|
Name |
Accession |
Description |
Interval |
E-value |
| AAA_6 |
pfam12774 |
Hydrolytic ATP binding site of dynein motor region; This domain is found in human cytoplasmic ... |
1496-1822 |
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 672068221 1496 YGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGTYVIVVNCSEGLDYKSMGRMYSG 1575
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1576 LAQTGAWGCFDEFNRINIEVLSVVAQQILSILSALTANLTRFYFEGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFR 1655
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1656 PIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLTDEEVLL 1735
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1736 LSMRDMNIAKLTSVDVPLFNAIVQDLFPNIELPVIDYGKLRDTIEQEIREMGLQITPFTLTKVLQLYETKNSRHSTMIVG 1815
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 672068221 1816 GTGSSKT 1822
Cdd:pfam12774 321 PTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
951-1359 |
6.66e-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: 6.66e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 951 LQNLEKELDALQQVWEITRDWEESWNQWKTGCFLTLQTEAMESMAHGLFRRLTRLAKEYKDrnWEVIETTRAKIEQFKRT 1030
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRD--WDVAEELKKKIDDFKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1031 MPLISDLRNPALRERHWDQVKEEIQREFDQESESFTLEQIVKLGMDQHVEKIAEISASATKELAIEVGLQNIAKTWDSTQ 1110
Cdd:pfam08393 79 LPLIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1111 LDIVPYKDKGHHRLRGTEEVFQALEDNQVALSTMKASRFVKAFEKDVDHWERCLSLILEVIEMVLTVQRQWMYLENIFLG 1190
Cdd:pfam08393 159 FELVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1191 EDIRKQLPNESALFDQVNNNWKGIMDRMNKDNNALRSTHYPGLLETLIEMNTILEDIQKSLDMYLETKRHMFPRFYFLSN 1270
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1271 DDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIQKvggsssKWEAVGMFSGDGEYIDFLHP-VLLEGAVESWLGDVERAMR 1349
Cdd:pfam08393 319 DELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE------NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMR 392
|
410
....*....|
gi 672068221 1350 MTLRDLLRNC 1359
Cdd:pfam08393 393 ETLRDLLKEA 402
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1018-3839 |
1.50e-134 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 477.17 E-value: 1.50e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1018 ETTRA-KIEQFKRTMPLISDL-----RNPALRE---RHWDQV----KEEIQREF-DQESESFtleqivkLGMDQHVEKIA 1083
Cdd:COG5245 480 EAGRFvKLCKIMRMFSFFNSLemfsrRTLANRMaivKYLSSVvrtgPLFLQRDFfGRMSELL-------MARDMFMEVDG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1084 EISASATKELA--IEVGLQNIAKTWDSTQLDivpykdkghhrlrgtEEVFQALEDNQVALSTMKASRFvkaFEKDVDhWE 1161
Cdd:COG5245 553 VLRLFFGGEWSgiVQLSGIRRAKRCVERQID---------------DEIREWCSSVLSDDFLEERAVR---VERGAD-GA 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1162 RCLSLILEvIEMVLTVQRQWMYLENiflgEDIRKQLPNESALFDQVNNNWKGIMDRMNKDNNALRSTHYPgLLETLIEMN 1241
Cdd:COG5245 614 RRLRASSG-SPVLRRLDEYLMMMSL----EDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFY 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1242 TILEDIQKSLDMYLETKRHMFPRFyfLSNDDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIqkvggSSSKWEAVGMFSGD 1321
Cdd:COG5245 688 KEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEEMKTV-----FSSRIQKKEPFSLD 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1322 GE-YIDFLHpvLLEGA-VESWLGDVERAMRMTLRDllrncrmALKKFLNKRDkwvkdwaGQMVITASQIQ--------WT 1391
Cdd:COG5245 761 SEaYVGFFR--LYEKSiVIRGINRSMGRVLSQYLE-------SVQEALEIED-------GSFFVSRHRVRdgglekgrGC 824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1392 ADVTKCLMTAKERSDKKILKVMKkkqvSILNKYSEAIRGnltkimrlKIVALVTIEIHARDVLEKLYKGGLMDVNAFDWL 1471
Cdd:COG5245 825 DAWENCFDPPLSEYFRILEKIFP----SEEGYFFDEVLK--------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSV 892
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1472 SQLRFYwEKDVDDCIIRQTNTQFQYGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSpkgpAGTGKTETVKDLGKAL 1551
Cdd:COG5245 893 SISELP-QGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGK 967
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1552 GTYVivvncsEGLDYKSmgRMYSGLAQTGAWGcFDEFNRINIEVLSVVA--QQILSILSALTANLTRFYFEGFeinLVWS 1629
Cdd:COG5245 968 GRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVVEHGL---KSPS 1035
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1630 CGIFITMNPgyagRTELPENLKSMFRPIAMVVPDSTlIAEIIlfgegfgncKILAKKVYTLYSLAVQQLSRQDHYDFglR 1709
Cdd:COG5245 1036 TPVEMIINE----RNIVLEIGRRALDMFLSNIPFGA-IKSRR---------ESLDREIGAFNNEVDGIAREEDELMF--Y 1099
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1710 ALTSLLRyagKKRRLQPDLTDEEVLLLSmrdmnIAKLTSVDVPLFNAIvqDLFPNIELPVIdygklRDTIEQEIREMGlQ 1789
Cdd:COG5245 1100 PMFKSLK---AKHRMLEEKTEYLNKILS-----ITGLPLISDTLRERI--DTLDAEWDSFC-----RISESLKKYESQ-Q 1163
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1790 ITPFTLTKVLQLYETKNSRHSTMIVGGTGSSKTTSWrilqaslTSLCragepnfnivkEFPLNPKALSLGELYGEYDLNT 1869
Cdd:COG5245 1164 VSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHY-------TDAC-----------DYLWHVKSPYVKKKYFDADMEL 1225
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1870 NEWTDGILSSVMRAACADEKpdeKWILFDGpvdtlWIESMNSVMDDNKVLTLINGERIAMpeqvsllfeVENLAvASPAT 1949
Cdd:COG5245 1226 RQFFLMFNREDMEARLADSK---MEYEVER-----YVEKTKAEVSSLKLELSSVGEGQVV---------VSNLG-SIGDK 1287
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1950 VSRCGMVYtDYVDLGWTPYVQSWLEKRPKAEIEPLQRMFE--------------KFINKILTFKKDnCNELVPVTEYSGI 2015
Cdd:COG5245 1288 VGRCLVEY-DSISRLSTKGVFLDELGDTKRYLDECLDFFScfeevqkeidelsmVFCADALRFSAD-LYHIVKERRFSGV 1365
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2016 ISLCKLYTVLATPENGVNpADTENHAFMVEMTFVFSMIWSVCASVDEDgRKKIDSYLREIEGSFPNKDTVYEYY------ 2089
Cdd:COG5245 1366 LAGSDASESLGGKSIELA-AILEHKDLIVEMKRGINDVLKLRIFGDKC-RESTPRFYLISDGDLIKDLNERSDYeemlim 1443
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2090 ---VNPKMRTWSSFEEQLPKSWR--YPPNapfykIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSl 2164
Cdd:COG5245 1444 mfnISAVITNNGSIAGFELRGERvmLRKE-----VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS- 1517
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2165 pSSQWSVLVVNMSAQTTSNNVQSIIESRVEK-RTKGVYVPFGG---KSMITFMDDLNMPAKDMFGSQPPLELIR-LWIDY 2239
Cdd:COG5245 1518 -ELITEVKYFNFSTCTMTPSKLSVLERETEYyPNTGVVRLYPKpvvKDLVLFCDEINLPYGFEYYPPTVIVFLRpLVERQ 1596
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2240 GFWYDrVKQTIKHIRDMFLMAAMGPPGG-GRTVISPRLQSRFNIINMTFPTESQIIRIFGTMINQKLQDFEEEVKPIGNV 2318
Cdd:COG5245 1597 GFWSS-IAVSWVTICGIILYGACNPGTDeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEET 1675
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2319 VTEATlDVYNTVVQRFlPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTK-ASITRLWIHECFRVFSDRLVDTTDMEAFI 2397
