|
Name |
Accession |
Description |
Interval |
E-value |
| mfd |
TIGR00580 |
transcription-repair coupling factor (mfd); All proteins in this family for which functions ... |
123-954 |
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: 1127.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 123 LFYYGYEILDLVEVEGEASFRGDIVDIYIPNSKAY-RLSFFDTECESIKELDPTTQMSLkEDLLEIEIPPTLFS-LDEPS 200
Cdd:TIGR00580 1 LVELGYERVDLVEEEGEFSVRGEILDIFPPGSELPvRIEFFGDEIESIREFDVDSQRSL-EELLEITILPAKEFiLLEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 201 YKDLKTKV----------------------------------EQSPLNSFSKDLT----SFGLWFLG---------EKAN 233
Cdd:TIGR00580 80 TIARLKDNaarvedakhletiealsegtlpageemflplffeDLSSLFDYLPDNTpillDDPERFHSaarflqrelEEFY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 234 DLLHAYKSVISP-KALEEIQELA------SLNELDCER----FKFLKVLENAQG---YGDLEIHAHALEGFIALHSNHKI 299
Cdd:TIGR00580 160 NALEEAKKLINPpRLDLDPSELAfeasaiSLSRVQLENehlsLKASEAIEGAQKhsrLEFGEILAFKEELFRWLKAGFKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 300 TLLAPNKTILDNAISALEK-------SNMECVIAPFVLN------------------FKTPDRIFISLNSFERKKKRQKS 354
Cdd:TIGR00580 240 TVAAESESQAERLKSLLAEhdiaaqvIDESCIIIPAVRYvmigalssgfilptaglaVITESELFGSRVLRRPKKSRLKS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 355 KLA--LNELNPGEWVVHDDYGVGVFSQLVQHSVLGSKRDFLEIAYLGEDKLLLPVENLHLIARYVAQSDSVPAKDRLGKG 432
Cdd:TIGR00580 320 KPIesLNELNPGDYVVHLDHGIGRFLGLETLEVGGIERDYLVLEYAGEDKLYVPVEQLHLISRYVGGSGKNPALDKLGGK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 433 SFLKLKAKVRTKLLEIASKIIELAAERNLILGKKMDVHLAELEVFKSHAGFEYTSDQEKAIAEISRDLSSHKVMDRLLSG 512
Cdd:TIGR00580 400 SWEKTKAKVKKSVREIAAKLIELYAKRKAIKGHAFPPDLEWQQEFEDSFPFEETPDQLKAIEEIKADMESPRPMDRLVCG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 513 DVGFGKTEVAMHAIFCAFLNGFQSALVVPTTLLAHQHFETLRARFENFGVKVARLDRY--ASEKNKLLKAVELGQVDALI 590
Cdd:TIGR00580 480 DVGFGKTEVAMRAAFKAVLDGKQVAVLVPTTLLAQQHFETFKERFANFPVTIELLSRFrsAKEQNEILKELASGKIDILI 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 591 GTHAILG--AKFKNLGLVVVDEEHKFGVKQKEALKELSKSVHFLSMSATPIPRTLNMALSQIKGISSLKTPPTDRKPSRT 668
Cdd:TIGR00580 560 GTHKLLQkdVKFKDLGLLIIDEEQRFGVKQKEKLKELRTSVDVLTLSATPIPRTLHMSMSGIRDLSIIATPPEDRLPVRT 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 669 FLKEKNDELLKEIIYRELRRNGQIFYIHNHIASISKVKTKLEELIPKLKIAILHSQINASESEEIMLEFAKGSYQVLLCT 748
Cdd:TIGR00580 640 FVMEYDPELVREAIRRELLRGGQVFYVHNRIESIEKLATQLRELVPEARIAIAHGQMTENELEEVMLEFYKGEFQVLVCT 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 749 SIVESGIHLPNANTIIIDNAQNFGLADLHQLRGRVGRGKKEGFCYFLIEDQKSLNEQALKRLLALEKNSYLGSGESIAYH 828
Cdd:TIGR00580 720 TIIETGIDIPNANTIIIERADKFGLAQLYQLRGRVGRSKKKAYAYLLYPHQKALTEDAQKRLEAIQEFSELGAGFKIALH 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 829 DLEIRGGGNLLGQDQSGHIKNIGYALYTRMLEDAIYELSGGK-KRLEKSVEIQLGVSAFLNPELIASDSLRLDLYRRLSL 907
Cdd:TIGR00580 800 DLEIRGAGNLLGEEQSGHIESIGFDLYMELLEEAIEELKGGKpPKLEEETDIELPYSAFIPDDYIADDSLRLEFYKRIAS 879
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1255383615 908 CENVDEVGQIHEEIEDRFGKIDDLSAQFLQIITLKILANQLGIIKLS 954
Cdd:TIGR00580 880 AETEEELEKIRDELIDRFGPLPEEARTLLDVARLKLLARKLGIRKLK 926
|
|
| Mfd |
COG1197 |
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and ... |
28-969 |
0e+00 |
|
Transcription-repair coupling factor (superfamily II helicase) [Replication, recombination and repair, Transcription];
Pssm-ID: 440810 [Multi-domain] Cd Length: 1130 Bit Score: 874.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 28 KLAKEvISYFKPNTKAILFPEF------RAKKNDDLRSffeeflQLLGGLRefyqALENKQEAIIIAPISALLHPLPKKE 101
Cdd:COG1197 42 RLAED-LRFFLPDLPVLLFPAWetlpydRFSPSPDIVS------ERLATLR----RLASGKPGIVVTPVRALLQRLPPPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 102 LLESFKITLL--EKYNLKDLKDKLFYYGYEILDLVEVEGEASFRGDIVDIYIPNSK-AYRLSFFDTECESIKELDPTTQM 178
Cdd:COG1197 111 LLAAASLSLKvgDELDLEELRERLVAAGYERVDQVEEPGEFAVRGGILDIFPPGSEhPVRIEFFGDEIESIRTFDPETQR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 179 SLkEDLLEIEIPP-TLFSLDE-----------------PSYKDLKTKVEQ----------SPLnsFSKDLTSF------- 223
Cdd:COG1197 191 SL-EKVDEVELLPaREFPLDEeaierfrerlrelfgldPKLDELYEALSEgiafagieyyLPL--FYEELATLfdylped 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 224 GLWFLGE------KANDLLH------------AYKSVISPKAL----EEIqeLASLNELDCERFKFLKVLENAQGYGDLE 281
Cdd:COG1197 268 ALVVLDEperieeAAEEFWEeieeryearrhdRGRPLLPPEELfldpEEL--FAALKRRPRVTLSPFAALPEGAGVVNLG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 282 IH------------AHALEGFIAlhSNHKITLLAPN----KTILD------------NAISALEKSNMECVIAP----FV 329
Cdd:COG1197 346 ARplpsfagqlealLEELKRLLK--DGGRVLLAAESegrrERLLEllrdhgiparlvESLAELSPGGVAITVGPlehgFE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 330 LNfkTPDRIFISLNSF--ERKKKRQKSKLA--------LNELNPGEWVVHDDYGVGVFSQLVQHSVLGSKRDFLEIAYLG 399
Cdd:COG1197 424 LP--DAKLAVITESELfgERVKRRRRKKKRsadafirdLSELKPGDYVVHVDHGIGRYLGLETLEVGGAERDYLVLEYAG 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 400 EDKLLLPVENLHLIARYVAQSDSVPAKDRLGKGSFLKLKAKVRTKLLEIASKIIELAAERNLILGKKM---DVHLAELEv 476
Cdd:COG1197 502 GDKLYVPVDQLDLISRYVGSEGEAPKLDKLGGSDWQKAKAKAKKAVRDIAAELLKLYAERAARKGFAFspdTPWQREFE- 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 477 fkshAGFEY--TSDQEKAIAEISRDLSSHKVMDRLLSGDVGFGKTEVAMHAIFCAFLNGFQSALVVPTTLLAHQHFETLR 554
