*....|.
gi 1958663403 2721 QALADNAQKDLEEALPALEEAMRALESLNKK 2751
Cdd:COG1340 222 QEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2636-2929 |
6.10e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2636 LGEKRQELLDQANKLRTGLF----KIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVII---VQQKREADEQQKAVTA 2708
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEeltaELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrlEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2709 NSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEptwAEAKR 2788
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV---AQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2789 QLGEQNfiKSLIYFDKdnisdkvlkkigaycaqpdfqpdiigRVSLAAKSLCMWVRAMELYGRlyrvvEPKRIRMNAAIA 2868
Cdd:TIGR02168 394 QIASLN--NEIERLEA--------------------------RLERLEDRRERLQQEIEELLK-----KLEEAELKELQA 440
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958663403 2869 QLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKlaqKEELRKKSEEMELKLERAGMLVSGL 2929
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEA---EQALDAAERELAQLQARLDSLERLQ 498
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2656-2941 |
6.49e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2656 KIDETREKVEVMSLELEDAKKKVAEFQKQceeylviIVQQKREADEQQKAVTANSEKIaieevkcqalaDNAQKDLEEAL 2735
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAE-------LEELNEEYNELQAELEALQAEI-----------DKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2736 PALEEAMRALeslnKKDIGEIKSYGRPPAQVEIVMQAvmilrgneptwaeakrqlgeqnfiksliyfdkDNISDkVLKKI 2815
Cdd:COG3883 79 AEIEERREEL----GERARALYRSGGSVSYLDVLLGS--------------------------------ESFSD-FLDRL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2816 GAYCAQPDFQPDIIGRVslaakslcmwvramelygrlyrvvepkrirmNAAIAQLQEKQAALAEAQEKLREVAEKLEMLK 2895
Cdd:COG3883 122 SALSKIADADADLLEEL-------------------------------KADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958663403 2896 KQYDEKLAQKEELRK--KSEEMELKLERAGMLVSGLAGEKARWEETVQ 2941
Cdd:COG3883 171 AELEAQQAEQEALLAqlSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2566-2956 |
8.48e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2566 REAllEVAEKYLvgvDLGTQENIHRKvaqifvtmhwsvaqysQKMLLELRRHNyvtptNYLELVSGYKKLLGEKRQELLD 2645
Cdd:COG1196 207 RQA--EKAERYR---ELKEELKELEA----------------ELLLLKLRELE-----AELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2646 QANKLRTglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL-VIIVQQKREADEQQKAVTANSEKIAIEEV--KCQA 2722
Cdd:COG1196 261 ELAELEA---ELEELRLELEELELELEEAQAEEYELLAELARLEqDIARLEERRRELEERLEELEEELAELEEEleELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2723 LADNAQKDLEEALPALEEAMRALESLNKkdigeiksygrppAQVEIVMQAVMILRGNEPTWAEAKRQLGEQNFIKSLIYF 2802
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEE-------------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2803 DKDNISDKVLKKIgaycaqpdfqpdiigrvslaakslcmwvRAMELYGRLYRVVEPKRIRMNAAIAQLQEKQAALAEAQE 2882
Cdd:COG1196 405 LEEAEEALLERLE----------------------------RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958663403 2883 KLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDCLI 2956
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2695-2947 |
8.63e-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: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2695 QKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKkdigEIKSygrppAQVEIvmqavm 2774
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----EIAE-----AEAEI------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2775 ilrgneptwAEAKRQLGEQnfIKSLiYfdkdnISDKVLKKIGAYCAQPDFQpDIIGRVSLaakslcmwvramelygrLYR 2854
Cdd:COG3883 82 ---------EERREELGER--ARAL-Y-----RSGGSVSYLDVLLGSESFS-DFLDRLSA-----------------LSK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2855 VVEpkriRMNAAIAQLQEKQAALAEAQEKLREVAEKLEmlkkqydeklAQKEELRKKSEEMELKLERAGMLVSGLAGEKA 2934
Cdd:COG3883 127 IAD----ADADLLEELKADKAELEAKKAELEAKLAELE----------ALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
250
....*....|...
