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Conserved domains on  [gi|695751015|ref|WP_032677266|]
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MULTISPECIES: DEAD/DEAH box helicase [Enterobacterales]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
288-798 6.84e-87

Replicative superfamily II helicase [Replication, recombination and repair];


:

Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 291.80  E-value: 6.84e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  288 VLRELFIGLLARRPRAEvdLWPSQIEAASRAVNQTDNLVVSLPTSAGKTRIAELSILRCLAGGRRAIVVTPLRALSAQTE 367
Cdd:COG1204     6 LPLEKVIEFLKERGIEE--LYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGKALYIVPLRALASEKY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  368 ATLQRTFGPLGKTISALYGSIGVsgfDEDAIRGRDIVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMIGSGEREVRYEV 447
Cdd:COG1204    84 REFKRDFEELGIKVGVSTGDYDS---DDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAHLIDDESRGPTLEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  448 QIQRLLRRkdADQRRIVCLSAILPDgdqMEDFSAWLRRDqpggPIKNDWRPTRLRFGevtwnsptarlnlrvgeerpfvp 527
Cdd:COG1204   161 LLARLRRL--NPEAQIVALSATIGN---AEEIAEWLDAE----LVKSDWRPVPLNEG----------------------- 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  528 rFLtgaapplfvppkKRRNRLFPDNQQELSLATAW---RLVRDGQTVLIYCPERRSVEPFAKVIVDLHSRGaLESLLTVE 604
Cdd:COG1204   209 -VL------------YDGVLRFDDGSRRSKDPTLAlalDLLEEGGQVLVFVSSRRDAESLAKKLADELKRR-LTPEEREE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  605 LTTLQIAIALGEEWLGTDSYILKCLRLGVALHHGALPTAYRKEIERLLREGILKVTISSPTLAQGLNLSATAVVMHSLYR 684
Cdd:COG1204   275 LEELAEELLEVSEETHTNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKR 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  685 HGEM-IKVSEFKNVIGRAGRAYIDVEGLVlypIFEDVNNRKHNKWVNLIEDHGAREMESGLIQ---LIFSLLSRMHSHIG 760
Cdd:COG1204   355 GGMVpIPVLEFKQMAGRAGRPGYDPYGEA---ILVAKSSDEADELFERYILGEPEPIRSKLANesaLRTHLLALIASGFA 431
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 695751015  761 GDLDHLIDYVVNNAAAWVFP-EVAGEKVDEREQALKEWD 798
Cdd:COG1204   432 NSREELLDFLENTFYAYQYDkGDLEEVVDDALEFLLENG 470
HepA super family cl33945
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
52-436 2.70e-03

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


The actual alignment was detected with superfamily member COG0553:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 41.75  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015   52 SFDLHSYAYGLLGLGLRLLESDGDPNQARIAFEQAATALESVMANGNREEADRDFHFLLAAASYHLAHLSARAYSLLAIV 131
Cdd:COG0553     1 LLLLLLLLALGALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  132 ADEANFSPIEHALTLLIRRDINSLRTRVYTFRLDGRGSDATITTFLQQHLTESIVADAAERDGKDFLFEGLNLALTDVFF 211
Cdd:COG0553    81 ALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  212 GAFSMFLLALDRGEYTLLEKAIAQLRENLDicgelnlipqwwvhRIAIHLLKDFWSNTFHEKVPLLPAGGVAPSWPVLRE 291
Cdd:COG0553   161 RLLLLALLLLALEALLLLGLLLALALLALL--------------ELALLAAEAELLLLLELLLELELLAEAAVDAFRLRR 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  292 LFIGLLARRPRAEVDLWPSQIEAASRAVNQTDN-----------LvvslptsaGKTRIAELSILRCLAGG--RRAIVVTP 358
Cdd:COG0553   227 LREALESLPAGLKATLRPYQLEGAAWLLFLRRLglgglladdmgL--------GKTIQALALLLELKERGlaRPVLIVAP 298
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695751015  359 LrALSAQTEATLQRtFGPLGKtISALYGSiGVSGFDEDAIRGRDIVVATpekLDFALRNDPSLLD-DVGLLVFDEGHMI 436
Cdd:COG0553   299 T-SLVGNWQRELAK-FAPGLR-VLVLDGT-RERAKGANPFEDADLVITS---YGLLRRDIELLAAvDWDLVILDEAQHI 370
 
Name Accession Description Interval E-value
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
288-798 6.84e-87

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 291.80  E-value: 6.84e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  288 VLRELFIGLLARRPRAEvdLWPSQIEAASRAVNQTDNLVVSLPTSAGKTRIAELSILRCLAGGRRAIVVTPLRALSAQTE 367
Cdd:COG1204     6 LPLEKVIEFLKERGIEE--LYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGKALYIVPLRALASEKY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  368 ATLQRTFGPLGKTISALYGSIGVsgfDEDAIRGRDIVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMIGSGEREVRYEV 447
Cdd:COG1204    84 REFKRDFEELGIKVGVSTGDYDS---DDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAHLIDDESRGPTLEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  448 QIQRLLRRkdADQRRIVCLSAILPDgdqMEDFSAWLRRDqpggPIKNDWRPTRLRFGevtwnsptarlnlrvgeerpfvp 527
Cdd:COG1204   161 LLARLRRL--NPEAQIVALSATIGN---AEEIAEWLDAE----LVKSDWRPVPLNEG----------------------- 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  528 rFLtgaapplfvppkKRRNRLFPDNQQELSLATAW---RLVRDGQTVLIYCPERRSVEPFAKVIVDLHSRGaLESLLTVE 604
Cdd:COG1204   209 -VL------------YDGVLRFDDGSRRSKDPTLAlalDLLEEGGQVLVFVSSRRDAESLAKKLADELKRR-LTPEEREE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  605 LTTLQIAIALGEEWLGTDSYILKCLRLGVALHHGALPTAYRKEIERLLREGILKVTISSPTLAQGLNLSATAVVMHSLYR 684
Cdd:COG1204   275 LEELAEELLEVSEETHTNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKR 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  685 HGEM-IKVSEFKNVIGRAGRAYIDVEGLVlypIFEDVNNRKHNKWVNLIEDHGAREMESGLIQ---LIFSLLSRMHSHIG 760
Cdd:COG1204   355 GGMVpIPVLEFKQMAGRAGRPGYDPYGEA---ILVAKSSDEADELFERYILGEPEPIRSKLANesaLRTHLLALIASGFA 431
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 695751015  761 GDLDHLIDYVVNNAAAWVFP-EVAGEKVDEREQALKEWD 798
Cdd:COG1204   432 NSREELLDFLENTFYAYQYDkGDLEEVVDDALEFLLENG 470
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
306-485 2.07e-53

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: 184.77  E-value: 2.07e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  306 DLWPSQIEAASRAVNQTDNLVVSLPTSAGKTRIAELSILRCLA-GGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISAL 384
Cdd:cd17921     1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALAtSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  385 YGSIGVSGFDedaIRGRDIVVATPEKLDFALRNDPS-LLDDVGLLVFDEGHMIGSGEREVRYEVQIQRLLRRkdADQRRI 463
Cdd:cd17921    81 TGDPSVNKLL---LAEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRI--NKNARF 155
                         170       180
                  ....*....|....*....|..
gi 695751015  464 VCLSAILPdgdQMEDFSAWLRR 485
Cdd:cd17921   156 VGLSATLP---NAEDLAEWLGV 174
PRK02362 PRK02362
ATP-dependent DNA helicase;
306-707 2.12e-45

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 176.30  E-value: 2.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  306 DLWPSQIEAASRAVNQTDNLVVSLPTSAGKTRIAELSILRCLAGGRRAIVVTPLRALSAQTEATLQRtFGPLGKTisaly 385
Cdd:PRK02362   23 ELYPPQAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIARGGKALYIVPLRALASEKFEEFER-FEELGVR----- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  386 gsIGVSGFDEDAiRG-----RDIVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMIGSGEREVRYEVQIQRLLRRKDADQ 460
Cdd:PRK02362   97 --VGISTGDYDS-RDewlgdNDIIVATSEKVDSLLRNGAPWLDDITCVVVDEVHLIDSANRGPTLEVTLAKLRRLNPDLQ 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  461 rrIVCLSAILPDGDQMEDfsaWLRrdqpGGPIKNDWRPTRLRFGeVTWNSptaRLNlrvgeerpfvprfltgaapplfvp 540
Cdd:PRK02362  174 --VVALSATIGNADELAD---WLD----AELVDSEWRPIDLREG-VFYGG---AIH------------------------ 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  541 pkkrrnrlFPDNQQELSLAT---AWRLVRD-----GQTvLIYCPERRSVEPFAKVIVDlhsrgALESLLTVELTTLQIAI 612
Cdd:PRK02362  217 --------FDDSQREVEVPSkddTLNLVLDtleegGQC-LVFVSSRRNAEGFAKRAAS-----ALKKTLTAAERAELAEL 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  613 AlgEEWLG-----TDSYILKCLRLGVALHHGALPTAYRKEIERLLREGILKVTISSPTLAQGLNLSATAVVMHSLYRH-- 685
Cdd:PRK02362  283 A--EEIREvsdteTSKDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYdg 360
                         410       420
                  ....*....|....*....|....*
gi 695751015  686 --GEM-IKVSEFKNVIGRAGRAYID 707
Cdd:PRK02362  361 gaGMQpIPVLEYHQMAGRAGRPGLD 385
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
308-472 4.63e-26

