|
Name |
Accession |
Description |
Interval |
E-value |
| Mfd |
COG1197 |
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ... |
36-1198 |
0e+00 |
|
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and repair, Transcription];
Pssm-ID: 440810 [Multi-domain] Cd Length: 1130 Bit Score: 1551.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 36 RPDELTLVG-PASARSFVASALAQQ--GPLLVVTATGREADDVTAELRGVFGEA-VALFPSWETLPHERLSPGVDTVGAR 111
Cdd:COG1197 1 GGGRLTLSGlPGSARALLLAALARAlgRPLLVVTADEREAERLAEDLRFFLPDLpVLLFPAWETLPYDRFSPSPDIVSER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 112 LLLLRRLAHPDDtrlgpplRVVVTAVRSLLQPMTP-QLGRQEPVSLSVGQEIGFDEVIARLVELAYTRVDMVGRRGEFAV 190
Cdd:COG1197 81 LATLRRLASGKP-------GIVVTPVRALLQRLPPpELLAAASLSLKVGDELDLEELRERLVAAGYERVDQVEEPGEFAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 191 RGGILDLFAPTAEHPVRVEFWGDEITEMRMFSVADQRSIPEIEvsTLVAVACRELLLTEDVRGRAAALAAQHPasenTVT 270
Cdd:COG1197 154 RGGILDIFPPGSEHPVRIEFFGDEIESIRTFDPETQRSLEKVD--EVELLPAREFPLDEEAIERFRERLRELF----GLD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 271 GSVIDMLAKLAEGIPTDGMEALLPVLRpDDHALLTDQLAEGTPVLVCDPEKVRTRAADLIKTGREFLEAswsvAAMGTDA 350
Cdd:COG1197 228 PKLDELYEALSEGIAFAGIEYYLPLFY-EELATLFDYLPEDALVVLDEPERIEEAAEEFWEEIEERYEA----RRHDRGR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 351 PV-DVEALggsgFAELDQVQTAASSSGHPwwTLSQLSE----ESATELEVRAAPSARGhqkDIDDIFAMLRAHVSTGGYA 425
Cdd:COG1197 303 PLlPPEEL----FLDPEELFAALKRRPRV--TLSPFAAlpegAGVVNLGARPLPSFAG---QLEALLEELKRLLKDGGRV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 426 VMVEPGTGTAHRMVERLAESDIPAAMLEPGAAPKLGVVGVLKGPLRDGVIVPGANLVVVTETNLTGNRATAVEGKRLAAK 505
Cdd:COG1197 374 LLAAESEGRRERLLELLRDHGIPARLVESLAELSPGGVAITVGPLEHGFELPDAKLAVITESELFGERVKRRRRKKKRSA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 506 RRNTVDPLALTAGDLVVHDQHGIGRFVEMVERTVGGARREYLVLEYAsakrggGSDKLYVPMDSLDQLSRYVG--GQAPA 583
Cdd:COG1197 454 DAFIRDLSELKPGDYVVHVDHGIGRYLGLETLEVGGAERDYLVLEYA------GGDKLYVPVDQLDLISRYVGseGEAPK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 584 LSRLGGSDWTNTKTKARKAVREIAGELVALYAKRQASPGHAFAPDTPWQAEMEDAFGFTETVDQLTAITEVKGDMEKSIP 663
Cdd:COG1197 528 LDKLGGSDWQKAKAKAKKAVRDIAAELLKLYAERAARKGFAFSPDTPWQREFEAAFPYEETPDQLRAIEEVKADMESPRP 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 664 MDRVICGDVGYGKTEIAVRAAFKAVQDGKQVAVLVPTTLLADQHLQTFTDRMAGFPVTVKGLSRFTDPAESRTVIEGMAD 743
Cdd:COG1197 608 MDRLVCGDVGFGKTEVALRAAFKAVMDGKQVAVLVPTTLLAQQHYETFKERFAGFPVRVEVLSRFRTAKEQKETLEGLAD 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 744 GSVDVVIGTHRLLQTGVRWKDLGLVVVDEEQRFGVEHKEHIKSLRSHVDVLTMSATPIPRTLEMSLAGIREMSTILTPPE 823
Cdd:COG1197 688 GKVDIVIGTHRLLSKDVKFKDLGLLIIDEEQRFGVRHKEKLKALRANVDVLTLTATPIPRTLQMSLSGIRDLSIIATPPE 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 824 ERYPVLTYVGPHDDKQIAAALRRELLRDGQAFYVHNRVSSIDDTAARIRKLVPEARVVVAHGQMPEDLLERTVQGFWQRE 903
Cdd:COG1197 768 DRLPVKTFVGEYDDALIREAILRELLRGGQVFYVHNRVEDIEKVAARLQELVPEARIAVAHGQMSERELERVMLDFYEGE 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 904 FDILVCTTIVETGLDISNANTLIVERADTFGLSQLHQLRGRVGRSRERGYAYFLYPPQAPLTETAYDRLATIAQNNELGA 983
Cdd:COG1197 848 FDVLVCTTIIETGIDIPNANTIIIERADRFGLAQLYQLRGRVGRSHRRAYAYLLYPPDKVLTEDAEKRLEAIQEFTELGA 927
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 984 GMAVALKDLEIRGAGNVLGVEQSGHVAGVGFDLYVRLVGEAVEAYRAaadGKmvtTPEEPKDVRIDLPVDAHLPPDYIGS 1063
Cdd:COG1197 928 GFKLAMHDLEIRGAGNLLGEEQSGHIAEVGFDLYLQMLEEAVAALKG---GK---EPEEEWEPEINLGVPALIPEDYIPD 1001
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 1064 DRLRLEAYRRLATATSDSGVAAVVDELIDRYGALPEPALRLVAVARLRLLCRASGITDVSA-PSSATVRLAPMDLPDSAq 1142
Cdd:COG1197 1002 VRQRLELYKRIASAESEEELDELQEELIDRFGPLPEEVENLLAVARLKLLARRLGIEKIDAgGKGIRIEFSPNTPLDPE- 1080
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*....