Cdd:COG1197 581 ----AAFPYeeTPDQLRAIEEVKADMESPRPMDRLVCGDVGFGKTEVALRAAFKAVMDGKQVAVLVPTTLLAQQHYETFK 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 555 ARFENFGVKVARLDRY--ASEKNKLLKAVELGQVDALIGTHAILGA--KFKNLGLVVVDEEHKFGVKQKEALKELSKSVH 630
Cdd:COG1197 657 ERFAGFPVRVEVLSRFrtAKEQKETLEGLADGKVDIVIGTHRLLSKdvKFKDLGLLIIDEEQRFGVRHKEKLKALRANVD 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 631 FLSMSATPIPRTLNMALSQIKGISSLKTPPTDRKPSRTFLKEKNDELLKEIIYRELRRNGQIFYIHNHIASISKVKTKLE 710
Cdd:COG1197 737 VLTLTATPIPRTLQMSLSGIRDLSIIATPPEDRLPVKTFVGEYDDALIREAILRELLRGGQVFYVHNRVEDIEKVAARLQ 816
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 711 ELIPKLKIAILHSQINASESEEIMLEFAKGSYQVLLCTSIVESGIHLPNANTIIIDNAQNFGLADLHQLRGRVGRGKKEG 790
Cdd:COG1197 817 ELVPEARIAVAHGQMSERELERVMLDFYEGEFDVLVCTTIIETGIDIPNANTIIIERADRFGLAQLYQLRGRVGRSHRRA 896
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 791 FCYFLIEDQKSLNEQALKRLLALEKNSYLGSGESIAYHDLEIRGGGNLLGQDQSGHIKNIGYALYTRMLEDAIYELSGGK 870
Cdd:COG1197 897 YAYLLYPPDKVLTEDAEKRLEAIQEFTELGAGFKLAMHDLEIRGAGNLLGEEQSGHIAEVGFDLYLQMLEEAVAALKGGK 976
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 871 KRLEK-SVEIQLGVSAFLNPELIASDSLRLDLYRRLSLCENVDEVGQIHEEIEDRFGKIDDLSAQFLQIITLKILANQLG 949
Cdd:COG1197 977 EPEEEwEPEINLGVPALIPEDYIPDVRQRLELYKRIASAESEEELDELQEELIDRFGPLPEEVENLLAVARLKLLARRLG 1056
|
1050 1060
....*....|....*....|
gi 1255383615 950 IIKLSNFNQNITLTYSDEKK 969
Cdd:COG1197 1057 IEKIDAGGKGIRIEFSPNTP 1076
|
|
| PRK10689 |
PRK10689 |
transcription-repair coupling factor; Provisional |
349-953 |
2.17e-161 |
|
transcription-repair coupling factor; Provisional
Pssm-ID: 182649 [Multi-domain] Cd Length: 1147 Bit Score: 505.43 E-value: 2.17e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 349 KKRQKSKLALN---------ELNPGEWVVHDDYGVGVFSQLVQHSVLGSKRDFLEIAYLGEDKLLLPVENLHLIARYVAQ 419
Cdd:PRK10689 456 RRRQDSRRTINpdtlirnlaELHPGQPVVHLEHGVGRYAGMTTLEAGGIKGEYLMLTYANDAKLYVPVSSLHLISRYAGG 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 420 SDSVPAKDRLGKGSFLKLKAKVRTKLLEIASKIIELAAERNLILGKKMDVHLAELEVFKSHAGFEYTSDQEKAIAEISRD 499
Cdd:PRK10689 536 AEENAPLHKLGGDAWSRARQKAAEKVRDVAAELLDIYAQRAAKEGFAFKHDREQYQLFCDSFPFETTPDQAQAINAVLSD 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 500 LSSHKVMDRLLSGDVGFGKTEVAMHAIFCAFLNGFQSALVVPTTLLAHQHFETLRARFENFGVKVARLDRY--ASEKNKL 577
Cdd:PRK10689 616 MCQPLAMDRLVCGDVGFGKTEVAMRAAFLAVENHKQVAVLVPTTLLAQQHYDNFRDRFANWPVRIEMLSRFrsAKEQTQI 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 578 LKAVELGQVDALIGTHAIL--GAKFKNLGLVVVDEEHKFGVKQKEALKELSKSVHFLSMSATPIPRTLNMALSQIKGISS 655
Cdd:PRK10689 696 LAEAAEGKIDILIGTHKLLqsDVKWKDLGLLIVDEEHRFGVRHKERIKAMRADVDILTLTATPIPRTLNMAMSGMRDLSI 775
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 656 LKTPPTDRKPSRTFLKEKNDELLKEIIYRELRRNGQIFYIHNHIASISKVKTKLEELIPKLKIAILHSQINASESEEIML 735
Cdd:PRK10689 776 IATPPARRLAVKTFVREYDSLVVREAILREILRGGQVYYLYNDVENIQKAAERLAELVPEARIAIGHGQMRERELERVMN 855
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 736 EFAKGSYQVLLCTSIVESGIHLPNANTIIIDNAQNFGLADLHQLRGRVGRGKKEGFCYFLIEDQKSLNEQALKRLLALEK 815
Cdd:PRK10689 856 DFHHQRFNVLVCTTIIETGIDIPTANTIIIERADHFGLAQLHQLRGRVGRSHHQAYAWLLTPHPKAMTTDAQKRLEAIAS 935
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 816 NSYLGSGESIAYHDLEIRGGGNLLGQDQSGHIKNIGYALYTRMLEDAIYELSGGKK-RLE----KSVEIQLGVSAFLNPE 890
Cdd:PRK10689 936 LEDLGAGFALATHDLEIRGAGELLGEEQSGQMETIGFSLYMELLENAVDALKAGREpSLEdltsQQTEVELRMPSLLPDD 1015
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1255383615 891 LIASDSLRLDLYRRLSLCENVDEVGQIHEEIEDRFGKIDDLSAQFLQIITLKILANQLGIIKL 953
Cdd:PRK10689 1016 FIPDVNTRLSFYKRIASAKNENELEEIKVELIDRFGLLPDPARNLLDIARLRQQAQKLGIRKL 1078
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
464-845 |
1.90e-113 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 365.14 E-value: 1.90e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 464 GKKMDVHLAELEVFKSHAGFEYTSDQEKAIAEISRDLSSHKVMDRLLSGDVGFGKTEVAMHAIFCAFLNGFQSALVVPTT 543
Cdd:COG1200 239 GPALPGDGELLEAFLAALPFELTGAQKRVIAEIAADLASPHPMNRLLQGDVGSGKTVVALLAMLAAVEAGYQAALMAPTE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 544 LLAHQHFETLRARFENFGVKVARL---DRyASEKNKLLKAVELGQVDALIGTHAIL--GAKFKNLGLVVVDEEHKFGVKQ 618
Cdd:COG1200 319 ILAEQHYRSLSKLLEPLGIRVALLtgsTK-AKERREILAALASGEADIVVGTHALIqdDVEFKNLGLVVIDEQHRFGVEQ 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 619 KEALKELSKSVHFLSMSATPIPRTLNMALSqikG---ISSLKTPPTDRKPSRTFL--KEKNDELLkEIIYRELRRNGQIF 693
Cdd:COG1200 398 RLALREKGEAPHVLVMTATPIPRTLAMTLY---GdldVSVIDELPPGRKPIKTRVvpEERRDEVY-ERIREEIAKGRQAY 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 694 YI--------HNHIASISKVKTKLEELIPKLKIAILHSQINASESEEIMLEFAKGSYQVLLCTSIVESGIHLPNANTIII 765
Cdd:COG1200 474 VVcplieeseKLDLQAAEETYEELREAFPGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVATTVIEVGVDVPNATVMVI 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 766 DNAQNFGLADLHQLRGRVGRGKKEGFCYFLIedQKSLNEQALKRLLALEKNSylgSGESIAYHDLEIRGGGNLLGQDQSG 845
Cdd:COG1200 554 ENAERFGLSQLHQLRGRVGRGSAQSYCLLLY--DAPLSETARERLEVMRETN---DGFEIAEEDLELRGPGEFLGTRQSG 628
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
474-845 |
1.95e-113 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 364.86 E-value: 1.95e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 474 LEVFKSHAGFEYTSDQEKAIAEISRDLSSHKVMDRLLSGDVGFGKTEVAMHAIFCAFLNGFQSALVVPTTLLAHQHFETL 553