gi 1958663403 2935 RWEETVQGLEEDL 2947
Cdd:COG3883 193 AAEAQLAELEAEL 205
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2636-2947 |
1.03e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2636 LGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEyLVIIVQQKREADEQQKAVTANSEKIAI 2715
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGLSG 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2716 EEvkcQALAD--NAQKDLEEALP-ALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEA---KRQ 2789
Cdd:TIGR02168 521 IL---GVLSEliSVDEGYEAAIEaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDReilKNI 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2790 LGEQNFIKSLIYFDKDnisdkvlkkigaycAQPDFQPdIIGRVsLAAKSLcmwVRAMELYGRL---YRVVEP--KRIRMN 2864
Cdd:TIGR02168 598 EGFLGVAKDLVKFDPK--------------LRKALSY-LLGGV-LVVDDL---DNALELAKKLrpgYRIVTLdgDLVRPG 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2865 AAIAQLQEKQAALAEAQEK-LREVAEKLEMLKKQYDEKLAQKEELRKKSEEME-------LKLERAGMLVSGLAGEKARW 2936
Cdd:TIGR02168 659 GVITGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlrKELEELSRQISALRKDLARL 738
|
330
....*....|.
gi 1958663403 2937 EETVQGLEEDL 2947
Cdd:TIGR02168 739 EAEVEQLEERI 749
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2053-2111 |
3.08e-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: 3.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663403 2053 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKG 2111
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG 61
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2862-2947 |
5.59e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2862 RMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQ 2941
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
....*.
gi 1958663403 2942 GLEEDL 2947
Cdd:COG4372 161 SLQEEL 166
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
2862-2922 |
6.04e-04 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 42.19 E-value: 6.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958663403 2862 RMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYD---EKLA-QKEELRKKSEEMELKLERA 2922
Cdd:pfam18595 51 KLEEAKKKLKELRDALEEKEIELRELERREERLQRQLEnaqEKLErLREQAEEKREAAQARLEEL 115
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2865-2947 |
6.41e-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: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2865 AAIAQLQE---KQAALA-EAQEKL-REV------AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAgmlvsglageK 2933
Cdd:pfam07926 22 AQLQKLQEdleKQAEIArEAQQNYeRELvlhaedIKALQALREELNELKAEIAELKAEAESAKAELEES----------E 91
|
90
....*....|....
gi 1958663403 2934 ARWEETVQGLEEDL 2947
Cdd:pfam07926 92 ESWEEQKKELEKEL 105
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2633-2751 |
8.05e-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: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2633 KKLLGEKRQELLDQANKLRtglfKIDETREKV--EVMSLELEDAKKKVAEFQKQCEEylviivQQKREADEQQKAVTANS 2710
Cdd:TIGR02794 71 KKLEQQAEEAEKQRAAEQA----RQKELEQRAaaEKAAKQAEQAAKQAEEKQKQAEE------AKAKQAAEAKAKAEAEA 140
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1958663403 2711 EKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKK 2751
Cdd:TIGR02794 141 ERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA 181
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2868-2947 |
1.05e-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: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2868 AQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 2947
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2862-2920 |
1.08e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 1.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958663403 2862 RMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLA----QKEELRKKSEEMELKLE 2920
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAeleaELEELEAEREELAAKIP 173
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2627-2938 |
1.32e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2627 ELVSGYKKLLgEKRQELLDQANKLRTglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAV 2706
Cdd:COG1340 54 ELREEAQELR-EKRDELNEKVKELKE---ERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2707 -TANSEKIAIEEVKcqaladnaqkDLEEALPALEEAMRALESLnKKDIGEIKsygrppaqvEIVMQAvmilrgneptwAE 2785
Cdd:COG1340 130 lSPEEEKELVEKIK----------ELEKELEKAKKALEKNEKL-KELRAELK---------ELRKEA-----------EE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2786 AKRQLGEqnfiksliYFDKdniSDKVLKKIGAycaqpdfqpdiigrvslaakslcmwvramelygrLYRVVEPKRIRMNA 2865
Cdd:COG1340 179 IHKKIKE--------LAEE---AQELHEEMIE----------------------------------LYKEADELRKEADE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2866 AIAQLQEKQAALAE-------AQEKLREVAEKLEMLKKQYD--EKLAQKEELRKKSEEMELKLERagmlvsglaGEKARW 2936
Cdd:COG1340 214 LHKEIVEAQEKADElheeiieLQKELRELRKELKKLRKKQRalKREKEKEELEEKAEEIFEKLKK---------GEKLTT 284
|
..