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: 105.79  E-value: 4.63e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015   308 WPSQIEAASrAVNQTDNLVVSLPTSAGKTRIAELSILRCLA---GGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISAL 384
Cdd:pfam00270    1 TPIQAEAIP-AILEGRDVLVQAPTGSGKTLAFLLPALEALDkldNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015   385 YGsiGVS-GFDEDAIRGRDIVVATPEKLDFALRNDpSLLDDVGLLVFDEGHMIGSGERevryEVQIQRLLRRKDADqRRI 463
Cdd:pfam00270   80 LG--GDSrKEQLEKLKGPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGF----GPDLEEILRRLPKK-RQI 151

                   ....*....
gi 695751015   464 VCLSAILPD 472
Cdd:pfam00270  152 LLLSATLPR 160
DEXDc smart00487
DEAD-like helicases superfamily;
307-468 7.95e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 106.42  E-value: 7.95e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015    307 LWPSQIEAASRAVNQTDNLVVSLPTSAGKTRIAELSILRCLA--GGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISAL 384
Cdd:smart00487    9 LRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKrgKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGL 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015    385 YGSIGVSGFDEDAIRGR-DIVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMIGSGERevryEVQIQRLLRRKdADQRRI 463
Cdd:smart00487   89 YGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGF----GDQLEKLLKLL-PKNVQL 163

                    ....*
gi 695751015    464 VCLSA 468
Cdd:smart00487  164 LLLSA 168
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
52-436 2.70e-03

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 41.75  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015   52 SFDLHSYAYGLLGLGLRLLESDGDPNQARIAFEQAATALESVMANGNREEADRDFHFLLAAASYHLAHLSARAYSLLAIV 131
Cdd:COG0553     1 LLLLLLLLALGALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  132 ADEANFSPIEHALTLLIRRDINSLRTRVYTFRLDGRGSDATITTFLQQHLTESIVADAAERDGKDFLFEGLNLALTDVFF 211
Cdd:COG0553    81 ALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  212 GAFSMFLLALDRGEYTLLEKAIAQLRENLDicgelnlipqwwvhRIAIHLLKDFWSNTFHEKVPLLPAGGVAPSWPVLRE 291
Cdd:COG0553   161 RLLLLALLLLALEALLLLGLLLALALLALL--------------ELALLAAEAELLLLLELLLELELLAEAAVDAFRLRR 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  292 LFIGLLARRPRAEVDLWPSQIEAASRAVNQTDN-----------LvvslptsaGKTRIAELSILRCLAGG--RRAIVVTP 358
Cdd:COG0553   227 LREALESLPAGLKATLRPYQLEGAAWLLFLRRLglgglladdmgL--------GKTIQALALLLELKERGlaRPVLIVAP 298
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695751015  359 LrALSAQTEATLQRtFGPLGKtISALYGSiGVSGFDEDAIRGRDIVVATpekLDFALRNDPSLLD-DVGLLVFDEGHMI 436
Cdd:COG0553   299 T-SLVGNWQRELAK-FAPGLR-VLVLDGT-RERAKGANPFEDADLVITS---YGLLRRDIELLAAvDWDLVILDEAQHI 370
 
Name Accession Description Interval E-value
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
288-798 6.84e-87

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 291.80  E-value: 6.84e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  288 VLRELFIGLLARRPRAEvdLWPSQIEAASRAVNQTDNLVVSLPTSAGKTRIAELSILRCLAGGRRAIVVTPLRALSAQTE 367
Cdd:COG1204     6 LPLEKVIEFLKERGIEE--LYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGGKALYIVPLRALASEKY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  368 ATLQRTFGPLGKTISALYGSIGVsgfDEDAIRGRDIVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMIGSGEREVRYEV 447
Cdd:COG1204    84 REFKRDFEELGIKVGVSTGDYDS---DDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAHLIDDESRGPTLEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  448 QIQRLLRRkdADQRRIVCLSAILPDgdqMEDFSAWLRRDqpggPIKNDWRPTRLRFGevtwnsptarlnlrvgeerpfvp 527
Cdd:COG1204   161 LLARLRRL--NPEAQIVALSATIGN---AEEIAEWLDAE----LVKSDWRPVPLNEG----------------------- 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  528 rFLtgaapplfvppkKRRNRLFPDNQQELSLATAW---RLVRDGQTVLIYCPERRSVEPFAKVIVDLHSRGaLESLLTVE 604
Cdd:COG1204   209 -VL------------YDGVLRFDDGSRRSKDPTLAlalDLLEEGGQVLVFVSSRRDAESLAKKLADELKRR-LTPEEREE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  605 LTTLQIAIALGEEWLGTDSYILKCLRLGVALHHGALPTAYRKEIERLLREGILKVTISSPTLAQGLNLSATAVVMHSLYR 684
Cdd:COG1204   275 LEELAEELLEVSEETHTNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKR 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  685 HGEM-IKVSEFKNVIGRAGRAYIDVEGLVlypIFEDVNNRKHNKWVNLIEDHGAREMESGLIQ---LIFSLLSRMHSHIG 760
Cdd:COG1204   355 GGMVpIPVLEFKQMAGRAGRPGYDPYGEA---ILVAKSSDEADELFERYILGEPEPIRSKLANesaLRTHLLALIASGFA 431
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 695751015  761 GDLDHLIDYVVNNAAAWVFP-EVAGEKVDEREQALKEWD 798
Cdd:COG1204   432 NSREELLDFLENTFYAYQYDkGDLEEVVDDALEFLLENG 470
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
306-485 2.07e-53

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: 184.77  E-value: 2.07e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  306 DLWPSQIEAASRAVNQTDNLVVSLPTSAGKTRIAELSILRCLA-GGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISAL 384
Cdd:cd17921     1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALAtSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  385 YGSIGVSGFDedaIRGRDIVVATPEKLDFALRNDPS-LLDDVGLLVFDEGHMIGSGEREVRYEVQIQRLLRRkdADQRRI 463
Cdd:cd17921    81 TGDPSVNKLL---LAEADILVATPEKLDLLLRNGGErLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRI--NKNARF 155
                         170       180
                  ....*....|....*....|..
gi 695751015  464 VCLSAILPdgdQMEDFSAWLRR 485
Cdd:cd17921   156 VGLSATLP---NAEDLAEWLGV 174
PRK02362 PRK02362
ATP-dependent DNA helicase;
306-707 2.12e-45

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 176.30  E-value: 2.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  306 DLWPSQIEAASRAVNQTDNLVVSLPTSAGKTRIAELSILRCLAGGRRAIVVTPLRALSAQTEATLQRtFGPLGKTisaly 385
Cdd:PRK02362   23 ELYPPQAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIARGGKALYIVPLRALASEKFEEFER-FEELGVR----- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  386 gsIGVSGFDEDAiRG-----RDIVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMIGSGEREVRYEVQIQRLLRRKDADQ 460
Cdd:PRK02362   97 --VGISTGDYDS-RDewlgdNDIIVATSEKVDSLLRNGAPWLDDITCVVVDEVHLIDSANRGPTLEVTLAKLRRLNPDLQ 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  461 rrIVCLSAILPDGDQMEDfsaWLRrdqpGGPIKNDWRPTRLRFGeVTWNSptaRLNlrvgeerpfvprfltgaapplfvp 540
Cdd:PRK02362  174 --VVALSATIGNADELAD---WLD----AELVDSEWRPIDLREG-VFYGG---AIH------------------------ 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  541 pkkrrnrlFPDNQQELSLAT---AWRLVRD-----GQTvLIYCPERRSVEPFAKVIVDlhsrgALESLLTVELTTLQIAI 612
Cdd:PRK02362  217 --------FDDSQREVEVPSkddTLNLVLDtleegGQC-LVFVSSRRNAEGFAKRAAS-----ALKKTLTAAERAELAEL 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  613 AlgEEWLG-----TDSYILKCLRLGVALHHGALPTAYRKEIERLLREGILKVTISSPTLAQGLNLSATAVVMHSLYRH-- 685
Cdd:PRK02362  283 A--EEIREvsdteTSKDLADCVAKGAAFHHAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYdg 360
                         410       420
                  ....*....|....*....|....*
gi 695751015  686 --GEM-IKVSEFKNVIGRAGRAYID 707
Cdd:PRK02362  361 gaGMQpIPVLEYHQMAGRAGRPGLD 385
PRK00254 PRK00254
ski2-like helicase; Provisional
300-710 1.71e-41

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 163.83  E-value: 1.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  300 RPRAEVDLWPSQIEAASRAVNQTDNLVVSLPTSAGKTRIAELSIL-RCLAGGRRAIVVTPLRALSAQTEATLQrTFGPLG 378
Cdd:PRK00254   17 KERGIEELYPPQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVnKLLREGGKAVYLVPLKALAEEKYREFK-DWEKLG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  379 KTISALYGSigvsgFD--EDAIRGRDIVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMIGSGEREVRYEVQIQRLLRRK 456
Cdd:PRK00254   96 LRVAMTTGD-----YDstDEWLGKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  457 dadqrRIVCLSAILPDGdqmEDFSAWLRRDQpggpIKNDWRPTRLR-----FGEVTWNSPtarlnlrvGEERpfvprflt 531
Cdd:PRK00254  171 -----QILGLSATVGNA---EELAEWLNAEL----VVSDWRPVKLRkgvfyQGFLFWEDG--------KIER-------- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  532 gaapplfvppkkrrnrlFPDNQQELslatAWRLVRDGQTVLIYCPERRSVEpfaKVIVDLhsRGALESLLTV-ELTTLQi 610
Cdd:PRK00254  223 -----------------FPNSWESL----VYDAVKKGKGALVFVNTRRSAE---KEALEL--AKKIKRFLTKpELRALK- 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  611 AIALGEEWLGTDSYILKCLRLGVALHHGALPTAYRKEIERLLREGILKVTISSPTLAQGLNLSATAVVMHSLYRHGEM-- 688
Cdd:PRK00254  276 ELADSLEENPTNEKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFgw 355
                         410       420
                  ....*....|....*....|....
gi 695751015  689 --IKVSEFKNVIGRAGRAYIDVEG 710
Cdd:PRK00254  356 edIPVLEIQQMMGRAGRPKYDEVG 379
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
289-721 3.46e-39