Cdd:PRK10917 251 LKKFLASLPFELTGAQKRVVAEILADLASPKPMNRLLQGDVGSGKTVVAALAALAAIEAGYQAALMAPTEILAEQHYENL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 554 RARFENFGVKVARL--DRYASEKNKLLKAVELGQVDALIGTHAIL--GAKFKNLGLVVVDEEHKFGVKQKEALKELSKSV 629
Cdd:PRK10917 331 KKLLEPLGIRVALLtgSLKGKERREILEAIASGEADIVIGTHALIqdDVEFHNLGLVIIDEQHRFGVEQRLALREKGENP 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 630 HFLSMSATPIPRTLNMALSQIKGISSLKTPPTDRKPSRTFL--KEKNDELLkEIIYRELRRNGQIFYI--------HNHI 699
Cdd:PRK10917 411 HVLVMTATPIPRTLAMTAYGDLDVSVIDELPPGRKPITTVVipDSRRDEVY-ERIREEIAKGRQAYVVcplieeseKLDL 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 700 ASISKVKTKLEELIPKLKIAILHSQINASESEEIMLEFAKGSYQVLLCTSIVESGIHLPNANTIIIDNAQNFGLADLHQL 779
Cdd:PRK10917 490 QSAEETYEELQEAFPELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVMVIENAERFGLAQLHQL 569
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1255383615 780 RGRVGRGKKEGFCYFLIEDQKSlnEQALKRLLALEKNSylgSGESIAYHDLEIRGGGNLLGQDQSG 845
Cdd:PRK10917 570 RGRVGRGAAQSYCVLLYKDPLS--ETARERLKIMRETN---DGFVIAEKDLELRGPGELLGTRQSG 630
|
|
| DEXHc_TRCF |
cd17991 |
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
470-658 |
1.59e-103 |
|
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: 321.06 E-value: 1.59e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 470 HLAELEVFKSHAGFEYTSDQEKAIAEISRDLSSHKVMDRLLSGDVGFGKTEVAMHAIFCAFLNGFQSALVVPTTLLAHQH 549
Cdd:cd17991 1 DGEEQEEFEASFPYEETPDQLKAIEEILKDMESGKPMDRLICGDVGFGKTEVAMRAAFKAVLSGKQVAVLVPTTLLAQQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 550 FETLRARFENFGVKVARLDRY--ASEKNKLLKAVELGQVDALIGTHAILG--AKFKNLGLVVVDEEHKFGVKQKEALKEL 625
Cdd:cd17991 81 YETFKERFANFPVNVELLSRFttAAEQREILEGLKEGKVDIVIGTHRLLSkdVEFKNLGLLIIDEEQRFGVKQKEKLKEL 160
|
170 180 190
....*....|....*....|....*....|...
gi 1255383615 626 SKSVHFLSMSATPIPRTLNMALSQIKGISSLKT 658
Cdd:cd17991 161 RPNVDVLTLSATPIPRTLHMALSGIRDLSVIAT 193
|
|
| recG |
TIGR00643 |
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair] |
433-848 |
4.92e-102 |
|
ATP-dependent DNA helicase RecG; [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273192 [Multi-domain] Cd Length: 630 Bit Score: 333.15 E-value: 4.92e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 433 SFLKLKAKVRTKLleIASKIIELA-AERNLILGKKMDVHLA-------ELEVFKSHAGFEYTSDQEKAIAEISRDLSSHK 504
Cdd:TIGR00643 178 KTLSLLELARRRL--IFDEFFYLQlAMLARRLGEKQQFSAPpanpseeLLTKFLASLPFKLTRAQKRVVKEILQDLKSDV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 505 VMDRLLSGDVGFGKTEVAMHAIFCAFLNGFQSALVVPTTLLAHQHFETLRARFENFGVKVARL--DRYASEKNKLLKAVE 582
Cdd:TIGR00643 256 PMNRLLQGDVGSGKTLVAALAMLAAIEAGYQVALMAPTEILAEQHYNSLRNLLAPLGIEVALLtgSLKGKRRKELLETIA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 583 LGQVDALIGTHAILGAK--FKNLGLVVVDEEHKFGVKQKEALKELSKS---VHFLSMSATPIPRTLNMALSQIKGISSLK 657
Cdd:TIGR00643 336 SGQIHLVVGTHALIQEKveFKRLALVIIDEQHRFGVEQRKKLREKGQGgftPHVLVMSATPIPRTLALTVYGDLDTSIID 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 658 TPPTDRKPSRTFL-KEKNDELLKEIIYRELRRNGQIFYIHNHIASISKVKTK--------LEELIPKLKIAILHSQINAS 728
Cdd:TIGR00643 416 ELPPGRKPITTVLiKHDEKDIVYEFIEEEIAKGRQAYVVYPLIEESEKLDLKaaealyerLKKAFPKYNVGLLHGRMKSD 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 729 ESEEIMLEFAKGSYQVLLCTSIVESGIHLPNANTIIIDNAQNFGLADLHQLRGRVGRGKKEGFCYFLIEDQKSlnEQALK 808
Cdd:TIGR00643 496 EKEAVMEEFREGEVDILVATTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYKNPKS--ESAKK 573
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1255383615 809 RLLALEKNSylgSGESIAYHDLEIRGGGNLLGQDQSGHIK 848
Cdd:TIGR00643 574 RLRVMADTL---DGFVIAEEDLELRGPGDLLGTKQSGYPE 610
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
665-815 |
1.66e-80 |
|
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: 258.04 E-value: 1.66e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 665 PSRTFLKEKNDELLKEIIYRELRRNGQIFYIHNHIASISKVKTKLEELIPKLKIAILHSQINASESEEIMLEFAKGSYQV 744
Cdd:cd18810 1 PVRTYVMPYDDELIREAIERELLRGGQVFYVHNRIESIEKLATQLRQLVPEARIAIAHGQMTENELEEVMLEFAKGEYDI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1255383615 745 LLCTSIVESGIHLPNANTIIIDNAQNFGLADLHQLRGRVGRGKKEGFCYFLIEDQKSLNEQALKRLLALEK 815
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 ... |
665-815 |
2.49e-66 |
|
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: 219.45 E-value: 2.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 665 PSRTFLKEKND-ELLKEIIYRELRRNGQIFYIHNHI--------ASISKVKTKLEELIPKLKIAILHSQINASESEEIML 735
Cdd:cd18792 1 PIRTYVIPHDDlDLVYEAIERELARGGQVYYVYPRIeesekldlKSIEALAEELKELVPEARVALLHGKMTEDEKEAVML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 736 EFAKGSYQVLLCTSIVESGIHLPNANTIIIDNAQNFGLADLHQLRGRVGRGKKEGFCYFLIEDQKSLNEQALKRLLALEK 815
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 ... |
464-647 |
4.97e-63 |
|
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: 213.16 E-value: 4.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 464 GKKMDVHLAELEVFKSHAGFEYTSDQEKAIAEISRDLSSHKVMDRLLSGDVGFGKTEVAMHAIFCAFLNGFQSALVVPTT 543
Cdd:cd17992 25 GIILEISGELLKKFLEALPFELTGAQKRVIDEILRDLASEKPMNRLLQGDVGSGKTVVAALAMLAAVENGYQVALMAPTE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 544 LLAHQHFETLRARFENFGVKVARL--DRYASEKNKLLKAVELGQVDALIGTHAIL--GAKFKNLGLVVVDEEHKFGVKQK 619
Cdd:cd17992 105 ILAEQHYDSLKKLLEPLGIRVALLtgSTKAKEKREILEKIASGEIDIVIGTHALIqeDVEFHNLGLVIIDEQHRFGVEQR 184
|
170 180
....*....|....*....|....*...
