|
Name |
Accession |
Description |
Interval |
E-value |
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
13-881 |
0e+00 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 1091.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 13 PAPRPLAEFHPVVRQWFERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALVVEGLAagGELADATQV 92
Cdd:COG1201 2 SAEDVLSLLHPAVRAWFAARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDELARRPRP--GELPDGLRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 93 VYVSPLKALSNDIRINLEQPLAGIREELarlGLPDVDIRSAVRTGDTPQVERGAMRKRPPHILVTTPESLYILLGSESGR 172
Cdd:COG1201 80 LYISPLKALANDIERNLRAPLEEIGEAA---GLPLPEIRVGVRTGDTPASERQRQRRRPPHILITTPESLALLLTSPDAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 173 QMLAGVRSVIVDEIHALAGSKRGSHLALSLERLQALCPRPLLRIGLSATQKPIEKVARFLVGAsGNPRDpaCRIVDVGYT 252
Cdd:COG1201 157 ELLRGVRTVIVDEIHALAGSKRGVHLALSLERLRALAPRPLQRIGLSATVGPLEEVARFLVGY-EDPRP--VTIVDAGAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 253 RPRDLGIEVPPVALEAV--MSNDTWELVYDRLAHLAGEHRTTLVFVNTRRMAERVTRFLAERLGSR--QVAAHHGSLAKE 328
Cdd:COG1201 234 KKPDLEVLVPVEDLIERfpWAGHLWPHLYPRVLDLIEAHRTTLVFTNTRSQAERLFQRLNELNPEDalPIAAHHGSLSRE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 329 LRLDAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSGHSVGGTPKGRLFPTSRDDLVECAAL 408
Cdd:COG1201 314 QRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAGHRVGEVSKGRLVPTHRDELVECAAA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 409 LDSVRRGELDSLVLPRQPLDVLAQQIVAEVACQEWREDDLYRLVIRAEPYAGLERERFDEVLRMLAEGYHS-RLGVRGAY 487
Cdd:COG1201 394 LEAARAGEIEARRPPRNPLDVLAQHIVAMAAGGPFDVDELYAEVRRAYPYRDLTREDFDAVLDFLAGGGPSlRAYERYAR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 488 LHRDALNGLLRGRRGARLTALTSGGTIPDTGDYSVLLEPQGLLVGTVNEDFAVESLAGDVFQLGNTSYRIIRIEPGRVRV 567
Cdd:COG1201 474 IVRDRVDGRLGARRGAARLARTNIGTIPDRGMLKVRLVRGGRRLGELEEEFVEELRPGDVFVLGGRSLRIERIRGMRVYV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 568 EDAQGQPPNIPFWLGEAPGRSDELSASVARLRDTLDEllgegqalpegrrLEPAIAWLGAtLGLDDGAARQIVEYLARAR 647
Cdd:COG1201 554 RPAPGKPPTVPSWFGERLPLSTELARAVGAFLRELAE-------------WEAARAWLRE-YGLDEPAARALREYLEEQR 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 648 QALGGLPGSRRLVLERFFDESGGMQLIIHSPHGSRLNRAWGLALRKRFCRSFNFELQAAATEDAIILSLSTshSFPLDEV 727
Cdd:COG1201 620 AATSALPTDDTLLVERFRDEEGDWHLVVHPFEGRRVHEALGLLLAYRLSRRFGIPLGFAANDYGFVLRLPD--PVPLLDL 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 728 WRYLHSASAEHLLVQAVLDAPLFGVRWRWNLTTSLGLPRYAGGRKVPPQLLRMKSEDLLASVfpdqvaclenivgeREVP 807
Cdd:COG1201 698 LRLFDPDNLEDDLEAALNGSELFKRRFRECAARALLIPRRYPGKRKSLRQQQASSDLLLDVL--------------REYP 763
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598468 808 DHPLVAQTLDDCLHEAMDCEGWLALLRDMESGAVDLLARDLPAPSALAAEILTarpyAYLDDAPLEERRTQAVQ 881
Cdd:COG1201 764 DHPLLRETYRECLEDLLDLPRLRELLERIEGGRIRVVEVELDRPSPFAFPLLV----ERGRDAVLAERRAADLL 833
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
21-876 |
0e+00 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 677.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 21 FHPVVRQWFERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALVveGLAAGGELADATQVVYVSPLKA 100
Cdd:PRK13767 18 LRPYVREWFKEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELF--RLGREGELEDKVYCLYVSPLRA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 101 LSNDIRINLEQPLAGIREELARLGLPDVDIRSAVRTGDTPQVERGAMRKRPPHILVTTPESLYILLGSESGRQMLAGVRS 180
Cdd:PRK13767 96 LNNDIHRNLEEPLTEIREIAKERGEELPEIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILLNSPKFREKLRTVKW 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 181 VIVDEIHALAGSKRGSHLALSLERLQALCPRPLLRIGLSATQKPIEKVARFLVGAS--GNPRDpaCRIVDVGYTRPRDLG 258
Cdd:PRK13767 176 VIVDEIHSLAENKRGVHLSLSLERLEELAGGEFVRIGLSATIEPLEEVAKFLVGYEddGEPRD--CEIVDARFVKPFDIK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 259 IEVPPVALEAVMSNDTWELVYDRLAHLAGEHRTTLVFVNTRRMAERVTRFLAERLGSR----QVAAHHGSLAKELRLDAE 334
Cdd:PRK13767 254 VISPVDDLIHTPAEEISEALYETLHELIKEHRTTLIFTNTRSGAERVLYNLRKRFPEEydedNIGAHHSSLSREVRLEVE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 335 QRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSGHSVGGTPKGRLFPTSRDDLVECAALLDSVRR 414
Cdd:PRK13767 334 EKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAGHRLGEVSKGRIIVVDRDDLVECAVLLKKARE 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 415 GELDSLVLPRQPLDVLAQQIVAEVACQEWREDDLYRLVIRAEPYAGLERERFDEVLRMLAeGYHSRLGVRGAY--LHRDA 492
Cdd:PRK13767 414 GKIDRVHIPKNPLDVLAQHIVGMAIERPWDIEEAYNIVRRAYPYRDLSDEDFESVLRYLA-GDYGGLEEKNVYakIWLDE 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 493 lNGLLRGRRG--ARLTALTSGGTIPDTGDYSVLLEpQGLLVGTVNEDFaVESLA-GDVFQLGNTSYRIIRIEPGRVRVED 569
Cdd:PRK13767 493 -EEGKFGKRGklARMIYYTNIGTIPDEFKCDVYTE-DGKYVGNLEEEF-LERLEpGDVFVLGGRTYEFLYSRGSKVYVDP 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 570 AQGQPPNIPFWLGEAPGRSDELSASVARLRDTLDELLGEGQalpegrrlEPAIAWLGATLGLDDGAARQIVEY-LARARQ 648
Cdd:PRK13767 570 AEGERPTVPSWFSEMLPLSYDLALEIGKFRREVAEMIEKGG--------EEAVELLLKEYPIDENAARSIYGYfLEQYLY 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 649 ALGGLPGSRRLVLERFFDESGGMQLIIHSPHGSRLNRAWGLALRKRFCRSFNFELQAAATEDAIILSLSTSHSFPLDEVW 728
Cdd:PRK13767 642 TGGSVPTDKRLLIEIYDDEEGRRNYIFHSLYGRRANDALSRAVAYILSKRLNANVRVSVTDNGFMLSVPLNRKLDIEEVL 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 729 RYLHSASAEHLLVQAVLDAPLFGVRWRWNLTTSLG-LPRYAgGRKVPPQLLRMKSEDLLASVfpdqvaclenivgeREVP 807
Cdd:PRK13767 722 ESLNPENVREILKEALDRTELLKRRFRHNATRSLMiLRRYK-GREKSAERQQVNAEMLLKFA--------------KELD 786
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598468 808 DHPLVAQTLDDCLHEAMDCEGWLALLRDMESGAVDLLARDLPAPSALAAEILTArpyAYLDDAPLEERR 876
Cdd:PRK13767 787 DFPVLKETYREILEDYMDIENAEEVLEKIRDGEIEVVIGPVPIPSPFAFNIATL---GASDVVLAEDKR 852
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
55-1443 |
0e+00 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 630.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 55 VAAPTGSGKTLTAFLAAIDALVVEGLAAGGELAD--ATQVVYVSPLKALSNDIRINLEQPLAGIREELARLGLPDVDIRS 132
Cdd:PRK09751 1 VIAPTGSGKTLAAFLYALDRLFREGGEDTREAHKrkTSRILYISPIKALGTDVQRNLQIPLKGIADERRRRGETEVNLRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 133 AVRTGDTPQVERGAMRKRPPHILVTTPESLYILLGSESgRQMLAGVRSVIVDEIHALAGSKRGSHLALSLERLQALCPRP 212
Cdd:PRK09751 81 GIRTGDTPAQERSKLTRNPPDILITTPESLYLMLTSRA-RETLRGVETVIIDEVHAVAGSKRGAHLALSLERLDALLHTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 213 LLRIGLSATQKPIEKVARFLVGASG----NPrdPACRIVDVGYTRPRDLGIEVPPVALE------AVMSNDTWELVYDRL 282
Cdd:PRK09751 160 AQRIGLSATVRSASDVAAFLGGDRPvtvvNP--PAMRHPQIRIVVPVANMDDVSSVASGtgedshAGREGSIWPYIETGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 283 AHLAGEHRTTLVFVNTRRMAERVTRFL----AERL-GSRQVAA--------------------------HHGSLAKELRL 331
Cdd:PRK09751 238 LDEVLRHRSTIVFTNSRGLAEKLTARLnelyAARLqRSPSIAVdaahfestsgatsnrvqssdvfiarsHHGSVSKEQRA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 332 DAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSGHSVGGTPKGRLFPTSRDDLVECAALLDS 411
Cdd:PRK09751 318 ITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAGHQVGGVSKGLFFPRTRRDLVDSAVIVEC 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 412 VRRGELDSLVLPRQPLDVLAQQIVAEVACQEWREDDLYRLVIRAEPYAGLERERFDEVLRMLAEGYHSrlGVRGAYLHR- 490
Cdd:PRK09751 398 MFAGRLENLTPPHNPLDVLAQQTVAAAAMDALQVDEWYSRVRRAAPWKDLPRRVFDATLDMLSGRYPS--GDFSAFRPKl 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 491 --DALNGLLRGRRGARLTALTSGGTIPDTGDYSVLLePQG------LLVGTVNEDFAVESLAGDVFQLGNTSYRIIRIEP 562
Cdd:PRK09751 476 vwNRETGILTARPGAQLLAVTSGGTIPDRGMYSVLL-PEGeeqagsRRVGELDEEMVYESRVNDIITLGATSWRIQQITR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 563 GRVRVEDAQGQPPNIPFWLGEAPGRSDELSASVARLRDTLDELLGEGQALPegrrlepaiAWLGatlglDDGAARQIVEY 642
Cdd:PRK09751 555 DQVIVTPAPGRSARLPFWRGEGNGRPAELGEMIGDFLHLLADGAFFSGTIP---------PWLA-----EENTIANIQGL 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 643 LARARQALGGLPGSRRLVLERFFDESGGMQLIIHSPHGSRLNRAWGLALRKRFCRSFNFELQAAATEDAIILSL-STSHS 721
Cdd:PRK09751 621 IDEQRNATGIVPGSRHLVLERCRDEIGDWRIILHSPYGRRVHEPWALAIAGRIHALWGADASVVASDDGIVARIpDTDGK 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 722 FPLDEVWRYlHSASAEHLLVQAVLDAPLFGVRWRWNLTTSLGLPRYAGGRKVPPQLLRMKSEDLLASVfpdqvacleniv 801
Cdd:PRK09751 701 LPDAAIFLF-EPEKLLQIVREAVGSSALFAARFRECAARALLMPGRTPGHRTPLWQQRLRASQLLEIA------------ 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 802 geREVPDHPLVAQTLDDCLHEAMDCEGWLALLRDMESGAVDLLARDLPAPSALAAEIL--TARPYAYLDDAPLEERRTQ- 878