gi 2271751697 1143 vRLKRMY--PGGHYR-ATTSTVQVPIPRDGgvgaprirDVELVQMVANLVTALAGKPQQ 1198
Cdd:COG1197 1081 -KLIRLIqkQPGRYKlDGDDKLVITLDLED--------PEERLEALEELLEALAKLAKE 1130
|
|
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
171-1123 |
0e+00 |
|
transcription-repair coupling factor (mfd); All proteins in this family for which functions are known are DNA-dependent ATPases that function in the process of transcription-coupled DNA repair in which the repair of the transcribed strand of actively transcribed genes is repaired at a higher rate than the repair of non-transcribed regions of the genome and than the non-transcribed strand of the same gene. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is closely related to the RecG and UvrB families. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273152 [Multi-domain] Cd Length: 926 Bit Score: 1291.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 171 LVELAYTRVDMVGRRGEFAVRGGILDLFAPTAEHPVRVEFWGDEITEMRMFSVADQRSIPEIEVSTLVAVACReLLLTED 250
Cdd:TIGR00580 1 LVELGYERVDLVEEEGEFSVRGEILDIFPPGSELPVRIEFFGDEIESIREFDVDSQRSLEELLEITILPAKEF-ILLEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 251 VRGRAAALAAQHPASENTVTgsvidmLAKLAEGIPTDGMEALLPVLRpDDHALLTDQLAEGTPVLVCDPEKVRTRAADLI 330
Cdd:TIGR00580 80 TIARLKDNAARVEDAKHLET------IEALSEGTLPAGEEMFLPLFF-EDLSSLFDYLPDNTPILLDDPERFHSAARFLQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 331 KTGREFLEASWSVAAMGTD--APVDVEALGGSGfaeldqvqtaasssghPWWTLSQLSEESAT-ELEVRAAPSARGHQKD 407
Cdd:TIGR00580 153 RELEEFYNALEEAKKLINPprLDLDPSELAFEA----------------SAISLSRVQLENEHlSLKASEAIEGAQKHSR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 408 IDD--IFAMLR---AHVSTGGYAVMVEPGTGTAHRMVERLAESDIPAAMLEPGAAPKLGVVGVLKGPLRDGVIVPGANLV 482
Cdd:TIGR00580 217 LEFgeILAFKEelfRWLKAGFKITVAAESESQAERLKSLLAEHDIAAQVIDESCIIIPAVRYVMIGALSSGFILPTAGLA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 483 VVTETNLTGNRATAVEGKRLAAKRRnTVDPLALTAGDLVVHDQHGIGRFVEMVERTVGGARREYLVLEYAsakrggGSDK 562
Cdd:TIGR00580 297 VITESELFGSRVLRRPKKSRLKSKP-IESLNELNPGDYVVHLDHGIGRFLGLETLEVGGIERDYLVLEYA------GEDK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 563 LYVPMDSLDQLSRYVGG--QAPALSRLGGSDWTNTKTKARKAVREIAGELVALYAKRQASPGHAFAPDTPWQAEMEDAFG 640
Cdd:TIGR00580 370 LYVPVEQLHLISRYVGGsgKNPALDKLGGKSWEKTKAKVKKSVREIAAKLIELYAKRKAIKGHAFPPDLEWQQEFEDSFP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 641 FTETVDQLTAITEVKGDMEKSIPMDRVICGDVGYGKTEIAVRAAFKAVQDGKQVAVLVPTTLLADQHLQTFTDRMAGFPV 720
Cdd:TIGR00580 450 FEETPDQLKAIEEIKADMESPRPMDRLVCGDVGFGKTEVAMRAAFKAVLDGKQVAVLVPTTLLAQQHFETFKERFANFPV 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 721 TVKGLSRFTDPAESRTVIEGMADGSVDVVIGTHRLLQTGVRWKDLGLVVVDEEQRFGVEHKEHIKSLRSHVDVLTMSATP 800
Cdd:TIGR00580 530 TIELLSRFRSAKEQNEILKELASGKIDILIGTHKLLQKDVKFKDLGLLIIDEEQRFGVKQKEKLKELRTSVDVLTLSATP 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 801 IPRTLEMSLAGIREMSTILTPPEERYPVLTYVGPHDDKQIAAALRRELLRDGQAFYVHNRVSSIDDTAARIRKLVPEARV 880
Cdd:TIGR00580 610 IPRTLHMSMSGIRDLSIIATPPEDRLPVRTFVMEYDPELVREAIRRELLRGGQVFYVHNRIESIEKLATQLRELVPEARI 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 881 VVAHGQMPEDLLERTVQGFWQREFDILVCTTIVETGLDISNANTLIVERADTFGLSQLHQLRGRVGRSRERGYAYFLYPP 960
Cdd:TIGR00580 690 AIAHGQMTENELEEVMLEFYKGEFQVLVCTTIIETGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKKKAYAYLLYPH 769
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 961 QAPLTETAYDRLATIAQNNELGAGMAVALKDLEIRGAGNVLGVEQSGHVAGVGFDLYVRLVGEAVEAYRAAadgkmvTTP 1040
Cdd:TIGR00580 770 QKALTEDAQKRLEAIQEFSELGAGFKIALHDLEIRGAGNLLGEEQSGHIESIGFDLYMELLEEAIEELKGG------KPP 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 1041 EEPKDVRIDLPVDAHLPPDYIGSDRLRLEAYRRLATATSDSGVAAVVDELIDRYGALPEPALRLVAVARLRLLCRASGIT 1120
Cdd:TIGR00580 844 KLEEETDIELPYSAFIPDDYIADDSLRLEFYKRIASAETEEELEKIRDELIDRFGPLPEEARTLLDVARLKLLARKLGIR 923
|
...
gi 2271751697 1121 DVS 1123
Cdd:TIGR00580 924 KLK 926
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
27-1124 |
0e+00 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 692.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 27 HQLIARASDRPDELTLVGPASARSFVASALAQQGPLLVVTATGREADDVTAELRGVFGEAVALFPSWETLPHERLSPGVD 106
Cdd:PRK10689 7 YTLPVKAGDQRQLGELTGAACATEVAEIAERHAGPVVLIAPDMQNALRLHDEIQQFTDQMVMNLADWETLPYDSFSPHQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 107 TVGARLLLLRRLahPDDTRlgpplRVVVTAVRSLLQPMTPQ--LGRQEPVsLSVGQEIGFDEVIARLVELAYTRVDMVGR 184
Cdd:PRK10689 87 IISSRLSTLYQL--PTMQR-----GVLILPVNTLMQRVCPHsfLHGHALV-MKKGQRLSRDALRAQLEQAGYRHVDQVME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 185 RGEFAVRGGILDLFAPTAEHPVRVEFWGDEITEMRMFSVADQRSIPEIEVSTLVAV-------ACRELLLTE-----DVR 252
Cdd:PRK10689 159 HGEYATRGALLDLFPMGSEEPYRIDFFDDEIDSLRVFDVDSQRTLEEVEAINLLPAhefptdkAAIELFRSQwrdtfEVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 253 gRAAALAAQhpasentvtgsvidmlaKLAEGIPTDGMEALLPVLRPDDHALLTDQLAEGTPVLVC-DPEKVRTRAADLIK 331
Cdd:PRK10689 239 -RDAEHIYQ-----------------QVSKGTLPAGIEYWQPLFFSEPLPPLFSYFPANTLLVNTgDLETSAERFWADTL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 332 TGREfleaSWSVAAMGTDAPVD-----VEALggsgFAELDQvqtaasssghpwWTLSQLSEE------SATELEVRAAP- 399
Cdd:PRK10689 301 ARFE----NRGVDPMRPLLPPEslwlrVDEL----FSELKN------------WPRVQLKTEhlptkaANTNLGYQKLPd 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 400 -SARGHQKD-IDDIFAMLRAHVSTGGYAVMVEPGTGTAHRMVERLAESDIPAAMLEPGAAPKLGVvgvLKGPLRDGVIVP 477
Cdd:PRK10689 361 lAVQAQQKApLDALRRFLESFDGPVVFSVESEGRREALGELLARIKIAPKRIMRLDEASDRGRYL---MIGAAEHGFIDT 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 478 GANLVVVTETNLTGNRATavegkRLAAKRRNTVDP------LA-LTAGDLVVHDQHGIGRFVEMVERTVGGARREYLVLE 550
Cdd:PRK10689 438 VRNLALICESDLLGERVA-----RRRQDSRRTINPdtlirnLAeLHPGQPVVHLEHGVGRYAGMTTLEAGGIKGEYLMLT 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 551 YAsakrggGSDKLYVPMDSLDQLSRYVGG---QAPaLSRLGGSDWTNTKTKARKAVREIAGELVALYAKRQASPGHAFAP 627
Cdd:PRK10689 513 YA------NDAKLYVPVSSLHLISRYAGGaeeNAP-LHKLGGDAWSRARQKAAEKVRDVAAELLDIYAQRAAKEGFAFKH 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 628 DTPWQAEMEDAFGFTETVDQLTAITEVKGDMEKSIPMDRVICGDVGYGKTEIAVRAAFKAVQDGKQVAVLVPTTLLADQH 707
Cdd:PRK10689 586 DREQYQLFCDSFPFETTPDQAQAINAVLSDMCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPTTLLAQQH 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 708 LQTFTDRMAGFPVTVKGLSRFTDPAESRTVIEGMADGSVDVVIGTHRLLQTGVRWKDLGLVVVDEEQRFGVEHKEHIKSL 787
Cdd:PRK10689 666 YDNFRDRFANWPVRIEMLSRFRSAKEQTQILAEAAEGKIDILIGTHKLLQSDVKWKDLGLLIVDEEHRFGVRHKERIKAM 745
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 788 RSHVDVLTMSATPIPRTLEMSLAGIREMSTILTPPEERYPVLTYVGPHDDKQIAAALRRELLRDGQAFYVHNRVSSIDDT 867
Cdd:PRK10689 746 RADVDILTLTATPIPRTLNMAMSGMRDLSIIATPPARRLAVKTFVREYDSLVVREAILREILRGGQVYYLYNDVENIQKA 825
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 868 AARIRKLVPEARVVVAHGQMPEDLLERTVQGFWQREFDILVCTTIVETGLDISNANTLIVERADTFGLSQLHQLRGRVGR 947
Cdd:PRK10689 826 AERLAELVPEARIAIGHGQMRERELERVMNDFHHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQLHQLRGRVGR 905
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 948 SRERGYAYFLYPPQAPLTETAYDRLATIAQNNELGAGMAVALKDLEIRGAGNVLGVEQSGHVAGVGFDLYVRLVGEAVEA 1027
Cdd:PRK10689 906 SHHQAYAWLLTPHPKAMTTDAQKRLEAIASLEDLGAGFALATHDLEIRGAGELLGEEQSGQMETIGFSLYMELLENAVDA 985
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 1028 YRAAADGKMVTTPEEPKDVRIDLPvdAHLPPDYIGSDRLRLEAYRRLATATSDSGVAAVVDELIDRYGALPEPALRLVAV 1107
Cdd:PRK10689 986 LKAGREPSLEDLTSQQTEVELRMP--SLLPDDFIPDVNTRLSFYKRIASAKNENELEEIKVELIDRFGLLPDPARNLLDI 1063
|
1130
....*....|....*..