gi 1255383615 620 EALKELSKSVHFLSMSATPIPRTLNMAL 647
Cdd:cd17992 185 LKLREKGETPHVLVMTATPIPRTLALTL 212
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
483-657 |
4.48e-57 |
|
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: 194.56 E-value: 4.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 483 FEYTSDQEKAIAEISRDLSSHKVMDRLLSGDVGFGKTEVAMHAIFCAFLNGFQSALVVPTTLLAHQHFETLRARFENFGV 562
Cdd:cd17918 14 FSLTKDQAQAIKDIEKDLHSPEPMDRLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEARKFLPFINV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 563 KVARLDRyaseknkllKAVELGQVDALIGTHAIL--GAKFKNLGLVVVDEEHKFGVKQKEALKELSKsVHFLSMSATPIP 640
Cdd:cd17918 94 ELVTGGT---------KAQILSGISLLVGTHALLhlDVKFKNLDLVIVDEQHRFGVAQREALYNLGA-THFLEATATPIP 163
|
170
....*....|....*..
gi 1255383615 641 RTLNMALSQIKGISSLK 657
Cdd:cd17918 164 RTLALALSGLLDLSVID 180
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
671-815 |
8.14e-33 |
|
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: 124.76 E-value: 8.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 671 KEKNDELLKEIIYRELRRNGQIFYIHNHIASISKVKTK---------LEELIPKLKIAILHSQINASESEEIMLEFAKGS 741
Cdd:cd18811 8 FHTRLDKVYEFVREEIAKGRQAYVIYPLIEESEKLDLKaavamyeylKERFRPELNVGLLHGRLKSDEKDAVMAEFREGE 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1255383615 742 YQVLLCTSIVESGIHLPNANTIIIDNAQNFGLADLHQLRGRVGRGKKEGFCYFLIEDQKSlnEQALKRLLALEK 815
Cdd:cd18811 88 VDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHQLRGRVGRGDHQSYCLLVYKDPLT--ETAKQRLRVMTE 159
|
|
| CarD_TRCF |
smart01058 |
CarD-like/TRCF domain; CarD is a Myxococcus xanthus protein required for the activation of ... |
360-457 |
1.99e-30 |
|
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: 115.63 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 360 ELNPGEWVVHDDYGVGVFSQLVQHSVLGSKRDFLEIAYLGEDKLLLPVENLHLIARYVAQSDSVPAK-DRLGKGSFLKLK 438
Cdd:smart01058 1 ELKIGDYVVHPDHGVGRYEGIETIEVGGEKREYLVLEYAGGDKLYVPVDNLDLGSRYVGSEGEVEPVlDKLGGGSWSKRK 80
|
90
....*....|....*....
gi 1255383615 439 AKVRTKLLEIASKIIELAA 457
Cdd:smart01058 81 RKAKSGIRDIAAELLRLYA 99
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
486-645 |
1.76e-25 |
|
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: 103.86 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 486 TSDQEKAIAEIsrdLSSHKVmdrLLSGDVGFGKTEVAMHAIFCAF---LNGFQSALVVPTTLLAHQHFETLRARFENFGV 562
Cdd:pfam00270 1 TPIQAEAIPAI---LEGRDV---LVQAPTGSGKTLAFLLPALEALdklDNGPQALVLAPTRELAEQIYEELKKLGKGLGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 563 KVARL---DRYASEKNKLLKavelgqVDALIGTHAILGA------KFKNLGLVVVDEEHK-----FGVKQKEALKELSKS 628
Cdd:pfam00270 75 KVASLlggDSRKEQLEKLKG------PDILVGTPGRLLDllqerkLLKNLKLLVLDEAHRlldmgFGPDLEEILRRLPKK 148
|
170
....*....|....*..
gi 1255383615 629 VHFLSMSATPiPRTLNM 645
Cdd:pfam00270 149 RQILLLSATL-PRNLED 164
|
|
| TRCF |
smart00982 |
This domain is found in proteins necessary for strand-specific repair in DNA such as TRCF in ... |
881-974 |
6.02e-25 |
|
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: 99.85 E-value: 6.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 881 LGVSAFLNPELIASDSLRLDLYRRLSLCENVDEVGQIHEEIEDRFGKIDDLSAQFLQIITLKILANQLGIIKLSNFNQNI 960
Cdd:smart00982 2 LPVPALIPEDYIPDVRQRLELYKRIASAETEEELDEIQEELIDRFGPLPEEVKNLLEVARLKLLAKKLGIEKIDAGGKGI 81
|
90
....*....|....
gi 1255383615 961 TLTYSDEKKESLKA 974
Cdd:smart00982 82 VIEFSPDTPIDPEK 95
|
|
| TRCF |
pfam03461 |
TRCF domain; |
881-971 |
4.55e-22 |
|
TRCF domain;
Pssm-ID: 460928 [Multi-domain] Cd Length: 95 Bit Score: 91.33 E-value: 4.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 881 LGVSAFLNPELIASDSLRLDLYRRLSLCENVDEVGQIHEEIEDRFGKIDDLSAQFLQIITLKILANQLGIIKLSNFNQNI 960
Cdd:pfam03461 1 LDVDAYIPDDYIPDESQRLELYKRLASIETEEELDDLQEELIDRFGPLPEEVENLLEIARLKLLAKKLGIEKIDLKGGGI 80
|
90
....*....|.