Cdd:PRK09751 768 --QGYPDFPVILETLRECLQDVYDLPALERLMRRLNGGEIQISDVTTTTPSPFATSLLfgYVAEFMYQSDAPLAERRASv 845
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 879 -AVQNRRWSDPESADDLGA-LDLEAIEAV-----RGEAWPEASNADEMHEALNSLGFLT-----------SGEAEAnpgw 940
Cdd:PRK09751 846 lSLDSELLRNLLGQVDPGElLDPQVIRQVeeelqRLAPGRRAKGEEGLFDLLRELGPMTvedlaqrhtgsSEEVAS---- 921
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 941 geWLAQLSEQRRAGRLDCAGSTLWLAAE---RLPAMRLVHPAAKVPDAFQAPRGYPPPDsaeaATVELTRARlggfGPRT 1017
Cdd:PRK09751 922 --YLENLLAVKRIFPAMISGQERLACMDdaaRLRDALGVRLPESLPEIYLHRVSYPLRD----LFLRYLRAH----ALVT 991
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 1018 AGQLAADLGIGLADQQYALAALEREGYVLRgrfspgATEEEWCERHLLARIHRYTVKRLRREIEPVERADFMRFLFDWQR 1097
Cdd:PRK09751 992 AEQLAHEFSLGIAIVEEQLQQLREQGLVMN------LQQDIWVSDEVFRRLRLRSLQAAREATRPVAATTYARLLLERQG 1065
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 1098 LAPGTRGR-------------GAESLATVVEQLEGFQAAAAAWESELLAARVADYASHWLDQLCRSGRIVWarlAGRSKA 1164
Cdd:PRK09751 1066 VLPATDGSpalfastspgvyeGVDGVMRVIEQLAGVGLPASLWESQILPARVRDYSPEMLDELLATGAVIW---SGQKKL 1142
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 1165 AGgplrSAPIVLLPRRELGLWSVLQRDAPEPELSPRAARVLEVLREQGASFFDELSQDA------HLLRSELENALGELV 1238
Cdd:PRK09751 1143 GE----DDGLVALHLQEYAAESFTPAEADQANRSALQQAIVAVLADGGAWFAQQISQRIrdkigeSVDLSALQEALWALV 1218
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 1239 SVGRVNADSFAGLRTLL----MPADKRSRQERRSRGLPGGMQD------------AGRWAPLRRAKAEEAGQRLPaevle 1302
Cdd:PRK09751 1219 WQGVITSDIWAPLRALTrsssNARTSTRRSHRARRGRPVYAQPvsprvsyntpnlAGRWSLLQVEPLNDTERMLA----- 1293
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 1303 hVARTLLRRYGVVAWRLLEREaDWLPPWRELLRVYHRLEARGEIRGGRFIAGLAGEQFALAEAVGLLREV---RKRPPDG 1379
Cdd:PRK09751 1294 -LAENMLDRYGIISRQAVIAE-NIPGGFPSMQTLCRSMEDSGRIMRGRFVEGLGGAQFAERLTIDRLRDLatqATQTRHY 1371
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 1380 AMLVVSAVDPLNLVGGLLP-----GERVPAVTGNRLLYRDGAPLAA-LVAGKVRMLAEVDGETAQQIRAL 1443
Cdd:PRK09751 1372 TPVALSANDPANVWGNLLPwpahpATLVPTRRAGALVVVSGGKLLLyLAQGGKKMLVWQEKEELLAPEVF 1441
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
23-875 |
2.19e-129 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 420.81 E-value: 2.19e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 23 PVVRQWFERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALvvegLAAGGELADATQVVYVSPLKALS 102
Cdd:TIGR04121 1 SPFEAWFAARGWTPRPFQLEMWAAALEGRSGLLIAPTGSGKTLAGFLPSLIDL----AGPEAPKEKGLHTLYITPLRALA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 103 NDIRINLEQPLAGireelarLGLPdvdIRSAVRTGDTPQVERGAMRKRPPHILVTTPESLYILLGSESGRQMLAGVRSVI 182
Cdd:TIGR04121 77 VDIARNLQAPIEE-------LGLP---IRVETRTGDTSSSERARQRKKPPDILLTTPESLALLLSYPDAARLFKDLRCVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 183 VDEIHALAGSKRGSHLALSLERLQALCPRpLLRIGLSATQKPIEKVARFLVGasgnPRDPACRIVDVGYTRPRDLGIEVP 262
Cdd:TIGR04121 147 VDEWHELAGSKRGDQLELALARLRRLAPG-LRRWGLSATIGNLEEARRVLLG----VGGAPAVLVRGKLPKAIEVISLLP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 263 PV----------ALEAVmsndtwELVYDRLAhlagEHRTTLVFVNTRRMAERVTRFL----AERLGsrQVAAHHGSLAKE 328
Cdd:TIGR04121 222 ESeerfpwaghlGLRAL------PEVYAEID----QARTTLVFTNTRSQAELWFQALweanPEFAL--PIALHHGSLDRE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 329 LRLDAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSGHSVGGTPKGRLFPTSRDDLVECAAL 408
Cdd:TIGR04121 290 QRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPVDLVIQIGSPKGVARLLQRAGRSNHRPGEPSRALLVPTNRLELLECAAA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 409 LDSVRRGELDSLVLPRQPLDVLAQQIVAeVACQE-WREDDLYRLVIRAEPYAGLERERFDEVLRMLAEGYHSrlgvRGAY 487
Cdd:TIGR04121 370 REAVAAGAVEGRPPPPGPLDVLAQHLLT-LACGGgFDPDELFAEVRSTAPYADLTREEFDWVLDFVATGGYA----LRAY 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 488 -----LHRDAlNGLLR--GRRGARLTALtSGGTIPDTGDYSVLLEPQGLLvGTVNEDFAVESLAGDVFQLGNTSYRIIRI 560
Cdd:TIGR04121 445 dryrkVVRDE-DGRYRvtDPRIARRHRL-NIGTIVSDAMLKVRLRGGGVL-GEIEEYFISRLKPGDTFLFAGRVLEFVRI 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 561 EPGRVRVEDAQGQPPNIPFWLGeapGR---SDELSasvARLRDTLDElLGEGQALPEGRRLEPaiaWLgatlglddgaAR 637
Cdd:TIGR04121 522 RDMTAYVRRAKGKDPKVPSWAG---GRmplSTQLA---HRVREMLAD-AAQWPSLPELRAVRP---WL----------EL 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 638 QiveylararQALGGLPGSRRLVLERfFDESGGMQLIIHSPHGSRLNRAWGLALRKRFCR----SFNFelqaAATEDAii 713
Cdd:TIGR04121 582 Q---------QRRSALPGADELLVET-FPTREGHHLFVYPFEGRLVHQGLGMLLARRLERlgpiPFSF----AANDYG-- 645
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 714 LSLSTSHSFPLDEV-WRYLHsaSAEHL---LVQAVLDAPLFGVRWRwNLTTSLGL--PRYAGGRKVPPQLlrMKSEDLLA 787
Cdd:TIGR04121 646 FELLSAQPVDDEEAlLDDLF--SPDMLgddLEAWLNASELAKRRFR-EIAVIAGLveQGYPGKRKSGRQV--QASSDLIY 720
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 788 SVFpdqvaclenivgEREVPDHPLVAQTLDDCLHEAMDCEGWLALLRDMESGAVDLLArdLPAPSALAAEILTARPYAYL 867
Cdd:TIGR04121 721 DVL------------RKHEPDHLLLRQARAEVLEGQLDLGRLGDALERIRGSRIVHKA--LDRPTPLAFPLLVERGRERV 786
|
....*...
gi 15598468 868 DDAPLEER 875
Cdd:TIGR04121 787 SGEKLDDR 794
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
50-232 |
1.85e-67 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from 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: 350680 [Multi-domain] Cd Length: 166 Bit Score: 224.38 E-value: 1.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 50 GLSTLVAAPTGSGKTLTAFLAAIDALVVEGLaaggelaDATQVVYVSPLKALSNDIRINLEQPLAGIreelarlglpDVD 129
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPE-------KGVQVLYISPLKALINDQERRLEEPLDEI----------DLE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 130 IRSAVRTGDTPQVERGAMRKRPPHILVTTPESLYILLGSESGRQMLAGVRSVIVDEIHALAGSKRGSHLALSLERLQALC 209
Cdd:cd17922 64 IPVAVRHGDTSQSEKAKQLKNPPGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHALLGSKRGVQLELLLERLRKLT 143
|
170 180
....*....|....*....|...
gi 15598468 210 PRPLLRIGLSATQKPIEKVARFL 232
Cdd:cd17922 144 GRPLRRIGLSATLGNLEEAAAFL 166
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
8-383 |
1.72e-56 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 210.85 E-value: 1.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 8 ARRAEPAPRPlAEFHPVVRQWFERH-FAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALVveglaaggEL 86
Cdd:COG1205 29 AREARYAPWP-DWLPPELRAALKKRgIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALL--------ED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 87 ADATqVVYVSPLKALSNDirinleQpLAGIREELARLGLpdvDIRSAVRTGDTPQVERGAMRKRPpHILVTTPESLY--I 164
Cdd:COG1205 100 PGAT-ALYLYPTKALARD------Q-LRRLRELAEALGL---GVRVATYDGDTPPEERRWIREHP-DIVLTNPDMLHygL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 165 LLGSESGRQMLAGVRSVIVDEIHALAGSkRGSHLALSLERLQALCPR----PLLrIGLSAT-QKPIEKVARF------LV 233
Cdd:COG1205 168 LPHHTRWARFFRNLRYVVIDEAHTYRGV-FGSHVANVLRRLRRICRHygsdPQF-ILASATiGNPAEHAERLtgrpvtVV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 234 GASGNPRdpacrivdvgytRPRDLGIEVPPVaLEAVMSNDTWELVYDRLAHLAGEHRTTLVFVNTRRMAERVTRFLAERL 313
Cdd:COG1205 246 DEDGSPR------------GERTFVLWNPPL-VDDGIRRSALAEAARLLADLVREGLRTLVFTRSRRGAELLARYARRAL 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598468 314 GSR----QVAAHHGSLAKELRLDAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSG 383
Cdd:COG1205 313 REPdladRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAG 386
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
253-397 |
4.52e-52 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family 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: 350183 [Multi-domain] Cd Length: 150 Bit Score: 179.77 E-value: 4.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 253 RPRDLGIEVPPVALEAVMSNDTWELVYDRLAHLAGEHRTTLVFVNTRRMAERVTRFLAERLGSR----QVAAHHGSLAKE 328
Cdd:cd18796 2 KKLDIKVILPVAPEIFPWAGESGADAYAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRvppdFIALHHGSLSRE 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598468 329 LRLDAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSGHSVGGTPKGRLFPT 397
Cdd:cd18796 82 LREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPGAASKGRLVPT 150
|
|
| DEAD_assoc |
pfam08494 |
DEAD/H associated; This domain is found in ATP-dependent helicases as well as a number of ... |
653-855 |
2.51e-45 |
|
DEAD/H associated; This domain is found in ATP-dependent helicases as well as a number of hypothetical proteins together with the helicase conserved C-terminal domain (pfam00270) and the pfam00271 domain.