Cdd:COG5245 1676 MSASV-ELYLSSKDKT-KFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPdVSLIIDWYCEAIREKIDRLVQQKESSTSR 1753
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2398 GILSDKLGTFFdltfhhlcpnkRPPIFGDFLKEPKVYEDLVDLS---VLKTAMETALNEY--NLSPSVVQMQLVLFREAI 2472
Cdd:COG5245 1754 QDLYDFGLRAI-----------REMIAGHIGEAEITFSMILFFGmacLLKKDLAVFVEEVrkIFGSSHLDVEAVAYKDAL 1822
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2473 EHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICEYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVELQATSFLFVD 2552
Cdd:COG5245 1823 LHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFE 1902
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2553 TQIADESFLEDINNILSSGEVPNLYKADEFEEIQNQIIDQARAEQIS-ESSDSLFAYLIERVRNNLHIVLCL-SPVGDPF 2630
Cdd:COG5245 1903 SIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEkDTEATLTRVFLVYMEENLPVVFSAcCSQDTSV 1982
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2631 RNWIRqYPALVNCTTINWFSEWPREALLEVAEKYL-----------VGVDLGTQE--NIHRKVAQIFVTMHWSVaqYSQK 2697
Cdd:COG5245 1983 LAGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVEtlsrdggrvffINGELGVGKgaLISEVFGDDAVVIEGRG--FEIS 2059
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2698 MLLELrrhNYVTPTNYLELVSGYKKLLGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL 2777
Cdd:COG5245 2060 MIEGS---LGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDAL 2136
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2778 VIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIV 2857
Cdd:COG5245 2137 SGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIE 2216
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2858 MQAVMILRGNEPT-WAEAKRQLGEQNFIKSLI-YFDKDNISDKVLKKIGA-YCAQPDFQPDIIGRVSLAAKSLCMWVRAM 2934
Cdd:COG5245 2217 MEDVCDLLGFEAKiWFGEQQSLRRDDFIRIIGkYPDEIEFDLEARRFREArECSDPSFTGSILNRASKACGPLKRWLVRE 2296
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2935 ELYGRLYRVVEPKRIRMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLV 3014
Cdd:COG5245 2297 CNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVS 2376
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3015 SGLAGEKARWEETVQGLEEDLGYLVGDCLIAAAFLSYMGPflTNYRDEIVNQIWIKKIWELQVPCSpRFAIDNFLTN-PT 3093
Cdd:COG5245 2377 EILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGT--LGFLCRAIEFGMSFIRISKEFRDK-EIRRRQFITEgVQ 2453
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3094 KVRDWNIQGLPSDSFSTENGIIVTRGNRWALMIDPQAQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQn 3173
Cdd:COG5245 2454 KIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIG- 2532
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3174 VQEYLDPSLNPVLNKSVARIGGRMLMRIADKEVEYNPNFR-FYLTTKLSNPHYSPEtSAKTTIVNFAVKEQGLEAQLLGI 3252
Cdd:COG5245 2533 DAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAvFWLSEGRSGDMGSIE-WKQLIQVMFVSKVLGCETEIPDA 2611
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3253 VVRKERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEVTEQLETSETTEINID 3332
Cdd:COG5245 2612 LEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRID 2691
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3333 LAREAYRPCAQRASVLFFVLNDMGRIDPMYQFSLDAYISLF-ILSIDKSHRSNKLEDRIEYLNDYhtyavyrytcrtLFE 3411
Cdd:COG5245 2692 ALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFeKWRRMKSKYLCAIRYMLMSSEWI------------LDH 2759
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3412 RHKLLFSFhmcakILETSGKLNMDEynfFLRGGVVLDREGQMDNPCTSWLADAYWDNITELDKLTNFhglMNSFEQYPRD 3491
Cdd:COG5245 2760 EDRSGFIH-----RLDVSFLLRTKR---FVSTLLEDKNYRQVLSSCSLYGNDVISHSCDRFDRDVYR---ALKHQMDNRT 2828
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3492 wHLWYTNSNpekamlpgeweNACNEMQRMLIVRSLRQ-DRVAFcvtsfivSNLGSRFieppvlnMKLVMEDSTPRSPLVF 3570
Cdd:COG5245 2829 -HSTILTSN-----------SKTNPYKEYTYNDSWAEaFEVED-------SGDLYKF-------EEGLLELIVGHAPLIY 2882
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3571 ILSPGVDptsaLLQLAEHTGMAHRfhaLSLGQGQAPIAARllregvnQGHWVFLANCHLSLSWMPN-LDKLVEQLQVEDP 3649
Cdd:COG5245 2883 AHKKSLE----NERNVDRLGSKEN---EVYAVLNSLFSRK-------EKSWFEVYNISLSFGWFKRyVEDVVYPIKASRV 2948
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3650 HPSF-RLWLSSSPHPDFPISILQASIKMTTEPPKGLKANMTRLYqlmtEAQFThcskPTKYK-----KLLFALCFFHSIL 3723
Cdd:COG5245 2949 CGKVkNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLV----EIDRY----PFDYTlviacDDAFYLSWEHAAV 3020
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3724 LERKKFLQLGWNIIYGFNDSDFEVSENLLS--LYLDEYEETPWDALKYLIAGVNYGGHVTDDWDRRLLTTYINDYFC--D 3799
Cdd:COG5245 3021 ASVISAGPKENNEEIYFGDKDFEFKTHLLKniLFLNHLNARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGAheT 3100
|
2890 2900 2910 2920
....*....|....*....|....*....|....*....|.
gi 672068221 3800 LSLTTPSYRLS-VLDTYYIPKDGSLASYKEYISLLPSMDPP 3839
Cdd:COG5245 3101 SSQILASVPGGdPELVKFHMEEMCRSSAFGVIGQLPDLALC 3141
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
3854-4154 |
2.58e-128 |
|
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein heavy chain. This domain is a complex structure comprising six alpha-helices and an incomplete six-stranded antiparallel beta-barrel. The shape of this domain is distinctively flat, spreading over the AAA1, AAA5 and AAA6 domain.
Pssm-ID: 465677 Cd Length: 301 Bit Score: 406.24 E-value: 2.58e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3854 ITEARTLFETLLSLQPQITPTRIGG-QSREEKVLELAADVKQKIPEMIDYE-GTRKLLALDPSPLNVVLLQEIQRYNKLM 3931
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGgSSREEIVLELAKDILEKLPEPFDIEeAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3932 KTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLWGKV-YPSQKPLASWTRDLAVRVEQFETWANRAHPPVLFWL 4010
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKsYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 4011 SGFTFPTGFLTAVLQSAARQNNISVDSLSWEFIV-STVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVC 4089
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVtKKVSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672068221 4090 LMPTIHFRPAE-SRKKSAKGMYSCPCYYYPNRAGSadraSFVIGIDLRSGaMTSDHWIKRGTALLM 4154
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 ... |
2463-2723 |
5.56e-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: 400.45 E-value: 5.56e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2463 MQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICEYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVE 2542
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2543 LQATSFLFVDTQIADESFLEDINNILSSGEVPNLYKADEFEEIQNQIIDQARAEQISESSDSLFAYLIERVRNNLHIVLC 2622
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2623 LSPVGDPFRNWIRQYPALVNCTTINWFSEWPREALLEVAEKYLvgVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLEL 2702
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFL--EDIEIPEELKSNVVKVFVYVHSSVEDMSKKFYEEL 238
|
250 260
....*....|....*....|.