gi 2271751697 1108 ARLRLLCRASGITDVSA 1124
Cdd:PRK10689 1064 ARLRQQAQKLGIRKLEG 1080
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
628-820 |
2.23e-116 |
|
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350749 [Multi-domain] Cd Length: 193 Bit Score: 359.58 E-value: 2.23e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 628 DTPWQAEMEDAFGFTETVDQLTAITEVKGDMEKSIPMDRVICGDVGYGKTEIAVRAAFKAVQDGKQVAVLVPTTLLADQH 707
Cdd:cd17991 1 DGEEQEEFEASFPYEETPDQLKAIEEILKDMESGKPMDRLICGDVGFGKTEVAMRAAFKAVLSGKQVAVLVPTTLLAQQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 708 LQTFTDRMAGFPVTVKGLSRFTDPAESRTVIEGMADGSVDVVIGTHRLLQTGVRWKDLGLVVVDEEQRFGVEHKEHIKSL 787
Cdd:cd17991 81 YETFKERFANFPVNVELLSRFTTAAEQREILEGLKEGKVDIVIGTHRLLSKDVEFKNLGLLIIDEEQRFGVKQKEKLKEL 160
|
170 180 190
....*....|....*....|....*....|...
gi 2271751697 788 RSHVDVLTMSATPIPRTLEMSLAGIREMSTILT 820
Cdd:cd17991 161 RPNVDVLTLSATPIPRTLHMALSGIRDLSVIAT 193
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
610-1007 |
1.89e-109 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 358.98 E-value: 1.89e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 610 LVALYAKRQASPGHAFAPDTPWQAEMEDAFGFTETVDQLTAITEVKGDMEKSIPMDRVICGDVGYGKTEIAVRAAFKAVQ 689
Cdd:COG1200 227 LLLRRARRRKRKGPALPGDGELLEAFLAALPFELTGAQKRVIAEIAADLASPHPMNRLLQGDVGSGKTVVALLAMLAAVE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 690 DGKQVAVLVPTTLLADQHLQTFTDRMAGFPVTVKGLSRFTDPAESRTVIEGMADGSVDVVIGTHRLLQTGVRWKDLGLVV 769
Cdd:COG1200 307 AGYQAALMAPTEILAEQHYRSLSKLLEPLGIRVALLTGSTKAKERREILAALASGEADIVVGTHALIQDDVEFKNLGLVV 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 770 VDEEQRFGVEHKEhikSLRS---HVDVLTMSATPIPRTLEMSLAG------IREMstiltpPEERYPVLTYVGPHDD-KQ 839
Cdd:COG1200 387 IDEQHRFGVEQRL---ALREkgeAPHVLVMTATPIPRTLAMTLYGdldvsvIDEL------PPGRKPIKTRVVPEERrDE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 840 IAAALRRELLRDGQAFYV--------HNRVSSIDDTAARIRKLVPEARVVVAHGQMPEDLLERTVQGFWQREFDILVCTT 911
Cdd:COG1200 458 VYERIREEIAKGRQAYVVcplieeseKLDLQAAEETYEELREAFPGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATT 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 912 IVETGLDISNANTLIVERADTFGLSQLHQLRGRVGRSRERGYAYFLYppQAPLTETAYDRLATIAQNNElgaGMAVALKD 991
Cdd:COG1200 538 VIEVGVDVPNATVMVIENAERFGLSQLHQLRGRVGRGSAQSYCLLLY--DAPLSETARERLEVMRETND---GFEIAEED 612
|
410
....*....|....*.
gi 2271751697 992 LEIRGAGNVLGVEQSG 1007
Cdd:COG1200 613 LELRGPGEFLGTRQSG 628
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
610-1007 |
9.26e-109 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 357.15 E-value: 9.26e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 610 LVALYAKRQASPGHAFAPDTPWQAEMEDAFGFTETVDQLTAITEVKGDMEKSIPMDRVICGDVGYGKTEIAVRAAFKAVQ 689
Cdd:PRK10917 229 LLLLRAGRRSKKAGPLPYDGELLKKFLASLPFELTGAQKRVVAEILADLASPKPMNRLLQGDVGSGKTVVAALAALAAIE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 690 DGKQVAVLVPTTLLADQHLQTFTDRMAGFPVTVKGLSRFTDPAESRTVIEGMADGSVDVVIGTHRLLQTGVRWKDLGLVV 769
Cdd:PRK10917 309 AGYQAALMAPTEILAEQHYENLKKLLEPLGIRVALLTGSLKGKERREILEAIASGEADIVIGTHALIQDDVEFHNLGLVI 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 770 VDEEQRFGVEHKEHIKSLRSHVDVLTMSATPIPRTLEMSLAGIREMSTILTPPEERYPVLTYVGPHDDK-QIAAALRREL 848
Cdd:PRK10917 389 IDEQHRFGVEQRLALREKGENPHVLVMTATPIPRTLAMTAYGDLDVSVIDELPPGRKPITTVVIPDSRRdEVYERIREEI 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 849 LRDGQAFYVHNRVS--------SIDDTAARIRKLVPEARVVVAHGQMPEDLLERTVQGFWQREFDILVCTTIVETGLDIS 920
Cdd:PRK10917 469 AKGRQAYVVCPLIEesekldlqSAEETYEELQEAFPELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVP 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 921 NANTLIVERADTFGLSQLHQLRGRVGRSRERGYAYFLYppQAPLTETAYDRLATIAQNNElgaGMAVALKDLEIRGAGNV 1000
Cdd:PRK10917 549 NATVMVIENAERFGLAQLHQLRGRVGRGAAQSYCVLLY--KDPLSETARERLKIMRETND---GFVIAEKDLELRGPGEL 623
|
....*..