Pssm-ID: 430030 [Multi-domain] Cd Length: 182 Bit Score: 161.86 E-value: 2.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 653 LPGSRRLVLERFFDESggMQLIIHSPHGSRLNRAWGLALRKRFCRSFNFELQAAATEDAIILSLSTSHSFPLDEVWRYLh 732
Cdd:pfam08494 1 LPTDRTLLVERFRDEL--WHLVVHSFFGRRVNEALGRLLAYRLSRRLGISVGVAATDYGFVLLSPLEERLPLLVDPDNL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 733 sasaEHLLVQAVLDAPLFGVRWRWNLTTSLGLPRYAGGRKVPPQLLRMKSEDLLASVfpdqvaclenivgeREVPDHPLV 812
Cdd:pfam08494 78 ----EDDLEAALNGSELFKRRFREVAARAGLLLRRYPGKRKPLWQQRLSSDLLLDVL--------------REYEDFPLL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598468 813 AQTLDDCLHEAMDCEGWLALLRDMESGAVDLLARDLPAPSALA 855
Cdd:pfam08494 140 REAYRECLEDVLDLERLRELLERIRSGEIRVVEVETPRPSPFA 182
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
37-231 |
3.02e-33 |
|
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: 126.59 E-value: 3.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 37 TPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALvveglaagGELADATQVVYVSPLKALSNDIRINLEQPLAGI 116
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL--------DKLDNGPQALVLAPTRELAEQIYEELKKLGKGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 117 REELarlglpdvdirSAVRTGDTPQVERGAMRKrpPHILVTTPESLYILLGSesgRQMLAGVRSVIVDEIHALAGSKRGS 196
Cdd:pfam00270 73 GLKV-----------ASLLGGDSRKEQLEKLKG--PDILVGTPGRLLDLLQE---RKLLKNLKLLVLDEAHRLLDMGFGP 136
|
170 180 190
....*....|....*....|....*....|....*
gi 15598468 197 HLALSLERLqalcPRPLLRIGLSATqkPIEKVARF 231
Cdd:pfam00270 137 DLEEILRRL----PKKRQILLLSAT--LPRNLEDL 165
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
37-351 |
1.14e-32 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 134.64 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 37 TPAQVEAWPA-IREGLSTLVAAPTGSGKTLTAFLAAIDALvveglAAGGEladatqVVYVSPLKALSNDIRinleqplag 115
Cdd:COG1204 24 YPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKAL-----LNGGK------ALYIVPLRALASEKY--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 116 irEELARLgLPDVDIRSAVRTGDTPQVERGAMRKRpphILVTTPESLYILLGSESGrqMLAGVRSVIVDEIHALAGSKRG 195
Cdd:COG1204 84 --REFKRD-FEELGIKVGVSTGDYDSDDEWLGRYD---ILVATPEKLDSLLRNGPS--WLRDVDLVVVDEAHLIDDESRG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 196 SHLALSLERLQALCPRPLLrIGLSATQKPIEKVARFLvgasgnprdpACRIVDVGYtRPRDLGIEVppVALEAVMSNDTW 275
Cdd:COG1204 156 PTLEVLLARLRRLNPEAQI-VALSATIGNAEEIAEWL----------DAELVKSDW-RPVPLNEGV--LYDGVLRFDDGS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 276 ELVYDRLAHLA----GEHRTTLVFVNTRRMAERVTRFLAERLGSRQ---------------------------------- 317
Cdd:COG1204 222 RRSKDPTLALAldllEEGGQVLVFVSSRRDAESLAKKLADELKRRLtpeereeleelaeellevseethtnekladclek 301
|
330 340 350
....*....|....*....|....*....|....*
gi 15598468 318 -VAAHHGSLAKELRLDAEQRLKAGQLKVLVATASL 351
Cdd:COG1204 302 gVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTL 336
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
28-232 |
2.13e-30 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 119.52 E-value: 2.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 28 WFERHFAAPTPAQVEAWPAIREGL-STLVAAPTGSGKTLTAFLAAIDALvveglaaggELADATQVVYVSPLKALSNDIR 106
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEAL---------KRGKGGRVLVLVPTRELAEQWA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 107 inleqplagirEELARLGLPDVDIRSAVRTGDTPQVERGAMRKRPPHILVTTPESLYILLgsESGRQMLAGVRSVIVDEI 186
Cdd:smart00487 72 -----------EELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLL--ENDKLSLSNVDLVILDEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598468 187 HALAGSKRGSHLALSLERLqalcPRPLLRIGLSATqkPIEKVARFL 232
Cdd:smart00487 139 HRLLDGGFGDQLEKLLKLL----PKNVQLLLLSAT--PPEEIENLL 178
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
40-221 |
3.60e-30 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 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: 350681 [Multi-domain] Cd Length: 182 Bit Score: 118.46 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 40 QVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALvveglaaggeLADA-TQVVYVSPLKALSNDirinleQpLAGIRE 118
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL----------LRDPgSRALYLYPTKALAQD------Q-LRSLRE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 119 ELARLGLpdvDIRSAVRTGDTPQVERGAMRKRPPHILVTTPESL-YILL-GSESGRQMLAGVRSVIVDEIHALAGSKrGS 196
Cdd:cd17923 68 LLEQLGL---GIRVATYDGDTPREERRAIIRNPPRILLTNPDMLhYALLpHHDRWARFLRNLRYVVLDEAHTYRGVF-GS 143
|
170 180
....*....|....*....|....*...
gi 15598468 197 HLALSLERLQALCPRPLLR---IGLSAT 221
Cdd:cd17923 144 HVALLLRRLRRLCRRYGADpqfILTSAT 171
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
23-383 |
1.42e-23 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 105.23 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 23 PVVRQWFERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLtAFLAAIdalvVEGLAAGGelADATQVVYVSPLKALS 102
Cdd:COG0513 12 PLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTA-AFLLPL----LQRLDPSR--PRAPQALILAPTRELA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 103 ndirinlEQplagIREELARLGlPDVDIRSAVRTGDTP-QVERGAMrKRPPHILVTTPESLYILLgsESGRQMLAGVRSV 181
Cdd:COG0513 85 -------LQ----VAEELRKLA-KYLGLRVATVYGGVSiGRQIRAL-KRGVDIVVATPGRLLDLI--ERGALDLSGVETL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 182 IVDE---------IHAlagskrgshlalsLERLQALCPRPLLRIGLSATQ-KPIEKVA-RFLvgasgnpRDPAcrIVDVg 250
Cdd:COG0513 150 VLDEadrmldmgfIED-------------IERILKLLPKERQTLLFSATMpPEIRKLAkRYL-------KNPV--RIEV- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 251 yTRPrdlGIEVPPVALEAVMSNDtwELVYDRLAHLAGEHRT--TLVFVNTRRMAERVTRFLAERLGSrqVAAHHGSLAKE 328
Cdd:COG0513 207 -APE---NATAETIEQRYYLVDK--RDKLELLRRLLRDEDPerAIVFCNTKRGADRLAEKLQKRGIS--AAALHGDLSQG 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598468 329 LRLDAEQRLKAGQLKVLVAT--ASleLGIDIGDVELVCQLSSPRSIAAFLQRVGRSG 383
Cdd:COG0513 279 QRERALDAFRNGKIRVLVATdvAA--RGIDIDDVSHVINYDLPEDPEDYVHRIGRTG 333
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
37-232 |
5.05e-23 |
|
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: 97.72 E-value: 5.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 37 TPAQVEAW-PAIREGLSTLVAAPTGSGKTLTAFLAAIDALVVEGlaaggeladaTQVVYVSPLKALSNdirinleQPLAG 115
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSG----------GKAVYIAPTRALVN-------QKEAD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 116 IREELARLGLPDVDIrsavrTGDtPQVERGAMRKrpPHILVTTPESLYILLGSESGRQMLAgVRSVIVDEIHALAGSKRG 195
Cdd:cd17921 66 LRERFGPLGKNVGLL-----TGD-PSVNKLLLAE--ADILVATPEKLDLLLRNGGERLIQD-VRLVVVDEAHLIGDGERG 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598468 196 SHLALSLERLQALCPRPLLrIGLSATQKPIEKVARFL 232
Cdd:cd17921 137 VVLELLLSRLLRINKNARF-VGLSATLPNAEDLAEWL 172
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
282-383 |
3.03e-21 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family 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: 350184 [Multi-domain] Cd Length: 146 Bit Score: 91.55 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 282 LAHLAGEHRTTLVFVNTRRMAERVTRFLAERLGSRQ-----VAAHHGSLAKELRLDAEQRLKAGQLKVLVATASLELGID 356
Cdd:cd18797 28 FADLVRAGVKTIVFCRSRKLAELLLRYLKARLVEEGplaskVASYRAGYLAEDRREIEAELFNGELLGVVATNALELGID 107
|
90 100
....*....|....*....|....*..
gi 15598468 357 IGDVELVCQLSSPRSIAAFLQRVGRSG 383
Cdd:cd18797 108 IGGLDAVVLAGYPGSLASLWQQAGRAG 134
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
53-221 |
5.39e-21 |
|
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: 90.93 E-value: 5.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 53 TLVAAPTGSGKTLTAFLAAIDALVVEGLaaggeladatQVVYVSPLKALSNDirinleqplagIREELARLGLPDVDIrs 132
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLLLKKGK----------KVLVLVPTKALALQ-----------TAERLRELFGPGIRV-- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 133 AVRTGDTPQVERGAMRKRPPHILVTTPESLYILLGSEsGRQMLAGVRSVIVDEIHALAGSKRGSHLALSLERLQALcpRP 212
Cdd:cd00046 61 AVLVGGSSAEEREKNKLGDADIIIATPDMLLNLLLRE-DRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGL--KN 137
|
....*....
gi 15598468 213 LLRIGLSAT 221
Cdd:cd00046 138 AQVILLSAT 146
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
292-383 |
1.79e-20 |
|
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: 88.04 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 292 TLVFVNTRRMAErvTRFLAERLGSRqVAAHHGSLAKELRLDAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRS 371
Cdd:pfam00271 18 VLIFSQTKKTLE--AELLLEKEGIK-VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINYDLPWN 94
|
90
....*....|..
gi 15598468 372 IAAFLQRVGRSG 383
Cdd:pfam00271 95 PASYIQRIGRAG 106
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
38-381 |
3.32e-20 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 96.63 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 38 PAQVEAWPAIREGLST-----LVAAPTGSGKTLTAfLAAIDalvveglaaggELADATQVVYVSPLKALsndirinLEQp 112
Cdd:COG1061 83 PYQQEALEALLAALERgggrgLVVAPTGTGKTVLA-LALAA-----------ELLRGKRVLVLVPRREL-------LEQ- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 113 lagIREELARLgLPDVDIRsavrtgdtpqverGAMRKRPPHILVTTPESLYILLgseSGRQMLAGVRSVIVDEIHaLAGS 192
Cdd:COG1061 143 ---WAEELRRF-LGDPLAG-------------GGKKDSDAPITVATYQSLARRA---HLDELGDRFGLVIIDEAH-HAGA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 193 KRgshLALSLERLQALCprpllRIGLSAT-----QKPIEkvARFLVG-----------ASGNPRDPACRIVDVGYTRPRD 256
Cdd:COG1061 202 PS---YRRILEAFPAAY-----RLGLTATpfrsdGREIL--LFLFDGivyeyslkeaiEDGYLAPPEYYGIRVDLTDERA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 257 LGIEVPPVALEAVMSNDtwELVYDRLAHLAGEH---RTTLVFVNTRRMAERVTRFLAERlgSRQVAAHHGSLAKELRLDA 333
Cdd:COG1061 272 EYDALSERLREALAADA--ERKDKILRELLREHpddRKTLVFCSSVDHAEALAELLNEA--GIRAAVVTGDTPKKEREEI 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15598468 334 EQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGR 381
Cdd:COG1061 348 LEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGR 395
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
24-185 |
6.47e-19 |
|
DEAD-box helicase domain of 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 86.34 E-value: 6.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 24 VVRQWFERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLtAF-LAAIDALvvegLAAGGELADATQVVYVSPLKALS 102
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTL-AFlLPILEKL----LPEPKKKGRGPQALVLAPTRELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 103 ndirinlEQplagIREELARLGlPDVDIRSAVRTGDTPQVERGAMRKRPPHILVTTPESLYILLgsESGRQMLAGVRSVI 182
Cdd:cd00268 76 -------MQ----IAEVARKLG-KGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLI--ERGKLDLSNVKYLV 141
|
...
gi 15598468 183 VDE 185
Cdd:cd00268 142 LDE 144
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
38-383 |
1.72e-18 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 90.59 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 38 PAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAidaLVVEGLAaggeladatqVVyVSPLKALSNDirinleQPlagir 117
Cdd:COG0514 20 PGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPA---LLLPGLT----------LV-VSPLIALMKD------QV----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 118 EELARLGLPDVDIRSAVRTGDTPQVERGAMRKRPpHILVTTPESLyillGSESGRQMLAGVR--SVIVDEIHALagSK-- 193
Cdd:COG0514 75 DALRAAGIRAAFLNSSLSAEERREVLRALRAGEL-KLLYVAPERL----LNPRFLELLRRLKisLFAIDEAHCI--SQwg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 194 ---RGSHLALSlERLQALCPRPllRIGLSATQKP--IEKVARFLvgasgNPRDPacRIVDVGYTRPrDLGIEVPPVALEA 268
Cdd:COG0514 148 hdfRPDYRRLG-ELRERLPNVP--VLALTATATPrvRADIAEQL-----GLEDP--RVFVGSFDRP-NLRLEVVPKPPDD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 269 VmsndtwelvYDRLAHLAGEHR--TTLVFVNTRRMAERVTRFLAERlgSRQVAAHHGSLAKELRLDAEQRLKAGQLKVLV 346
Cdd:COG0514 217 K---------LAQLLDFLKEHPggSGIVYCLSRKKVEELAEWLREA--GIRAAAYHAGLDAEEREANQDRFLRDEVDVIV 285
|
330 340 350
....*....|....*....|....*....|....*..