Superfamily II RNA helicase [Replication, recombination and repair];


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 157.02  E-value: 3.46e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  289 LRELFIGLLARRPRaevDLWPSQIEAAsRAVNQTDNLVVSLPTSAGKTRIAELSILRCLAGGRRAIVVTPLRALSAQTEA 368
Cdd:COG4581    11 RLEALADFAEERGF---ELDPFQEEAI-LALEAGRSVLVAAPTGSGKTLVAEFAIFLALARGRRSFYTAPIKALSNQKFF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  369 TLQRTFGPlgktisalyGSIG-VSGfdeDAIRGRD--IVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMIGSGEREVRY 445
Cdd:COG4581    87 DLVERFGA---------ENVGlLTG---DASVNPDapIVVMTTEILRNMLYREGADLEDVGVVVMDEFHYLADPDRGWVW 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  446 EVQIQRLlrrkdADQRRIVCLSAILPDgdqMEDFSAWLRRdqpggpikndwrptrlRFGEVTwnsptarlnLRVGEERPf 525
Cdd:COG4581   155 EEPIIHL-----PARVQLVLLSATVGN---AEEFAEWLTR----------------VRGETA---------VVVSEERP- 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  526 VPRFLTGAAPPLFVPPKkrrnRLFPDNQQELSLATAW-RLVRDGQTVLIY-CPERRSVEpfakvivdlhsrGALESLLTV 603
Cdd:COG4581   201 VPLEFHYLVTPRLFPLF----RVNPELLRPPSRHEVIeELDRGGLLPAIVfIFSRRGCD------------EAAQQLLSA 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  604 ELTT----LQIAIALGEE----WLGTDSYILKCLRLGVALHHGALPTAYRKEIERLLREGILKVTISSPTLAQGLNLSAT 675
Cdd:COG4581   265 RLTTkeerAEIREAIDEFaedfSVLFGKTLSRLLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPAR 344
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 695751015  676 AVVMHSL-----YRHgEMIKVSEFKNVIGRAGRAYIDVEG--LVLYPIFEDVN 721
Cdd:COG4581   345 TVVFTKLskfdgERH-RPLTAREFHQIAGRAGRRGIDTEGhvVVLAPEHDDPK 396
PRK01172 PRK01172
ATP-dependent DNA helicase;
306-711 2.79e-36

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 147.34  E-value: 2.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  306 DLWPSQIEAASRaVNQTDNLVVSLPTSAGKTRIAELSILRCLAGGRRAIVVTPLRALSAQTEATLQRtFGPLGKTISAly 385
Cdd:PRK01172   22 ELYDHQRMAIEQ-LRKGENVIVSVPTAAGKTLIAYSAIYETFLAGLKSIYIVPLRSLAMEKYEELSR-LRSLGMRVKI-- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  386 gSIGVSGFDEDAIRGRDIVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMIGSGEREVRYEVQIQrLLRRKDADQrRIVC 465
Cdd:PRK01172   98 -SIGDYDDPPDFIKRYDVVILTSEKADSLIHHDPYIINDVGLIVADEIHIIGDEDRGPTLETVLS-SARYVNPDA-RILA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  466 LSAILPDGDQMedfSAWLRrdqpGGPIKNDWRPTRLRFGEVTwnsptarlnlrvgeerpfvprfltgaapplfvppkkrR 545
Cdd:PRK01172  175 LSATVSNANEL---AQWLN----ASLIKSNFRPVPLKLGILY-------------------------------------R 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  546 NRLFPDNQQ-----ELSLATawRLVRDGQTVLIYCPERRSVEPFAKVIVDLHSrgaleslltvELTTLQIAialGEEWLG 620
Cdd:PRK01172  211 KRLILDGYErsqvdINSLIK--ETVNDGGQVLVFVSSRKNAEDYAEMLIQHFP----------EFNDFKVS---SENNNV 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  621 TDSYILKCLRLGVALHHGALPTAYRKEIERLLREGILKVTISSPTLAQGLNLSATAVVMHSLYRHGEM----IKVSEFKN 696
Cdd:PRK01172  276 YDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPARLVIVRDITRYGNGgiryLSNMEIKQ 355
                         410
                  ....*....|....*
gi 695751015  697 VIGRAGRAYIDVEGL 711
Cdd:PRK01172  356 MIGRAGRPGYDQYGI 370
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
307-483 2.23e-31

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: 121.29  E-value: 2.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  307 LWPSQIEAASRAVNQTDNLVVSLPTSAGKTRIAELSILRCLAGGRRAIVVTPLRALSAQTeatlQRTFgplgKTISALYG 386
Cdd:cd18028     2 LYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGKALYLVPLRALASEK----YEEF----KKLEEIGL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  387 SIGVS--GFDEDA--IRGRDIVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMIGSGEREVRYEVQIQRLlrRKDADQRR 462
Cdd:cd18028    74 KVGIStgDYDEDDewLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESIVARL--RRLNPNTQ 151
                         170       180
                  ....*....|....*....|.
gi 695751015  463 IVCLSAILPDGDQMedfSAWL 483
Cdd:cd18028   152 IIGLSATIGNPDEL---AEWL 169
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
308-472 4.63e-26

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: 105.79  E-value: 4.63e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015   308 WPSQIEAASrAVNQTDNLVVSLPTSAGKTRIAELSILRCLA---GGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISAL 384
Cdd:pfam00270    1 TPIQAEAIP-AILEGRDVLVQAPTGSGKTLAFLLPALEALDkldNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015   385 YGsiGVS-GFDEDAIRGRDIVVATPEKLDFALRNDpSLLDDVGLLVFDEGHMIGSGERevryEVQIQRLLRRKDADqRRI 463
Cdd:pfam00270   80 LG--GDSrKEQLEKLKGPDILVGTPGRLLDLLQER-KLLKNLKLLVLDEAHRLLDMGF----GPDLEEILRRLPKK-RQI 151

                   ....*....
gi 695751015   464 VCLSAILPD 472
Cdd:pfam00270  152 LLLSATLPR 160
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
311-505 7.04e-26

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: 106.67  E-value: 7.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  311 QIEAASRAVNQTDNLVVSLPTSAGKTRIAELSILRCLA-------GGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISA 383
Cdd:cd18023     6 QSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKernplpwGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSCAE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  384 LYGSIGVSGFDEdaIRGRDIVVATPEKLDFALR---NDPSLLDDVGLLVFDEGHMIGSgEREVRYEVQIQRL-------- 452
Cdd:cd18023    86 LTGDTEMDDTFE--IQDADIILTTPEKWDSMTRrwrDNGNLVQLVALVLIDEVHIIKE-NRGATLEVVVSRMktlsssse 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 695751015  453 LRRKDADQRRIVCLSAILPDgdqMEDFSAWLRrdqpggpiknDWRPTRLRFGE 505
Cdd:cd18023   163 LRGSTVRPMRFVAVSATIPN---IEDLAEWLG----------DNPAGCFSFGE 202
DEXDc smart00487
DEAD-like helicases superfamily;
307-468 7.95e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 106.42  E-value: 7.95e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015    307 LWPSQIEAASRAVNQTDNLVVSLPTSAGKTRIAELSILRCLA--GGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISAL 384
Cdd:smart00487    9 LRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKrgKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGL 88
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015    385 YGSIGVSGFDEDAIRGR-DIVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMIGSGERevryEVQIQRLLRRKdADQRRI 463
Cdd:smart00487   89 YGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGF----GDQLEKLLKLL-PKNVQL 163

                    ....*
gi 695751015    464 VCLSA 468
Cdd:smart00487  164 LLLSA 168
DEXHc_POLQ-like cd18026
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ...
305-484 6.27e-22

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: 94.98  E-value: 6.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  305 VDLWPSQIEAASRA-VNQTDNLVVSLPTSAGKTRIAELSILRC-LAGGRRAIVVTPLRALSAQTEATLQRTFGPLGKTIS 382
Cdd:cd18026    15 KKLYDWQKECLSLPgLLEGRNLVYSLPTSGGKTLVAEILMLKRlLERRKKALFVLPYVSIVQEKVDALSPLFEELGFRVE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  383 ALYGSIGVSGFDEDaiRGRDIVVATPEKLDfALRNdpSL-----LDDVGLLVFDEGHMIGSGEREVRYEVQIQRLL--RR 455
Cdd:cd18026    95 GYAGNKGRSPPKRR--KSLSVAVCTIEKAN-SLVN--SLieegrLDELGLVVVDELHMLGDGHRGALLELLLTKLLyaAQ 169
                         170       180
                  ....*....|....*....|....*....
gi 695751015  456 KDAdqrRIVCLSAILPDgdqMEDFSAWLR 484
Cdd:cd18026   170 KNI---QIVGMSATLPN---LEELASWLR 192
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
323-703 9.10e-19