gi 2271751697 1001 LGVEQSG 1007
Cdd:PRK10917 624 LGTRQSG 630
|
|
| recG |
TIGR00643 |
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair] |
596-1007 |
2.96e-106 |
|
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273192 [Multi-domain] Cd Length: 630 Bit Score: 348.56 E-value: 2.96e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 596 KTKARKavREIAGELVAL--------YAKRQASPGHAFAPDTPWQAEMEDAFGFTETVDQLTAITEVKGDMEKSIPMDRV 667
Cdd:TIGR00643 183 LELARR--RLIFDEFFYLqlamlarrLGEKQQFSAPPANPSEELLTKFLASLPFKLTRAQKRVVKEILQDLKSDVPMNRL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 668 ICGDVGYGKTEIAVRAAFKAVQDGKQVAVLVPTTLLADQHLQTFTDRMAGFPVTVKGLSRFTDPAESRTVIEGMADGSVD 747
Cdd:TIGR00643 261 LQGDVGSGKTLVAALAMLAAIEAGYQVALMAPTEILAEQHYNSLRNLLAPLGIEVALLTGSLKGKRRKELLETIASGQIH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 748 VVIGTHRLLQTGVRWKDLGLVVVDEEQRFGVEHKEHIK---SLRSHVDVLTMSATPIPRTLEMSLAGIREMSTILTPPEE 824
Cdd:TIGR00643 341 LVVGTHALIQEKVEFKRLALVIIDEQHRFGVEQRKKLRekgQGGFTPHVLVMSATPIPRTLALTVYGDLDTSIIDELPPG 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 825 RYPVLTYVGPHDDKQIA-AALRRELLRDGQAFYVHNRVSSIDDTAA--------RIRKLVPEARVVVAHGQMPEDLLERT 895
Cdd:TIGR00643 421 RKPITTVLIKHDEKDIVyEFIEEEIAKGRQAYVVYPLIEESEKLDLkaaealyeRLKKAFPKYNVGLLHGRMKSDEKEAV 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 896 VQGFWQREFDILVCTTIVETGLDISNANTLIVERADTFGLSQLHQLRGRVGRSRERGYAYFLYPPqaPLTETAYDRLATI 975
Cdd:TIGR00643 501 MEEFREGEVDILVATTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYKN--PKSESAKKRLRVM 578
|
410 420 430
....*....|....*....|....*....|..
gi 2271751697 976 AQNNElgaGMAVALKDLEIRGAGNVLGVEQSG 1007
Cdd:TIGR00643 579 ADTLD---GFVIAEEDLELRGPGDLLGTKQSG 607
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
827-977 |
3.72e-82 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 264.98 E-value: 3.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 827 PVLTYVGPHDDKQIAAALRRELLRDGQAFYVHNRVSSIDDTAARIRKLVPEARVVVAHGQMPEDLLERTVQGFWQREFDI 906
Cdd:cd18810 1 PVRTYVMPYDDELIREAIERELLRGGQVFYVHNRIESIEKLATQLRQLVPEARIAIAHGQMTENELEEVMLEFAKGEYDI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2271751697 907 LVCTTIVETGLDISNANTLIVERADTFGLSQLHQLRGRVGRSRERGYAYFLYPPQAPLTETAYDRLATIAQ 977
Cdd:cd18810 81 LVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKERAYAYFLYPDQKKLTEDALKRLEAIQE 151
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
827-977 |
1.29e-69 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 229.85 E-value: 1.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 827 PVLTYVGPHDDK-QIAAALRRELLRDGQAFYVHNRVS--------SIDDTAARIRKLVPEARVVVAHGQMPEDLLERTVQ 897
Cdd:cd18792 1 PIRTYVIPHDDLdLVYEAIERELARGGQVYYVYPRIEesekldlkSIEALAEELKELVPEARVALLHGKMTEDEKEAVML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 898 GFWQREFDILVCTTIVETGLDISNANTLIVERADTFGLSQLHQLRGRVGRSRERGYAYFLYPPQAPLTETAYDRLATIAQ 977
Cdd:cd18792 81 EFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHQLRGRVGRGKHQSYCYLLYPDPKKLTETAKKRLRAIAE 160
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
610-822 |
1.06e-59 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350750 [Multi-domain] Cd Length: 225 Bit Score: 204.30 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 610 LVALYAKRQASPGHAFAPDTPWQAEMEDAFGFTETVDQLTAITEVKGDMEKSIPMDRVICGDVGYGKTEIAVRAAFKAVQ 689
Cdd:cd17992 13 LLLRRRKIEELKGIILEISGELLKKFLEALPFELTGAQKRVIDEILRDLASEKPMNRLLQGDVGSGKTVVAALAMLAAVE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 690 DGKQVAVLVPTTLLADQHLQTFTDRMAGFPVTVKGLSRFTDPAESRTVIEGMADGSVDVVIGTHRLLQTGVRWKDLGLVV 769
Cdd:cd17992 93 NGYQVALMAPTEILAEQHYDSLKKLLEPLGIRVALLTGSTKAKEKREILEKIASGEIDIVIGTHALIQEDVEFHNLGLVI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2271751697 770 VDEEQRFGVEHKEHIKSLRSHVDVLTMSATPIPRTLEMSLAGIREMSTILTPP 822
Cdd:cd17992 173 IDEQHRFGVEQRLKLREKGETPHVLVMTATPIPRTLALTLYGDLDVSIIDELP 225
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
633-818 |
2.58e-49 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 172.99 E-value: 2.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 633 AEMEDAFGFTETVDQLTAITEVKGDMEKSIPMDRVICGDVGYGKTEIAVRAAFKAVQDGKQVAVLVPTTLLADQHLQTFT 712
Cdd:cd17918 6 QELCKSLPFSLTKDQAQAIKDIEKDLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 713 DRMAGFPVT-VKGLSRFTDPAEsrtviegmadgsVDVVIGTHRLLQTGVRWKDLGLVVVDEEQRFGVEHKEHIKSLRShV 791
Cdd:cd17918 86 KFLPFINVElVTGGTKAQILSG------------ISLLVGTHALLHLDVKFKNLDLVIVDEQHRFGVAQREALYNLGA-T 152
|
170 180
....*....|....*....|....*..
gi 2271751697 792 DVLTMSATPIPRTLEMSLAGIREMSTI 818
Cdd:cd17918 153 HFLEATATPIPRTLALALSGLLDLSVI 179
|
|
| CarD_TRCF |
smart01058 |
CarD-like/TRCF domain; CarD is a Myxococcus xanthus protein required for the activation of ... |
515-615 |
4.04e-39 |
|
CarD-like/TRCF domain; CarD is a Myxococcus xanthus protein required for the activation of light- and starvation-inducible genes. This family includes the presumed N-terminal domain. CarD interacts with the zinc-binding protein CarG, to form a complex that regulates multiple processes in Myxococcus xanthus. This family also includes a domain to the N-terminal side of the DEAD helicase of TRCF proteins. TRCF displaces RNA polymerase stalled at a lesion, binds to the damage recognition protein UvrA, and increases the template strand repair rate during transcription. This domain is involved in binding to the stalled RNA polymerase.