gi 672068221 2703 RRHNYVTPTNYLELVSGYKKL 2723
Cdd:pfam12780 239 KRKNYVTPKSYLELLRLYKNL 259
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
3-448 |
5.96e-118 |
|
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: 387.32 E-value: 5.96e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3 PKDISDKLPKLISLIRIIWVNSPHYNTRERLTGLFRKMSNEIIRLCCHSVSLDRIFEGYVSSSKEDLQGCISCCHAWKEH 82
Cdd:pfam08385 111 PPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQCKKYLSPEGIFDGDVEEALEKLQECIELLEAWKEE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 83 YLRAVQ-MHTQFSNRGWVLDQTSIFAQVDAFVQRCKDLIEVCDCQYHFARwldgtqgpLPCFFGAQGPQITRNLLEIEDI 161
Cdd:pfam08385 191 YKKTREkLEESPRERPWDFSERYIFGRFDAFLERLEKILELFETIEQFSK--------LEKIGGTKGPELEGVIEEILEE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 162 FHKNLQTLRAVRGGILDVKNTSWHEDYNKFRAGIKDLEVMTQNLITSAFELVRDVEHGVLLLDTFHRLANREAIMRTYEK 241
Cdd:pfam08385 263 FQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 242 KAVDLYMLFNSELALVNRELNKKW---PYLEPYMAQYSGQAHWVRILRRRIDRVMNCLSGAHFLPHIGTGEETVHTYQQM 318
Cdd:pfam08385 343 KYTDLLQMFKKELDAVKKIFDKQKynpSPIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLLKHAEGKKVIKKYNEL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 319 VQAIDELVRKTFQEWTATLDKDCIRRLDMPLLRISQEKAGMLDVNFDKTLLILFVEIDYWERLLFETPHYVMNVADRAED 398
Cdd:pfam08385 423 AKKLDEYERLIYEAWLKEVEEASEGNLKRPLLVRHPETGKLLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEER 502
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 672068221 399 LRILRENLLLVARDYNRIIAMLSPDEQALFKERIRFLDKKIHPGLKKLNW 448
Cdd:pfam08385 503 LRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTW 552
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2141-2283 |
1.05e-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: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2141 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPfgGKSMITFMDDLNMPA 2220
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK--AKPGVLFIDEIDSLS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672068221 2221 KDMFGSQppLELIRLWIDYGFWYDRVKqtikhirdmFLMAAMGPPGGGrtvISPRLQSRFNII 2283
Cdd:cd00009 98 RGAQNAL--LRVLETLNDLRIDRENVR---------VIGATNRPLLGD---LDRALYDRLDIR 146
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2744-3035 |
7.40e-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: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2744 KIDETREKVEVMSLELEDAKKkVAEFQKQCEEY-LVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEA 2822
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAER-YQALLKEKREYeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2823 LPALEEAMRALESLN-------KKDIGEIKsygrppAQVEivmQAVMILRGNEptwAEAKRQLGEQNFIKSLIYFDKDNI 2895
Cdd:TIGR02169 271 EQLLEELNKKIKDLGeeeqlrvKEKIGELE------AEIA---SLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2896 sDKVLKKIGAYCAQpdfqpdiigRVSLAAKslcmwvramelygrlyrvVEPKRIRMNAAIAQLQEKQAALAEAQEKLREV 2975
Cdd:TIGR02169 339 -EELEREIEEERKR---------RDKLTEE------------------YAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2976 AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 3035
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2701-2845 |
9.95e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2701 ELRRHNYVTPTNYLELVSGYKKLLGE---KRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL 2777
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672068221 2778 VIIVQQKREADEQQKAVtansekiaiEEVKcqaLADNAQKDLEEALPALEEAMRALESLNKKDIGEIK 2845
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKA---------EEAK---KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2141-2199 |
3.14e-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: 3.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 672068221 2141 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKG 2199
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 ... |
1496-1822 |
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 672068221 1496 YGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSPKGPAGTGKTETVKDLGKALGTYVIVVNCSEGLDYKSMGRMYSG 1575
Cdd:pfam12774 1 YGYEYLGNSGRLVITPLTDRCYLTLTQALHLHLGGAPAGPAGTGKTETVKDLAKALAKQVVVFNCSDGLDYKSMGRIFKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1576 LAQTGAWGCFDEFNRINIEVLSVVAQQILSILSALTANLTRFYFEGFEINLVWSCGIFITMNPGYAGRTELPENLKSMFR 1655
Cdd:pfam12774 81 LAQCGAWGCFDEFNRIDIEVLSVVAQQILTIQQALAANLKTFVFEGSEIKLNPSCGIFITMNPGYAGRTELPDNLKALFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1656 PIAMVVPDSTLIAEIILFGEGFGNCKILAKKVYTLYSLAVQQLSRQDHYDFGLRALTSLLRYAGKKRRLQPDLTDEEVLL 1735
Cdd:pfam12774 161 PVAMMVPDYALIAEIMLFSEGFSDAKVLAKKLVTLYKLCSEQLSKQDHYDFGLRALKSVLVTAGSLKRSNPNLNEDVLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1736 LSMRDMNIAKLTSVDVPLFNAIVQDLFPNIELPVIDYGKLRDTIEQEIREMGLQITPFTLTKVLQLYETKNSRHSTMIVG 1815
Cdd:pfam12774 241 RALRDMNLPKLVADDVPLFLGLISDLFPGVELPPSDYGELEEAIEEVCKELGLQPHDAFILKVIQLYETMLVRHGVMLVG 320
|
....*..
gi 672068221 1816 GTGSSKT 1822
Cdd:pfam12774 321 PTGSGKT 327
|
|
| DHC_N2 |
pfam08393 |
Dynein heavy chain, N-terminal region 2; Dyneins are described as motor proteins of eukaryotic ... |
951-1359 |
6.66e-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: 6.66e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 951 LQNLEKELDALQQVWEITRDWEESWNQWKTGCFLTLQTEAMESMAHGLFRRLTRLAKEYKDrnWEVIETTRAKIEQFKRT 1030
Cdd:pfam08393 1 LEEIKKELEPLKKLWDLVSEWQESLEEWKNGPFSDLDVEELEEELEEFLKELKKLPKELRD--WDVAEELKKKIDDFKKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1031 MPLISDLRNPALRERHWDQVKEEIQREFDQESESFTLEQIVKLGMDQHVEKIAEISASATKELAIEVGLQNIAKTWDSTQ 1110
Cdd:pfam08393 79 LPLIEDLRNPALRERHWKQLSEILGFDFDPLSEFFTLGDLLDLNLHKYEEEIEEISEQASKEYSIEKALKKIEEEWKTME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1111 LDIVPYKDKGHHRLRGTEEVFQALEDNQVALSTMKASRFVKAFEKDVDHWERCLSLILEVIEMVLTVQRQWMYLENIFLG 1190
Cdd:pfam08393 159 FELVPYKDTGTFILKGWDEIQELLDDHLVKLQSMKSSPYVKPFEEEVSEWEKKLSLLQEILDEWLKVQRKWLYLEPIFSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1191 EDIRKQLPNESALFDQVNNNWKGIMDRMNKDNNALRSTHYPGLLETLIEMNTILEDIQKSLDMYLETKRHMFPRFYFLSN 1270
Cdd:pfam08393 239 EDIRKQLPEEAKRFQNVDKEWKKIMKKAVKDPNVLEACNIPGLLEKLEELNELLEKIQKSLNEYLEKKRLAFPRFYFLSN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1271 DDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIQKvggsssKWEAVGMFSGDGEYIDFLHP-VLLEGAVESWLGDVERAMR 1349
Cdd:pfam08393 319 DELLEILSQTKDPTRVQPHLKKCFEGIASLEFDE------NKEITGMISKEGEVVPFSKPpVEAKGNVEEWLNELEEEMR 392
|
410
....*....|
gi 672068221 1350 MTLRDLLRNC 1359
Cdd:pfam08393 393 ETLRDLLKEA 402
|
|
| DYN1 |
COG5245 |
Dynein, heavy chain [Cytoskeleton]; |
1018-3839 |
1.50e-134 |
|
Dynein, heavy chain [Cytoskeleton];
Pssm-ID: 227570 [Multi-domain] Cd Length: 3164 Bit Score: 477.17 E-value: 1.50e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1018 ETTRA-KIEQFKRTMPLISDL-----RNPALRE---RHWDQV----KEEIQREF-DQESESFtleqivkLGMDQHVEKIA 1083
Cdd:COG5245 480 EAGRFvKLCKIMRMFSFFNSLemfsrRTLANRMaivKYLSSVvrtgPLFLQRDFfGRMSELL-------MARDMFMEVDG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1084 EISASATKELA--IEVGLQNIAKTWDSTQLDivpykdkghhrlrgtEEVFQALEDNQVALSTMKASRFvkaFEKDVDhWE 1161
Cdd:COG5245 553 VLRLFFGGEWSgiVQLSGIRRAKRCVERQID---------------DEIREWCSSVLSDDFLEERAVR---VERGAD-GA 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1162 RCLSLILEvIEMVLTVQRQWMYLENiflgEDIRKQLPNESALFDQVNNNWKGIMDRMNKDNNALRSTHYPgLLETLIEMN 1241
Cdd:COG5245 614 RRLRASSG-SPVLRRLDEYLMMMSL----EDLMPLIPHAVHRKMSLVSGVRGIYKRVVSGCEAINTILED-VGDDLDLFY 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1242 TILEDIQKSLDMYLETKRHMFPRFyfLSNDDLLEILGQSRNPEAVQPHLKKCFDNIKLLKIqkvggSSSKWEAVGMFSGD 1321
Cdd:COG5245 688 KEMDQVFMSIEKVLGLRWREVERA--SEVEELMDRVRELENRVYSYRFFVKKIAKEEMKTV-----FSSRIQKKEPFSLD 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1322 GE-YIDFLHpvLLEGA-VESWLGDVERAMRMTLRDllrncrmALKKFLNKRDkwvkdwaGQMVITASQIQ--------WT 1391