Superfamily II helicase, archaea-specific [Replication, recombination and repair];


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 92.26  E-value: 9.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  323 DNLVVSlPTSAGKTRIAELS-ILRCLAGGRRAIVVTPLRALSAQTEATLQRTFGPLGKTiSALYGSIGVSGFDEDAIRGR 401
Cdd:COG1202   227 DQLVVS-ATATGKTLIGELAgIKNALEGKGKMLFLVPLVALANQKYEDFKDRYGDGLDV-SIRVGASRIRDDGTRFDPNA 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  402 DIVVATPEKLDFALRNDPSlLDDVGLLVFDEGHMIGSGEREVRYEVQIQRLlrRKDADQRRIVCLSAIlpdgdqmedfsa 481
Cdd:COG1202   305 DIIVGTYEGIDHALRTGRD-LGDIGTVVIDEVHMLEDPERGHRLDGLIARL--KYYCPGAQWIYLSAT------------ 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  482 wlrrdqpggpIKNdwrPTRLrfgevtwnspTARLNLRV--GEERPfVP--RFLTgaapplfvppkkrrnrlFPDNQQELS 557
Cdd:COG1202   370 ----------VGN---PEEL----------AKKLGAKLveYEERP-VPleRHLT-----------------FADGREKIR 408
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  558 LATawRLVRD-----------GQTvLIYCPERRSVEpfakvivdlhsrgaleslltvelttlQIAIALGeewlgtdsyil 626
Cdd:COG1202   409 IIN--KLVKRefdtksskgyrGQT-IIFTNSRRRCH--------------------------EIARALG----------- 448
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695751015  627 kclrLGVALHHGALPTAYRKEIERLLREGILKVTISSPTLAQGLNLSATAVVMHSLYRHGEMIKVSEFKNVIGRAGR 703
Cdd:COG1202   449 ----YKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSLAMGIEWLSVQEFHQMLGRAGR 521
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
309-483 1.05e-17

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: 82.31  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  309 PSQIEAASRAVNQTDNLVVSLPTSAGKTRIAELSILRCLA--GGRRAIVVTPLRALSAQTEATLQRTFGP-LGKTISALY 385
Cdd:cd18021     6 PIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRqnPKGRAVYIAPMQELVDARYKDWRAKFGPlLGKKVVKLT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  386 GSIGVsgfDEDAIRGRDIVVATPEKLDFALR--NDPSLLDDVGLLVFDEGHMIGSGEREVrYEVQIQRLlrRKDADQR-- 461
Cdd:cd18021    86 GETST---DLKLLAKSDVILATPEQWDVLSRrwKQRKNVQSVELFIADELHLIGGENGPV-YEVVVSRM--RYISSQLek 159
                         170       180
                  ....*....|....*....|....
gi 695751015  462 --RIVCLSAILPDGDqmeDFSAWL 483
Cdd:cd18021   160 piRIVGLSSSLANAR---DVGEWL 180
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
324-468 4.16e-17

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 79.37  E-value: 4.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  324 NLVVSLPTSAGKTRIAELSIL-RCLAGGRRAIVVTPLRALSAQTEATLQRTFGPlGKTISALYGSIGVSGFDEDAIRGRD 402
Cdd:cd00046     3 NVLITAPTGSGKTLAALLAALlLLLKKGKKVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAEEREKNKLGDAD 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695751015  403 IVVATPEKLDFAL-RNDPSLLDDVGLLVFDEGHMIGSGEREVRYEVQIQRLLRRKDAdqrRIVCLSA 468
Cdd:cd00046    82 IIIATPDMLLNLLlREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNA---QVILLSA 145
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
318-479 1.00e-16

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: 79.78  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  318 AVNQTDNLVVSLPTSAGKTRIAELSILRCLA-----GGR------RAIVVTPLRALSAQTEATLQRTFGPLGKTISALYG 386
Cdd:cd18020    13 AYKTNENMLICAPTGAGKTNIAMLTILHEIRqhvnqGGVikkddfKIVYIAPMKALAAEMVEKFSKRLAPLGIKVKELTG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  387 SIGVSgfdEDAIRGRDIVVATPEKLDFALR---NDPSLLDDVGLLVFDEGHMIgSGEREVRYEVQIQRLLRRKDADQR-- 461
Cdd:cd18020    93 DMQLT---KKEIAETQIIVTTPEKWDVVTRkssGDVALSQLVRLLIIDEVHLL-HDDRGPVIESLVARTLRQVESTQSmi 168
                         170
                  ....*....|....*...
gi 695751015  462 RIVCLSAILPDGDQMEDF 479
Cdd:cd18020   169 RIVGLSATLPNYLDVADF 186
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
536-710 1.06e-16

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: 78.36  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  536 PLFVPPKKRRNRLFPDNQQELSLATawRLVRDGQTVLIYCPERRSVEPFAKVIVdlhsrgaleslltvelttlqiaialg 615
Cdd:cd18795    13 NGLGIKLRVDVMNKFDSDIIVLLKI--ETVSEGKPVLVFCSSRKECEKTAKDLA-------------------------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  616 eewlgtdsyilkclrlGVALHHGALPTAYRKEIERLLREGILKVTISSPTLAQGLNLSATAVVMHSLYR----HGEMIKV 691
Cdd:cd18795    65 ----------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRydgkGYRELSP 128
                         170
                  ....*....|....*....
gi 695751015  692 SEFKNVIGRAGRAYIDVEG 710
Cdd:cd18795   129 LEYLQMIGRAGRPGFDTRG 147
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
318-490 1.55e-16

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: 79.72  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  318 AVNQTDNLVVSLPTSAGKTRIAELSILRCLAGGRRA-----------IVVTPLRALSAQTEATLQRTFGPLGKTISALYG 386
Cdd:cd18019    29 AFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPdgtinldafkiVYIAPMKALVQEMVGNFSKRLAPYGITVAELTG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  387 SIGVSGfdeDAIRGRDIVVATPEKLDFALR--NDPSLLDDVGLLVFDEGHMIgSGEREVRYEVQIQRLLRRKDADQR--R 462
Cdd:cd18019   109 DQQLTK---EQISETQIIVTTPEKWDIITRksGDRTYTQLVRLIIIDEIHLL-HDDRGPVLESIVARTIRQIEQTQEyvR 184
                         170       180
                  ....*....|....*....|....*...
gi 695751015  463 IVCLSAILPDgdqMEDFSAWLRRDQPGG 490
Cdd:cd18019   185 LVGLSATLPN---YEDVATFLRVDPKKG 209
DEXHc_Mtr4-like cd18024
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ...
327-497 5.15e-15

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: 75.17  E-value: 5.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  327 VSLPTSAGKTRIAELSILRCLAGGRRAIVVTPLRALSAQTEATLQRTFGPLGktisALYGSIGVSgfdEDAirgrDIVVA 406
Cdd:cd18024    52 VSAHTSAGKTVVAEYAIAQSLRDKQRVIYTSPIKALSNQKYRELQEEFGDVG----LMTGDVTIN---PNA----SCLVM 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  407 TPEKLDFALRNDPSLLDDVGLLVFDEGHMIGSGEREVRYEVQIQRLlrrkdADQRRIVCLSAILPDGDQmedFSAWLRR- 485
Cdd:cd18024   121 TTEILRSMLYRGSEIMREVAWVIFDEIHYMRDKERGVVWEETIILL-----PDKVRYVFLSATIPNARQ---FAEWICKi 192
                         170
                  ....*....|...
gi 695751015  486 -DQPGGPIKNDWR 497
Cdd:cd18024   193 hKQPCHVVYTDYR 205
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
299-468 3.36e-13

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 73.91  E-value: 3.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  299 RRPRAEVDLWPSQIEAASRAV----NQTDNLVVSLPTSAGKTRIAeLSILRCLAGGRRAIVVTPLRALSAQTEATLQRTF 374
Cdd:COG1061    73 EASGTSFELRPYQQEALEALLaaleRGGGRGLVVAPTGTGKTVLA-LALAAELLRGKRVLVLVPRRELLEQWAEELRRFL 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  375 gplgktisalyGSIGVSGFDEDaiRGRDIVVATPEKLDFALRNDpSLLDDVGLLVFDEGHMIGSGerevryevQIQRLLR 454
Cdd:COG1061   152 -----------GDPLAGGGKKD--SDAPITVATYQSLARRAHLD-ELGDRFGLVIIDEAHHAGAP--------SYRRILE 209
                         170
                  ....*....|....
gi 695751015  455 RKDAdqRRIVCLSA 468
Cdd:COG1061   210 AFPA--AYRLGLTA 221
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
269-704 6.81e-13