gi 15598468 347 ATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSG 383
Cdd:COG0514 286 ATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAG 322
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
30-357 |
7.83e-18 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 89.49 E-value: 7.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 30 ERHFAAPTPAQVEAWPA-IREGLSTLVAAPTGSGKTLTAFLAAIDALVVEGLAAggeladatqvVYVSPLKALSNDirin 108
Cdd:PRK00254 18 ERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLREGGKA----------VYLVPLKALAEE---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 109 leqplaGIRE--ELARLGLpdvdiRSAVRTGDTPQVERGAMRKrppHILVTTPESLYILLgsESGRQMLAGVRSVIVDEI 186
Cdd:PRK00254 84 ------KYREfkDWEKLGL-----RVAMTTGDYDSTDEWLGKY---DIIIATAEKFDSLL--RHGSSWIKDVKLVVADEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 187 HALAGSKRGSHLALSLERLqalcprpLLR---IGLSATQKPIEKVARFL----VGASGNPRDPACRIVDVGYTRPRDLGI 259
Cdd:PRK00254 148 HLIGSYDRGATLEMILTHM-------LGRaqiLGLSATVGNAEELAEWLnaelVVSDWRPVKLRKGVFYQGFLFWEDGKI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 260 EVPPVALEavmsndtwELVYDRLAHLAGehrtTLVFVNTRRMAER--------VTRFL-----------AERLGSRQ--- 317
Cdd:PRK00254 221 ERFPNSWE--------SLVYDAVKKGKG----ALVFVNTRRSAEKealelakkIKRFLtkpelralkelADSLEENPtne 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15598468 318 ---------VAAHHGSLAKELRLDAEQRLKAGQLKVLVATASLELGIDI 357
Cdd:PRK00254 289 klkkalrggVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINL 337
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
38-232 |
2.05e-17 |
|
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: 81.61 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 38 PAQVEAwpaIREGL----STLVAAPTGSGKTLTAFLAAIDALVVEGLAaggeladatqvVYVSPLKALSNDirinleqpl 113
Cdd:cd18028 4 PPQAEA---VRAGLlkgeNLLISIPTASGKTLIAEMAMVNTLLEGGKA-----------LYLVPLRALASE--------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 114 agIREELARLGLPDVdiRSAVRTGDTPQVERGAMRKrppHILVTTPESLYILLgsESGRQMLAGVRSVIVDEIHALAGSK 193
Cdd:cd18028 61 --KYEEFKKLEEIGL--KVGISTGDYDEDDEWLGDY---DIIVATYEKFDSLL--RHSPSWLRDVGVVVVDEIHLISDEE 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 15598468 194 RGSHLALSLERLQALCPRPLLrIGLSATQKPIEKVARFL 232
Cdd:cd18028 132 RGPTLESIVARLRRLNPNTQI-IGLSATIGNPDELAEWL 169
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
307-383 |
1.37e-16 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 75.71 E-value: 1.37e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598468 307 RFLAERLGSRQ--VAAHHGSLAKELRLDAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSG 383
Cdd:smart00490 1 EELAELLKELGikVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
292-383 |
2.50e-16 |
|
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: 76.78 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 292 TLVFVNTRRMAERVTRFLaERLGSRqVAAHHGSLAKELRLDAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRS 371
Cdd:cd18787 30 AIIFVNTKKRVDRLAELL-EELGIK-VAALHGDLSQEERERALKKFRSGKVRVLVATDVAARGLDIPGVDHVINYDLPRD 107
|
90
....*....|..
gi 15598468 372 IAAFLQRVGRSG 383
Cdd:cd18787 108 AEDYVHRIGRTG 119
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
289-409 |
1.40e-15 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. 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: 350181 [Multi-domain] Cd Length: 134 Bit Score: 74.94 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 289 HRTTLVFVNTRRMAERVTRFLAERLGSRqvAAHHGSLAKELRLDAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSS 368
Cdd:cd18794 30 GGSGIIYCLSRKECEQVAARLQSKGISA--AAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSL 107
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15598468 369 PRSIAAFLQRVGRSGhsvggtpkgrlfptsRDDLVECAALL 409
Cdd:cd18794 108 PKSMESYYQESGRAG---------------RDGLPSECILF 133
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
57-381 |
1.67e-15 |
|
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: 81.28 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 57 APTGSGKTLTAFLAAidalvveglaagGELADATQ---VVYVSPLKALSNDIRinleqplagirEELARLGLPDV----- 128
Cdd:COG1203 154 APTGGGKTEAALLFA------------LRLAAKHGgrrIIYALPFTSIINQTY-----------DRLRDLFGEDVllhhs 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 129 ---DIRSAVRTGDTPQVERGAMRKR----PphILVTTP----ESLYILLGSESgRQMLAGVRSVIV-DEIHALaGSKRGS 196
Cdd:COG1203 211 ladLDLLEEEEEYESEARWLKLLKElwdaP--VVVTTIdqlfESLFSNRKGQE-RRLHNLANSVIIlDEVQAY-PPYMLA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 197 HLALSLERLQALCPRPLLrigLSATQKPIEKVARFlvgasgNPRDPACRIVDVGYTRPRDLGIEVPPVALEAVMSNDTWE 276
Cdd:COG1203 287 LLLRLLEWLKNLGGSVIL---MTATLPPLLREELL------EAYELIPDEPEELPEYFRAFVRKRVELKEGPLSDEELAE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 277 LVYDRLAhlagEHRTTLVFVNTRRMAERVTRFLAERLGSRQVAAHHGSLAKELRLDAEQ----RLKAGQLKVLVATASLE 352
Cdd:COG1203 358 LILEALH----KGKSVLVIVNTVKDAQELYEALKEKLPDEEVYLLHSRFCPADRSEIEKeikeRLERGKPCILVSTQVVE 433
|
330 340 350
....*....|....*....|....*....|
gi 15598468 353 LGIDIgDVELVC-QLSSPRSIAaflQRVGR 381
Cdd:COG1203 434 AGVDI-DFDVVIrDLAPLDSLI---QRAGR 459
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
54-232 |
7.80e-13 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350778 [Multi-domain] Cd Length: 199 Bit Score: 69.00 E-value: 7.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 54 LVAAPTGSGKTLTAFLAAIDALvVEGLAAGGELA-DATQVVYVSPLKALSNDIRINLEQplagireELARLGLpdvdirs 132
Cdd:cd18020 21 LICAPTGAGKTNIAMLTILHEI-RQHVNQGGVIKkDDFKIVYIAPMKALAAEMVEKFSK-------RLAPLGI------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 133 AVR--TGDTpQVERGAMRKrpPHILVTTPESLYILLGSESGRQMLAG-VRSVIVDEIHALAGsKRGSHLALSLERLQALC 209
Cdd:cd18020 86 KVKelTGDM-QLTKKEIAE--TQIIVTTPEKWDVVTRKSSGDVALSQlVRLLIIDEVHLLHD-DRGPVIESLVARTLRQV 161
|
170 180
....*....|....*....|....*.
gi 15598468 210 PR--PLLRI-GLSATQKPIEKVARFL 232
Cdd:cd18020 162 EStqSMIRIvGLSATLPNYLDVADFL 187
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
40-232 |
1.77e-12 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 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: 350781 [Multi-domain] Cd Length: 206 Bit Score: 68.15 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 40 QVEAWPAIREG-LSTLVAAPTGSGKTlTAFLAAIDALVVEglaAGGELADATQVVYVSPLKALSNdirinleQPLAGIRE 118
Cdd:cd18023 6 QSEVFPDLLYSdKNFVVSAPTGSGKT-VLFELAILRLLKE---RNPLPWGNRKVVYIAPIKALCS-------EKYDDWKE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 119 ELARLGLPDVDIrsavrTGDTPQVERGAMRKrpPHILVTTPESLYIL--LGSESGRqMLAGVRSVIVDEIHALaGSKRGS 196
Cdd:cd18023 75 KFGPLGLSCAEL-----TGDTEMDDTFEIQD--ADIILTTPEKWDSMtrRWRDNGN-LVQLVALVLIDEVHII-KENRGA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598468 197 HLALSLERLQALCPRPLLR---------IGLSATQKPIEKVARFL 232
Cdd:cd18023 146 TLEVVVSRMKTLSSSSELRgstvrpmrfVAVSATIPNIEDLAEWL 190
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
52-243 |
2.05e-12 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 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: 350780 [Multi-domain] Cd Length: 189 Bit Score: 67.40 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 52 STLVAAPTGSGKTLTAFLAAIDALvveglaaggELADATQVVYVSPLKALS----NDIRINLEQPLAGIREELarlglpd 127
Cdd:cd18022 19 NVLLGAPTGSGKTIAAELAMFRAF---------NKYPGSKVVYIAPLKALVrervDDWKKRFEEKLGKKVVEL------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 128 vdirsavrTGD-TPQVErgAMRKrpPHILVTTPESLYILLGSESGRQMLAGVRSVIVDEIHALaGSKRGSHLALSLERLQ 206
Cdd:cd18022 83 --------TGDvTPDMK--ALAD--ADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLL-GSDRGPVLEVIVSRMN 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598468 207 ALCprpllriglSATQKPIEKVArfLVGASGNPRDPA 243
Cdd:cd18022 150 YIS---------SQTEKPVRLVG--LSTALANAGDLA 175
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
40-383 |
2.54e-12 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 71.45 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 40 QVEAWPAIREGLSTLVAAPTGSGKTLTAFLAaidalVVEGLAAGgeladaTQVVYVSPLKALSndirinLEQplagiREE 119
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIAYSA-----IYETFLAG------LKSIYIVPLRSLA------MEK-----YEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 120 LARLglPDVDIRSAVRTGD---TPQvergaMRKRPPHILVTTPESLYILlgsESGRQMLAGVRSVIVDEIHALAGSKRGS 196
Cdd:PRK01172 85 LSRL--RSLGMRVKISIGDyddPPD-----FIKRYDVVILTSEKADSLI---HHDPYIINDVGLIVADEIHIIGDEDRGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 197 HLALSLERLQALCPRPLLrIGLSATQKPIEKVARFLvgasgnprdPACRIVDVGYTRPRDLGIevppvaleavmsndtwe 276
Cdd:PRK01172 155 TLETVLSSARYVNPDARI-LALSATVSNANELAQWL---------NASLIKSNFRPVPLKLGI----------------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 277 LVYDRLaHLAGEHRT-----------------TLVFVNTRRMAERVTRFLAERLGS-----------------------R 316
Cdd:PRK01172 208 LYRKRL-ILDGYERSqvdinsliketvndggqVLVFVSSRKNAEDYAEMLIQHFPEfndfkvssennnvyddslnemlpH 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598468 317 QVAAHHGSLAKELRLDAEQRLKAGQLKVLVATASLELGID-------IGDVELVCQL-SSPRSIAAFLQRVGRSG 383
Cdd:PRK01172 287 GVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNlparlviVRDITRYGNGgIRYLSNMEIKQMIGRAG 361
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
13-355 |
2.86e-12 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 71.51 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 13 PAPRPLAEFHPVVRQWFERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAflaaiDALVVEGLAAGGeladatQV 92
Cdd:COG4581 3 LSPARADARLEALADFAEERGFELDPFQEEAILALEAGRSVLVAAPTGSGKTLVA-----EFAIFLALARGR------RS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 93 VYVSPLKALSNdirinleqplagirEELARLglpdVDIRSAVR----TGDTpQVERGAmrkrpPHILVTTpESLYILLGS 168
Cdd:COG4581 72 FYTAPIKALSN--------------QKFFDL----VERFGAENvgllTGDA-SVNPDA-----PIVVMTT-EILRNMLYR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 169 ESGRqmLAGVRSVIVDEIHALAGSKRGSHLALSLerlqALCPRPLLRIGLSATQKPIEKVARFLVGASGnprdpACRIVd 248
Cdd:COG4581 127 EGAD--LEDVGVVVMDEFHYLADPDRGWVWEEPI----IHLPARVQLVLLSATVGNAEEFAEWLTRVRG-----ETAVV- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 249 VGYTRP---------RDLGIEVPPVALEAVMSNDTWELVydrlAHLAGEHRT-TLVFVNTRRMA-ERVTRFLAERLGSRQ 317
Cdd:COG4581 195 VSEERPvplefhylvTPRLFPLFRVNPELLRPPSRHEVI----EELDRGGLLpAIVFIFSRRGCdEAAQQLLSARLTTKE 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598468 318 -------------------------------VAAHHGSLAKELRLDAEQRLKAGQLKVLVATASLELGI 355
Cdd:COG4581 271 eraeireaidefaedfsvlfgktlsrllrrgIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGI 339
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
54-232 |
3.33e-12 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350777 [Multi-domain] Cd Length: 214 Bit Score: 67.40 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 54 LVAAPTGSGKTLTAFLAAIDALVVEGLAAGGELADATQVVYVSPLKALSNDIRINLEQPLA--GIR-EELarlglpdvdi 130
Cdd:cd18019 37 LLCAPTGAGKTNVALLTILREIGKHRNPDGTINLDAFKIVYIAPMKALVQEMVGNFSKRLApyGITvAEL---------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 131 rsavrTGDTpQVERGAMRKrpPHILVTTPESLYILLGSESGRQMLAGVRSVIVDEIHALAGSkRGShlalSLERLQALCP 210
Cdd:cd18019 107 -----TGDQ-QLTKEQISE--TQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHDD-RGP----VLESIVARTI 173
|
170 180
....*....|....*....|....*....