Cdd:COG5245 761 SEaYVGFFR--LYEKSiVIRGINRSMGRVLSQYLE-------SVQEALEIED-------GSFFVSRHRVRdgglekgrGC 824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1392 ADVTKCLMTAKERSDKKILKVMKkkqvSILNKYSEAIRGnltkimrlKIVALVTIEIHARDVLEKLYKGGLMDVNAFDWL 1471
Cdd:COG5245 825 DAWENCFDPPLSEYFRILEKIFP----SEEGYFFDEVLK--------RLDPGHEIKSRIEEIIRMVTVKYDFCLEVLGSV 892
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1472 SQLRFYwEKDVDDCIIRQTNTQFQYGYEYLGNSGRLVITPLTDRCYMTLTTALHLHRGGSpkgpAGTGKTETVKDLGKAL 1551
Cdd:COG5245 893 SISELP-QGLYKRFIKVRSSYRSAEMFAKNTIPFFVFEHSMDTSQHQKLFEAVCDEVCRF----VDTENSRVYGMLVAGK 967
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1552 GTYVivvncsEGLDYKSmgRMYSGLAQTGAWGcFDEFNRINIEVLSVVA--QQILSILSALTANLTRFYFEGFeinLVWS 1629
Cdd:COG5245 968 GRIY------DGTEPRS--RIEAGPICEEERG-TEESALLDEISRTILVdeYLNSDEFRMLEELNSAVVEHGL---KSPS 1035
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1630 CGIFITMNPgyagRTELPENLKSMFRPIAMVVPDSTlIAEIIlfgegfgncKILAKKVYTLYSLAVQQLSRQDHYDFglR 1709
Cdd:COG5245 1036 TPVEMIINE----RNIVLEIGRRALDMFLSNIPFGA-IKSRR---------ESLDREIGAFNNEVDGIAREEDELMF--Y 1099
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1710 ALTSLLRyagKKRRLQPDLTDEEVLLLSmrdmnIAKLTSVDVPLFNAIvqDLFPNIELPVIdygklRDTIEQEIREMGlQ 1789
Cdd:COG5245 1100 PMFKSLK---AKHRMLEEKTEYLNKILS-----ITGLPLISDTLRERI--DTLDAEWDSFC-----RISESLKKYESQ-Q 1163
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1790 ITPFTLTKVLQLYETKNSRHSTMIVGGTGSSKTTSWrilqaslTSLCragepnfnivkEFPLNPKALSLGELYGEYDLNT 1869
Cdd:COG5245 1164 VSGLDVAQFVSFLRSVDTGAFHAEYFRVFLCKIKHY-------TDAC-----------DYLWHVKSPYVKKKYFDADMEL 1225
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1870 NEWTDGILSSVMRAACADEKpdeKWILFDGpvdtlWIESMNSVMDDNKVLTLINGERIAMpeqvsllfeVENLAvASPAT 1949
Cdd:COG5245 1226 RQFFLMFNREDMEARLADSK---MEYEVER-----YVEKTKAEVSSLKLELSSVGEGQVV---------VSNLG-SIGDK 1287
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1950 VSRCGMVYtDYVDLGWTPYVQSWLEKRPKAEIEPLQRMFE--------------KFINKILTFKKDnCNELVPVTEYSGI 2015
Cdd:COG5245 1288 VGRCLVEY-DSISRLSTKGVFLDELGDTKRYLDECLDFFScfeevqkeidelsmVFCADALRFSAD-LYHIVKERRFSGV 1365
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2016 ISLCKLYTVLATPENGVNpADTENHAFMVEMTFVFSMIWSVCASVDEDgRKKIDSYLREIEGSFPNKDTVYEYY------ 2089
Cdd:COG5245 1366 LAGSDASESLGGKSIELA-AILEHKDLIVEMKRGINDVLKLRIFGDKC-RESTPRFYLISDGDLIKDLNERSDYeemlim 1443
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2090 ---VNPKMRTWSSFEEQLPKSWR--YPPNapfykIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSl 2164
Cdd:COG5245 1444 mfnISAVITNNGSIAGFELRGERvmLRKE-----VVIPTSDTGFVDSFSNEALNTLRSYIYCGPPGSGKEMLMCPSLRS- 1517
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2165 pSSQWSVLVVNMSAQTTSNNVQSIIESRVEK-RTKGVYVPFGG---KSMITFMDDLNMPAKDMFGSQPPLELIR-LWIDY 2239
Cdd:COG5245 1518 -ELITEVKYFNFSTCTMTPSKLSVLERETEYyPNTGVVRLYPKpvvKDLVLFCDEINLPYGFEYYPPTVIVFLRpLVERQ 1596
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2240 GFWYDrVKQTIKHIRDMFLMAAMGPPGG-GRTVISPRLQSRFNIINMTFPTESQIIRIFGTMINQKLQDFEEEVKPIGNV 2318
Cdd:COG5245 1597 GFWSS-IAVSWVTICGIILYGACNPGTDeGRVKYYERFIRKPVFVFCCYPELASLRNIYEAVLMGSYLCFDEFNRLSEET 1675
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2319 VTEATlDVYNTVVQRFlPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTK-ASITRLWIHECFRVFSDRLVDTTDMEAFI 2397
Cdd:COG5245 1676 MSASV-ELYLSSKDKT-KFFLQMNYGYKPRELTRSLRAIFGYAETRIDTPdVSLIIDWYCEAIREKIDRLVQQKESSTSR 1753
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2398 GILSDKLGTFFdltfhhlcpnkRPPIFGDFLKEPKVYEDLVDLS---VLKTAMETALNEY--NLSPSVVQMQLVLFREAI 2472
Cdd:COG5245 1754 QDLYDFGLRAI-----------REMIAGHIGEAEITFSMILFFGmacLLKKDLAVFVEEVrkIFGSSHLDVEAVAYKDAL 1822
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2473 EHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICEYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVELQATSFLFVD 2552
Cdd:COG5245 1823 LHILRSRRGLLVVGGHGVLKGVLIRGACDAREFVCWLNPRNMREIFGHRDELTGDFRDSLKVQDLRRNIHGGRECLFIFE 1902
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2553 TQIADESFLEDINNILSSGEVPNLYKADEFEEIQNQIIDQARAEQIS-ESSDSLFAYLIERVRNNLHIVLCL-SPVGDPF 2630
Cdd:COG5245 1903 SIPVESSFLEDFNPLLDNNRFLCLFSGNERIRIPENLRFVFESTSLEkDTEATLTRVFLVYMEENLPVVFSAcCSQDTSV 1982
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2631 RNWIRqYPALVNCTTINWFSEWPREALLEVAEKYL-----------VGVDLGTQE--NIHRKVAQIFVTMHWSVaqYSQK 2697
Cdd:COG5245 1983 LAGIR-SPALKNRCFIDFKKLWDTEEMSQYANSVEtlsrdggrvffINGELGVGKgaLISEVFGDDAVVIEGRG--FEIS 2059
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2698 MLLELrrhNYVTPTNYLELVSGYKKLLGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL 2777
Cdd:COG5245 2060 MIEGS---LGESKIKFIGGLKVYDARCVIYIEELDCTNVNLVEGVRKYNEYGRGMGELKEQLSNTVVILGVKEKNADDAL 2136
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2778 VIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIV 2857
Cdd:COG5245 2137 SGTPGERLEREVKSVFVEAPRDMLFLLEEEVRKRKGSVMKFKSSKKPAVLEAVLFVYKIKKASLREIRSFIRPPGDLCIE 2216
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2858 MQAVMILRGNEPT-WAEAKRQLGEQNFIKSLI-YFDKDNISDKVLKKIGA-YCAQPDFQPDIIGRVSLAAKSLCMWVRAM 2934
Cdd:COG5245 2217 MEDVCDLLGFEAKiWFGEQQSLRRDDFIRIIGkYPDEIEFDLEARRFREArECSDPSFTGSILNRASKACGPLKRWLVRE 2296
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2935 ELYGRLYRVVEPKRIRMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLV 3014
Cdd:COG5245 2297 CNRSKVLEVKIPLREEEKRIDGEAFLVEDRLTLGKGLSSDLMTFKLRRRSYYSLDILRVHGKIADMDTVHKDVLRSIFVS 2376
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3015 SGLAGEKARWEETVQGLEEDLGYLVGDCLIAAAFLSYMGPflTNYRDEIVNQIWIKKIWELQVPCSpRFAIDNFLTN-PT 3093
Cdd:COG5245 2377 EILINEDSEWGGVFSEVPKLMVELDGDGHPSSCLHPYIGT--LGFLCRAIEFGMSFIRISKEFRDK-EIRRRQFITEgVQ 2453
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3094 KVRDWNIQGLPSDSFSTENGIIVTRGNRWALMIDPQAQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQn 3173
Cdd:COG5245 2454 KIEDFKEEACSTDYGLENSRIRKDLQDLTAVLNDPSSKIVTSQRQMYDEKKAILGSFREMEFAFGLSQARREGSDKIIG- 2532
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3174 VQEYLDPSLNPVLNKSVARIGGRMLMRIADKEVEYNPNFR-FYLTTKLSNPHYSPEtSAKTTIVNFAVKEQGLEAQLLGI 3252
Cdd:COG5245 2533 DAEALDEEIGRLIKEEFKSNLSEVKVMINPPEIVRSTVEAvFWLSEGRSGDMGSIE-WKQLIQVMFVSKVLGCETEIPDA 2611
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3253 VVRKERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEVTEQLETSETTEINID 3332
Cdd:COG5245 2612 LEKLVSGPLFVHEKALNALKACGSLFLWVLARYLLAKLMLSISNMEQTDEIAVLLHNLKKSRKEIEEEESESMEIEDRID 2691
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3333 LAREAYRPCAQRASVLFFVLNDMGRIDPMYQFSLDAYISLF-ILSIDKSHRSNKLEDRIEYLNDYhtyavyrytcrtLFE 3411
Cdd:COG5245 2692 ALKSEYNASVKRLESIRVEIAMFDEKALMYNKSICELSSEFeKWRRMKSKYLCAIRYMLMSSEWI------------LDH 2759
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3412 RHKLLFSFhmcakILETSGKLNMDEynfFLRGGVVLDREGQMDNPCTSWLADAYWDNITELDKLTNFhglMNSFEQYPRD 3491
Cdd:COG5245 2760 EDRSGFIH-----RLDVSFLLRTKR---FVSTLLEDKNYRQVLSSCSLYGNDVISHSCDRFDRDVYR---ALKHQMDNRT 2828
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3492 wHLWYTNSNpekamlpgeweNACNEMQRMLIVRSLRQ-DRVAFcvtsfivSNLGSRFieppvlnMKLVMEDSTPRSPLVF 3570
Cdd:COG5245 2829 -HSTILTSN-----------SKTNPYKEYTYNDSWAEaFEVED-------SGDLYKF-------EEGLLELIVGHAPLIY 2882
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3571 ILSPGVDptsaLLQLAEHTGMAHRfhaLSLGQGQAPIAARllregvnQGHWVFLANCHLSLSWMPN-LDKLVEQLQVEDP 3649
Cdd:COG5245 2883 AHKKSLE----NERNVDRLGSKEN---EVYAVLNSLFSRK-------EKSWFEVYNISLSFGWFKRyVEDVVYPIKASRV 2948
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3650 HPSF-RLWLSSSPHPDFPISILQASIKMTTEPPKGLKANMTRLYqlmtEAQFThcskPTKYK-----KLLFALCFFHSIL 3723
Cdd:COG5245 2949 CGKVkNMWTSMVDADMLPIQLLIAIDSFVSSTYPETGCGYADLV----EIDRY----PFDYTlviacDDAFYLSWEHAAV 3020
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3724 LERKKFLQLGWNIIYGFNDSDFEVSENLLS--LYLDEYEETPWDALKYLIAGVNYGGHVTDDWDRRLLTTYINDYFC--D 3799
Cdd:COG5245 3021 ASVISAGPKENNEEIYFGDKDFEFKTHLLKniLFLNHLNARKWGNNRDLIFTIVYGKKHSLMEDSKVVDKYCRGYGAheT 3100
|
2890 2900 2910 2920
....*....|....*....|....*....|....*....|.