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: 73.33  E-value: 6.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  269 TFHEKVPLLPAGgVAPSWPVLRELFIGLLARRprAEVDLWPSQIEAASRAVNQtDNLVVSLPTSAGKTRIAELSILRCLA 348
Cdd:COG1205    22 VHVRTIPAREAR-YAPWPDWLPPELRAALKKR--GIERLYSHQAEAIEAARAG-KNVVIATPTASGKSLAYLLPVLEALL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  349 GGR--RAIVVTPLRALSAQTEATLQRTFGPLGKTISalygsigVSGFDED-------AIRGR-DIVVATPEKLDFA-LRN 417
Cdd:COG1205    98 EDPgaTALYLYPTKALARDQLRRLRELAEALGLGVR-------VATYDGDtppeerrWIREHpDIVLTNPDMLHYGlLPH 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  418 DP---SLLDDVGLLVFDEGHM----IGSgerEVRYEVQ-IQRLLRRKDADQrRIVCLSAILPDGDQM------EDFSAwl 483
Cdd:COG1205   171 HTrwaRFFRNLRYVVIDEAHTyrgvFGS---HVANVLRrLRRICRHYGSDP-QFILASATIGNPAEHaerltgRPVTV-- 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  484 rrdqpggpIKNDWRPT-RLRFgeVTWNSPTARLNLRvgeerpfvpRFLTGAAPPLFVppkkrrnrlfpdnqqelslataw 562
Cdd:COG1205   245 --------VDEDGSPRgERTF--VLWNPPLVDDGIR---------RSALAEAARLLA----------------------- 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  563 RLVRDGQTVLIYCPERRSvepfakvivdlhsrgaleslltVELTTLQIAIALGEEWLGTDsyilkclrlgVALHHGALPT 642
Cdd:COG1205   283 DLVREGLRTLVFTRSRRG----------------------AELLARYARRALREPDLADR----------VAAYRAGYLP 330
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695751015  643 AYRKEIERLLREGILKVTISSPTLAQGLNLSA-TAVVMH----SlyrhgemikVSEFKNVIGRAGRA 704
Cdd:COG1205   331 EERREIERGLRSGELLGVVSTNALELGIDIGGlDAVVLAgypgT---------RASFWQQAGRAGRR 388
DEXHc_ASCC3_2 cd18022
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
320-483 2.09e-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: 67.01  E-value: 2.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  320 NQTDNLVVSLPTSAGKTRIAELSILRCLAG--GRRAIVVTPLRAL-SAQTEATLQRTFGPLGKTISALYGSIGVsgfDED 396
Cdd:cd18022    15 HTDNNVLLGAPTGSGKTIAAELAMFRAFNKypGSKVVYIAPLKALvRERVDDWKKRFEEKLGKKVVELTGDVTP---DMK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  397 AIRGRDIVVATPEKLDFALRN--DPSLLDDVGLLVFDEGHMIGSgEREVRYEVQIQRL--LRRKDADQRRIVCLSAILPD 472
Cdd:cd18022    92 ALADADIIITTPEKWDGISRSwqTREYVQQVSLIIIDEIHLLGS-DRGPVLEVIVSRMnyISSQTEKPVRLVGLSTALAN 170
                         170
                  ....*....|.
gi 695751015  473 GdqmEDFSAWL 483
Cdd:cd18022   171 A---GDLANWL 178
DEXHc_SKIV2L cd18027
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ...
308-485 3.34e-12

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: 66.13  E-value: 3.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  308 WPSQIEA----ASRAVNQTDNLVVSLPTSAGKTRIAELSILRCLAGGRRAIVVTPLRALSAQTEATLQRTFGPLGktisA 383
Cdd:cd18027     5 WPFELDVfqkqAILHLEAGDSVFVAAHTSAGKTVVAEYAIALAQKHMTRTIYTSPIKALSNQKFRDFKNTFGDVG----L 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  384 LYGSIGVSgfdedaiRGRDIVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMIGSGEREVRYEVQIQRLlrrkdADQRRI 463
Cdd:cd18027    81 ITGDVQLN-------PEASCLIMTTEILRSMLYNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIML-----PDHVSI 148
                         170       180
                  ....*....|....*....|..
gi 695751015  464 VCLSAILPDGdqmEDFSAWLRR 485
Cdd:cd18027   149 ILLSATVPNT---VEFADWIGR 167
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
307-438 2.90e-11

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: 62.71  E-value: 2.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  307 LWPSQIEAASRAV--NQTDNLVVSLPTSAGKTRIAELSIlrCLAGGRRAIVVTPLRALSAQTEATLQRTFGPlgKTISAL 384
Cdd:cd17926     1 LRPYQEEALEAWLahKNNRRGILVLPTGSGKTLTALALI--AYLKELRTLIVVPTDALLDQWKERFEDFLGD--SSIGLI 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 695751015  385 YGSIgvsgfdEDAIRGRDIVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMIGS 438
Cdd:cd17926    77 GGGK------KKDFDDANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEAHHLPA 124
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
311-468 1.22e-10

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 62.28  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  311 QIEAASRAVNQtdNLVVSLPTSAGKTRIAELSILR-------CLAGGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISA 383
Cdd:cd18034     7 QLELFEAALKR--NTIVVLPTGSGKTLIAVMLIKEmgelnrkEKNPKKRAVFLVPTVPLVAQQAEAIRSHTDLKVGEYSG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  384 LYG-SIGVSGFDEDAIRGRDIVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMIGSGE--REVryevqIQRLLRRKDADQ 460
Cdd:cd18034    85 EMGvDKWTKERWKEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDECHHATGDHpyARI-----MKEFYHLEGRTS 159

                  ....*....
gi 695751015  461 R-RIVCLSA 468
Cdd:cd18034   160 RpRILGLTA 168
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
311-468 1.74e-10

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 61.68  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  311 QIEAASRAVNQTdNLVVSLPTSAGKTRIA------ELSILRCLAGGRRAIVVTPLRALSAQTEAtLQRTFGPLGKTISAL 384
Cdd:cd17927     7 QLELAQPALKGK-NTIICLPTGSGKTFVAvlicehHLKKFPAGRKGKVVFLANKVPLVEQQKEV-FRKHFERPGYKVTGL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  385 YGSIGVSGFDEDAIRGRDIVVATPEKLDFALRN--DPSlLDDVGLLVFDEGHmigSGEREVRYEVQIQRLLRRKDADQR- 461
Cdd:cd17927    85 SGDTSENVSVEQIVESSDVIIVTPQILVNDLKSgtIVS-LSDFSLLVFDECH---NTTKNHPYNEIMFRYLDQKLGSSGp 160

                  ....*....
gi 695751015  462 --RIVCLSA 468
Cdd:cd17927   161 lpQILGLTA 169
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
323-479 7.45e-10

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: 59.13  E-value: 7.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  323 DNLVVSLPTSAGKTRIAELSILRCLA----GGRRAIVVTPLRALSAQTEATLQR--TFGPLGKTISALYGSIGVSGFDED 396
Cdd:cd17922     2 RNVLIAAPTGSGKTEAAFLPALSSLAdepeKGVQVLYISPLKALINDQERRLEEplDEIDLEIPVAVRHGDTSQSEKAKQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  397 AIRGRDIVVATPEKLDFALRND--PSLLDDVGLLVFDEGHMIGSGEREVRYEVQIQRLLRRKDADQRRIvCLSAILPDGD 474
Cdd:cd17922    82 LKNPPGILITTPESLELLLVNKklRELFAGLRYVVVDEIHALLGSKRGVQLELLLERLRKLTGRPLRRI-GLSATLGNLE 160

                  ....*
gi 695751015  475 QMEDF 479
Cdd:cd17922   161 EAAAF 165
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
311-434 2.73e-09

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 57.91  E-value: 2.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  311 QIEAASRAVNQtdNLVVSLPTSAGKTRIAELSIL-RCLAGGRRAIVVTPLRALSAQTEATLQRTFGPLGKtISALYGSIG 389
Cdd:cd18035     7 QVLIAAVALNG--NTLIVLPTGLGKTIIAILVAAdRLTKKGGKVLILAPSRPLVEQHAENLKRVLNIPDK-ITSLTGEVK 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 695751015  390 VSGFDEDAIRGRdIVVATPEKLDFALRNDPSLLDDVGLLVFDEGH 434
Cdd:cd18035    84 PEERAERWDASK-IIVATPQVIENDLLAGRITLDDVSLLIFDEAH 127
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
311-434 3.22e-09

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 61.28  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  311 QIEAASRAVNqtDNLVVSLPTSAGKTRIAELSILRCLA-GGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISALYGSIG 389
Cdd:COG1111     8 QLNLAASALR--KNTLVVLPTGLGKTAVALLVIAERLHkKGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVS 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 695751015  390 VSGFDEDAIRGRdIVVATPEKLDFALRNDPSLLDDVGLLVFDEGH 434
Cdd:COG1111    86 PEKRKELWEKAR-IIVATPQVIENDLIAGRIDLDDVSLLIFDEAH 129
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
307-474 5.52e-09

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members 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: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 57.49  E-value: 5.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  307 LWPSQIEAASRAVNqTDNLVVSLPTSAGKTRIAELSILRCLAGGR------RAIVVTPLRALSAQTEATLQRTFGPlGKT 380
Cdd:cd18036     3 LRNYQLELVLPALR-GKNTIICAPTGSGKTRVAVYICRHHLEKRRsagekgRVVVLVNKVPLVEQQLEKFFKYFRK-GYK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  381 ISALYGSIGVSGFDEDAIRGRDIVVATPEKLDFALRN----DPSLLDDVGLLVFDEGHmigSGEREVRYEVQIQRLLRRK 456
Cdd:cd18036    81 VTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSgreeERVYLSDFSLLIFDECH---HTQKEHPYNKIMRMYLDKK 157
                         170       180
                  ....*....|....*....|.
gi 695751015  457 DADQR---RIVCLSAILPDGD 474
Cdd:cd18036   158 LSSQGplpQILGLTASPGVGG 178
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
324-472 9.69e-09