gi 15598468 211 R-------PLLRIGLSATQKPIEKVARFL 232
Cdd:cd18019 174 RqieqtqeYVRLVGLSATLPNYEDVATFL 202
|
|
| DEXHc_DDX60 |
cd18025 |
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ... |
40-221 |
8.40e-12 |
|
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 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: 350783 [Multi-domain] Cd Length: 192 Bit Score: 65.85 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 40 QVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALvveglaaggELADATQVVYVSPLKALSNDIrinleqplagIREE 119
Cdd:cd18025 6 QRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVL---------RESDDGVVVYVAPTKALVNQV----------VAEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 120 LARLG---LPDVDIRSAVRTGDtpqvergaMRKRPP---HILVTTPESLYILLGSESGRQMLAGVRSVIVDEIHALAGSK 193
Cdd:cd18025 67 YARFSkkyPPSGKSLWGVFTRD--------YRHNNPmncQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSE 138
|
170 180
....*....|....*....|....*...
gi 15598468 194 RGshlaLSLERLQALCPRPLLriGLSAT 221
Cdd:cd18025 139 DG----AVWEQLLLLIPCPFL--ALSAT 160
|
|
| Cas3_I-D |
cd09710 |
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ... |
40-383 |
1.58e-10 |
|
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; 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; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D
Pssm-ID: 187841 [Multi-domain] Cd Length: 353 Bit Score: 64.51 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 40 QVEAWPAIREGLSTLV--AAPTGSGKTLTAFLAAIDalvvEGLAAggeladatqvVYVSPLKALSNDIRINLEqplaGIR 117
Cdd:cd09710 2 QVATFEALQSKDADIIfnTAPTGAGKTLAWLTPLLH----GENKA----------IALYPTNALIEDQTEAIK----EFV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 118 EELArlglPDVDIRSAVRTGDTPQVE----------------RGAMRKRPPHILVTTPESLYILL------GSESGRQML 175
Cdd:cd09710 64 DDAN----PRHQVKSLSASDITLWPNdknvgsskgeklynllRNDIGTSTPIILLTNPDIFVYLTrfayidRGDIAAGFY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 176 AGVRSVIVDEIHALAGSKRGSHLALSLERLQA---LCPRPLlrIGLSATQKP--IEKV--ARFlVGASGNPRDPAC-RIV 247
Cdd:cd09710 140 TKFSTVIFDEFHLYDAKQLVGLLFYLAYMQLIrffECRRKF--VFLSATPDPalILRLqnAKQ-AGVKIAPIDGEAgQFP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 248 DVGYTRPRDLGIE----VPPVALEAVMSND---TW-----ELVYDRLAHLAGEhRTTLVFvNTRRMAERVTRFLAERLGS 315
Cdd:cd09710 217 DNPELEQQLKNTSfrpvLPPVELELIPAPDfkeEWlaelaAEVIERFRQLPGE-RGAIIL-DSLDEVNRLSDLLQQQGLG 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598468 316 RQVAAHHGslakeLRLDAEqRLKAGQLKVLVATASLELGIDIGDVELvcqLSSPRSIAAFLQRVGRSG 383
Cdd:cd09710 295 DDIGRITG-----FAPKKD-RERAMQFDILLGTSTVDVGVDFKRDWL---IFSARDAAAFWQRLGRLG 353
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
33-383 |
1.59e-10 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 65.57 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 33 FAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALVVEGLAAGGelaDATQVVYVSPLKALSndirinlEQp 112
Cdd:PTZ00110 150 FTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYG---DGPIVLVLAPTRELA-------EQ- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 113 lagIREELARLGLpDVDIRSAVRTGDTPQVERGAMRKRPPHILVTTPESLYILLgsESGRQMLAGVRSVIVDE------- 185
Cdd:PTZ00110 219 ---IREQCNKFGA-SSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFL--ESNVTNLRRVTYLVLDEadrmldm 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 186 -----IHALAGSKRGSHLALSlerlqalcprpllrigLSAT-QKPIEKVARFLvgasgnprdpaCRIVDVgytrprdlGI 259
Cdd:PTZ00110 293 gfepqIRKIVSQIRPDRQTLM----------------WSATwPKEVQSLARDL-----------CKEEPV--------HV 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 260 EVPPVALEAVMSNDTWELVYDR----------LAHLAGEHRTTLVFVNTRRMAERVTRFLaeRLGSRQVAAHHGSLAKEL 329
Cdd:PTZ00110 338 NVGSLDLTACHNIKQEVFVVEEhekrgklkmlLQRIMRDGDKILIFVETKKGADFLTKEL--RLDGWPALCIHGDKKQEE 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15598468 330 RLDAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSG 383
Cdd:PTZ00110 416 RTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTG 469
|
|
| cas3_cyano |
TIGR03158 |
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short ... |
40-383 |
2.29e-10 |
|
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family is a CRISPR-associated (Cas) family strictly associated with the Cyano subtype of CRISPR/Cas locus, found in several species of Cyanobacteria and several archaeal species. It contains helicase motifs and appears to represent the Cas3 protein of the Cyano subtype of CRISPR/Cas system.
Pssm-ID: 274457 [Multi-domain] Cd Length: 357 Bit Score: 64.15 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 40 QVEAWPAIREGLSTLV--AAPTGSGKTLTAFLAAIDalvveglaagGELadatQVVYVSPLKALSNDIRINLEqplaGIR 117
Cdd:TIGR03158 2 QVATFEALQSKDADIIfnTAPTGAGKTLAWLTPLLH----------GEN----DTIALYPTNALIEDQTEAIK----EFV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 118 EELArlGLPDVDIRSAVRT---------GDTPQVERG---------AMRKRPPHILVTTPESLYILL------GSESGRQ 173
Cdd:TIGR03158 64 DVFK--PERDVNLLHVSKAtlkdikeyaNDKVGSSKGeklynllrnPIGTSTPIILLTNPDIFVYLTrfayidRGDIAAG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 174 MLAGVRSVIVDEIHALAGSKRGSHLALSLERLQA---LCPRPLlrIGLSATQKP---------------IEKVARFLVGA 235
Cdd:TIGR03158 142 FYTKFSTVIFDEFHLYDAKQLVGMLFLLAYMQLIrffECRRKF--VFLSATPDPalilrlqnakqagvkIAPIDGEKYQF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 236 SGNPrDPACRIVDVGYtRPRDLGIE---VPPVALEAVMSNDTWELVYDRLAHLAGEhRTTLVFvNTRRMAERVTRFLAER 312
Cdd:TIGR03158 220 PDNP-ELEADNKTQSF-RPVLPPVElelIPAPDFKEEELSELAEEVIERFRQLPGE-RGAIIL-DSLDEVNRLSDLLQQQ 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598468 313 LGSRQVAAHHGslakeLRLDAEqRLKAGQLKVLVATASLELGIDIGDVELvcqLSSPRSIAAFLQRVGRSG 383
Cdd:TIGR03158 296 GLGDDIGRITG-----FAPKKD-RERAMQFDILLGTSTVDVGVDFKRDWL---IFSARDAAAFWQRLGRLG 357
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
24-383 |
6.39e-10 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 62.92 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 24 VVRQWFERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLT---AFLAAIDALVVeglaaggeladATQVVYVSPLKA 100
Cdd:PTZ00424 39 LLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATfviAALQLIDYDLN-----------ACQALILAPTRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 101 LSNDIrinleQPLAgireelarLGLPD-VDIRSAVRTGDTPQVERGAMRKRPPHILVTTPESLYILLgsESGRQMLAGVR 179
Cdd:PTZ00424 108 LAQQI-----QKVV--------LALGDyLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMI--DKRHLRVDDLK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 180 SVIVDEIHALAGSKRGSHLALSLERLQalcprPLLRIGL-SAT--QKPIEKVARFLvgasgnpRDPAcRIVdvgyTRPRD 256
Cdd:PTZ00424 173 LFILDEADEMLSRGFKGQIYDVFKKLP-----PDVQVALfSATmpNEILELTTKFM-------RDPK-RIL----VKKDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 257 L---GIEVPPVALEavmsNDTWELvyDRLAHLAGEHRTT--LVFVNTRRMAERVTRFLAERLGSrqVAAHHGSLAKELRL 331
Cdd:PTZ00424 236 LtleGIRQFYVAVE----KEEWKF--DTLCDLYETLTITqaIIYCNTRRKVDYLTKKMHERDFT--VSCMHGDMDQKDRD 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15598468 332 DAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSG 383
Cdd:PTZ00424 308 LIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSG 359
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
29-185 |
1.28e-09 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 59.53 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 29 FERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLtAFLAAIDALVVEGLAAGGELAdatqvVYVSPLKALSndirin 108
Cdd:cd17957 6 EESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTL-AFLIPILQKLGKPRKKKGLRA-----LILAPTRELA------ 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598468 109 lEQplagIREELARLGLPDvDIRSAVRT-GDTPQVERGAMRKRPPHILVTTPESLYILLgsESGRQMLAGVRSVIVDE 185
Cdd:cd17957 74 -SQ----IYRELLKLSKGT-GLRIVLLSkSLEAKAKDGPKSITKYDILVSTPLRLVFLL--KQGPIDLSSVEYLVLDE 143
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
30-185 |
2.09e-09 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 59.13 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 30 ERHFAAPTPAQVEAWPAI-REGLSTLVAAPTGSGKTLtAFLA-AIDALVvEGLAAGGelADATQVVYVSPLKALSndiri 107
Cdd:cd17964 11 RMGFETMTPVQQKTLKPIlSTGDDVLARAKTGTGKTL-AFLLpAIQSLL-NTKPAGR--RSGVSALIISPTRELA----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 108 nlEQplagIREELARL--GLPDVDIRSAVrtGDTPQ-VERGAMRKRPPHILVTTPESLYILLGSESGRQMLAGVRSVIVD 184
Cdd:cd17964 82 --LQ----IAAEAKKLlqGLRKLRVQSAV--GGTSRrAELNRLRRGRPDILVATPGRLIDHLENPGVAKAFTDLDYLVLD 153
|
.
gi 15598468 185 E 185
Cdd:cd17964 154 E 154
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
38-355 |
1.11e-08 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 59.97 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 38 PAQVEAWPA-IREGLSTLVAAPTGSGKTLTAFLAAIDAlvvegLAAGGeladatQVVYVSPLKALSNDIRINLeqplagi 116
Cdd:PRK02362 26 PPQAEAVEAgLLDGKNLLAAIPTASGKTLIAELAMLKA-----IARGG------KALYIVPLRALASEKFEEF------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 117 rEELARLGlpdvdIRSAVRTGDTPQVERGAMRKrppHILVTTPESLYILLGSESGrqMLAGVRSVIVDEIHALAGSKRGS 196
Cdd:PRK02362 88 -ERFEELG-----VRVGISTGDYDSRDEWLGDN---DIIVATSEKVDSLLRNGAP--WLDDITCVVVDEVHLIDSANRGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 197 HLALSLERLQALCPRpLLRIGLSATqkpiekvarflvgaSGNPRDPA----CRIVDVGYtRPRDLGIEV----------P 262
Cdd:PRK02362 157 TLEVTLAKLRRLNPD-LQVVALSAT--------------IGNADELAdwldAELVDSEW-RPIDLREGVfyggaihfddS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 263 PVALEAVMSNDTWELVYDRLAhlagEHRTTLVFVNTRRMAE----RVTRF---------------LAERLGS-------- 315
Cdd:PRK02362 221 QREVEVPSKDDTLNLVLDTLE----EGGQCLVFVSSRRNAEgfakRAASAlkktltaaeraelaeLAEEIREvsdtetsk 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15598468 316 -------RQVAAHHGSLAKELRLDAEQRLKAGQLKVLVATASLELGI 355
Cdd:PRK02362 297 dladcvaKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGL 343
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
33-383 |
2.89e-08 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 58.03 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 33 FAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLtAFLaaidalvvegLAAGGELAD-------ATQVVYVSPLKALSNDI 105
Cdd:PRK11192 21 YTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTA-AFL----------LPALQHLLDfprrksgPPRILILTPTRELAMQV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 106 RinlEQPlagirEELARlglpDVDIRSAVRTGDTPQVERGAMRKRPPHILVTTPESL--YIllgsESGRQMLAGVRSVIV 183
Cdd:PRK11192 90 A---DQA-----RELAK----HTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLlqYI----KEENFDCRAVETLIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 184 DE------------IHALAGSKRGshlalsleRLQALCprpllrigLSATQKPiEKVARFlvgasgnprdpACRIVDvgy 251
Cdd:PRK11192 154 DEadrmldmgfaqdIETIAAETRW--------RKQTLL--------FSATLEG-DAVQDF-----------AERLLN--- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 252 trprdlgievPPVALEAVMSN-------------DTWELVYDRLAH-LAGEHRT-TLVFVNTRrmaERVtRFLAERLGSR 316
Cdd:PRK11192 203 ----------DPVEVEAEPSRrerkkihqwyyraDDLEHKTALLCHlLKQPEVTrSIVFVRTR---ERV-HELAGWLRKA 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598468 317 QVAAHH--GSLAKELRLDAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSG 383
Cdd:PRK11192 269 GINCCYleGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTG 337
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
292-383 |
3.23e-08 |
|
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: 54.10 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 292 TLVFVNTRRMAERVTRFLAerlGsrqVAAHHGSLAKELRLDAEQRLKAGQLKVLVATASLELGID------------IGD 359
Cdd:cd18795 46 VLVFCSSRKECEKTAKDLA---G---IAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpartviikgtqRYD 119
|
90 100
....*....|....*....|....