Pssm-ID: 215001 [Multi-domain] Cd Length: 99 Bit Score: 140.67 E-value: 4.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 515 LTAGDLVVHDQHGIGRFVEMVERTVGGARREYLVLEYAsakrggGSDKLYVPMDSLDQLSRYVGGQA---PALSRLGGSD 591
Cdd:smart01058 2 LKIGDYVVHPDHGVGRYEGIETIEVGGEKREYLVLEYA------GGDKLYVPVDNLDLGSRYVGSEGevePVLDKLGGGS 75
|
90 100
....*....|....*....|....
gi 2271751697 592 WTNTKTKARKAVREIAGELVALYA 615
Cdd:smart01058 76 WSKRKRKAKSGIRDIAAELLRLYA 99
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
827-977 |
3.25e-38 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 140.17 E-value: 3.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 827 PVLTYVGPHDDK-QIAAALRRELLRDGQAFYVHNRVSSID--------DTAARIRKLV-PEARVVVAHGQMPEDLLERTV 896
Cdd:cd18811 1 PITTYLIFHTRLdKVYEFVREEIAKGRQAYVIYPLIEESEkldlkaavAMYEYLKERFrPELNVGLLHGRLKSDEKDAVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 897 QGFWQREFDILVCTTIVETGLDISNANTLIVERADTFGLSQLHQLRGRVGRSRERGYAYFLYPPqaPLTETAYDRLATIA 976
Cdd:cd18811 81 AEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYKD--PLTETAKQRLRVMT 158
|
.
gi 2271751697 977 Q 977
Cdd:cd18811 159 E 159
|
|
| TRCF |
smart00982 |
This domain is found in proteins necessary for strand-specific repair in DNA such as TRCF in ... |
1049-1147 |
2.49e-32 |
|
This domain is found in proteins necessary for strand-specific repair in DNA such as TRCF in Escherichia coli; A lesion in the template strand blocks the RNA polymerase complex (RNAP). The RNAP-DNA-RNA complex is specifically recognised by the transcription-repair-coupling factor (TRCF) which releases RNAP and the truncated transcript.
Pssm-ID: 198050 [Multi-domain] Cd Length: 100 Bit Score: 121.03 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 1049 DLPVDAHLPPDYIGSDRLRLEAYRRLATATSDSGVAAVVDELIDRYGALPEPALRLVAVARLRLLCRASGITDVSA-PSS 1127
Cdd:smart00982 1 DLPVPALIPEDYIPDVRQRLELYKRIASAETEEELDEIQEELIDRFGPLPEEVKNLLEVARLKLLAKKLGIEKIDAgGKG 80
|
90 100
....*....|....*....|
gi 2271751697 1128 ATVRLAPMDLPDSAQVRLKR 1147
Cdd:smart00982 81 IVIEFSPDTPIDPEKLILLI 100
|
|
| UvrB_inter |
pfam17757 |
UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the ... |
154-233 |
1.72e-28 |
|
UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the UvrA protein.
Pssm-ID: 465486 [Multi-domain] Cd Length: 91 Bit Score: 109.79 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 154 VSLSVGQEIGFDEVIARLVELAYTRVDMVGRRGEFAVRGGILDLFAPTAE-HPVRVEFWGDEITEMRMFSVADQRSIPEI 232
Cdd:pfam17757 1 LSLKVGQEIDRDELLRKLVELGYERNDIVFERGTFRVRGDIVDIFPAYSEdEAIRIEFFGDEIESIREFDPLTGRSLEKL 80
|
.
gi 2271751697 233 E 233
Cdd:pfam17757 81 D 81
|
|
| CarD_CdnL_TRCF |
pfam02559 |
CarD-like/TRCF domain; CarD is a Myxococcus xanthus protein required for the activation of ... |
515-614 |
4.21e-28 |
|
CarD-like/TRCF domain; CarD is a Myxococcus xanthus protein required for the activation of light- and starvation-inducible genes. This family includes the presumed N-terminal domain, CdnL. CarD interacts with the zinc-binding protein CarG to form a complex that regulates multiple processes in Myxococcus xanthus. This family also includes a domain to the N-terminal side of the DEAD helicase of TRCF (transcription-repair-coupling factor) proteins. TRCF displaces RNA polymerase stalled at a lesion, binds to the damage recognition protein UvrA, and increases the template strand repair rate during transcription. This domain is involved in binding to the stalled RNA polymerase. The family includes members otherwise referred to as CdnL, for CarD N-terminal like, which differ functionally from CarD. The TRCF domain mentioned above is the RNA polymerase-interacting domain or RID.
Pssm-ID: 460590 [Multi-domain] Cd Length: 89 Bit Score: 108.69 E-value: 4.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 515 LTAGDLVVHDQHGIGRFVEMVERTVggarREYLVLEYAsakrggGSDKLYVPMDSLDQLSRYVGGQapALSRLG-GSDWT 593
Cdd:pfam02559 1 LKVGDYVVHPDHGIGRIEGIEKLET----KDYYVLEYA------GGDKLYVPVDNLDLIRKYISKG--ELDKLGdGRRWR 68
|
90 100
....*....|....*....|.
gi 2271751697 594 NTKTKARKAVREIAGELVALY 614
Cdd:pfam02559 69 KYKEKLKSGDIEEAAELIKLY 89
|
|
| TRCF |
pfam03461 |
TRCF domain; |
1050-1143 |
5.31e-28 |
|
TRCF domain;
Pssm-ID: 460928 [Multi-domain] Cd Length: 95 Bit Score: 108.67 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 1050 LPVDAHLPPDYIGSDRLRLEAYRRLATATSDSGVAAVVDELIDRYGALPEPALRLVAVARLRLLCRASGITDVSA-PSSA 1128
Cdd:pfam03461 1 LDVDAYIPDDYIPDESQRLELYKRLASIETEEELDDLQEELIDRFGPLPEEVENLLEIARLKLLAKKLGIEKIDLkGGGI 80
|
90
....*....|....*
gi 2271751697 1129 TVRLAPMDLPDSAQV 1143
Cdd:pfam03461 81 RITFSEDAKIDPEKL 95
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
644-807 |
4.57e-24 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 100.01 E-value: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 644 TVDQLTAITEVKGDMeksipmDRVICGDVGYGKTEIAVRAAFKAV---QDGKQVAVLVPTTLLADQHLQTFTDRMAGFPV 720
Cdd:pfam00270 1 TPIQAEAIPAILEGR------DVLVQAPTGSGKTLAFLLPALEALdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 721 TVKGLSRFTDPAESRTVIEGmadgsVDVVIGTH----RLLQTGVRWKDLGLVVVDEEQR-----FGVEHKEHIKSLRSHV 791
Cdd:pfam00270 75 KVASLLGGDSRKEQLEKLKG-----PDILVGTPgrllDLLQERKLLKNLKLLVLDEAHRlldmgFGPDLEEILRRLPKKR 149
|
170
....*....|....*.
gi 2271751697 792 DVLTMSATPiPRTLEM 807
Cdd:pfam00270 150 QILLLSATL-PRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
636-825 |
3.91e-22 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 95.64 E-value: 3.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 636 EDAFGFTETVDQLTAITEVKgdmekSIPMDRVICGDVGYGKTEIAVRAAFKAVQ--DGKQVAVLVPTTLLADQHLQTFTD 713
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALL-----SGLRDVILAAPTGSGKTLAALLPALEALKrgKGGRVLVLVPTRELAEQWAEELKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 714 RMAGFPVTVKGLsrfTDPAESRTVIEGMADGSVDVVIGT-----HRLLQTGVRWKDLGLVVVDEEQR-----FGVEHKEH 783
Cdd:smart00487 77 LGPSLGLKVVGL---YGGDSKREQLRKLESGKTDILVTTpgrllDLLENDKLSLSNVDLVILDEAHRlldggFGDQLEKL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2271751697 784 IKSLRSHVDVLTMSATP---IPRTLEMSLAGIREMSTILTPPEER 825
Cdd:smart00487 154 LKLLPKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPI 198
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
154-221 |
3.87e-17 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 86.64 E-value: 3.87e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2271751697 154 VSLSVGQEIGFDEVIARLVELAYTRVDMVGRRGEFAVRGGILDLF-APTAEHPVRVEFWGDEITEMRMF 221
Cdd:PRK05298 159 LSLRVGQEIDRRELLRRLVDLQYERNDIDFQRGTFRVRGDVIEIFpAYYEERAIRIEFFGDEIERISEF 227
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
842-947 |
2.03e-16 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 76.10 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 842 AALRREL--LRDGQAFYVHNRVSSIDDTAARIRKlvpEARVVVAHGQMPEDLLERTVQGFWQREFDILVCTTIVETGLDI 919
Cdd:pfam00271 4 EALLELLkkERGGKVLIFSQTKKTLEAELLLEKE---GIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*...