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: 56.68  E-value: 9.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  324 NLVVSLPTSAGKT---------RIAELSILRclAGGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISALYGSIGVSGFD 394
Cdd:cd00268    29 DVIGQAQTGSGKTlafllpileKLLPEPKKK--GRGPQALVLAPTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  395 EDAIRGRDIVVATPEKL-DFALRNDPSlLDDVGLLVFDEG-HMIGSGerevrYEVQIQRLLRRKDADqRRIVCLSAILPD 472
Cdd:cd00268   107 EALKKGPDIVVGTPGRLlDLIERGKLD-LSNVKYLVLDEAdRMLDMG-----FEEDVEKILSALPKD-RQTLLFSATLPE 179
ResIII pfam04851
Type III restriction enzyme, res subunit;
304-434 2.38e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 54.60  E-value: 2.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015   304 EVDLWPSQIEA-----ASRAVNQTDNLVVsLPTSAGKTRIAELSILRCL--AGGRRAIVVTPLRALSAQTEATLQRTFGP 376
Cdd:pfam04851    1 KLELRPYQIEAienllESIKNGQKRGLIV-MATGSGKTLTAAKLIARLFkkGPIKKVLFLVPRKDLLEQALEEFKKFLPN 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015   377 lgktiSALYGSIGVSGFDEDAIRGRDIVVATPEKLDFALRND--PSLLDDVGLLVFDEGH 434
Cdd:pfam04851   80 -----YVEIGEIISGDKKDESVDDNKIVVTTIQSLYKALELAslELLPDFFDVIIIDEAH 134
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
324-433 3.72e-08

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: 54.90  E-value: 3.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  324 NLVVSLPTSAGKTrIAEL--SILRCLA----GGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISALYGSI-GVSGFDED 396
Cdd:cd17957    29 DLLACAPTGSGKT-LAFLipILQKLGKprkkKGLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKSLeAKAKDGPK 107
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 695751015  397 AIRGRDIVVATPEKLDFALRNDPSLLDDVGLLVFDEG 433
Cdd:cd17957   108 SITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEA 144
HELICc smart00490
helicase superfamily c-terminal domain;
623-704 6.36e-08

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 51.06  E-value: 6.36e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015    623 SYILKCLRLGVALHHGALPTAYRKEIERLLREGILKVTISSPTLAQGLNL-SATAVVMHSLYRHgemikVSEFKNVIGRA 701
Cdd:smart00490    4 AELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLpGVDLVIIYDLPWS-----PASYIQRIGRA 78

                    ...
gi 695751015    702 GRA 704
Cdd:smart00490   79 GRA 81
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
323-472 1.01e-07

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: 53.74  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  323 DNLVVSLPTSAGKTrIAEL-----SILRCLAGGRR----AIVVTPLRALSAQ--TEATLQRTFGPLGKTISAlygsIGVS 391
Cdd:cd17964    33 DDVLARAKTGTGKT-LAFLlpaiqSLLNTKPAGRRsgvsALIISPTRELALQiaAEAKKLLQGLRKLRVQSA----VGGT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  392 GFDEDAIR----GRDIVVATPEKLDFALRNDPSL--LDDVGLLVFDEG-HMIGSG-EREVRyevQIQRLLRRKDADQRRI 463
Cdd:cd17964   108 SRRAELNRlrrgRPDILVATPGRLIDHLENPGVAkaFTDLDYLVLDEAdRLLDMGfRPDLE---QILRHLPEKNADPRQT 184

                  ....*....
gi 695751015  464 VCLSAILPD 472
Cdd:cd17964   185 LLFSATVPD 193
DEXHc_RLR-3 cd18075
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ...
306-463 3.67e-07

DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of genetics and physiology 2 or LGP2 and DHX58) appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. RLR-3 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. RNA binding is required for RLR-3-mediated enhancement of MDA5 activation. RLR-3 end-binding may promote nucleation of MDA5 oligomerization on dsRNA. RLR-3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350833 [Multi-domain]  Cd Length: 200  Bit Score: 52.17  E-value: 3.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  306 DLWPSQIEAASRAVnQTDNLVVSLPTSAGKTRIAELSILRCL---AGGRRAIVVTPLRALSAQteatLQRTFGPLGK--T 380
Cdd:cd18075     2 ELHGYQWEVVAPAL-RGKNSIIWLPTGAGKTRAAVYVARRHLetkRGAKVAVLVNKVHLVDQH----LEKEFHVLLDkyT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  381 ISALYGSIGVSGFDEDAIRGRDIVVATPEKLDFALRNDPS----LLDDVGLLVFDEGHMIgsgEREVRYEVQIQRLLRRK 456
Cdd:cd18075    77 VTAISGDSSHKCFFGQLARGSDVVICTAQILQNALLSGEEeahvELTDFSLLVIDECHHT---HKEAVYNKIMLSYLEKK 153

                  ....*..
gi 695751015  457 DADQRRI 463
Cdd:cd18075   154 LSRQGDL 160
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
307-468 1.21e-06

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: 49.89  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  307 LWPSQIEAAsRAVNQTDNLVVSLPTSAGKTRIAELSILRCLAG--GRRAIVVTPLRALsAQTEatLQRtfgpLGKTISAL 384
Cdd:cd17923     1 LYSHQAEAI-EAARAGRSVVVTTGTASGKSLCYQLPILEALLRdpGSRALYLYPTKAL-AQDQ--LRS----LRELLEQL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  385 YGSIGVSGFD--------EDAIRGR-DIVVATPEKLDFAL----RNDPSLLDDVGLLVFDEGHM----IGSgerEVRYEV 447
Cdd:cd17923    73 GLGIRVATYDgdtpreerRAIIRNPpRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEAHTyrgvFGS---HVALLL 149
                         170       180
                  ....*....|....*....|..
gi 695751015  448 -QIQRLLRRKDADQrRIVCLSA 468
Cdd:cd17923   150 rRLRRLCRRYGADP-QFILTSA 170
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
288-436 6.41e-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: 48.30  E-value: 6.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  288 VLRELFiGLLARRPraevdlwpSQIEAASRAVNQTDNLVVsLPTSAGKTRIAEL--SILRCLaggrrAIVVTPLRAL-SA 364
Cdd:cd17920     3 ILKEVF-GYDEFRP--------GQLEAINAVLAGRDVLVV-MPTGGGKSLCYQLpaLLLDGV-----TLVVSPLISLmQD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  365 QTEAtLQRtfgpLGKTISALYGSIGVSGFDEDAIRGR----DIVVATPEKL---DF--ALRNDPSlLDDVGLLVFDEGHM 435
Cdd:cd17920    68 QVDR-LQQ----LGIRAAALNSTLSPEEKREVLLRIKngqyKLLYVTPERLlspDFleLLQRLPE-RKRLALIVVDEAHC 141

                  .
gi 695751015  436 I 436
Cdd:cd17920   142 V 142
DEXHc_DDX60 cd18025
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ...
318-488 1.29e-05

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: 47.36  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  318 AVNQTDNLVVSLPTSAGKTRIAELSILRCLAGGRRAIVV--TPLRALSAQTEATLQRTFG----PLGKTISALYGsigvS 391
Cdd:cd18025    12 IVDRRESALIVAPTSSGKTFISYYCMEKVLRESDDGVVVyvAPTKALVNQVVAEVYARFSkkypPSGKSLWGVFT----R 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  392 GFDEDAIRGRDIVVATPEKLDFAL--RNDPSLLDDVGLLVFDEGHMIGSGEREVRYEvqiqRLLRRKDADqrrIVCLSAI 469
Cdd:cd18025    88 DYRHNNPMNCQVLITVPECLEILLlsPHNASWVPRIKYVIFDEIHSIGQSEDGAVWE----QLLLLIPCP---FLALSAT 160
                         170
                  ....*....|....*....
gi 695751015  470 LPDgdqMEDFSAWLRRDQP 488
Cdd:cd18025   161 IGN---PQKFHEWLQSVQR 176
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
309-432 2.08e-05

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 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: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 46.86  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  309 PSQIEAAS--RAVNQTDnLVVSLPTSAGKTRIAELSILRCL------AGGRRAIVVTPLRALSAQTEATLQR--TFGPLg 378
Cdd:cd17947    13 PTPIQAAAipLALLGKD-ICASAVTGSGKTAAFLLPILERLlyrpkkKAATRVLVLVPTRELAMQCFSVLQQlaQFTDI- 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 695751015  379 kTISALYGSIGVSGfDEDAIRGR-DIVVATPEKLDFALRNDPSL-LDDVGLLVFDE 432
Cdd:cd17947    91 -TFALAVGGLSLKA-QEAALRARpDIVIATPGRLIDHLRNSPSFdLDSIEILVLDE 144
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
331-480 2.43e-05

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: 46.99  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  331 TSAGKTRIAELSILRCL--------AGGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISALYGSIGVSGFDEDAIRGRD 402
Cdd:cd17953    58 TGSGKTLAFLLPMFRHIkdqrpvkpGEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAE 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  403 IVVATPEKL-DFALRNDPSL--LDDVGLLVFDEG-HMIGSGerevrYEVQIQRLLR--RKDadqRRIVCLSAILPdgDQM 476
Cdd:cd17953   138 IVVCTPGRMiDILTANNGRVtnLRRVTYVVLDEAdRMFDMG-----FEPQIMKIVNniRPD---RQTVLFSATFP--RKV 207

                  ....
gi 695751015  477 EDFS 480
Cdd:cd17953   208 EALA 211
DEADc_DDX43_DDX53 cd17958
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ...
309-473 2.44e-05