gi 15598468 360 VELVCQLssprSIAAFLQRVGRSG 383
Cdd:cd18795 120 GKGYREL----SPLEYLQMIGRAG 139
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
38-195 |
4.51e-08 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 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: 350782 [Multi-domain] Cd Length: 205 Bit Score: 55.14 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 38 PAQVEAWPAIREGLSTLVAAPTGSGKTltaflaaidalVVEGLAAGGELADATQVVYVSPLKALSNdirinleQPLAGIR 117
Cdd:cd18024 35 PFQKTAIACIERNESVLVSAHTSAGKT-----------VVAEYAIAQSLRDKQRVIYTSPIKALSN-------QKYRELQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 118 EELARLGLpdvdirsavRTGD---TPQVErgamrkrpphILVTTPESLYILL--GSESGRQmlagVRSVIVDEIHALAGS 192
Cdd:cd18024 97 EEFGDVGL---------MTGDvtiNPNAS----------CLVMTTEILRSMLyrGSEIMRE----VAWVIFDEIHYMRDK 153
|
...
gi 15598468 193 KRG 195
Cdd:cd18024 154 ERG 156
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
764-1287 |
7.51e-08 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 57.57 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 764 LPRYAGGRKVPPQLLrmkSEDLLASVFPDQVACLENIVGEREVPDHPLVAQTLDDCLHEAMDCEGWLALLRDMESGAVDL 843
Cdd:COG3321 863 LPTYPFQREDAAAAL---LAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAA 939
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 844 LARDLPAPSALAAEILTARPYAYLDDAPLEERRTQAVQNRRWSDPESADDLGALDLEAIEAVRGEAWPEASNADEMHEAL 923
Cdd:COG3321 940 AALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAA 1019
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 924 NSLGFLTSGEAEANPGWGEWLAQLSEQRRAGRLDCAGSTLWLAAERLPAMRLVHPAAKVPDAFQAPRGYPPPDSAEAATV 1003
Cdd:COG3321 1020 ALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALAL 1099
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 1004 ELTRARLGGFGPRTAGQLAADLGIGLADqqyALAALEREGYVLRGRFSPGATEEEWCERHLLARIHRYTVKRLRREIEPV 1083
Cdd:COG3321 1100 AALAAALLLLALLAALALAAAAAALLAL---AALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLA 1176
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 1084 ERADFMRFLFDWQRLAPGTRGRGAESLATVVEQLEGFQAAAAAWESELLAARVADYASHWLDQLCRSGRIVWARLAGRSK 1163
Cdd:COG3321 1177 LALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALL 1256
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 1164 AAGGPLRSAPIVLLPRRELGLWSVLQRDAPEPELSPRAARVLEVLREQGASFF---DELSQDAHLLRSELENALGELVSV 1240
Cdd:COG3321 1257 AALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAaaaAAAAAAAALAAALLAAALAALAAA 1336
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15598468 1241 GRVNADSFAGLRTLLMPADKRSRQERRSRGLPGGMQDAGRWAPLRRA 1287
Cdd:COG3321 1337 VAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAA 1383
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
19-185 |
1.93e-07 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350810 [Multi-domain] Cd Length: 264 Bit Score: 54.20 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 19 AEFHPVVRQWFER-HFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALVVEGLAAGG-ELADATQVVYVS 96
Cdd:cd18052 48 ANLCETLLKNIRKaGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSfSEVQEPQALIVA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 97 PLKALSNdiRINLEqplagireelARLGLPDVDIRSAVRTGDTP------QVERGAmrkrppHILVTTPESLYILLGseS 170
Cdd:cd18052 128 PTRELAN--QIFLE----------ARKFSYGTCIRPVVVYGGVSvghqirQIEKGC------HILVATPGRLLDFIG--R 187
|
170
....*....|....*
gi 15598468 171 GRQMLAGVRSVIVDE 185
Cdd:cd18052 188 GKISLSKLKYLILDE 202
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
33-189 |
1.96e-07 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 53.04 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 33 FAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALVVEglaaggelADATQVVYVSPlkalSNDIRINleqp 112
Cdd:cd17943 10 FQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLE--------RRHPQVLILAP----TREIAVQ---- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598468 113 lagIREELARLGLPDVDIRSAVRTGDTPqVERGAMRKRPPHILVTTPESLYILLgsESGRQMLAGVRSVIVDEIHAL 189
Cdd:cd17943 74 ---IHDVFKKIGKKLEGLKCEVFIGGTP-VKEDKKKLKGCHIAVGTPGRIKQLI--ELGALNVSHVRLFVLDEADKL 144
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
36-189 |
2.40e-07 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 52.71 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 36 PTPAQVEAWPAIREGLSTLVAAPTGSGKTlTAF----LAAIDALVVEglaAGGELADATQvvyvSPLKALSNDIRinleq 111
Cdd:cd17938 22 PTDIQAEAIPLILGGGDVLMAAETGSGKT-GAFclpvLQIVVALILE---PSRELAEQTY----NCIENFKKYLD----- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598468 112 plagireelarlglpDVDIRSAVRTGDTPQVERGAMRKRPPHILVTTPESLYILLgsESGRQMLAGVRSVIVDEIHAL 189
Cdd:cd17938 89 ---------------NPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLI--KTGKLDLSSVRFFVLDEADRL 149
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
41-221 |
3.10e-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: 51.15 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 41 VEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALVveglaaggeladaTQVVYVSPLKALSNDIRINLEQPlaGIREEL 120
Cdd:cd17926 9 LEAWLAHKNNRRGILVLPTGSGKTLTALALIAYLKE-------------LRTLIVVPTDALLDQWKERFEDF--LGDSSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 121 ARLGLPDVD-IRSAVrtgdtpqvergamrkrpphILVTTPESLYILLgsESGRQMLAGVRSVIVDEIHalagskrgsHL- 198
Cdd:cd17926 74 GLIGGGKKKdFDDAN-------------------VVVATYQSLSNLA--EEEKDLFDQFGLLIVDEAH---------HLp 123
|
170 180
....*....|....*....|...
gi 15598468 199 ALSLERLQALCPRPlLRIGLSAT 221
Cdd:cd17926 124 AKTFSEILKELNAK-YRLGLTAT 145
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
293-388 |
6.42e-07 |
|
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: 50.43 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 293 LVFVNTRRMAERVTRFL---------AERLGSRQVAAHHGSLAKElRLDAEQRLKAGQLKVLVATASLELGIDIGDVELV 363
Cdd:cd18801 34 IIFSEFRDSAEEIVNFLskirpgiraTRFIGQASGKSSKGMSQKE-QKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLI 112
|
90 100
....*....|....*....|....*.
gi 15598468 364 -CQLSSPRSIaAFLQRVGRSGHSVGG 388
Cdd:cd18801 113 iCYDASPSPI-RMIQRMGRTGRKRQG 137
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
36-189 |
1.03e-06 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 51.60 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 36 PTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALVVEGLAAGGELaDATQVVYVSPLKALSNDIRinleqplaG 115
Cdd:cd17948 13 PTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPF-NAPRGLVITPSRELAEQIG--------S 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598468 116 IREELARlglpDVDIRSAVRTGDtpqveRGAMRKRPPH-----ILVTTPESLYILLgsESGRQMLAGVRSVIVDEIHAL 189
Cdd:cd17948 84 VAQSLTE----GLGLKVKVITGG-----RTKRQIRNPHfeevdILVATPGALSKLL--TSRIYSLEQLRHLVLDEADTL 151
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
45-232 |
1.06e-06 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 51.06 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 45 PAIREGLSTLVAAPTGSGKTLTAFLAAIDALVVEGLAAggeladatqvVYVSPLKALSN---DIRINLEQPLaGIR-EEL 120
Cdd:cd18026 28 PGLLEGRNLVYSLPTSGGKTLVAEILMLKRLLERRKKA----------LFVLPYVSIVQekvDALSPLFEEL-GFRvEGY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 121 ArlglpdvdirsavrtGDTpqveRGAMRKRP--PHILVTTPESLYILLGS--ESGRQMLAGVrsVIVDEIHALAGSKRGS 196
Cdd:cd18026 97 A---------------GNK----GRSPPKRRksLSVAVCTIEKANSLVNSliEEGRLDELGL--VVVDELHMLGDGHRGA 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598468 197 HLALSLERLQALCPRPLLRIGLSATQKPIEKVARFL 232
Cdd:cd18026 156 LLELLLTKLLYAAQKNIQIVGMSATLPNLEELASWL 191
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
10-185 |
1.06e-06 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 51.55 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 10 RAEPAPRPLAEFHP------VVRQWFERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALVVEGLAAG 83
Cdd:cd18049 15 RGHNCPKPVLNFYEanfpanVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLER 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 84 GelaDATQVVYVSPLKALSNDIrinleQPLAGIREELARLglpdvdiRSAVRTGDTPQVERGAMRKRPPHILVTTPESLY 163
Cdd:cd18049 95 G---DGPICLVLAPTRELAQQV-----QQVAAEYGRACRL-------KSTCIYGGAPKGPQIRDLERGVEICIATPGRLI 159
|
170 180
....*....|....*....|..
gi 15598468 164 ILLgsESGRQMLAGVRSVIVDE 185
Cdd:cd18049 160 DFL--EAGKTNLRRCTYLVLDE 179
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
33-187 |
1.38e-06 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 50.61 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 33 FAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAaidALVVEGLaaggeladatqVVYVSPLKALSNDirinleQp 112
Cdd:cd17920 10 YDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLP---ALLLDGV-----------TLVVSPLISLMQD------Q- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 113 lagiREELARLGLPDVDIRSAVRTGDTPQVERgAMRKRPPHILVTTPESlyilLGSESGRQMLAGVRS------VIVDEI 186
Cdd:cd17920 69 ----VDRLQQLGIRAAALNSTLSPEEKREVLL-RIKNGQYKLLYVTPER----LLSPDFLELLQRLPErkrlalIVVDEA 139
|
.
gi 15598468 187 H 187
Cdd:cd17920 140 H 140
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
292-396 |
1.52e-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: 47.31 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 292 TLVFVNTRRMAERVTRflaerlgsrqvaahhgslakelrldaeqrlkagQLKVLVATASLELGIDIGDVELVCQLSSPRS 371
Cdd:cd18785 6 IIVFTNSIEHAEEIAS---------------------------------SLEILVATNVLGEGIDVPSLDTVIFFDPPSS 52
|
90 100
....*....|....*....|....*
gi 15598468 372 IAAFLQRVGRSGHsvGGTPKGRLFP 396
Cdd:cd18785 53 AASYIQRVGRAGR--GGKDEGEVIL 75
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
24-185 |
2.14e-06 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350724 [Multi-domain] Cd Length: 197 Bit Score: 50.06 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 24 VVRQWFERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALVVEGLAAGGelaDATQVVYVSPLKALSN 103
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERG---DGPIVLVLAPTRELAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 104 DirinleqplagIREELARLGlPDVDIRSAVRTGDTPQVERGAMRKRPPHILVTTPESLYILLgsESGRQMLAGVRSVIV 183
Cdd:cd17966 78 Q-----------IQQEANKFG-GSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFL--DQGKTNLRRVTYLVL 143
|
..
gi 15598468 184 DE 185
Cdd:cd17966 144 DE 145
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1035-1448 |
2.35e-06 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 52.57 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 1035 ALAALEREGYVLRGRFSPGATEEEWCERHLLARIHRYTVKRLRREIEpvERADFMRFL---------FDWQRLAPGTRGR 1105
Cdd:COG3321 782 AVEALLADGVRVFLEVGPGPVLTGLVRQCLAAAGDAVVLPSLRRGED--ELAQLLTALaqlwvagvpVDWSALYPGRGRR 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 1106 GAeSLATVV--EQLEGFQAAAAAWESELLAARVADYASHWLDQLCRSGRIVWARLAGRSKAAGGPLRSAPIVLLPRRELG 1183
Cdd:COG3321 860 RV-PLPTYPfqREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAA 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 1184 LWSVLQRDAPEPELSPRAARVLEVLREQGASFFDELSQDAHLLRSELENALGELVSVGRVNAdsfAGLRTLLMPADKRSR 1263
Cdd:COG3321 939 AAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAA---ALALLAAAALLLAAA 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 1264 QERRSRGLPGGMQDAGRWAPLRRAKAEEAGQRLPAEVLEHVARTLLRRYGVVAWRLLEREADWLPPWRELLRVYHRLEAR 1343
Cdd:COG3321 1016 AAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAAL 1095
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 1344 GEIRGGRFIAGLAGEQFALAEAVGLLREVRKRPPDGAMLVVSAVDPLNLVGGLLPGERVPAVTGNRLLYRDGAPLAALVA 1423
Cdd:COG3321 1096 ALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLL 1175
|
410 420
....*....|....*....|....*
gi 15598468 1424 GKVRMLAEVDGETAQQIRALLIRRH 1448
Cdd:COG3321 1176 ALALALAAALAAALAGLAALLLAAL 1200
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
292-396 |
2.37e-06 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins 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: 350186 [Multi-domain] Cd Length: 116 Bit Score: 47.94 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 292 TLVFVNTRRMAERVTRFLAErLGSRQVAAHHGSLAKELRLDAEQRLKAGQLK--VLVATASLELGIDIGDVELVCQLSSP 369
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNE-AGIDAVALNSDYSDRERGDEALILLFFGELKppILVTVDLLTTGVDIPEVDNVVFLRPT 87
|
90 100
....*....|....*....|....*..