gi 2271751697 920 SNANTLIVERADtFGLSQLHQLRGRVGR 947
Cdd:pfam00271 81 PDVDLVINYDLP-WNPASYIQRIGRAGR 107
|
|
| UvrB |
COG0556 |
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair]; |
154-221 |
2.29e-16 |
|
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
Pssm-ID: 440322 [Multi-domain] Cd Length: 657 Bit Score: 84.29 E-value: 2.29e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2271751697 154 VSLSVGQEIGFDEVIARLVELAYTRVDMVGRRGEFAVRGGILDLF-APTAEHPVRVEFWGDEITEMRMF 221
Cdd:COG0556 156 LSLRVGEEIDRDELLRRLVELQYERNDIDFTRGTFRVRGDVIEIFpAYSEERAIRIEFFGDEIERISEF 224
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
664-799 |
4.02e-14 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 70.90 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 664 MDRVICGDVGYGKTEIAVRAAF-KAVQDGKQVAVLVPTTLLADQHLQTFTDRmAGFPVTVKGLSRFTDPAESRTVIEGMA 742
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALlLLLKKGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSSAEEREKNKLGDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 743 dgsvDVVIGTHRLLQT------GVRWKDLGLVVVDEEQRFGVEHKE-------HIKSLRSHVDVLTMSAT 799
Cdd:cd00046 81 ----DIIIATPDMLLNlllredRLFLKDLKLIIVDEAHALLIDSRGalildlaVRKAGLKNAQVILLSAT 146
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
673-957 |
1.00e-12 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 72.36 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 673 GYGKTEIAVRAAfKAVQDGKQVAVLVPTTLLADQHLQTFTDRMAGFPVTvkglsrftdpaesrtviEGMADGSVDVVIGT 752
Cdd:COG1061 110 GTGKTVLALALA-AELLRGKRVLVLVPRRELLEQWAEELRRFLGDPLAG-----------------GGKKDSDAPITVAT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 753 HRLLQTGVRWKDL----GLVVVDEEQRFGVEHKEHIKSLRSHVDVLTMSATPIpRT-----LEMSLAGIR---------- 813
Cdd:COG1061 172 YQSLARRAHLDELgdrfGLVIIDEAHHAGAPSYRRILEAFPAAYRLGLTATPF-RSdgreiLLFLFDGIVyeyslkeaie 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 814 ----------EMSTILTPPEERYPVLT------YVGPHDDK-QIAAALRRELLRDGQAFYVHNRVSSIDDTAARIRKLVP 876
Cdd:COG1061 251 dgylappeyyGIRVDLTDERAEYDALSerlreaLAADAERKdKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGI 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 877 EARVVvaHGQMPEDLLERTVQGFWQREFDILVCTTIVETGLDISNANTLIVERAdTFGLSQLHQLRGRVGRSRERG-YAY 955
Cdd:COG1061 331 RAAVV--TGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRP-TGSPREFIQRLGRGLRPAPGKeDAL 407
|
..
gi 2271751697 956 FL 957
Cdd:COG1061 408 VY 409
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
673-773 |
1.78e-12 |
|
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' superfamily 2 DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350687 [Multi-domain] Cd Length: 178 Bit Score: 66.85 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 673 GYGKTEIAVRAAFKAVQDGKQVAVLVPTTLLADQHLQTFTDRMaGFPVTVKGlSRFTDpAESRTVIEGMADGSVDVVIGT 752
Cdd:cd17929 25 GSGKTEVYIELIEKVLAKGKQVLVLVPEISLTPQLIKRFKKRF-GDKVAVLH-SKLSD-KERADEWRKIKRGEAKVVIGA 101
|
90 100
....*....|....*....|.
gi 2271751697 753 HRLLQTGVrwKDLGLVVVDEE 773
Cdd:cd17929 102 RSALFAPF--KNLGLIIVDEE 120
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
879-947 |
3.91e-12 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 63.00 E-value: 3.91e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2271751697 879 RVVVAHGQMPEDLLERTVQGFWQREFDILVCTTIVETGLDISNANTLIVERADtFGLSQLHQLRGRVGR 947
Cdd:smart00490 13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-WSPASYIQRIGRAGR 80
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
673-951 |
1.53e-10 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 64.90 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 673 GYGKTEIAVRAAFKAVQDGKQVAVLVPTTllaDQHLQTFTdRM-AGFPvtvkglsrftdpaesRTVIEGMADGSVD---- 747
Cdd:COG4098 139 GAGKTEMLFPAIAEALKQGGRVCIATPRV---DVVLELAP-RLqQAFP---------------GVDIAALYGGSEEkyry 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 748 ---VVIGTHRLLqtgvRWKD-LGLVVVDE---------EQ-RFGVEhkehiKSLRSHVDVLTMSATPiPRTLEMSLA-GI 812
Cdd:COG4098 200 aqlVIATTHQLL----RFYQaFDLLIIDEvdafpysgdPMlQYAVK-----RARKPDGKLIYLTATP-SKALQRQVKrGK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 813 REMSTILTppeeRY-------PVLTYVGPHDDK--------QIAAALRRELLRDGQAFYVhnrVSSIDDT---AARIRKL 874
Cdd:COG4098 270 LKVVKLPA----RYhghplpvPKFKWLGNWKKRlrrgklprKLLKWLKKRLKEGRQLLIF---VPTIELLeqlVALLQKL 342
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2271751697 875 VPEARVVVAHGQMPEDllERTVQGFWQREFDILVCTTIVETGLDISNANTLIVErAD--TFGLSQLHQLRGRVGRSRER 951
Cdd:COG4098 343 FPEERIAGVHAEDPER--KEKVQAFRDGEIPILVTTTILERGVTFPNVDVAVLG-ADhpVFTEAALVQIAGRVGRSADY 418
|
|
| priA |
TIGR00595 |
primosomal protein N'; All proteins in this family for which functions are known are ... |
670-806 |
1.97e-09 |
|
primosomal protein N'; All proteins in this family for which functions are known are components of the primosome which is involved in replication, repair, and recombination.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273162 [Multi-domain] Cd Length: 505 Bit Score: 61.63 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 670 GDVGYGKTEIAVRAAFKAVQDGKQVAVLVPTTLLADQHLQTFTDRMaGFPVTV--KGLSRftdpAESRTVIEGMADGSVD 747
Cdd:TIGR00595 4 GVTGSGKTEVYLQAIEKVLALGKSVLVLVPEIALTPQMIQRFKYRF-GSQVAVlhSGLSD----SEKLQAWRKVKNGEIL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2271751697 748 VVIGTHRLLQTGVrwKDLGLVVVDEEQRFGVE-------HKEHIKSLRSH---VDVLTMSATPiprTLE 806
Cdd:TIGR00595 79 VVIGTRSALFLPF--KNLGLIIVDEEHDSSYKqeegpryHARDVAVYRAKkfnCPVVLGSATP---SLE 142
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
590-952 |
2.20e-09 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 61.64 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 590 SDWTNT--KTKARKAVREIAGELVALYAKRQASPGhafAPDTPWQAEM-EDAFGFTETVDQLTAITevkgdmeksIPMdr 666
Cdd:COG1203 91 ADWLDSanFDMARQALDHLLAERLERLLPKKSKPR---TPINPLQNEAlELALEAAEEEPGLFILT---------APT-- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 667 vicgdvGYGKTEIAVRAAFKAVQDGKQ--VAVLVPTTLLADQHLQTFTDRmagFPVTVK---GLSRFtDPAESRTVIEGM 741
Cdd:COG1203 157 ------GGGKTEAALLFALRLAAKHGGrrIIYALPFTSIINQTYDRLRDL---FGEDVLlhhSLADL-DLLEEEEEYESE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 742 ADGSVD--------VVIGT-----HRLLQTGVRW--KDLGL----VVVDEEQRFGVE-----HK--EHIKSLRSHVdVLt 795
Cdd:COG1203 227 ARWLKLlkelwdapVVVTTidqlfESLFSNRKGQerRLHNLansvIILDEVQAYPPYmlallLRllEWLKNLGGSV-IL- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 796 MSATpIPRTLEMSLAGIREMSTILTPPEERYP-------VLTYVGPHDDKQIAAALRRELLRDGQAFYVHNRVSSIDDTA 868
Cdd:COG1203 305 MTAT-LPPLLREELLEAYELIPDEPEELPEYFrafvrkrVELKEGPLSDEELAELILEALHKGKSVLVIVNTVKDAQELY 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 869 ARIRKLVPEARVVVAHGQMP----EDLLERTVQGFWQREFDILVCTTIVETGLDISnANTLIVERAdtfGLSQLHQLRGR 944
Cdd:COG1203 384 EALKEKLPDEEVYLLHSRFCpadrSEIEKEIKERLERGKPCILVSTQVVEAGVDID-FDVVIRDLA---PLDSLIQRAGR 459
|
....*...