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: 46.69  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  309 PSQIEA-ASRAVNQTDNLVVSLPTSAGKT---------RIAELSILRCLAGGRRAIVVTPLRALSAQTEATLQRtFGPLG 378
Cdd:cd17958    13 PSPIQSqAWPIILQGIDLIGVAQTGTGKTlayllpgfiHLDLQPIPREQRNGPGVLVLTPTRELALQIEAECSK-YSYKG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  379 KTISALYGSIGVSGFDEDAIRGRDIVVATPEKLDFALRNDPSLLDDVGLLVFDEG-HMIGSGerevrYEVQIQRLLRRKD 457
Cdd:cd17958    92 LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEAdRMLDMG-----FEPQIRKILLDIR 166
                         170
                  ....*....|....*.
gi 695751015  458 ADqRRIVCLSAILPDG 473
Cdd:cd17958   167 PD-RQTIMTSATWPDG 181
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
352-476 2.44e-05

DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. 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. DDX3 and DDX4 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: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 46.71  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  352 RAIVVTPLRALSAQT--EAT--LQRTfgplGKTISALYGSIGVSGFDEDAIRGRDIVVATPEKL-DFALRNDPSlLDDVG 426
Cdd:cd17967    80 SALILAPTRELAIQIyeEARkfSYRS----GVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLvDFIERGRIS-LSSIK 154
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 695751015  427 LLVFDEG-HMIGSGerevrYEVQIQRLLRRKD---ADQRRIVCLSAILPDGDQM 476
Cdd:cd17967   155 FLVLDEAdRMLDMG-----FEPQIRKIVEHPDmppKGERQTLMFSATFPREIQR 203
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
318-474 2.85e-05

DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to 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: 438711 [Multi-domain]  Cd Length: 174  Bit Score: 45.79  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  318 AVNQTDNLVVSLPTSAGKTRIAELSILRCLAGGRRAIVVTPLRALSAQTEAtlQRTFGPLGKTISALYGSiGVSGfdeDA 397
Cdd:cd17990    13 ALDAGGQVVLEAPPGAGKTTRVPLALLAELWIAGGKIIVLEPRRVAARAAA--RRLATLLGEAPGETVGY-RVRG---ES 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  398 IRGRD--IVVATPEKLDFALRNDPSlLDDVGLLVFDEGHmigsgEREVRYEV------QIQRLLRrkdaDQRRIVCLSAI 469
Cdd:cd17990    87 RVGRRtrVEVVTEGVLLRRLQRDPE-LSGVGAVILDEFH-----ERSLDADLalalllEVQQLLR----DDLRLLAMSAT 156

                  ....*
gi 695751015  470 LpDGD 474
Cdd:cd17990   157 L-DGD 160
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
623-704 4.78e-05

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: 43.74  E-value: 4.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015   623 SYILKCLRLGVALHHGALPTAYRKEIERLLREGILKVTISSPTLAQGLNL-SATAVVMHSLYRHgemikVSEFKNVIGRA 701
Cdd:pfam00271   31 ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLpDVDLVINYDLPWN-----PASYIQRIGRA 105

                   ...
gi 695751015   702 GRA 704
Cdd:pfam00271  106 GRA 108
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
324-473 5.71e-05

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 47.06  E-value: 5.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  324 NLVVSLPTSAGKTrIA-ELSILRCLAGGR----RAIVVTPLRALSAQTEATLQRTFGPLGKTISALYGsiGVS-GFDEDA 397
Cdd:COG0513    41 DVLGQAQTGTGKT-AAfLLPLLQRLDPSRprapQALILAPTRELALQVAEELRKLAKYLGLRVATVYG--GVSiGRQIRA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  398 I-RGRDIVVATPEKL-DFALRNdpSL-LDDVGLLVFDEG-HMIGSGEREvryevQIQRLLRRKDADqRRIVCLSAILPDG 473
Cdd:COG0513   118 LkRGVDIVVATPGRLlDLIERG--ALdLSGVETLVLDEAdRMLDMGFIE-----DIERILKLLPKE-RQTLLFSATMPPE 189
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
325-432 6.87e-05

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It 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: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 45.70  E-value: 6.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  325 LVVSLPTSAGKTRIAELSILRCLAGGR----RAIVVTPLRALSAQTEATLQRtfgpLGKTISALYGSIGVSGFDEDAIRG 400
Cdd:cd17956    39 LCVSAPTGSGKTLAYVLPIVQALSKRVvprlRALIVVPTKELVQQVYKVFES----LCKGTGLKVVSLSGQKSFKKEQKL 114
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 695751015  401 R------------DIVVATPEKLDFALRNDPS-LLDDVGLLVFDE 432
Cdd:cd17956   115 LlvdtsgrylsrvDILVATPGRLVDHLNSTPGfTLKHLRFLVIDE 159
PRK13766 PRK13766
Hef nuclease; Provisional
311-434 2.65e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 45.25  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  311 QIEAASRAVNQtDNLVVsLPTSAGKTRIAELSIL-RCLAGGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISALYGSIG 389
Cdd:PRK13766   20 QQLLAATALKK-NTLVV-LPTGLGKTAIALLVIAeRLHKKGGKVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVS 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 695751015  390 VSGFDEDAIRGRdIVVATPEkldfALRNDpsL------LDDVGLLVFDEGH 434
Cdd:PRK13766   98 PEKRAELWEKAK-VIVATPQ----VIEND--LiagrisLEDVSLLIFDEAH 141
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
324-473 3.06e-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: 43.33  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  324 NLVVSLPTSAGKTRIAELSILRCLA--------GGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISA--LYGSIGVSGF 393
Cdd:cd17960    29 DVVVEAVTGSGKTLAFLIPVLEILLkrkanlkkGQVGALIISPTRELATQIYEVLQSFLEHHLPKLKCqlLIGGTNVEED 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  394 DEDAIRGR-DIVVATPEKLD--FALRNDPSLLDDVGLLVFDEghmigsGER--EVRYEVQIQRLLRR--KdadQRRIVCL 466
Cdd:cd17960   109 VKKFKRNGpNILVGTPGRLEelLSRKADKVKVKSLEVLVLDE------ADRllDLGFEADLNRILSKlpK---QRRTGLF 179

                  ....*..
gi 695751015  467 SAILPDG 473
Cdd:cd17960   180 SATQTDA 186
SF2_C_suv3 cd18805
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ...
625-703 3.13e-04

C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene encodes a DNA and RNA helicase, which is localized in mitochondria and is a subunit of the degradosome complex involved in regulation of RNA surveillance and turnover. SUV3 exhibits DNA and RNA-dependent ATPase, DNA and RNA-binding and DNA and RNA unwinding activities. SUV3 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: 350192 [Multi-domain]  Cd Length: 135  Bit Score: 42.16  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  625 ILKCLRLGVALHHGALPTAYRKEIERLLREG--ILKVTISSPTLAQGLNLSATAVVMHSLYRH-GEM---IKVSEFKNVI 698
Cdd:cd18805    37 IEKRTGLKCAVIYGALPPETRRQQARLFNDPesGYDVLVASDAIGMGLNLNIRRVIFSSLSKFdGNEmrpLSPSEVKQIA 116

                  ....*
gi 695751015  699 GRAGR 703
Cdd:cd18805   117 GRAGR 121
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
309-436 4.19e-04

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: 43.01  E-value: 4.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  309 PSQIEAASRAVNQTDNLVVsLPTSAGKTRIAEL-SILRCLAGGRRAIVVTPLRALSAQTEATLQRTFgPLGKTISALygS 387
Cdd:cd18018    15 PGQEEAIARLLSGRSTLVV-LPTGAGKSLCYQLpALLLRRRGPGLTLVVSPLIALMKDQVDALPRAI-KAAALNSSL--T 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 695751015  388 IGVSGFDEDAIRGR--DIVVATPEKL-DFALRNDPSLLDDVGLLVFDEGHMI 436
Cdd:cd18018    91 REERRRILEKLRAGevKILYVSPERLvNESFRELLRQTPPISLLVVDEAHCI 142
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
324-468 7.83e-04

DEAH-box helicase domain of FANCM; 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. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM 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: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 41.92  E-value: 7.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  324 NLVVSLPTSAGKTRIAELSIL---RCLAGGrRAIVVTPLRAL-SAQTEATLQRTFGPLGKTISaLYGSIGVSGfDEDAIR 399
Cdd:cd18033    18 NTLVALPTGLGKTFIAAVVMLnyyRWFPKG-KIVFMAPTKPLvSQQIEACYKITGIPSSQTAE-LTGSVPPTK-RAELWA 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695751015  400 GRDIVVATPEKLDFALRNDPSLLDDVGLLVFDEGHMiGSGEREvrYEVQIQRLLRRKdaDQRRIVCLSA 468
Cdd:cd18033    95 SKRVFFLTPQTLENDLKEGDCDPKSIVCLVIDEAHR-ATGNYA--YCQVVRELMRYN--SHFRILALTA 158
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
311-434 8.24e-04

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 41.39  E-value: 8.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  311 QIEA-----ASRAVNQTDNLVVsLPTSAGKTRIAELSILRCLAGGR--RAIVVTPLRALSAQTEATLQRTFGPlgktisa 383
Cdd:cd18032     5 QQEAiealeEAREKGQRRALLV-MATGTGKTYTAAFLIKRLLEANRkkRILFLAHREELLEQAERSFKEVLPD------- 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 695751015  384 lyGSIGVSGFDEDAIRGRDIVVATPEKLDFALRNDPSLLDDVGLLVFDEGH 434
Cdd:cd18032    77 --GSFGNLKGGKKKPDDARVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAH 125
DEADc_MRH4 cd17965
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ...
352-432 1.39e-03

DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 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: 350723 [Multi-domain]  Cd Length: 251  Bit Score: 41.98  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  352 RAIVVTPLRALSAQTEATLQRTFGPLGKTISALYGSIGVSGFD-EDAIRGR-DIVVATPEKLDFALRNDPSLLDDVGLLV 429
Cdd:cd17965   111 RSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRlQLAFKGRiDILVTTPGKLASLAKSRPKILSRVTHLV 190

                  ...
gi 695751015  430 FDE 432
Cdd:cd17965   191 VDE 193
DEADc_DDX23 cd17945
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ...
330-462 1.58e-03

DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 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: 350703 [Multi-domain]  Cd Length: 220  Bit Score: 41.54  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  330 PTSAGKT---------RIAELSILRCLAG--GRRAIVVTPLRALSAQTEATLQRTFGPLGKTISALYGsiGVSgFDEDAI 398
Cdd:cd17945    35 ETGSGKTaaflipllvYISRLPPLDEETKddGPYALILAPTRELAQQIEEETQKFAKPLGIRVVSIVG--GHS-IEEQAF 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695751015  399 R---GRDIVVATPEKLDFALRNDPSLLDDVGLLVFDEG-HMIGSGerevrYEVQIQRLLRRKDADQRR 462
Cdd:cd17945   112 SlrnGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEAdRMIDMG-----FEPQVTKILDAMPVSNKK 174
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
52-436 2.70e-03

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 41.75  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015   52 SFDLHSYAYGLLGLGLRLLESDGDPNQARIAFEQAATALESVMANGNREEADRDFHFLLAAASYHLAHLSARAYSLLAIV 131
Cdd:COG0553     1 LLLLLLLLALGALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  132 ADEANFSPIEHALTLLIRRDINSLRTRVYTFRLDGRGSDATITTFLQQHLTESIVADAAERDGKDFLFEGLNLALTDVFF 211
Cdd:COG0553    81 ALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  212 GAFSMFLLALDRGEYTLLEKAIAQLRENLDicgelnlipqwwvhRIAIHLLKDFWSNTFHEKVPLLPAGGVAPSWPVLRE 291
Cdd:COG0553   161 RLLLLALLLLALEALLLLGLLLALALLALL--------------ELALLAAEAELLLLLELLLELELLAEAAVDAFRLRR 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  292 LFIGLLARRPRAEVDLWPSQIEAASRAVNQTDN-----------LvvslptsaGKTRIAELSILRCLAGG--RRAIVVTP 358
Cdd:COG0553   227 LREALESLPAGLKATLRPYQLEGAAWLLFLRRLglgglladdmgL--------GKTIQALALLLELKERGlaRPVLIVAP 298
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695751015  359 LrALSAQTEATLQRtFGPLGKtISALYGSiGVSGFDEDAIRGRDIVVATpekLDFALRNDPSLLD-DVGLLVFDEGHMI 436
Cdd:COG0553   299 T-SLVGNWQRELAK-FAPGLR-VLVLDGT-RERAKGANPFEDADLVITS---YGLLRRDIELLAAvDWDLVILDEAQHI 370
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
324-442 3.06e-03

DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 40.09  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  324 NLVVSLPTSAGKTRIAELSILRCLAGGRRAIVVTPLRALSAQTEATLQRTFGPLgkTISALYGsigvsGFDEDAIRGRDI 403
Cdd:cd17918    38 DRLLSGDVGSGKTLVALGAALLAYKNGKQVAILVPTEILAHQHYEEARKFLPFI--NVELVTG-----GTKAQILSGISL 110
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 695751015  404 VVATPekldfALRNDPSLLDDVGLLVFDEGHMIGSGERE 442
Cdd:cd17918   111 LVGTH-----ALLHLDVKFKNLDLVIVDEQHRFGVAQRE 144
DEXHc_TRCF cd17991
DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair ...
334-442 3.64e-03

DEXH/Q-box helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350749 [Multi-domain]  Cd Length: 193  Bit Score: 39.86  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  334 GKTRIAELSILRCLAGGRRAIVVTPLRALSAQTEATLQRTFGPLGKTISALYGSIG-------VSGFDEDAIrgrDIVVA 406
Cdd:cd17991    48 GKTEVAMRAAFKAVLSGKQVAVLVPTTLLAQQHYETFKERFANFPVNVELLSRFTTaaeqreiLEGLKEGKV---DIVIG 124
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 695751015  407 TpekldFALRNDPSLLDDVGLLVFDEGHMIGSGERE 442
Cdd:cd17991   125 T-----HRLLSKDVEFKNLGLLIIDEEQRFGVKQKE 155
DEXHc_RLR-2 cd18074
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma ...
307-461 4.45e-03

DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma differentiation-associated protein 5 or Mda5 and IFIH1) is a viral double-stranded RNA (dsRNA) receptor that shares sequence similarity and signaling pathways with RIG-I, yet plays essential functions in antiviral immunity through distinct specificity for viral RNA. RLR-2 recognizes the internal duplex structure, whereas RIG-I recognizes the terminus of dsRNA. RLR-2 uses direct protein-protein contacts to stack along dsRNA in a head-to-tail arrangement. The signaling domain (tandem CARD), which decorates the outside of the core RLR-2 filament, also has an intrinsic propensity to oligomerize into an elongated structure that activates the signaling adaptor, MAVS. RLR-2 uses long dsRNA as a signaling platform to cooperatively assemble the core filament, which in turn promotes stochastic assembly of the tandem CARD oligomers for signaling. LGP2 appears to positively and negatively regulate RLR-2 and RIG-I signaling, respectively. RLR-2 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: 350832 [Multi-domain]  Cd Length: 216  Bit Score: 39.84  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  307 LWPSQIEAASRAVNqTDNLVVSLPTSAGKTR----IAELSILRCLAGGRRAIVVTPLRALSAqTEATLQRTFGPLGKTis 382
Cdd:cd18074     3 LRDYQMEVAKPALE-GKNIIICLPTGSGKTRvavyITKDHLDKKRKASEPGKVIVLVNKVPL-VEQHYRKEFNPFLKH-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  383 aLYGSIGVSGFDE------DAIRGRDIVVATPEKLDFALRN-----DPSL-LDDVGLLVFDEGHMIgsgEREVRYEVQIQ 450
Cdd:cd18074    79 -WYQVIGLSGDSQlkisfpEVVKRYDVIICTAQILENSLLNateeeDEGVqLSDFSLIIIDECHHT---QKEAVYNNIMR 154
                         170
                  ....*....|.
gi 695751015  451 RLLRRKDADQR 461
Cdd:cd18074   155 RYLKQKIKNRK 165
DEXDc_ComFA cd17925
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon ...
313-421 4.65e-03

DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon protein 1) is part of the complex mediating the binding and uptake of single-stranded DNA. ComFA is required for DNA uptake but not for binding. It 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: 350683 [Multi-domain]  Cd Length: 143  Bit Score: 38.82  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  313 EAASRAVNQTDNLVVSLPTSAGKTRIAELSILRCLAGGRRAIVVTP----LRALSAQteatLQRTFgpLGKTISALYGSi 388
Cdd:cd17925     7 NALVETIDAKEDLLVWAVTGAGKTEMLFPAIAQALRQGGRVAIASPridvCLELAPR----LKAAF--PGAAIVLLHGG- 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 695751015  389 gvsgfDEDAIRGRDIVVATPEKL----------------DFALRNDPSL 421
Cdd:cd17925    80 -----SEDQYQRSPLVIATTHQLlrfyrafdlliidevdAFPYAGDPML 123
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
633-666 5.41e-03

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: 38.78  E-value: 5.41e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 695751015  633 VALHHGALPTAYRKEIERLLREGILKVTISSPTL 666
Cdd:cd18796    71 IALHHGSLSRELREEVEAALKRGDLKVVVATSSL 104
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
311-434 5.97e-03

DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain]  Cd Length: 202  Bit Score: 39.42  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  311 QIEAASRAVnQTDNLVVSLPTSAGKTRIAeLSI----LRCLAGGRRAIVVTPLRALSA--QTEATLQRTFGPLGKTISAL 384
Cdd:cd18073     7 QLELALPAM-KGKNTIICAPTGCGKTFVS-LLIcehhLKKFPQGQKGKVVFFATKVPVyeQQKSVFSKYFERHGYRVTGI 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 695751015  385 YGSIGVSGFDEDAIRGRDIVVATPEKLDFALRND--PSlLDDVGLLVFDEGH 434
Cdd:cd18073    85 SGATAENVPVEQIIENNDIIILTPQILVNNLKKGtiPS-LSIFTLMIFDECH 135
PRK13767 PRK13767
ATP-dependent helicase; Provisional
324-471 9.66e-03

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 40.25  E-value: 9.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  324 NLVVSLPTSAGKTRIAELSILRCLAG-GRR--------AIVVTPLRALSAQTEATLQRtfgPLgKTISALYGSIGVsGFD 394
Cdd:PRK13767   49 NVLISSPTGSGKTLAAFLAIIDELFRlGREgeledkvyCLYVSPLRALNNDIHRNLEE---PL-TEIREIAKERGE-ELP 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695751015  395 E--DAIRGRD---------------IVVATPEKLDFALrNDPSL---LDDVGLLVFDEGHMIGSGEREVRYEVQIQRLLR 454
Cdd:PRK13767  124 EirVAIRTGDtssyekqkmlkkpphILITTPESLAILL-NSPKFrekLRTVKWVIVDEIHSLAENKRGVHLSLSLERLEE 202
                         170
                  ....*....|....*..
gi 695751015  455 RKDADQRRIVCLSAILP 471
Cdd:PRK13767  203 LAGGEFVRIGLSATIEP 219
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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