gi 15598468 370 RSIAAFLQRVGRsghsvgGTpkgRLFP 396
Cdd:cd18799 88 ESRTLFLQMLGR------GL---RLHE 105
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
26-221 |
2.81e-06 |
|
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: 49.19 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 26 RQW-FErhfaaPTPAQVEAWPAIREGLSTLVAAPTGSGKTltaflaaidalVVEGLAAGGELADATQVVYVSPLKALSNd 104
Cdd:cd18027 3 FKWpFE-----LDVFQKQAILHLEAGDSVFVAAHTSAGKT-----------VVAEYAIALAQKHMTRTIYTSPIKALSN- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 105 irinleQPLAGIREELARLGLpdvdirsavRTGDTpQVERGAmrkrppHILVTTPESLYILLgsESGRQMLAGVRSVIVD 184
Cdd:cd18027 66 ------QKFRDFKNTFGDVGL---------ITGDV-QLNPEA------SCLIMTTEILRSML--YNGSDVIRDLEWVIFD 121
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598468 185 EIHALAGSKRGshlaLSLERLQALCPRPLLRIGLSAT 221
Cdd:cd18027 122 EVHYINDAERG----VVWEEVLIMLPDHVSIILLSAT 154
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
33-185 |
3.67e-06 |
|
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350719 [Multi-domain] Cd Length: 206 Bit Score: 49.50 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 33 FAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALVVEGLAAGGElaDATQVVYVSPLKALSNDIRINLEQP 112
Cdd:cd17961 14 WEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEE--QGTRALILVPTRELAQQVSKVLEQL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598468 113 LAGIReelarlglpdVDIRSA-VRTGDTPQVERGAMRKrPPHILVTTPESLYILLgsESGR-QMLAGVRSVIVDE 185
Cdd:cd17961 92 TAYCR----------KDVRVVnLSASSSDSVQRALLAE-KPDIVVSTPARLLSHL--ESGSlLLLSTLKYLVIDE 153
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
33-382 |
5.58e-06 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 50.94 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 33 FAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTaFLAAIDALVVEGLAAGGELADATQVVYVSPLKALSNDIrinleqp 112
Cdd:PLN00206 141 YEFPTPIQMQAIPAALSGRSLLVSADTGSGKTAS-FLVPIISRCCTIRSGHPSEQRNPLAMVLTPTRELCVQV------- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 113 lagirEELARL---GLPdvdIRSAVRTGDTP---QVERgamRKRPPHILVTTPESLYILLGSESGRqmLAGVRSVIVDEI 186
Cdd:PLN00206 213 -----EDQAKVlgkGLP---FKTALVVGGDAmpqQLYR---IQQGVELIVGTPGRLIDLLSKHDIE--LDNVSVLVLDEV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 187 HALAgsKRGSHLALsLERLQALC-PRPLLrigLSATQKP-IEKVARFLVgasgnpRDPAcrIVDVGytRPRDLGIEVPPV 264
Cdd:PLN00206 280 DCML--ERGFRDQV-MQIFQALSqPQVLL---FSATVSPeVEKFASSLA------KDII--LISIG--NPNRPNKAVKQL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 265 ALeAVMSNDTWELVYDRLAHLAGEHRTTLVFVNTRRMAERVTRFLAERLGSRQVAAHHGSLAKElRLDAEQRLKAGQLKV 344
Cdd:PLN00206 344 AI-WVETKQKKQKLFDILKSKQHFKPPAVVFVSSRLGADLLANAITVVTGLKALSIHGEKSMKE-RREVMKSFLVGEVPV 421
|
330 340 350
....*....|....*....|....*....|....*...
gi 15598468 345 LVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRS 382
Cdd:PLN00206 422 IVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRA 459
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
30-185 |
6.10e-06 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350711 [Multi-domain] Cd Length: 222 Bit Score: 48.91 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 30 ERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALVVEGLAAGGELADAtqvVYVSPLKALSNDIRINL 109
Cdd:cd17953 29 KLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEGPIG---LIMAPTRELALQIYVEC 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598468 110 eQPLAgireelarlglPDVDIRSAVRTGDTPQVERGAMRKRPPHILVTTPESLYILLGSESGRQM-LAGVRSVIVDE 185
Cdd:cd17953 106 -KKFS-----------KALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGRVTnLRRVTYVVLDE 170
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
38-383 |
9.51e-06 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 50.10 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 38 PAQVEAWPAIREGLSTLVAAPTGSGKTLTAflaAIDALVVEGLAaggeladatqvVYVSPLKALSNDiriNLEQPLA-GI 116
Cdd:PRK11057 28 PGQQEIIDAVLSGRDCLVVMPTGGGKSLCY---QIPALVLDGLT-----------LVVSPLISLMKD---QVDQLLAnGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 117 ----------REELarlglpdVDIRSAVRTGDTPQV----ERGAMRKRPPHILVTTPeslyillgsesgrQMLAgvrsvi 182
Cdd:PRK11057 91 aaaclnstqtREQQ-------LEVMAGCRTGQIKLLyiapERLMMDNFLEHLAHWNP-------------ALLA------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 183 VDEIHALA--GSK-RGSHLALSLERlQALCPRPLLRIGLSATQKPIEKVARFLvgasgNPRDPacrIVDVG-YTRPrdlg 258
Cdd:PRK11057 145 VDEAHCISqwGHDfRPEYAALGQLR-QRFPTLPFMALTATADDTTRQDIVRLL-----GLNDP---LIQISsFDRP---- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 259 ievppvaleavmsNDTWELV-----YDRLAHLAGEHR--TTLVFVNTRRMAERvtrfLAERLGSR--QVAAHHGSLAKEL 329
Cdd:PRK11057 212 -------------NIRYTLVekfkpLDQLMRYVQEQRgkSGIIYCNSRAKVED----TAARLQSRgiSAAAYHAGLDNDV 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15598468 330 RLDAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSG 383
Cdd:PRK11057 275 RADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAG 328
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
36-221 |
1.03e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 47.28 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 36 PTPAQVEAWPAIREGLST-----LVAAPTGSGKTLTAFlAAIDALVveglaaggELADATQVVYVSPLKALsndirinLE 110
Cdd:pfam04851 4 LRPYQIEAIENLLESIKNgqkrgLIVMATGSGKTLTAA-KLIARLF--------KKGPIKKVLFLVPRKDL-------LE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 111 QplagIREELARLgLPDVDIRSAVRTGDTPQVERGAMRkrpphILVTTPESLYILLGSESGRQMLAGVRSVIVDEIHala 190
Cdd:pfam04851 68 Q----ALEEFKKF-LPNYVEIGEIISGDKKDESVDDNK-----IVVTTIQSLYKALELASLELLPDFFDVIIIDEAH--- 134
|
170 180 190
....*....|....*....|....*....|.
gi 15598468 191 gskRGShlALSLERLqALCPRPLLRIGLSAT 221
Cdd:pfam04851 135 ---RSG--ASSYRNI-LEYFKPAFLLGLTAT 159
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
288-381 |
1.11e-05 |
|
C-terminal helicase domain of the 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. Dicer exists throughout eukaryotes, and a subset has 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 helicase domains 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: 350189 [Multi-domain] Cd Length: 142 Bit Score: 46.82 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 288 EHRTTLVFVNTRRMAERVTRFLAERLGSRQ-------VAAHHGSLAKELRL------DAEQRLKAGQLKVLVATASLELG 354
Cdd:cd18802 24 PDFRGIIFVERRATAVVLSRLLKEHPSTLAfircgflIGRGNSSQRKRSLMtqrkqkETLDKFRDGELNLLIATSVLEEG 103
|
90 100
....*....|....*....|....*..
gi 15598468 355 IDIGDVELVCQLSSPRSIAAFLQRVGR 381
Cdd:cd18802 104 IDVPACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
292-382 |
2.36e-05 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 48.79 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 292 TLVFVNTRRMAERVTRFLaERLGSRqVAAHHGSLAKELRLDAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRS 371
Cdd:PRK04537 260 TMVFVNTKAFVERVARTL-ERHGYR-VGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFD 337
|
90
....*....|.
gi 15598468 372 IAAFLQRVGRS 382
Cdd:PRK04537 338 AEDYVHRIGRT 348
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
33-185 |
3.13e-05 |
|
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.
Pssm-ID: 350704 [Multi-domain] Cd Length: 235 Bit Score: 46.85 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 33 FAAPTPAQVEAWP-AIREGLSTLVAAPTGSGKTLtAFlaAIDalVVEGLaaggeladatqvvyvspLKALSNDIRINLEQ 111
Cdd:cd17946 10 FSEPTPIQALALPaAIRDGKDVIGAAETGSGKTL-AF--GIP--ILERL-----------------LSQKSSNGVGGKQK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 112 PLAG------------IREELARLgLPDVDIRSAVRTGDTPQVERGAMRKRPPHILVTTPESLYILLgsESGRQMLAGVR 179
Cdd:cd17946 68 PLRAliltptrelavqVKDHLKAI-AKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELI--QEGNEHLANLK 144
|
....*....
gi 15598468 180 SV---IVDE 185
Cdd:cd17946 145 SLrflVLDE 153
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
53-235 |
3.39e-05 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 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: 350688 [Multi-domain] Cd Length: 186 Bit Score: 46.13 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 53 TLVAAPTGSGKTLTAFLAAidalvvEGLAAGGEladATQVVYVSPLKALSNDI--RINLEQPLAGIREEL------ARLG 124
Cdd:cd17930 4 VILEAPTGSGKTEAALLWA------LKLAARGG---KRRIIYALPTRATINQMyeRIREILGRLDDEDKVlllhskAALE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 125 LPDVDIRSAVRTGDTPQVERGAMRKRPPHILVTTPES-LYILLGSESGRQMLAG-VRSVIV-DEIHALAgskrGSHLALS 201
Cdd:cd17930 75 LLESDEEPDDDPVEAVDWALLLKRSWLAPIVVTTIDQlLESLLKYKHFERRLHGlANSVVVlDEVQAYD----PEYMALL 150
|
170 180 190
....*....|....*....|....*....|....*
gi 15598468 202 LERLQALCPRPLLRIGL-SATQKPIEKvaRFLVGA 235
Cdd:cd17930 151 LKALLELLGELGGPVVLmTATLPALLR--DELLEA 183
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
292-388 |
8.05e-05 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB 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: 350177 [Multi-domain] Cd Length: 171 Bit Score: 44.93 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 292 TLVFVNTRRMAERVTRFLAErLGSRQVAAHHGSLAKElRLDAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSS--- 368
Cdd:cd18790 30 VLVTTLTKRMAEDLTEYLQE-LGVKVRYLHSEIDTLE-RVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDAdke 107
|
90 100
....*....|....*....|..
gi 15598468 369 --PRSIAAFLQRVGRSGHSVGG 388
Cdd:cd18790 108 gfLRSETSLIQTIGRAARNVNG 129
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
22-185 |
8.43e-05 |
|
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350713 [Multi-domain] Cd Length: 204 Bit Score: 45.29 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 22 HPVVRQWFERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLtAF-------LA----AIDALVvegLAAGGELAdat 90
Cdd:cd17955 8 SWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTA-AFalpilqrLSedpyGIFALV---LTPTRELA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 91 qvvyvsplkalsndirinleqplAGIREELARLGLPdVDIRSAVRTGDTPQVERG-AMRKRpPHILVTTPESLYILLGSE 169
Cdd:cd17955 81 -----------------------YQIAEQFRALGAP-LGLRCCVIVGGMDMVKQAlELSKR-PHIVVATPGRLADHLRSS 135
|
170
....*....|....*..