gi 2271751697 945 VGRSRERG 952
Cdd:COG1203 460 CNRHGRKE 467
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
673-773 |
2.68e-08 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 58.21 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 673 GYGKTEIAVRAAFKAVQDGKQVAVLVPTTLLADQHLQTFTDRMaGFPVTV--KGLSrftdPAESRTVIEGMADGSVDVVI 750
Cdd:COG1198 224 GSGKTEVYLQAIAEVLAQGKQALVLVPEIALTPQTVERFRARF-GARVAVlhSGLS----DGERLDEWRRARRGEARIVI 298
|
90 100
....*....|....*....|....*....
gi 2271751697 751 GThrllqtgvR------WKDLGLVVVDEE 773
Cdd:COG1198 299 GT--------RsalfapFPNLGLIIVDEE 319
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
670-773 |
4.82e-08 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 57.47 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 670 GDVGYGKTEIAVRAAFKAVQDGKQVAVLVPTTLLADQHLQTFTDRMaGFPVTV--KGLSrftdPAESRTVIEGMADGSVD 747
Cdd:PRK05580 169 GVTGSGKTEVYLQAIAEVLAQGKQALVLVPEIALTPQMLARFRARF-GAPVAVlhSGLS----DGERLDEWRKAKRGEAK 243
|
90 100 110
....*....|....*....|....*....|..
gi 2271751697 748 VVIGThrllqtgvR------WKDLGLVVVDEE 773
Cdd:PRK05580 244 VVIGA--------RsalflpFKNLGLIIVDEE 267
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
667-799 |
6.12e-07 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 51.11 E-value: 6.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 667 VICGDVGYGKTEIAVRAAFKAVQDGKQVAV-LVPTTLLADQHLQTFTDRMAGFPVTVKGLSrfTDPAESRTviegmADGS 745
Cdd:cd17921 21 LVSAPTSSGKTLIAELAILRALATSGGKAVyIAPTRALVNQKEADLRERFGPLGKNVGLLT--GDPSVNKL-----LLAE 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2271751697 746 VDVVIGTH-----RLLQTGVRW-KDLGLVVVDEEQRFGVEHK--------EHIKSLRSHVDVLTMSAT 799
Cdd:cd17921 94 ADILVATPekldlLLRNGGERLiQDVRLVVVDEAHLIGDGERgvvlelllSRLLRINKNARFVGLSAT 161
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
902-959 |
2.37e-06 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 46.54 E-value: 2.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2271751697 902 REFDILVCTTIVETGLDISNANTLIVERADTFgLSQLHQLRGRVGRSRERGYAYFLYP 959
Cdd:cd18785 21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSS-AASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
675-957 |
2.71e-06 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 51.43 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 675 GKTEIAVRAAFKAVQDGKQVAVLVPTTLLADQHLQTFTDRMAGFPVTVKGLSRFTDPAESRTviegmadGSVDVVIGT-- 752
Cdd:COG1204 50 GKTLIAELAILKALLNGGKALYIVPLRALASEKYREFKRDFEELGIKVGVSTGDYDSDDEWL-------GRYDILVATpe 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 753 --HRLLQTGVRW-KDLGLVVVDE------EQR-FGVEHK-EHIKSLRSHVDVLTMSATpiprtlemsLAGIREMSTILTP 821
Cdd:COG1204 123 klDSLLRNGPSWlRDVDLVVVDEahliddESRgPTLEVLlARLRRLNPEAQIVALSAT---------IGNAEEIAEWLDA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 822 P----EERyPVLTYVGPHDD-------------KQIAAALRRELLRDGQAFYVHNRVSSIDDTAARIRKLVPE------- 877
Cdd:COG1204 194 ElvksDWR-PVPLNEGVLYDgvlrfddgsrrskDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRrltpeer 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 878 -----------------------ARVV---VA--HGQMPEDLLERTVQGFWQREFDILVCTTIVETGLdisN--ANTLIV 927
Cdd:COG1204 273 eeleelaeellevseethtneklADCLekgVAfhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGV---NlpARRVII 349
|
330 340 350
....*....|....*....|....*....|....*..
gi 2271751697 928 ERADTFGLSQL-----HQLRGRVGRSR--ERGYAYFL 957
Cdd:COG1204 350 RDTKRGGMVPIpvlefKQMAGRAGRPGydPYGEAILV 386
|
|
| CdnL |
COG1329 |
RNA polymerase-interacting regulator, CarD/CdnL/TRCF family [Transcription]; |
518-573 |
5.20e-06 |
|
RNA polymerase-interacting regulator, CarD/CdnL/TRCF family [Transcription];
Pssm-ID: 440940 [Multi-domain] Cd Length: 155 Bit Score: 47.82 E-value: 5.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2271751697 518 GDLVVHDQHGIGRFVEMVERTVGGARREYLVLeyasaKRGGGSDKLYVPMDSLDQL 573
Cdd:COG1329 4 GDKVVYPMHGVGVIEAIEEKEIAGEKKEYYVL-----RFPYDDMTIMVPVDKAESV 54
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
667-799 |
2.56e-04 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 43.09 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 667 VICGDVGYGKTEIAVRAAFKAVQDGKQVAVLVPTTLLADQHLQTFTDRMA-GFPVTVK-GLSRFTDpaesrtviEGMADg 744
Cdd:cd18028 21 LISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFKKLEEiGLKVGIStGDYDEDD--------EWLGD- 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2271751697 745 sVDVVIGTHR----LLQTGVRW-KDLGLVVVDEEQRFGVEHK--------EHIKSLRSHVDVLTMSAT 799
Cdd:cd18028 92 -YDIIVATYEkfdsLLRHSPSWlRDVGVVVVDEIHLISDEERgptlesivARLRRLNPNTQIIGLSAT 158
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
673-800 |
3.87e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 41.91 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 673 GYGKTEIAVRAAFKAVQDGkqVAVLVPTTLLADQhlqtftdrmagfpvTVKGLSRFTDPAESRTVIEGMADGSVD--VVI 750
Cdd:cd17926 28 GSGKTLTALALIAYLKELR--TLIVVPTDALLDQ--------------WKERFEDFLGDSSIGLIGGGKKKDFDDanVVV 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2271751697 751 GT----HRLLQTGVRWKDL-GLVVVDEEQRFGVEHKEHIKSLRSHVDVLTMSATP 800
Cdd:cd17926 92 ATyqslSNLAEEEKDLFDQfGLLIVDEAHHLPAKTFSEILKELNAKYRLGLTATP 146
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
667-958 |
4.36e-04 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 43.96 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 667 VICGDVGYGKTEIAVRAAFKAVQDGK--QVAVLVPT-TLLADQHLQ---TFTDRMAGFpvTVKGLSRFTDPAESRTVIEG 740
Cdd:cd09639 3 VIEAPTGYGKTEAALLWALHSLKSQKadRVIIALPTrATINAMYRRakeAFGETGLYH--SSILSSRIKEMGDSEEFEHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 741 MADGSvdvvIGTHRLLQTGV-----------RWKDLG------------LVVVDEEQRFGVEHKEHIKSLRSH-----VD 792
Cdd:cd09639 81 FPLYI----HSNDTLFLDPItvctidqvlksVFGEFGhyeftlasiansLLIFDEVHFYDEYTLALILAVLEVlkdndVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 793 VLTMSATpIPRTLEMSLAGI---REMSTILTPPEERYP----VLTYVGphdDKQIAAALRRELLRDGQAFYVHNRVSSID 865
Cdd:cd09639 157 ILLMSAT-LPKFLKEYAEKIgyvEENEPLDLKPNERAPfikiESDKVG---EISSLERLLEFIKKGGSVAIIVNTVDRAQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 866 DTAARIRKLVPEARVVVAHGQMPE----DLLERTVQGFWQREFDILVCTTIVETGLDISnANTLIVERADtfgLSQLHQL 941
Cdd:cd09639 233 EFYQQLKEKGPEEEIMLIHSRFTEkdraKKEAELLLEFKKSEKFVIVATQVIEASLDIS-VDVMITELAP---IDSLIQR 308
|
330
....*....|....*..