gi 672068221 3800 LSLTTPSYRLS-VLDTYYIPKDGSLASYKEYISLLPSMDPP 3839
Cdd:COG5245 3101 SSQILASVPGGdPELVKFHMEEMCRSSAFGVIGQLPDLALC 3141
|
|
| Dynein_C |
pfam18199 |
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein ... |
3854-4154 |
2.58e-128 |
|
Dynein heavy chain C-terminal domain; This family represents the C-terminal domain of dynein heavy chain. This domain is a complex structure comprising six alpha-helices and an incomplete six-stranded antiparallel beta-barrel. The shape of this domain is distinctively flat, spreading over the AAA1, AAA5 and AAA6 domain.
Pssm-ID: 465677 Cd Length: 301 Bit Score: 406.24 E-value: 2.58e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3854 ITEARTLFETLLSLQPQITPTRIGG-QSREEKVLELAADVKQKIPEMIDYE-GTRKLLALDPSPLNVVLLQEIQRYNKLM 3931
Cdd:pfam18199 1 TNETNELLSTLLSLQPRSDSGGGGGgSSREEIVLELAKDILEKLPEPFDIEeAEEKYPVGYEDPLNTVLLQEIERFNKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3932 KTILFSLTDLEKGIQGLIVMSTSLEEIFNCIFDAHVPPLWGKV-YPSQKPLASWTRDLAVRVEQFETWANRAHPPVLFWL 4010
Cdd:pfam18199 81 KVIRRSLQDLQKAIKGLVVMSSELEELANSLLNGKVPESWAKKsYPSLKPLGSWIRDLLERLKQLQDWLDDEGPPKVFWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 4011 SGFTFPTGFLTAVLQSAARQNNISVDSLSWEFIV-STVDDSNLVYPPKDGVWVRGLYLEGAGWDRKNSCLVEAEPMQLVC 4089
Cdd:pfam18199 161 SGFFFPQAFLTAVLQNYARKNGWPIDKLSFDFEVtKKVSPEEVTEPPEDGVYVHGLFLEGARWDRKNGCLVESEPKELFS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672068221 4090 LMPTIHFRPAE-SRKKSAKGMYSCPCYYYPNRAGSadraSFVIGIDLRSGaMTSDHWIKRGTALLM 4154
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 ... |
2463-2723 |
5.56e-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: 400.45 E-value: 5.56e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2463 MQLVLFREAIEHITRIVRVIGQPRGNMLLVGIGGSGRQSLARLASSICEYNTFQIEVTKHYRKQEFRDDIKRLYRQAGVE 2542
Cdd:pfam12780 1 MDLVLFRDALEHLCRICRILRQPRGHALLVGVGGSGRQSLTKLAAFIAGYELFQIEVTRNYDMNEFREDLKKVLKKAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2543 LQATSFLFVDTQIADESFLEDINNILSSGEVPNLYKADEFEEIQNQIIDQARAEQISESSDSLFAYLIERVRNNLHIVLC 2622
Cdd:pfam12780 81 GKPTVFLLSDTQIIEESFLEDINNLLNSGEVPNLFTDEEKEEIIESVRDDAKAQNIEDSREAVYNYFVKRCRNNLHIVLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2623 LSPVGDPFRNWIRQYPALVNCTTINWFSEWPREALLEVAEKYLvgVDLGTQENIHRKVAQIFVTMHWSVAQYSQKMLLEL 2702
Cdd:pfam12780 161 MSPVGEAFRNRLRMFPSLVNCCTIDWFNEWPEEALLAVAEKFL--EDIEIPEELKSNVVKVFVYVHSSVEDMSKKFYEEL 238
|
250 260
....*....|....*....|.
gi 672068221 2703 RRHNYVTPTNYLELVSGYKKL 2723
Cdd:pfam12780 239 KRKNYVTPKSYLELLRLYKNL 259
|
|
| AAA_9 |
pfam12781 |
ATP-binding dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. ... |
3096-3317 |
2.53e-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: 2.53e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3096 RDWNIQGLPSDSFSTENGIIVTRGNRWALMIDPQAQALKWIKNMEGNQGLKIIDLQMHDYLRVLEHAIQFGFPVLLQNVQ 3175
Cdd:pfam12781 1 REWNIQGLPNDELSIENAIIVTNSRRWPLLIDPQGQANKWIKNMEKDNGLKVTSFTDKNFLKTLENAIRFGKPLLIEDVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3176 EYLDPSLNPVLNKSVARIGGRMLMRIADKEVEYNPNFRFYLTTKLSNPHYSPETSAKTTIVNFAVKEQGLEAQLLGIVVR 3255
Cdd:pfam12781 81 EELDPILDPVLLKEIFKGGGRKVIKLGDKEVDYNPNFRLYLTTKLPNPHYPPEVAAKVTLINFTVTRSGLEDQLLGIVVK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672068221 3256 KERPELEEQKDSLVINIAAGKRKLKELEDEILRLLNEATGSLLDDVQLVNTLQTSKITATEV 3317
Cdd:pfam12781 161 KERPDLEEQRNELIKEIAENKKQLKELEDKLLELLSSSEGNILDDEELIETLETSKKTSEEI 222
|
|
| DHC_N1 |
pfam08385 |
Dynein heavy chain, N-terminal region 1; Dynein heavy chains interact with other heavy chains ... |
3-448 |
5.96e-118 |
|
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: 387.32 E-value: 5.96e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3 PKDISDKLPKLISLIRIIWVNSPHYNTRERLTGLFRKMSNEIIRLCCHSVSLDRIFEGYVSSSKEDLQGCISCCHAWKEH 82
Cdd:pfam08385 111 PPEIIEAIPPLMNTIRLIWSISRYYNTSERMTVLLEKISNQLIEQCKKYLSPEGIFDGDVEEALEKLQECIELLEAWKEE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 83 YLRAVQ-MHTQFSNRGWVLDQTSIFAQVDAFVQRCKDLIEVCDCQYHFARwldgtqgpLPCFFGAQGPQITRNLLEIEDI 161
Cdd:pfam08385 191 YKKTREkLEESPRERPWDFSERYIFGRFDAFLERLEKILELFETIEQFSK--------LEKIGGTKGPELEGVIEEILEE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 162 FHKNLQTLRAVRGGILDVKNTSWHEDYNKFRAGIKDLEVMTQNLITSAFELVRDVEHGVLLLDTFHRLANREAIMRTYEK 241
Cdd:pfam08385 263 FQEAYKVFKSKTYDILDVSNEGFDDDYEEFKERIKDLERRLQAFIDQAFDDARSTESAFKLLRIFEFLLERPIIRGALEE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 242 KAVDLYMLFNSELALVNRELNKKW---PYLEPYMAQYSGQAHWVRILRRRIDRVMNCLSGAHFLPHIGTGEETVHTYQQM 318
Cdd:pfam08385 343 KYTDLLQMFKKELDAVKKIFDKQKynpSPIAKNMPPVAGAIIWARQLFRRIQEPMKRFKEELGLLKHAEGKKVIKKYNEL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 319 VQAIDELVRKTFQEWTATLDKDCIRRLDMPLLRISQEKAGMLDVNFDKTLLILFVEIDYWERLLFETPHYVMNVADRAED 398
Cdd:pfam08385 423 AKKLDEYERLIYEAWLKEVEEASEGNLKRPLLVRHPETGKLLSVNFDPQLLALLREVKYLQKLGFEIPESALNIALKEER 502
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 672068221 399 LRILRENLLLVARDYNRIIAMLSPDEQALFKERIRFLDKKIHPGLKKLNW 448
Cdd:pfam08385 503 LRPYAESLELLVRWYNKIRSTLLPVERPLLAPHLKDIDEKLEPGLTTLTW 552
|
|
| AAA_7 |
pfam12775 |
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
2110-2288 |
8.93e-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: 8.93e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2110 YPPNAPFYKIMVPTVDTVRYNYLVSTLVANQNPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSII 2189
Cdd:pfam12775 1 IPPDVPFSEILVPTVDTVRYTYLLDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDKEKYLPLFINFSAQTTSNQTQDII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2190 ESRVEKRTKGVYVPFGGKSMITFMDDLNMPAKDMFGSQPPLELIRLWIDYGFWYDRVKQTIKHIRDMFLMAAMGPPGGGR 2269
Cdd:pfam12775 81 ESKLEKRRKGVYGPPGGKKLVVFIDDLNMPAVDTYGAQPPIELLRQWLDYGGWYDRKKLTFKEIVDVQFVAAMGPPGGGR 160
|
170
....*....|....*....