gi 1255383615 961 TLTYSDEKKES 971
Cdd:pfam03461 81 RITFSEDAKID 91
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
477-664 |
3.20e-21 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 92.55 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 477 FKSHAGFEYTSDQEKAIAEISRDLsshkvMDRLLSGDVGFGKTEVAMHAIFCAFLNGF--QSALVVPTTLLAHQHFETLR 554
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGL-----RDVILAAPTGSGKTLAALLPALEALKRGKggRVLVLVPTRELAEQWAEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 555 ARFENFGVKVARLDRyASEKNKLLKAVELGQVDALIGTHAIL-------GAKFKNLGLVVVDEEHKFGVKQ-----KEAL 622
Cdd:smart00487 76 KLGPSLGLKVVGLYG-GDSKREQLRKLESGKTDILVTTPGRLldllendKLSLSNVDLVILDEAHRLLDGGfgdqlEKLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1255383615 623 KELSKSVHFLSMSATP---IPRTLNMALSQIKGISSLKTPPTDRK 664
Cdd:smart00487 155 KLLPKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIE 199
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
672-785 |
7.32e-18 |
|
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: 79.95 E-value: 7.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 672 EKNDELLKEIiyrELRRNGQIFYIHNhiaSISKVKTKLEELIPKLKIAILHSQINASESEEIMLEFAKGSYQVLLCTSIV 751
Cdd:pfam00271 1 EKLEALLELL---KKERGGKVLIFSQ---TKKTLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVA 74
|
90 100 110
....*....|....*....|....*....|....
gi 1255383615 752 ESGIHLPNANTIIIDNAQnFGLADLHQLRGRVGR 785
Cdd:pfam00271 75 ERGLDLPDVDLVINYDLP-WNPASYIQRIGRAGR 107
|
|
| DEXHc_priA |
cd17929 |
DEXH-box helicase domain of PriA; PriA, also known as replication factor Y or primosomal ... |
489-657 |
1.18e-17 |
|
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: 81.87 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 489 QEKAIAEISRDLSSHKVMdrLLSGDVGFGKTEVAMHAIFCAFLNGFQSALVVPTTLLAHQhfetLRARFEN-FGVKVARL 567
Cdd:cd17929 1 QRKAYEAIVSSLGGFKTF--LLHGVTGSGKTEVYIELIEKVLAKGKQVLVLVPEISLTPQ----LIKRFKKrFGDKVAVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 568 DRYASEKNKL--LKAVELGQVDALIGTHAILGAKFKNLGLVVVDEEHKFGVKQKEAL----KELS------KSVHFLSMS 635
Cdd:cd17929 75 HSKLSDKERAdeWRKIKRGEAKVVIGARSALFAPFKNLGLIIVDEEHDSSYKQDSGPryhaRDVAiyraklENAPVVLGS 154
|
170 180
....*....|....*....|..
gi 1255383615 636 ATPIPRTLNMALSQIKGISSLK 657
Cdd:cd17929 155 ATPSLESYYNAQQGKYRLLQLT 176
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
506-637 |
8.71e-17 |
|
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: 78.21 E-value: 8.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 506 MDRLLSGDVGFGKTEVAMHAIFCAFL-NGFQSALVVPTTLLAHQHFETLRARFeNFGVKVARLDRYASEknKLLKAVELG 584
Cdd:cd00046 2 ENVLITAPTGSGKTLAALLAALLLLLkKGKKVLVLVPTKALALQTAERLRELF-GPGIRVAVLVGGSSA--EEREKNKLG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1255383615 585 QVDALIGTH--------AILGAKFKNLGLVVVDEEHKFGVKQKEAL-------KELSKSVHFLSMSAT 637
Cdd:cd00046 79 DADIIIATPdmllnlllREDRLFLKDLKLIIVDEAHALLIDSRGALildlavrKAGLKNAQVILLSAT 146
|
|
| CarD_CdnL_TRCF |
pfam02559 |
CarD-like/TRCF domain; CarD is a Myxococcus xanthus protein required for the activation of ... |
361-455 |
1.32e-16 |
|
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: 75.56 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 361 LNPGEWVVHDDYGVGVFSQLVQHSvlgsKRDFLEIAYLGEDKLLLPVENLHLIARYVAQSDSvpakDRLGKGS-FLKLKA 439
Cdd:pfam02559 1 LKVGDYVVHPDHGIGRIEGIEKLE----TKDYYVLEYAGGDKLYVPVDNLDLIRKYISKGEL----DKLGDGRrWRKYKE 72
|
90
....*....|....*.
gi 1255383615 440 KVRTKLLEIASKIIEL 455
Cdd:pfam02559 73 KLKSGDIEEAAELIKL 88
|
|
| UvrB_inter |
pfam17757 |
UvrB interaction domain; This domain is found in the UvrB protein where it interacts with the ... |
112-191 |
3.28e-16 |
|
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: 74.74 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 112 EKYNLKDLKDKLFYYGYEILDLVEVEGEASFRGDIVDIYIPNS--KAYRLSFFDTECESIKELDPTTQMSLkEDLLEIEI 189
Cdd:pfam17757 7 QEIDRDELLRKLVELGYERNDIVFERGTFRVRGDIVDIFPAYSedEAIRIEFFGDEIESIREFDPLTGRSL-EKLDEVTI 85
|
..
gi 1255383615 190 PP 191
Cdd:pfam17757 86 YP 87
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
489-925 |
2.33e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 80.45 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 489 QEKAIAEISRDLSSHKvmDR-LLSGDVGFGKTEVAMHAIfcAFLNGFQSALV-VPTTLLAHQHFETLRARFENFGVKVAR 566
Cdd:COG1061 85 QQEALEALLAALERGG--GRgLVVAPTGTGKTVLALALA--AELLRGKRVLVlVPRRELLEQWAEELRRFLGDPLAGGGK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 567 LDRYAseknkllkavelgqvDALIGTHAILGAK------FKNLGLVVVDEEHKFGVKQKEALKELSKSVHFLSMSATPIp 640
Cdd:COG1061 161 KDSDA---------------PITVATYQSLARRahldelGDRFGLVIIDEAHHAGAPSYRRILEAFPAAYRLGLTATPF- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 641 RT--LNMALSQIKGI------------------------SSLKTPPTDRKPSRTFLKEK-------NDELLKEIIyRELR 687
Cdd:COG1061 225 RSdgREILLFLFDGIvyeyslkeaiedgylappeyygirVDLTDERAEYDALSERLREAlaadaerKDKILRELL-REHP 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 688 RNGQIFYIHNHIASISKVKTKLEELipKLKIAILHSQINASESEEIMLEFAKGSYQVLLCTSIVESGIHLPNANTIII-D 766
Cdd:COG1061 304 DDRKTLVFCSSVDHAEALAELLNEA--GIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILlR 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 767 NAQNFGLadLHQLRGRVGRGKKEG-FCYFL--IEDQKSLNEQALKRLLALEKNSY------LGSGESIAYHDLEIRGGGN 837
Cdd:COG1061 382 PTGSPRE--FIQRLGRGLRPAPGKeDALVYdfVGNDVPVLEELAKDLRDLAGYRVefldeeESEELALLIAVKPALEVKG 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 838 LLGQDQSGHIKNIGYALYTRMLEDAIYELSGGKKRLEKSVEIQLGVSAFLNPELIASDSLRLDLYRRLSLCENVDEVGQI 917
Cdd:COG1061 460 ELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELL 539
|
....*...