gi 15598468 170 SGRQM-LAGVRSVIVDE 185
Cdd:cd17955 136 DDTTKvLSRVKFLVLDE 152
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
46-221 |
2.01e-04 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 45.88 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 46 AIREglSTLVAAPTGSGKTLTAFLAAIDALVVEGlaaggeladaTQVVYVSPLKALSndirinlEQPLAGIREELArlgL 125
Cdd:COG1111 15 ALRK--NTLVVLPTGLGKTAVALLVIAERLHKKG----------GKVLFLAPTKPLV-------EQHAEFFKEALN---I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 126 PDVDIrsAVRTGDTPQVERGAMRKRpPHILVTTPESlyILLGSESGRQMLAGVRSVIVDEIHALAGSKRGSHLAlslERL 205
Cdd:COG1111 73 PEDEI--VVFTGEVSPEKRKELWEK-ARIIVATPQV--IENDLIAGRIDLDDVSLLIFDEAHRAVGNYAYVYIA---ERY 144
|
170
....*....|....*.
gi 15598468 206 QALCPRPLLrIGLSAT 221
Cdd:COG1111 145 HEDAKDPLI-LGMTAS 159
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
52-229 |
2.10e-04 |
|
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 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: 350779 [Multi-domain] Cd Length: 191 Bit Score: 43.79 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 52 STLVAAPTGSGKTLTAFLAAIDALVVEGLAAggeladatqVVYVSPLKALSnDIRinleqpLAGIREELARLGlpdvDIR 131
Cdd:cd18021 21 NVFVGAPTGSGKTVCAELALLRHWRQNPKGR---------AVYIAPMQELV-DAR------YKDWRAKFGPLL----GKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 132 SAVRTGDTPQ----VERGamrkrppHILVTTPESLYILLGSESGRQMLAGVRSVIVDEIHaLAGSKRGShlalsleRLQA 207
Cdd:cd18021 81 VVKLTGETSTdlklLAKS-------DVILATPEQWDVLSRRWKQRKNVQSVELFIADELH-LIGGENGP-------VYEV 145
|
170 180
....*....|....*....|..
gi 15598468 208 LCPRplLRIGLSATQKPIEKVA 229
Cdd:cd18021 146 VVSR--MRYISSQLEKPIRIVG 165
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
10-72 |
3.92e-04 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350808 [Multi-domain] Cd Length: 271 Bit Score: 43.85 E-value: 3.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598468 10 RAEPAPRPLAEFHP------VVRQWFERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAI 72
Cdd:cd18050 53 RGVGCPKPVFAFHQanfpqyVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAI 121
|
|
| Lhr_WH |
pfam19306 |
Helicase Lhr winged helix domain; Mycobacterial Lhr is a DNA damage-inducible superfamily 2 ... |
425-560 |
4.23e-04 |
|
Helicase Lhr winged helix domain; Mycobacterial Lhr is a DNA damage-inducible superfamily 2 helicase that uses adenosine triphosphate (ATP) hydrolysis to drive unidirectional 3' to 5' translocation along single-stranded DNA (ssDNA). This entry represents the third domain which has a winged helix domain fold.
Pssm-ID: 437138 [Multi-domain] Cd Length: 147 Bit Score: 42.07 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 425 QPLDVLAQQIVAeVACQE-WREDDLYRLVIRAEPYAGLERERFDEVLRMLAEGYHSrLgvrGAY-----LHRDAlNGLLR 498
Cdd:pfam19306 1 LPLDVLVQHLVT-LAVGDgFEPEELLEEIRSTFAFQDLTDEEWQWCLNFITRGGQS-L---KAYpeykkVEIEE-DGRYK 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598468 499 --GRRGARLTALtSGGTIpdTGDYSVLLEPQ-GLLVGTVNEDFaVESLA-GDVFQLGNTSYRIIRI 560
Cdd:pfam19306 75 vtSRRIAMRHRM-NIGTI--VSDAMLRVKYLsGGYIGTVEESF-ISKLKpGDVFTFAGRNLELVRI 136
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
33-69 |
4.43e-04 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 43.22 E-value: 4.43e-04
10 20 30
....*....|....*....|....*....|....*..
gi 15598468 33 FAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLtAFL 69
Cdd:cd17958 10 FEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTL-AYL 45
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
292-400 |
6.97e-04 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 44.07 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 292 TLVFVNTRRMAERVTRFLaERLGSRQvAAHHGSLAKELRLDAEQRLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRS 371
Cdd:PRK11634 248 AIIFVRTKNATLEVAEAL-ERNGYNS-AALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMD 325
|
90 100
....*....|....*....|....*....
gi 15598468 372 IAAFLQRVGRSGHSvGGTPKGRLFPTSRD 400
Cdd:PRK11634 326 SESYVHRIGRTGRA-GRAGRALLFVENRE 353
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
38-383 |
8.90e-04 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 44.12 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 38 PAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIdalvvegLAAGGELAdatqvvyVSPLKALSNDIRINLEQPlagir 117
Cdd:PLN03137 463 PNQREIINATMSGYDVFVLMPTGGGKSLTYQLPAL-------ICPGITLV-------ISPLVSLIQDQIMNLLQA----- 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 118 eelarlGLPDVDIRSAVRTGDTPQVERGAMRKRPPH-ILVTTPE------SLYILLGSESGRQMLAgvRSVIvDEIHALa 190
Cdd:PLN03137 524 ------NIPAASLSAGMEWAEQLEILQELSSEYSKYkLLYVTPEkvaksdSLLRHLENLNSRGLLA--RFVI-DEAHCV- 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 191 gSKRGSHLALSLERLQALCPR----PLLRIGLSATQKPIEKV--ARFLVGasgnprdpaCRIVDVGYTRPrDLGIEVPPV 264
Cdd:PLN03137 594 -SQWGHDFRPDYQGLGILKQKfpniPVLALTATATASVKEDVvqALGLVN---------CVVFRQSFNRP-NLWYSVVPK 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 265 ALEAVMSNDTW--ELVYDRLAhlagehrttLVFVNTRRMAERVTRFLAErlGSRQVAAHHGSLAKELRLDAEQRLKAGQL 342
Cdd:PLN03137 663 TKKCLEDIDKFikENHFDECG---------IIYCLSRMDCEKVAERLQE--FGHKAAFYHGSMDPAQRAFVQKQWSKDEI 731
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15598468 343 KVLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSG 383
Cdd:PLN03137 732 NIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAG 772
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
33-185 |
9.76e-04 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 42.18 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 33 FAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLtAFLAAidalVVEGLAAGGELADATQV--VYVSPLKALSNDIRINLE 110
Cdd:cd17960 10 FTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTL-AFLIP----VLEILLKRKANLKKGQVgaLIISPTRELATQIYEVLQ 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598468 111 QPLAGIREELarlglpdvdiRSAVRTGDTPQVERGAMRKRP-PHILVTTPESLYILLGSESGRQMLAGVRSVIVDE 185
Cdd:cd17960 85 SFLEHHLPKL----------KCQLLIGGTNVEEDVKKFKRNgPNILVGTPGRLEELLSRKADKVKVKSLEVLVLDE 150
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
22-185 |
1.08e-03 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 41.91 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 22 HPVVRQWFERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLtAFLAAIDALVVEGLAAGGeladaTQVVYVSPLKAL 101
Cdd:cd17959 10 PPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTA-AFLIPMIEKLKAHSPTVG-----ARALILSPTREL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 102 SndirinlEQPLAGIReELARLglpdVDIRSAVRTGDTPQVERGAMRKRPPHILVTTPESLYILLgSESGRQmLAGVRSV 181
Cdd:cd17959 84 A-------LQTLKVTK-ELGKF----TDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLL-VEMNLK-LSSVEYV 149
|
....
gi 15598468 182 IVDE 185
Cdd:cd17959 150 VFDE 153
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
33-72 |
1.12e-03 |
|
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350707 [Multi-domain] Cd Length: 214 Bit Score: 42.19 E-value: 1.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 15598468 33 FAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLtAFLAAI 72
Cdd:cd17949 11 IEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTL-AYLLPI 49
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
30-72 |
1.30e-03 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350709 [Multi-domain] Cd Length: 206 Bit Score: 41.94 E-value: 1.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 15598468 30 ERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAI 72
Cdd:cd17951 7 KKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLI 49
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
268-383 |
1.72e-03 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 42.59 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 268 AVMSNDTWELVYDRLAHLAGEHrtTLVFVN----TRRMAERVTRflaerlGSRQVAAHHGSLAKELRLDAEQRLKAGQLK 343
Cdd:PRK01297 316 AVAGSDKYKLLYNLVTQNPWER--VMVFANrkdeVRRIEERLVK------DGINAAQLSGDVPQHKRIKTLEGFREGKIR 387
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15598468 344 VLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSG 383
Cdd:PRK01297 388 VLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTG 427
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
30-101 |
3.45e-03 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 40.35 E-value: 3.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598468 30 ERHFAAPTPAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAIDALVVEGLAAGgelaDATQVVYVSPLKAL 101
Cdd:cd17941 7 EAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPE----DGLGALIISPTREL 74
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
27-187 |
5.25e-03 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of 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. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 39.93 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 27 QWFERHFAAPT--PAQVEAWPAIREGLSTLVAAPTGSGKTLTAFLAAidalvvegLAAGGELADATQVvyVSPLKALSND 104
Cdd:cd18018 2 KLLRRVFGHPSfrPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPA--------LLLRRRGPGLTLV--VSPLIALMKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 105 IRINLEqplAGIREELARLGLPDVDIRSAVRtgdtpQVERGAMrkrppHILVTTPESLYillgSESGRQMLAGVRSV--- 181
Cdd:cd18018 72 QVDALP---RAIKAAALNSSLTREERRRILE-----KLRAGEV-----KILYVSPERLV----NESFRELLRQTPPIsll 134
|
....*.
gi 15598468 182 IVDEIH 187
Cdd:cd18018 135 VVDEAH 140
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
293-388 |
5.63e-03 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 41.40 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 293 LVFVNTRRMAERVTRFL-------------AERLGSRqvaahhGSLAKElRLDAEQRLKAGQLKVLVATASLELGIDIGD 359
Cdd:PRK13766 369 IVFTQYRDTAEKIVDLLekegikavrfvgqASKDGDK------GMSQKE-QIEILDKFRAGEFNVLVSTSVAEEGLDIPS 441
|
90 100 110
....*....|....*....|....*....|...
gi 15598468 360 VELVCQL----SSPRSIaaflQRVGRSGHSVGG 388
Cdd:PRK13766 442 VDLVIFYepvpSEIRSI----QRKGRTGRQEEG 470
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
37-383 |
6.61e-03 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 40.55 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 37 TPAQVEAWPAIREGLSTLVAAPTGSGKTlTAF----LAAID-------ALVvegLAAGGELADatQVvyvsplkalSNDI 105
Cdd:PRK11776 28 TPIQAQSLPAILAGKDVIAQAKTGSGKT-AAFglglLQKLDvkrfrvqALV---LCPTRELAD--QV---------AKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 106 RinleqplagireELARlGLPDVDIrsAVRTGDTP---QV---ERGAmrkrppHILVTTPESLYILLgsESGRQMLAGVR 179
Cdd:PRK11776 93 R------------RLAR-FIPNIKV--LTLCGGVPmgpQIdslEHGA------HIIVGTPGRILDHL--RKGTLDLDALN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 180 SVIVDE------------IHALAGSkrgshlalslerlqalCPRP---LLrigLSATQKP-IEKVA-RFLvgasgnpRDP 242
Cdd:PRK11776 150 TLVLDEadrmldmgfqdaIDAIIRQ----------------APARrqtLL---FSATYPEgIAAISqRFQ-------RDP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 243 ACRIVDVGYTRP--RDLGIEVPPVA-LEAVMSndtwelvydrlahLAGEHR--TTLVFVNTRrmaeRVTRFLAERLGSR- 316
Cdd:PRK11776 204 VEVKVESTHDLPaiEQRFYEVSPDErLPALQR-------------LLLHHQpeSCVVFCNTK----KECQEVADALNAQg 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598468 317 -QVAAHHGSLakELRlDAEQ---RLKAGQLKVLVATASLELGIDIGDVELVCQLSSPRSIAAFLQRVGRSG 383
Cdd:PRK11776 267 fSALALHGDL--EQR-DRDQvlvRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTG 334
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
282-383 |
7.07e-03 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 40.56 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598468 282 LAHLAGEH--RTTLVFVNTRRMAERvtrfLAERLGSRQV--AAHHGSLAKELRLDAEQRLKAGQLKVLVATASLELGIDI 357
Cdd:PRK10590 236 LSQMIGKGnwQQVLVFTRTKHGANH----LAEQLNKDGIrsAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDI 311
|
90 100
....*....|....*....|....*.
gi 15598468 358 GDVELVCQLSSPRSIAAFLQRVGRSG 383
Cdd:PRK10590 312 EELPHVVNYELPNVPEDYVHRIGRTG 337
|
|
| |