gi 672068221 2270 TVISPRLQSRFNIINMTFP 2288
Cdd:pfam12775 161 NDITPRLLRHFNVFNITFP 179
|
|
| AAA_lid_11 |
pfam18198 |
Dynein heavy chain AAA lid domain; This family represents the AAA lid domain found neat the ... |
3709-3848 |
7.97e-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: 7.97e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3709 YKKLLFALCFFHSILLERKKFLQLGWNIIYGFNDSDFEVSENLLSLYLDEY-EETPWDALKYLIAGVNYGGHVTDDWDRR 3787
Cdd:pfam18198 1 WKKLLFGLCFFHAVVQERRKFGPLGWNIPYEFNESDLRISVQQLQMYLDEYdEKIPWDALRYLIGEINYGGRVTDDWDRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672068221 3788 LLTTYINDYFCDlSLTTPSYRLSVlDTYYIPKDGSLASYKEYISLLPSMDPPEAFGQHPNA 3848
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 ... |
3563-3677 |
1.40e-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: 1.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 3563 TPRSPLVFILSPGVDPTSALLQLAEHTGMAHRFHALSLGQGQAPIAARLLREGVNQGHWVFLANCHLSLSWMPNLDKLVE 3642
Cdd:pfam03028 1 SPTTPLIFILSPGSDPTADLEKLAKKLGFGGKLHSISLGQGQGPIAEKLIEEAAKEGGWVLLQNCHLALSWMPELEKILE 80
|
90 100 110
....*....|....*....|....*....|....*
gi 672068221 3643 QLQVEDPHPSFRLWLSSSPHPDFPISILQASIKMT 3677
Cdd:pfam03028 81 ELPEETLHPDFRLWLTSEPSPKFPISILQNSIKIT 115
|
|
| MT |
pfam12777 |
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ... |
2737-3072 |
3.55e-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: 3.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2737 KLRTGLFKIDETREKVEvmsleleDAKKKVA----EFQKQCE--EYLVIIVQQKREADEQQKAVTANSE-KIAIEEVKCQ 2809
Cdd:pfam12777 2 RLENGLLKLHSTAAQVD-------DLKAKLAaqeaELKQKNEdaDKLIQVVGIEADKVSKEKAIADEEEqKVAVIMKEVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2810 ALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMIL---RGNEP---TWAEAKRQLGE-QN 2882
Cdd:pfam12777 75 EKQKACEEDLAKAEPALLAAQAALDTLNKNNLTELKSFGSPPDAVSNVSAAVMILmapGGKIPkdkSWKAAKIMMAKvDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2883 FIKSLIYFDKDNISDKVLKKIGAYCAQPDFQPDIIGRVSLAAKSLCMWVRAMELYGRLYRVVEPKRIRMNAAIAQLQEKQ 2962
Cdd:pfam12777 155 FLDSLIKFDKEHIHEACLKAFKPYLGDPEFDPEFIASKSTAAAGLCSWCINIVRFYEVFCDVAPKRQALEEANADLAAAQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2963 AALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDC 3042
Cdd:pfam12777 235 EKLAAIKAKIAELNANLAKLTAAFEKATADKIKCQQEADATARTILLANRLVGGLASENIRWADAVENFKQQERTLCGDI 314
|
330 340 350
....*....|....*....|....*....|
gi 672068221 3043 LIAAAFLSYMGPFLTNYRDEIVNQIWIKKI 3072
Cdd:pfam12777 315 LLISAFISYLGFFTKKYRNELLDKFWIPYI 344
|
|
| Dynein_AAA_lid |
pfam17852 |
Dynein heavy chain AAA lid domain; This entry corresponds to the extension domain of AAA ... |
1984-2102 |
5.49e-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: 5.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1984 LQRMFEKFINKILTFKKDNCNELVPVTEYSGIISLCKLYTVLATP---ENGVNPADTENHAFMVEMTFVFSMIWSVCASV 2060
Cdd:pfam17852 1 LEPLFEWLVPPALEFVRKNCKEIVPTSDLNLVQSLCRLLESLLDEvleYNGVHPLSPDKLKEYLEKLFLFALVWSIGGTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 672068221 2061 DEDGRKKIDSYLREIEGS----FPNKDTVYEYYVNPKMRTWSSFEE 2102
Cdd:pfam17852 81 DEDSRKKFDEFLRELFSGldlpPPEKGTVYDYFVDLEKGEWVPWSD 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
2142-2280 |
2.55e-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: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2142 PVLLVGPVGTGKTSIAQSVLQSLpsSQWSVLVVNMSAQTTSNNVQSIIESRVE--KRTKGVYVPFGGKSMITFMDDLNMP 2219
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAAL--SNRPVFYVQLTRDTTEEDLFGRRNIDPGgaSWVDGPLVRAAREGEIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672068221 2220 AKDMFGSQ-PPLELIRLWIDYGFWYDRVKQTikhirDMFLMAAMGPPGGGRTVISPRLQSRF 2280
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. |
2321-2409 |
9.56e-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: 9.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2321 EATLDVYNTVVQRFLPTPAKIHYLFNLRDISKVFQGMLRANKDFHDTKASITRLWIHECFRVFSDRLVDTTDMEAFIGIL 2400
Cdd:pfam17857 3 AAALAFHQKIAATFLPTAIKFHYIFNLRDFANIFQGILFSSAECLKSPLDLIRLWLHESERVYGDKMVDEKDFDLFDKIQ 82
|
....*....
gi 672068221 2401 SDKLGTFFD 2409
Cdd:pfam17857 83 MASLKKFFD 91
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
2141-2283 |
1.05e-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: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2141 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKGVYVPfgGKSMITFMDDLNMPA 2220
Cdd:cd00009 20 KNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK--AKPGVLFIDEIDSLS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672068221 2221 KDMFGSQppLELIRLWIDYGFWYDRVKqtikhirdmFLMAAMGPPGGGrtvISPRLQSRFNII 2283
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 ... |
1812-1953 |
1.23e-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: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1812 MIVGGTGSSKTTSWRILqASLtsLCRAgepNFNIVkefpLNPKALSLGELYGEYDLNTN--EWTDGILssvMRAAcadek 1889
Cdd:pfam07728 3 LLVGPPGTGKTELAERL-AAA--LSNR---PVFYV----QLTRDTTEEDLFGRRNIDPGgaSWVDGPL---VRAA----- 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672068221 1890 pDEKWILFDGPVDTL---WIESMNSVMDDNKVLTLINGERI-AMPEQVSLLFEVENL----AVASPATVSRC 1953
Cdd:pfam07728 65 -REGEIAVLDEINRAnpdVLNSLLSLLDERRLLLPDGGELVkAAPDGFRLIATMNPLdrglNELSPALRSRF 135
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2658-3002 |
4.64e-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: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2658 LEVAEKYLVGVDLGTQENIHRKVAQIFVTMhwSVAQYSQKMLLELRRHNYVTPTNYLELVSGYKKLLGEKR---QELLDQ 2734
Cdd:pfam05483 434 LKGKEQELIFLLQAREKEIHDLEIQLTAIK--TSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKeltQEASDM 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2735 ANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKRE-----------ADEQQKAVTANSEKIAI 2803
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEvkckldkseenARSIEYEVLKKEKQMKI 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2804 EEVKCqalaDNAQKDLEEALPALEEAMRALESLNKKDIGEIKsygrppaQVEIVMQAVMILrgnEPTWAEAKRQLGE--Q 2881
Cdd:pfam05483 592 LENKC----NNLKKQIENKNKNIEELHQENKALKKKGSAENK-------QLNAYEIKVNKL---ELELASAKQKFEEiiD 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2882 NFIKSLIyfDKDNISDKVLKKIGAYCAQPD----FQPDIIGRVSlaaKSLCMWVRAMELYGRLY-RVVEPKRIRMNAAIA 2956
Cdd:pfam05483 658 NYQKEIE--DKKISEEKLLEEVEKAKAIADeavkLQKEIDKRCQ---HKIAEMVALMEKHKHQYdKIIEERDSELGLYKN 732
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 672068221 2957 QLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEE 3002
Cdd:pfam05483 733 KEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
1533-1654 |
2.27e-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: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 1533 KGPAGTGKTETVKDLGKALGTY-VIVVNCSE---------GLDYKSMG--RMYSGL---AQTGAWGCFDEFNRINIEVLS 1597
Cdd:pfam07728 5 VGPPGTGKTELAERLAAALSNRpVFYVQLTRdtteedlfgRRNIDPGGasWVDGPLvraAREGEIAVLDEINRANPDVLN 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672068221 1598 VVaqqiLSILSA----LTANLTRFYFEGFEINLVwscgifITMNPGYAGRTELPENLKSMF 1654
Cdd:pfam07728 85 SL----LSLLDErrllLPDGGELVKAAPDGFRLI------ATMNPLDRGLNELSPALRSRF 135
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2744-3035 |
7.40e-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: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2744 KIDETREKVEVMSLELEDAKKkVAEFQKQCEEY-LVIIVQQKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEA 2822
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAER-YQALLKEKREYeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2823 LPALEEAMRALESLN-------KKDIGEIKsygrppAQVEivmQAVMILRGNEptwAEAKRQLGEQNFIKSLIYFDKDNI 2895
Cdd:TIGR02169 271 EQLLEELNKKIKDLGeeeqlrvKEKIGELE------AEIA---SLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2896 sDKVLKKIGAYCAQpdfqpdiigRVSLAAKslcmwvramelygrlyrvVEPKRIRMNAAIAQLQEKQAALAEAQEKLREV 2975