gi 1255383615 918 HEEIEDRF 925
Cdd:COG1061 540 ELLAALLR 547
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
715-785 |
3.62e-15 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 71.47 E-value: 3.62e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1255383615 715 KLKIAILHSQINASESEEIMLEFAKGSYQVLLCTSIVESGIHLPNANTIIIDNAQnFGLADLHQLRGRVGR 785
Cdd:smart00490 11 GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLP-WSPASYIQRIGRAGR 80
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
437-623 |
1.35e-14 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 78.27 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 437 LKAKVRTKLLEIAS-KIIELAAERNLILGKKMDVHLAELEVFKSHAGFEYTSDQEKAIAEIsRDLSSHKVMdrLLSGDVG 515
Cdd:PRK05580 96 LRLALLAELALAASsAVLKGLVKKGLIELEEVEVLRLRPPPDPAFEPPTLNPEQAAAVEAI-RAAAGFSPF--LLDGVTG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 516 FGKTEVAMHAIfCAFLNGFQSALV-VPTTLLAHQhfetLRARFEN-FGVKVARL-----DRyasEKNKLLKAVELGQVDA 588
Cdd:PRK05580 173 SGKTEVYLQAI-AEVLAQGKQALVlVPEIALTPQ----MLARFRArFGAPVAVLhsglsDG---ERLDEWRKAKRGEAKV 244
|
170 180 190
....*....|....*....|....*....|....*
gi 1255383615 589 LIGTHAILGAKFKNLGLVVVDEEHKFGVKQKEALK 623
Cdd:PRK05580 245 VIGARSALFLPFKNLGLIIVDEEHDSSYKQQEGPR 279
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
517-866 |
1.89e-13 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 74.16 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 517 GKTEVAMHAIFCAFLNGFQSALVVPTTLLAHQHFETLRARFENFGVKVAR------LDRYASEKNKLLKAV-ElgQVDAL 589
Cdd:COG1204 50 GKTLIAELAILKALLNGGKALYIVPLRALASEKYREFKRDFEELGIKVGVstgdydSDDEWLGRYDILVATpE--KLDSL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 590 IGTHAILgakFKNLGLVVVDEEHKFGVKQK--------EALKELSKSVHFLSMSATpIPrtlNMA-LSQIKGISSLKTP- 659
Cdd:COG1204 128 LRNGPSW---LRDVDLVVVDEAHLIDDESRgptlevllARLRRLNPEAQIVALSAT-IG---NAEeIAEWLDAELVKSDw 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 660 -PTDR-----KPSRTFLKEKNDELLKEIIY---RELRRNGQ--IF------------YIHNHIA--SISKVKTKLEELIP 714
Cdd:COG1204 201 rPVPLnegvlYDGVLRFDDGSRRSKDPTLAlalDLLEEGGQvlVFvssrrdaeslakKLADELKrrLTPEEREELEELAE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 715 KLK-------------------IAILHSQINASESEEIMLEFAKGSYQVLLCTSIVESGIHLPnANTIIIDNAQNFGLA- 774
Cdd:COG1204 281 ELLevseethtnekladclekgVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIIRDTKRGGMVp 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 775 ----DLHQLRGRVGR-GK-KEGFCYFLIEDQKSLNEQALKRLLA-LEK-NSYLGSGESIAYHDL-EIRGGGNLLGQDQSG 845
Cdd:COG1204 360 ipvlEFKQMAGRAGRpGYdPYGEAILVAKSSDEADELFERYILGePEPiRSKLANESALRTHLLaLIASGFANSREELLD 439
|
410 420
....*....|....*....|....*..
gi 1255383615 846 HIKNIGYALYTRM------LEDAIYEL 866
Cdd:COG1204 440 FLENTFYAYQYDKgdleevVDDALEFL 466
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
428-612 |
2.08e-12 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 71.30 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 428 RLGKGSFLKLKAKVRTKLLE-------------------IASKIIELAAERNLILGKKMDVHLAELE-VFKSHAGFEYTS 487
Cdd:COG1198 119 RLTLGEELPKRAPKQRRVLEalrehggpltlselakeagVSRSVLKALVKKGLLEIEEREVDRDPFApDVPAEPPPTLNE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 488 DQEKAIAEISRDLSSHKVMdrLLSGDVGFGKTEVAMHAIfCAFLNGFQSALV-VPTTLLAHQhfetLRARFEN-FGVKVA 565
Cdd:COG1198 199 EQQAAVEAIRAAAGGFSVF--LLHGVTGSGKTEVYLQAI-AEVLAQGKQALVlVPEIALTPQ----TVERFRArFGARVA 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1255383615 566 ----RLDryASEKNKLLKAVELGQVDALIGTH-AILgAKFKNLGLVVVDEEH 612
Cdd:COG1198 272 vlhsGLS--DGERLDEWRRARRGEARIVIGTRsALF-APFPNLGLIIVDEEH 320
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
671-793 |
1.31e-09 |
|
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: 57.13 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 671 KEKNDELLKEIIYRELRRNGQIFYihNHIASISKVKTKLEELipKLKIAILHSQINASESEEIMLEFAKGSYQVLLCTSI 750
Cdd:cd18787 11 EEKKLLLLLLLLEKLKPGKAIIFV--NTKKRVDRLAELLEEL--GIKVAALHGDLSQEERERALKKFRSGKVRVLVATDV 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1255383615 751 VESGIHLPNANTIIidnaqNFGLAD-----LHqlR-GRVGRGKKEGFCY 793
Cdd:cd18787 87 AARGLDIPGVDHVI-----NYDLPRdaedyVH--RiGRTGRAGRKGTAI 128
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
716-796 |
1.98e-08 |
|
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: 51.94 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 716 LKIAILHSQINasESEEIMLEFakgsyQVLLCTSIVESGIHLPNANTIIIDNAQNFgLADLHQLRGRVGRGKKEGFCYFL 795
Cdd:cd18785 4 VKIIVFTNSIE--HAEEIASSL-----EILVATNVLGEGIDVPSLDTVIFFDPPSS-AASYIQRVGRAGRGGKDEGEVIL 75
|
.
gi 1255383615 796 I 796
Cdd:cd18785 76 F 76
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
517-637 |
2.73e-08 |
|
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: 54.58 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 517 GKTEVAMHAIFCAFLNGFQSAL-VVPTTLLAHQHFETLRARFENFGVKVARLDRYASEKNKllkavELGQVDALIGTHAI 595
Cdd:cd17921 29 GKTLIAELAILRALATSGGKAVyIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPSVNKL-----LLAEADILVATPEK 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1255383615 596 L--------GAKFKNLGLVVVDEEHKFGVKQKEA--------LKELSKSVHFLSMSAT 637
Cdd:cd17921 104 LdlllrnggERLIQDVRLVVVDEAHLIGDGERGVvlelllsrLLRINKNARFVGLSAT 161
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
515-638 |
4.19e-07 |
|
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: 50.38 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 515 GFGKTEVAMhAIFCAFLNGFqSALVVPTTLLAHQhfetLRARFENFGVKVA-RLDRYASEKNKLLKAVELGQVDALIGTH 593
Cdd:cd17926 28 GSGKTLTAL-ALIAYLKELR-TLIVVPTDALLDQ----WKERFEDFLGDSSiGLIGGGKKKDFDDANVVVATYQSLSNLA 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1255383615 594 AILGAKFKNLGLVVVDEEHKFGVKQ-KEALKELSKSVhFLSMSATP 638
Cdd:cd17926 102 EEEKDLFDQFGLLIVDEAHHLPAKTfSEILKELNAKY-RLGLTATP 146
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
702-790 |
3.78e-06 |
|
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: 49.17 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 702 ISKVKTKLEELIPKLKIAILHSQINASES--EEIMLEFAKGSYQVLLCTSIVESGIHLPNANTIIIDNAQN-FGLAD--- 775
Cdd:cd18804 103 TERVEEELKTLFPEARIARIDRDTTRKKGalEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVGILNADSgLNSPDfra 182
|
90 100
....*....|....*....|..