gi 2271751697 942 RGRVGRsRERGYAYFLY 958
Cdd:cd09639 309 LGRLHR-YGEKNGEEVY 324
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
871-971 |
2.70e-03 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 40.69 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 871 IRKLVPEARVV------VAHGQMPEDLLERtvqgFWQREFDILVCTTIVETGLDISNANTLIVERAD------------- 931
Cdd:cd18804 110 LKTLFPEARIAridrdtTRKKGALEKLLDQ----FERGEIDILIGTQMIAKGLDFPNVTLVGILNADsglnspdfraser 185
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2271751697 932 TFGLsqLHQLRGRVGRSRERGYAYF-LYPPQAPLTETAYDR 971
Cdd:cd18804 186 AFQL--LTQVSGRAGRGDKPGKVIIqTYNPEHPLIQAAKEE 224
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
831-955 |
3.04e-03 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 39.03 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 831 YVGPHDDKQIAAALRRELLRDGQA--FyvhnrVSSIDdTAARIRKLVPEARVVVA--HGQMPEDLLERTVQGFWQREFDI 906
Cdd:cd18787 7 VVEEEEKKLLLLLLLLEKLKPGKAiiF-----VNTKK-RVDRLAELLEELGIKVAalHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2271751697 907 LVCTTIVETGLDISNANtLIV-----ERADTFglsqLHqlR-GRVGRSRERGYAY 955
Cdd:cd18787 81 LVATDVAARGLDIPGVD-HVInydlpRDAEDY----VH--RiGRTGRAGRKGTAI 128
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|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
667-800 |
3.59e-03 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 40.11 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 667 VICGDVGYGKTEIAVRAA------FKAVQDGKqVAVLVPTTLLADQHLQTFTDRMAGFPVTVKGLSRFTDPAES-RTVIE 739
Cdd:cd17927 21 IICLPTGSGKTFVAVLICehhlkkFPAGRKGK-VVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENVSvEQIVE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2271751697 740 gmadgSVDVVIGTHRLLQ------TGVRWKDLGLVVVDEEQRFGVEH----------KEHIKSLRSHVDVLTMSATP 800
Cdd:cd17927 100 -----SSDVIIVTPQILVndlksgTIVSLSDFSLLVFDECHNTTKNHpyneimfrylDQKLGSSGPLPQILGLTASP 171
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
673-801 |
3.81e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 39.58 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 673 GYGKTEIAVRAAFKAVQDG--KQVAVLVPTTLLADQHLQTFTdRMAGFPVTVKGLSrftdpaESRTVIEGMADGSVdVVI 750
Cdd:pfam04851 33 GSGKTLTAAKLIARLFKKGpiKKVLFLVPRKDLLEQALEEFK-KFLPNYVEIGEII------SGDKKDESVDDNKI-VVT 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2271751697 751 GTHRLLQTGVRWKDL------GLVVVDEEQRFGVEHKEHIKSLRSHVDVLTMSATPI 801
Cdd:pfam04851 105 TIQSLYKALELASLEllpdffDVIIIDEAHRSGASSYRNILEYFKPAFLLGLTATPE 161
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
659-801 |
4.03e-03 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 39.94 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 659 EKSIPMDRVICGDVGYGKTEIAVRAA-------FKAVQDGKQVAVLVPTTLLADQ---HLQTFTdrmagfPVTVKGLSRF 728
Cdd:cd18034 12 EAALKRNTIVVLPTGSGKTLIAVMLIkemgelnRKEKNPKKRAVFLVPTVPLVAQqaeAIRSHT------DLKVGEYSGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 729 TDPAESRTVIEGMADGSVDVVIGTHR----LLQTG-VRWKDLGLVVVDEEQRFGVEHK--------EHIKSLRSHVDVLT 795
Cdd:cd18034 86 MGVDKWTKERWKEELEKYDVLVMTAQilldALRHGfLSLSDINLLIFDECHHATGDHPyarimkefYHLEGRTSRPRILG 165
|
....*.
gi 2271751697 796 MSATPI 801
Cdd:cd18034 166 LTASPV 171
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
855-957 |
5.47e-03 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 38.49 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 855 FYVHNRV---SSIDDTAARI-RKLVPEARVVVAH---GQ--------MPEDLLERTVQGFWQREFDILVCTTIVETGLDI 919
Cdd:cd18801 27 EGSDTRViifSEFRDSAEEIvNFLSKIRPGIRATrfiGQasgksskgMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDI 106
|
90 100 110
....*....|....*....|....*....|....*...
gi 2271751697 920 SNANTLIVERADTFGLSQLhQLRGRVGRSRErGYAYFL 957
Cdd:cd18801 107 GEVDLIICYDASPSPIRMI-QRMGRTGRKRQ-GRVVVL 142
|
|
| DEXHc_RLR-3 |
cd18075 |
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ... |
673-805 |
8.43e-03 |
|
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of genetics and physiology 2 or LGP2 and DHX58) appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. RLR-3 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. RNA binding is required for RLR-3-mediated enhancement of MDA5 activation. RLR-3 end-binding may promote nucleation of MDA5 oligomerization on dsRNA. RLR-3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350833 [Multi-domain] Cd Length: 200 Bit Score: 39.07 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2271751697 673 GYGKTEIAVRAAFKAVQ--DGKQVAVLVPTTLLADQHLQTFTdRMAGFPVTVKGLSRFTDPaesRTVIEGMADGSvDVVI 750
Cdd:cd18075 27 GAGKTRAAVYVARRHLEtkRGAKVAVLVNKVHLVDQHLEKEF-HVLLDKYTVTAISGDSSH---KCFFGQLARGS-DVVI 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2271751697 751 GTHRLLQTG---------VRWKDLGLVVVDEEQRfgvEHKEHI--KSLRSHVDVLTMSATPIPRTL 805
Cdd:cd18075 102 CTAQILQNAllsgeeeahVELTDFSLLVIDECHH---THKEAVynKIMLSYLEKKLSRQGDLPQIL 164
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