Cdd:TIGR02169 339 -EELEREIEEERKR---------RDKLTEE------------------YAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2976 AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 3035
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2701-2845 |
9.95e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2701 ELRRHNYVTPTNYLELVSGYKKLLGE---KRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL 2777
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672068221 2778 VIIVQQKREADEQQKAVtansekiaiEEVKcqaLADNAQKDLEEALPALEEAMRALESLNKKDIGEIK 2845
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKA---------EEAK---KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2724-3038 |
1.76e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2724 LGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL--VIIVQQKREADEQQKAVTANSEKI 2801
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrLEELEERHELYEEAKAKKEELERL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2802 AiEEVKCQALaDNAQKDLEEALPALEEAMRALESLNKKdIGEIKSygrppaQVEIVMQAVMILRGNEPTWAEAKRQLGEQ 2881
Cdd:PRK03918 378 K-KRLTGLTP-EKLEKELEELEKAKEEIEEEISKITAR-IGELKK------EIKELKKAIEELKKAKGKCPVCGRELTEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2882 nfiksliyfDKDNISDKVLKKIGaycaqpDFQPDIIgrvSLAAKSLCMWVRAMELYGRLYRvvEPKRIRMNAAIAQLQEK 2961
Cdd:PRK03918 449 ---------HRKELLEEYTAELK------RIEKELK---EIEEKERKLRKELRELEKVLKK--ESELIKLKELAEQLKEL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2962 QAALAEAQ-EKLREVAEKLEMLKKQYD----------EKLAQKEELRKKSEEMELKLERAGMLVSGLAGE-KARWEETVQ 3029
Cdd:PRK03918 509 EEKLKKYNlEELEKKAEEYEKLKEKLIklkgeikslkKELEKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVE 588
|
....*....
gi 672068221 3030 GLEEDLGYL 3038
Cdd:PRK03918 589 ELEERLKEL 597
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2745-3009 |
4.56e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2745 IDETREKVEVMSLELEDAKKKVAEFQKQCE--EYLVII------VQQKREADEQ---QKAVTANSEKIAIEEVKCQA--L 2811
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLEraEDLVEAedrierLEERREDLEEliaERRETIEEKRERAEELRERAaeL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2812 ADNAQKDLEEALPALEEAMRALESLNK--KDIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAKRQLGEQNfiksliy 2889
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAElnSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELN------- 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2890 fdkDNISDKvlkkigaycaqpdfqpdiigrvsLAAKSlcmwVRAMELYGRlyrvVEPKRIrmNAAIAQLQEKQAALAEAQ 2969
Cdd:PRK02224 623 ---DERRER-----------------------LAEKR----ERKRELEAE----FDEARI--EEAREDKERAEEYLEQVE 666
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 672068221 2970 EKLREVAEKLEMLKKQ---YDEKLAQKEELRKKSEEMELKLER 3009
Cdd:PRK02224 667 EKLDELREERDDLQAEigaVENELEELEELRERREALENRVEA 709
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2729-2839 |
5.52e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2729 QELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAVTANSEKIaieeVKC 2808
Cdd:COG1340 146 EKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEI----VEA 221
|
90 100 110
....*....|....*....|....*....|.
gi 672068221 2809 QALADNAQKDLEEALPALEEAMRALESLNKK 2839
Cdd:COG1340 222 QEKADELHEEIIELQKELRELRKELKKLRKK 252
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2726-2832 |
5.53e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2726 EKRQELLDQANKLRtglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQ-KREADEQQKAVTANSEKIAiE 2804
Cdd:PRK09510 91 ELQQKQAAEQERLK----QLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAaKAKAEAEAKRAAAAAKKAA-A 165
|
90 100
....*....|....*....|....*...
gi 672068221 2805 EVKCQALADNAQKDLEEALPALEEAMRA 2832
Cdd:PRK09510 166 EAKKKAEAEAAKKAAAEAKKKAEAEAAA 193
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2724-3017 |
5.59e-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: 49.67 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2724 LGEKRQELLDQANKLRTGLF----KIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVII---VQQKREADEQQKAVTA 2796
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEeltaELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrlEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2797 NSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEptwAEAKR 2876
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV---AQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2877 QLGEQNfiKSLIYFDKdnisdkvlkkigaycaqpdfqpdiigRVSLAAKSLCMWVRAMELYGRlyrvvEPKRIRMNAAIA 2956
Cdd:TIGR02168 394 QIASLN--NEIERLEA--------------------------RLERLEDRRERLQQEIEELLK-----KLEEAELKELQA 440
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672068221 2957 QLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKlaqKEELRKKSEEMELKLERAGMLVSGL 3017
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEA---EQALDAAERELAQLQARLDSLERLQ 498
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2744-3029 |
6.63e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2744 KIDETREKVEVMSLELEDAKKKVAEFQKQceeylviIVQQKREADEQQKAVTANSEKIaieevkcqalaDNAQKDLEEAL 2823
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAE-------LEELNEEYNELQAELEALQAEI-----------DKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2824 PALEEAMRALeslnKKDIGEIKSYGRPPAQVEIVMQAvmilrgneptwaeakrqlgeqnfiksliyfdkDNISDkVLKKI 2903
Cdd:COG3883 79 AEIEERREEL----GERARALYRSGGSVSYLDVLLGS--------------------------------ESFSD-FLDRL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2904 GAYCAQPDFQPDIIGRVslaakslcmwvramelygrlyrvvepkrirmNAAIAQLQEKQAALAEAQEKLREVAEKLEMLK 2983
Cdd:COG3883 122 SALSKIADADADLLEEL-------------------------------KADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 672068221 2984 KQYDEKLAQKEELRK--KSEEMELKLERAGMLVSGLAGEKARWEETVQ 3029
Cdd:COG3883 171 AELEAQQAEQEALLAqlSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2654-3044 |
7.77e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2654 REAllEVAEKYLvgvDLGTQENIHRKvaqifvtmhwsvaqysQKMLLELRRHNyvtptNYLELVSGYKKLLGEKRQELLD 2733
Cdd:COG1196 207 RQA--EKAERYR---ELKEELKELEA----------------ELLLLKLRELE-----AELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2734 QANKLRTglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYL-VIIVQQKREADEQQKAVTANSEKIAIEEV--KCQA 2810
Cdd:COG1196 261 ELAELEA---ELEELRLELEELELELEEAQAEEYELLAELARLEqDIARLEERRRELEERLEELEEELAELEEEleELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2811 LADNAQKDLEEALPALEEAMRALESLNKkdigeiksygrppAQVEIVMQAVMILRGNEPTWAEAKRQLGEQNFIKSLIYF 2890
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEE-------------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2891 DKDNISDKVLKKIgaycaqpdfqpdiigrvslaakslcmwvRAMELYGRLYRVVEPKRIRMNAAIAQLQEKQAALAEAQE 2970
Cdd:COG1196 405 LEEAEEALLERLE----------------------------RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672068221 2971 KLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDLGYLVGDCLI 3044
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2783-3035 |
8.83e-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: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2783 QKREADEQQKAVTANSEKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKkdigEIKSygrppAQVEIvmqavm 2862
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----EIAE-----AEAEI------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2863 ilrgneptwAEAKRQLGEQnfIKSLiYfdkdnISDKVLKKIGAYCAQPDFQpDIIGRVSLaakslcmwvramelygrLYR 2942
Cdd:COG3883 82 ---------EERREELGER--ARAL-Y-----RSGGSVSYLDVLLGSESFS-DFLDRLSA-----------------LSK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2943 VVEpkriRMNAAIAQLQEKQAALAEAQEKLREVAEKLEmlkkqydeklAQKEELRKKSEEMELKLERAGMLVSGLAGEKA 3022
Cdd:COG3883 127 IAD----ADADLLEELKADKAELEAKKAELEAKLAELE----------ALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
250
....*....|...