gi 1255383615 776 -------LHQLRGRVGRGKKEG 790
Cdd:cd18804 183 serafqlLTQVSGRAGRGDKPG 204
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
508-609 |
4.62e-06 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs 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: 350682 [Multi-domain] Cd Length: 189 Bit Score: 48.09 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 508 RLLSGD-------VGFGKTEVAM-HAIFCAfLNGFQSALVVPTTLLAHQHFETLRARFENFGVKVARLDRY----ASEKN 575
Cdd:cd17924 28 RLLRGKsfaiiapTGVGKTTFGLaTSLYLA-SKGKRSYLIFPTKSLVKQAYERLSKYAEKAGVEVKILVYHsrlkKKEKE 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 1255383615 576 KLLKAVELGQVDALIGTHAILGAKFKNLG-----LVVVD 609
Cdd:cd17924 107 ELLEKIEKGDFDILVTTNQFLSKNFDLLSnkkfdFVFVD 145
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
517-830 |
9.26e-06 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 49.50 E-value: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 517 GKTEVAMHAIFCAFLNGFQSALVVPTTLLAHQHFETLrARFENFGVKVA-RLDRYASE----KNKLLKAVELGQVDALIG 591
Cdd:PRK01172 49 GKTLIAYSAIYETFLAGLKSIYIVPLRSLAMEKYEEL-SRLRSLGMRVKiSIGDYDDPpdfiKRYDVVILTSEKADSLIH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 592 THAILgakFKNLGLVVVDEEHKFGVKQK--------EALKELSKSVHFLSMSAT-----PIPRTLNMAL--SQIKGIsSL 656
Cdd:PRK01172 128 HDPYI---INDVGLIVADEIHIIGDEDRgptletvlSSARYVNPDARILALSATvsnanELAQWLNASLikSNFRPV-PL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 657 KTPPTDRKPSRTFLKEKND----ELLKEII--------YRELRRNG--------QIFYIHNHIASISKVKTKLEELIPKL 716
Cdd:PRK01172 204 KLGILYRKRLILDGYERSQvdinSLIKETVndggqvlvFVSSRKNAedyaemliQHFPEFNDFKVSSENNNVYDDSLNEM 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 717 ---KIAILHSQINASESEEIMLEFAKGSYQVLLCTSIVESGIHLPnANTIIIDNAQNFGLA--------DLHQLRGRVGR 785
Cdd:PRK01172 284 lphGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLP-ARLVIVRDITRYGNGgirylsnmEIKQMIGRAGR 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1255383615 786 GKKEGFCYFLIEDQKSLNEQALKRLLALEKN---SYLGSGESIAYHDL 830
Cdd:PRK01172 363 PGYDQYGIGYIYAASPASYDAAKKYLSGEPEpviSYMGSQRKVRFNTL 410
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
112-191 |
3.29e-05 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 47.73 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 112 EKYNLKDLKDKLFYYGYEILDLVEVEGEASFRGDIVDIYIPNS--KAYRLSFFDTECESIKELDPTTqMSLKEDLLEIEI 189
Cdd:PRK05298 165 QEIDRRELLRRLVDLQYERNDIDFQRGTFRVRGDVIEIFPAYYeeRAIRIEFFGDEIERISEFDPLT-GEVLGELDRVTI 243
|
..
gi 1255383615 190 PP 191
Cdd:PRK05298 244 YP 245
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
672-796 |
3.84e-05 |
|
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: 44.65 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 672 EKNDELLKEIIYRE-LRRNGQIFYIHNHIASISKVKTKLEELIPKLKIAILHSQINASESE--------EIMLEFAKGSY 742
Cdd:cd18801 12 EKLEEIVKEHFKKKqEGSDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATRFIGQASGKSSKgmsqkeqkEVIEQFRKGGY 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1255383615 743 QVLLCTSIVESGIHLPNANTIIIDNAQNFGLADLhQLRGRVGRgKKEGFCYFLI 796
Cdd:cd18801 92 NVLVATSIGEEGLDIGEVDLIICYDASPSPIRMI-QRMGRTGR-KRQGRVVVLL 143
|
|
| UvrB |
COG0556 |
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair]; |
143-176 |
1.06e-04 |
|
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
Pssm-ID: 440322 [Multi-domain] Cd Length: 657 Bit Score: 46.16 E-value: 1.06e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1255383615 143 RGDIVDIYIPNS--KAYRLSFFDTECESIKELDPTT 176
Cdd:COG0556 193 RGDVIEIFPAYSeeRAIRIEFFGDEIERISEFDPLT 228
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
509-685 |
1.85e-04 |
|
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA 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: 350769 [Multi-domain] Cd Length: 207 Bit Score: 43.82 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 509 LLSGDVGFGKT-EVAMhaIFCAFL--NGFQSALVV-PTTLLAHQHFEtLRARFenfGVKVARLDRYASEKNKLLKAVELG 584
Cdd:cd18011 21 LLADEVGLGKTiEAGL--IIKELLlrGDAKRVLILcPASLVEQWQDE-LQDKF---GLPFLILDRETAAQLRRLIGNPFE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 585 QVDALI--------GTHAILGAKFKNLGLVVVDEEHKFGVKQK-------EALKELSKSV-HFLSMSATPIPRTLNMALS 648
Cdd:cd18011 95 EFPIVIvsldllkrSEERRGLLLSEEWDLVVVDEAHKLRNSGGgketkryKLGRLLAKRArHVLLLTATPHNGKEEDFRA 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1255383615 649 QIkgisSLKTPPTDRKPSRTFLKEKNDELLKEIIYRE 685
Cdd:cd18011 175 LL----SLLDPGRFAVLGRFLRLDGLREVLAKVLLRR 207
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
718-785 |
4.68e-04 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases 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: 350182 [Multi-domain] Cd Length: 154 Bit Score: 41.77 E-value: 4.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1255383615 718 IAILHSQINASESEEIMLEFAKGSYQVLLCTSIVESGIHLPnANTIII--------DNAQNFGLADLHQLRGRVGR 785
Cdd:cd18795 66 IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLP-ARTVIIkgtqrydgKGYRELSPLEYLQMIGRAGR 140
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
605-813 |
5.39e-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: 43.57 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 605 LVVVDEEH-------KFGVKQKEALKElsKSVHFLSMSATpIPRTLNMALSQIKGISSLKTPPT---DRKPSRTFLKEKN 674
Cdd:cd09639 126 LLIFDEVHfydeytlALILAVLEVLKD--NDVPILLMSAT-LPKFLKEYAEKIGYVEENEPLDLkpnERAPFIKIESDKV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 675 -DELLKEIIYRELRRNGQIFYIHNHIASISKVKTKLEELIPKLKIAILHSQI----NASESEEIMLEFAKGSYQVLLCTS 749
Cdd:cd09639 203 gEISSLERLLEFIKKGGSVAIIVNTVDRAQEFYQQLKEKGPEEEIMLIHSRFtekdRAKKEAELLLEFKKSEKFVIVATQ 282
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1255383615 750 IVESGIHLpNANTIIIDNAQnfgLADLHQLRGRVGR-GKKEGFCYFLIEDQKSLNEQAL--KRLLAL 813