gi 1958663403 2937 EE 2938
Cdd:COG1340 285 EE 286
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2866-2951 |
2.56e-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: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2866 AIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEE 2945
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
....*.
gi 1958663403 2946 DLGYLV 2951
Cdd:TIGR02168 310 RLANLE 315
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2860-2920 |
3.51e-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: 3.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958663403 2860 RIRMNAAIAQLQEKQaaLAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLE 2920
Cdd:pfam13868 100 REQMDEIVERIQEED--QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL 158
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2641-2751 |
3.89e-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: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2641 QELLDQANKLRTGLfkidET-----REKVEVMSLELEDAKKKVAEFQKQCEEYlviiVQQKREADEQQKAVT-ANSE--- 2711
Cdd:pfam05622 310 QQLLEDANRRKNEL----ETqnrlaNQRILELQQQVEELQKALQEQGSKAEDS----SLLKQKLEEHLEKLHeAQSElqk 381
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958663403 2712 -KIAIEEVKCQALADNAQK--DLEEALPALEEAMRALESLNKK 2751
Cdd:pfam05622 382 kKEQIEELEPKQDSNLAQKidELQEALRKKDEDMKAMEERYKK 424
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2636-2947 |
4.72e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2636 LGEKRQELLDQANKLRTGLFKIDETREKVEvmslELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQ-QKAVTANSEKIA 2714
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2715 IEEVKcQALADNAQKDLEEALPALEEAMRALESLNKkdIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAkRQLGEQN 2794
Cdd:COG4717 210 ELEEE-LEEAQEELEELEEELEQLENELEAAALEER--LKEARLLLLIAAALLALLGLGGSLLSLILTIAGV-LFLVLGL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2795 FIKSLIYFDKDNISdkVLKKIGAYCAQPDFQpdiigrvSLAAKSLCMWVRAMELYGRLyrvvEPKRIRMN-AAIAQLQEK 2873
Cdd:COG4717 286 LALLFLLLAREKAS--LGKEAEELQALPALE-------ELEEEELEELLAALGLPPDL----SPEELLELlDRIEELQEL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2874 QAALAEAQEKLREV---AEKLEMLKK-------QYDEKLAQKEELRKKSEEME-----LKLERAGMLVSGLAGEKARWEE 2938
Cdd:COG4717 353 LREAEELEEELQLEeleQEIAALLAEagvedeeELRAALEQAEEYQELKEELEeleeqLEELLGELEELLEALDEEELEE 432
|
....*....
gi 1958663403 2939 TVQGLEEDL 2947
Cdd:COG4717 433 ELEELEEEL 441
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2865-2932 |
5.85e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 42.71 E-value: 5.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958663403 2865 AAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGE 2932
Cdd:pfam05701 121 AAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIE 188
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2862-2922 |
8.28e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 8.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2862 RMNAAIAQLQEK-QAALAEAQEKL-REVAEK-------LEMLKKQYDEKLAQKEELRKKSEEMELKLERA 2922
Cdd:COG1842 62 ELEAEAEKWEEKaRLALEKGREDLaREALERkaeleaqAEALEAQLAQLEEQVEKLKEALRQLESKLEEL 131
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2869-2950 |
8.67e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2869 QLQEKQAALAEAQEKLREVAEKLEMLKKQYDEklaqkEELRKKSEEMeLKLERAgmlVSGLAGEKARWEETVQGLEEDLG 2948
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSE-----EEYEELREEY-LELSRE---LAGLRAELEELEKRREEIKKTLE 697
|
..
gi 1958663403 2949 YL 2950
Cdd:PRK03918 698 KL 699
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2856-2947 |
8.82e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663403 2856 VEPKRIRMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKAR 2935
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90
....*....|..
gi 1958663403 2936 WEETVQGLEEDL 2947
Cdd:COG4372 134 LEAQIAELQSEI 145
|
|
| |