gi 672068221 3023 RWEETVQGLEEDL 3035
Cdd:COG3883 193 AAEAQLAELEAEL 205
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2724-3035 |
9.34e-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: 48.90 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2724 LGEKRQELLDQANKLRTGLFKIDETREKVEVMSLELEDAKKKVAEFQKQCEEyLVIIVQQKREADEQQKAVTANSEKIAI 2803
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGLSG 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2804 EEvkcQALAD--NAQKDLEEALP-ALEEAMRALESLNKKDIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEA---KRQ 2877
Cdd:TIGR02168 521 IL---GVLSEliSVDEGYEAAIEaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDReilKNI 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2878 LGEQNFIKSLIYFDKDnisdkvlkkigaycAQPDFQPdIIGRVsLAAKSLcmwVRAMELYGRL---YRVVEP--KRIRMN 2952
Cdd:TIGR02168 598 EGFLGVAKDLVKFDPK--------------LRKALSY-LLGGV-LVVDDL---DNALELAKKLrpgYRIVTLdgDLVRPG 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2953 AAIAQLQEKQAALAEAQEK-LREVAEKLEMLKKQYDEKLAQKEELRKKSEEME-------LKLERAGMLVSGLAGEKARW 3024
Cdd:TIGR02168 659 GVITGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlrKELEELSRQISALRKDLARL 738
|
330
....*....|.
gi 672068221 3025 EETVQGLEEDL 3035
Cdd:TIGR02168 739 EAEVEQLEERI 749
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
2141-2199 |
3.14e-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: 3.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 672068221 2141 NPVLLVGPVGTGKTSIAQSVLQSLPSSQWSVLVVNMSAQTTSNNVQSIIESRVEKRTKG 2199
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG 61
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2950-3035 |
4.85e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2950 RMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQ 3029
Cdd:COG4372 81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
....*.
gi 672068221 3030 GLEEDL 3035
Cdd:COG4372 161 SLQEEL 166
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2953-3035 |
5.35e-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: 43.01 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2953 AAIAQLQE---KQAALA-EAQEKL-REV------AEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAgmlvsglageK 3021
Cdd:pfam07926 22 AQLQKLQEdleKQAEIArEAQQNYeRELvlhaedIKALQALREELNELKAEIAELKAEAESAKAELEES----------E 91
|
90
....*....|....
gi 672068221 3022 ARWEETVQGLEEDL 3035
Cdd:pfam07926 92 ESWEEQKKELEKEL 105
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
2950-3010 |
6.00e-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: 6.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672068221 2950 RMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYD---EKLA-QKEELRKKSEEMELKLERA 3010
Cdd:pfam18595 51 KLEEAKKKLKELRDALEEKEIELRELERREERLQRQLEnaqEKLErLREQAEEKREAAQARLEEL 115
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2721-2839 |
8.23e-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: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2721 KKLLGEKRQELLDQANKLRtglfKIDETREKV--EVMSLELEDAKKKVAEFQKQCEEylviivQQKREADEQQKAVTANS 2798
Cdd:TIGR02794 71 KKLEQQAEEAEKQRAAEQA----RQKELEQRAaaEKAAKQAEQAAKQAEEKQKQAEE------AKAKQAAEAKAKAEAEA 140
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 672068221 2799 EKIAIEEVKCQALADNAQKDLEEALPALEEAMRALESLNKK 2839
Cdd:TIGR02794 141 ERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA 181
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2956-3035 |
1.04e-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: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2956 AQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEEDL 3035
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2950-3008 |
1.07e-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: 1.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672068221 2950 RMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLA----QKEELRKKSEEMELKLE 3008
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAeleaELEELEAEREELAAKIP 173
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2715-3026 |
1.22e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2715 ELVSGYKKLLgEKRQELLDQANKLRTglfKIDETREKVEVMSLELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQQKAV 2794
Cdd:COG1340 54 ELREEAQELR-EKRDELNEKVKELKE---ERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2795 -TANSEKIAIEEVKcqaladnaqkDLEEALPALEEAMRALESLnKKDIGEIKsygrppaqvEIVMQAvmilrgneptwAE 2873
Cdd:COG1340 130 lSPEEEKELVEKIK----------ELEKELEKAKKALEKNEKL-KELRAELK---------ELRKEA-----------EE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2874 AKRQLGEqnfiksliYFDKdniSDKVLKKIGAycaqpdfqpdiigrvslaakslcmwvramelygrLYRVVEPKRIRMNA 2953
Cdd:COG1340 179 IHKKIKE--------LAEE---AQELHEEMIE----------------------------------LYKEADELRKEADE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2954 AIAQLQEKQAALAE-------AQEKLREVAEKLEMLKKQYD--EKLAQKEELRKKSEEMELKLERagmlvsglaGEKARW 3024
Cdd:COG1340 214 LHKEIVEAQEKADElheeiieLQKELRELRKELKKLRKKQRalKREKEKEELEEKAEEIFEKLKK---------GEKLTT 284
|
..
gi 672068221 3025 EE 3026
Cdd:COG1340 285 EE 286
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2954-3039 |
2.60e-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: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2954 AIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKARWEETVQGLEE 3033
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
....*.
gi 672068221 3034 DLGYLV 3039
Cdd:TIGR02168 310 RLANLE 315
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2948-3026 |
3.23e-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: 3.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672068221 2948 RIRMNAAIAQLQEKQaaLAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAgmlvsglAGEKARWEE 3026
Cdd:pfam13868 100 REQMDEIVERIQEED--QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEY-------LKEKAEREE 169
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2729-2839 |
3.91e-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: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2729 QELLDQANKLRTGLfkidET-----REKVEVMSLELEDAKKKVAEFQKQCEEYlviiVQQKREADEQQKAVT-ANSE--- 2799
Cdd:pfam05622 310 QQLLEDANRRKNEL----ETqnrlaNQRILELQQQVEELQKALQEQGSKAEDS----SLLKQKLEEHLEKLHeAQSElqk 381
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 672068221 2800 -KIAIEEVKCQALADNAQK--DLEEALPALEEAMRALESLNKK 2839
Cdd:pfam05622 382 kKEQIEELEPKQDSNLAQKidELQEALRKKDEDMKAMEERYKK 424
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2726-3035 |
4.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2726 EKRQELLDQANKLRTGLFKIDETREKVEvmslELEDAKKKVAEFQKQCEEYLVIIVQQKREADEQ-QKAVTANSEKIAIE 2804
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLAEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2805 EVKcQALADNAQKDLEEALPALEEAMRALESLNKkdIGEIKSYGRPPAQVEIVMQAVMILRGNEPTWAEAkRQLGEQNFI 2884
Cdd:COG4717 212 EEE-LEEAQEELEELEEELEQLENELEAAALEER--LKEARLLLLIAAALLALLGLGGSLLSLILTIAGV-LFLVLGLLA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2885 KSLIYFDKDNISdkVLKKIGAYCAQPDFQpdiigrvSLAAKSLCMWVRAMELYGRLyrvvEPKRIRMN-AAIAQLQEKQA 2963
Cdd:COG4717 288 LLFLLLAREKAS--LGKEAEELQALPALE-------ELEEEELEELLAALGLPPDL----SPEELLELlDRIEELQELLR 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2964 ALAEAQEKLREV---AEKLEMLKK-------QYDEKLAQKEELRKKSEEME-----LKLERAGMLVSGLAGEKARWEETV 3028
Cdd:COG4717 355 EAEELEEELQLEeleQEIAALLAEagvedeeELRAALEQAEEYQELKEELEeleeqLEELLGELEELLEALDEEELEEEL 434
|
....*..
gi 672068221 3029 QGLEEDL 3035
Cdd:COG4717 435 EELEEEL 441
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2953-3020 |
5.64e-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: 5.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672068221 2953 AAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGE 3020
Cdd:pfam05701 121 AAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIE 188
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2944-3035 |
7.46e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2944 VEPKRIRMNAAIAQLQEKQAALAEAQEKLREVAEKLEMLKKQYDEKLAQKEELRKKSEEMELKLERAGMLVSGLAGEKAR 3023
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90
....*....|..
gi 672068221 3024 WEETVQGLEEDL 3035
Cdd:COG4372 134 LEAQIAELQSEI 145
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2950-3010 |
7.52e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 7.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2950 RMNAAIAQLQEK-QAALAEAQEKL-REVAEK-------LEMLKKQYDEKLAQKEELRKKSEEMELKLERA 3010
Cdd:COG1842 62 ELEAEAEKWEEKaRLALEKGREDLaREALERkaeleaqAEALEAQLAQLEEQVEKLKEALRQLESKLEEL 131
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2957-3038 |
8.86e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672068221 2957 QLQEKQAALAEAQEKLREVAEKLEMLKKQYDEklaqkEELRKKSEEMeLKLERAgmlVSGLAGEKARWEETVQGLEEDLG 3036
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSE-----EEYEELREEY-LELSRE---LAGLRAELEELEKRREEIKKTLE 697
|
..
gi 672068221 3037 YL 3038
Cdd:PRK03918 698 KL 699
|
|
| |