Cdd:cd09639 283 VIEASLDI-SVDVMITELAP---IDSLIQRLGRLHRyGEKNGEEVYIITDAPDGKGQKPypYDLVER 345
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
515-639 |
5.41e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 41.50 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 515 GFGKTEVAMHAIFCAFLNGF-QSAL-VVPTTLLAHQhfetLRARFENFGVKVARLDRYASEKNKLlkaVELGQVDALIGT 592
Cdd:pfam04851 33 GSGKTLTAAKLIARLFKKGPiKKVLfLVPRKDLLEQ----ALEEFKKFLPNYVEIGEIISGDKKD---ESVDDNKIVVTT 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1255383615 593 HAILGAKFKNL---------GLVVVDEEHKFGVKQKEALKELSKSVHFLSMSATPI 639
Cdd:pfam04851 106 IQSLYKALELAslellpdffDVIIIDEAHRSGASSYRNILEYFKPAFLLGLTATPE 161
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
509-643 |
2.21e-03 |
|
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L 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: 350759 [Multi-domain] Cd Length: 232 Bit Score: 40.82 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 509 LLSGDVGFGKTevaMHAifCAFLNG-FQSAL------VVPTTLLAH--QHFE--TLRAR-FENFGVKVArldryasEKNK 576
Cdd:cd18001 23 ILADDMGLGKT---VQI--CAFLSGmFDSGLiksvlvVMPTSLIPHwvKEFAkwTPGLRvKVFHGTSKK-------ERER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 577 LLKAVELGQvDALIGTHAILGAKFKNLG----------LVVVDEEHKFgvkqKEALKELSKSVHFLS------MSATPIP 640
Cdd:cd18001 91 NLERIQRGG-GVLLTTYGMVLSNTEQLSaddhdefkwdYVILDEGHKI----KNSKTKSAKSLREIPaknriiLTGTPIQ 165
|
...
gi 1255383615 641 RTL 643
Cdd:cd18001 166 NNL 168
|
|
| DEAD-like_helicase_N |
cd17912 |
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ... |
509-549 |
4.44e-03 |
|
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.
Pssm-ID: 350670 [Multi-domain] Cd Length: 81 Bit Score: 37.11 E-value: 4.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1255383615 509 LLSGDVGFGKTEVAMHAIFCAFLNGFQSALVVPTTLLAHQH 549
Cdd:cd17912 3 LHLGPTGSGKTLVAIQKIASAMSSGKSVLVVTPTKLLAHEI 43
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
483-646 |
4.66e-03 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs 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: 350785 [Multi-domain] Cd Length: 179 Bit Score: 39.17 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 483 FEYTSDQEKAIAEISRDLSShkvmdrLLSGDVGFGKTEVAMHAIFCAFLNGFQSALVVPTTLLAHQHFETLRARFENFGV 562
Cdd:cd18027 7 FELDVFQKQAILHLEAGDSV------FVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGDVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 563 KVARLDRYaSEKNKLLKAVELGQVDALIGTHAIlgakfKNLGLVVVDEEHKF-----GVKQKEALKELSKSVHFLSMSAT 637
Cdd:cd18027 81 ITGDVQLN-PEASCLIMTTEILRSMLYNGSDVI-----RDLEWVIFDEVHYIndaerGVVWEEVLIMLPDHVSIILLSAT 154
|
....*....
gi 1255383615 638 pIPRTLNMA 646
Cdd:cd18027 155 -VPNTVEFA 162
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
509-637 |
5.61e-03 |
|
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: 38.85 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 509 LLSGDVGFGKTEVAMHAIFCAFLNGFQSALVVPTTLLAHQHFETLRaRFENFGVKVA-------RLDRYASEKNKLLKAV 581
Cdd:cd18028 21 LISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFK-KLEEIGLKVGistgdydEDDEWLGDYDIIVATY 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1255383615 582 ElgQVDALIgTHAIlgAKFKNLGLVVVDEEHKFGVKQKEA--------LKELSKSVHFLSMSAT 637
Cdd:cd18028 100 E--KFDSLL-RHSP--SWLRDVGVVVVDEIHLISDEERGPtlesivarLRRLNPNTQIIGLSAT 158
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
592-794 |
7.41e-03 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 40.35 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 592 THAILGAKFKNLGLVVVDE--EH-KFGVKQKEALKELSKSVH--FLsMSAT---PIPRTL----NMALSQIKGisslktp 659
Cdd:PHA02653 281 THKLTLNKLFDYGTVIIDEvhEHdQIGDIIIAVARKHIDKIRslFL-MTATledDRDRIKeffpNPAFVHIPG------- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 660 PTDRKPSRTFLKEKNDELLKEIIYRELRRN---------------GQIFYihnhiASISKV---KTKLEELIPKLKIAIL 721
Cdd:PHA02653 353 GTLFPISEVYVKNKYNPKNKRAYIEEEKKNivtalkkytppkgssGIVFV-----ASVSQCeeyKKYLEKRLPIYDFYII 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 722 HSQI-NASEseeiMLE--FAKGSYQVLLCTSIVESGIHLPNAnTIIIDN-----AQNFGLADLH-------QLRGRVGRG 786
Cdd:PHA02653 428 HGKVpNIDE----ILEkvYSSKNPSIIISTPYLESSVTIRNA-THVYDTgrvyvPEPFGGKEMFisksmrtQRKGRVGRV 502
|
....*...
gi 1255383615 787 KKEGFCYF 794
Cdd:PHA02653 503 SPGTYVYF 510
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
509-640 |
7.68e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 40.21 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 509 LLSGDVGFGKT-EVAMHAIFCAFLNGFQSALVV-PTTLLAHQHFETlrARFeNFGVKVARLDryaSEKNKLLKAVELGQV 586
Cdd:COG0553 264 LLADDMGLGKTiQALALLLELKERGLARPVLIVaPTSLVGNWQREL--AKF-APGLRVLVLD---GTRERAKGANPFEDA 337
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1255383615 587 DALIGTHAILGAKFKNL-----GLVVVDEEHKF---GVKQKEALKELsKSVHFLSMSATPIP 640
Cdd:COG0553 338 DLVITSYGLLRRDIELLaavdwDLVILDEAQHIknpATKRAKAVRAL-KARHRLALTGTPVE 398
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
692-793 |
8.40e-03 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members 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: 350178 [Multi-domain] Cd Length: 171 Bit Score: 38.28 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255383615 692 IFYIHNH------------IASISKVKTKLEELI-----PKLKIAILHSQINASESEEIMLEFAKGSYQVLLCTSIVESG 754
Cdd:cd18791 34 ILQIHRTeepgdilvflpgQEEIERLCELLREELlspdlGKLLVLPLHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETS 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1255383615 755 IHLPNAnTIIID---------NAQNfGL----------ADLHQLRGRVGRgKKEGFCY 793
Cdd:cd18791 114 ITIPGV-VYVIDsglvkekvyDPRT-GLsslvtvwiskASAEQRAGRAGR-TRPGKCY 168
|
|
| |
