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Conserved domains on  [gi|1370452148|ref|XP_024309476|]
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probable ATP-dependent DNA helicase HFM1 isoform X15 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
280-488 2.67e-130

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: 386.71  E-value: 2.67e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 280 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEV-PLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIG 358
Cdd:cd18023     1 YFNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERnPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 359 LNCKELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDN-SLVQLVRLFLIDEVHIVKdENRGPTLEVVVSRMKTVQS 437
Cdd:cd18023    81 LSCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIK-ENRGATLEVVVSRMKTLSS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370452148 438 VSQTlkNTSTAIPMRFVAVSATIPNAEDIAEWLSDGerPAVCLKMDESHRP 488
Cdd:cd18023   160 SSEL--RGSTVRPMRFVAVSATIPNIEDLAEWLGDN--PAGCFSFGESFRP 206
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
264-785 6.86e-101

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


:

Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 322.23  E-value: 6.86e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 264 VTEIP-AKFRSIFKEFPY--FNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIK 340
Cdd:COG1204     3 VAELPlEKVIEFLKERGIeeLYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN------GGKALYIVPLR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 341 ALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRK---WRDNslvqlVRLFLIDEVHIVK 417
Cdd:COG1204    77 ALASEKYREFKRDFEELGIKVGVSTGDYDSDDE-WLGRYDILVATPEKLDSLLRNgpsWLRD-----VDLVVVDEAHLID 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 418 DENRGPTLEVVVSRMKTVqsvsqtlkntstAIPMRFVAVSATIPNAEDIAEWLsdgERPAVclkmDESHRPVKLQKVVLg 497
Cdd:COG1204   151 DESRGPTLEVLLARLRRL------------NPEAQIVALSATIGNAEEIAEWL---DAELV----KSDWRPVPLNEGVL- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 498 fpcSSNQTEF--KFDLTLNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVR---- 571
Cdd:COG1204   211 ---YDGVLRFddGSRRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLevse 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 572 ----DSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTmHYAGGlfEEYSETD 647
Cdd:COG1204   288 ethtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-KRGGM--VPIPVLE 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 648 ILQMIGRAGRPQFDTTATAVIMTR-LSTRDKYIQMLACRDT--VESSLH--RHLIEHLNAEIVLHTITDVNIAVEWIRST 722
Cdd:COG1204   365 FKQMAGRAGRPGYDPYGEAILVAKsSDEADELFERYILGEPepIRSKLAneSALRTHLLALIASGFANSREELLDFLENT 444
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370452148 723 LLYIRAlknpshygfasglNKDGIEAKLQElclkNLNDLSSLDLIKMDEGvNFKPTvSAGHRV 785
Cdd:COG1204   445 FYAYQY-------------DKGDLEEVVDD----ALEFLLENGFIEEDGD-RLRAT-KLGKLV 488
 
Name Accession Description Interval E-value
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
280-488 2.67e-130

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: 386.71  E-value: 2.67e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 280 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEV-PLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIG 358
Cdd:cd18023     1 YFNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERnPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 359 LNCKELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDN-SLVQLVRLFLIDEVHIVKdENRGPTLEVVVSRMKTVQS 437
Cdd:cd18023    81 LSCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIK-ENRGATLEVVVSRMKTLSS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370452148 438 VSQTlkNTSTAIPMRFVAVSATIPNAEDIAEWLSDGerPAVCLKMDESHRP 488
Cdd:cd18023   160 SSEL--RGSTVRPMRFVAVSATIPNIEDLAEWLGDN--PAGCFSFGESFRP 206
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
264-785 6.86e-101

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 322.23  E-value: 6.86e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 264 VTEIP-AKFRSIFKEFPY--FNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIK 340
Cdd:COG1204     3 VAELPlEKVIEFLKERGIeeLYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN------GGKALYIVPLR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 341 ALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRK---WRDNslvqlVRLFLIDEVHIVK 417
Cdd:COG1204    77 ALASEKYREFKRDFEELGIKVGVSTGDYDSDDE-WLGRYDILVATPEKLDSLLRNgpsWLRD-----VDLVVVDEAHLID 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 418 DENRGPTLEVVVSRMKTVqsvsqtlkntstAIPMRFVAVSATIPNAEDIAEWLsdgERPAVclkmDESHRPVKLQKVVLg 497
Cdd:COG1204   151 DESRGPTLEVLLARLRRL------------NPEAQIVALSATIGNAEEIAEWL---DAELV----KSDWRPVPLNEGVL- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 498 fpcSSNQTEF--KFDLTLNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVR---- 571
Cdd:COG1204   211 ---YDGVLRFddGSRRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLevse 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 572 ----DSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTmHYAGGlfEEYSETD 647
Cdd:COG1204   288 ethtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-KRGGM--VPIPVLE 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 648 ILQMIGRAGRPQFDTTATAVIMTR-LSTRDKYIQMLACRDT--VESSLH--RHLIEHLNAEIVLHTITDVNIAVEWIRST 722
Cdd:COG1204   365 FKQMAGRAGRPGYDPYGEAILVAKsSDEADELFERYILGEPepIRSKLAneSALRTHLLALIASGFANSREELLDFLENT 444
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370452148 723 LLYIRAlknpshygfasglNKDGIEAKLQElclkNLNDLSSLDLIKMDEGvNFKPTvSAGHRV 785
Cdd:COG1204   445 FYAYQY-------------DKGDLEEVVDD----ALEFLLENGFIEEDGD-RLRAT-KLGKLV 488
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
487-671 3.81e-60

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: 200.47  E-value: 3.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 487 RPVKLQKVVLGFPCSSNQTEFKFDLT--LNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVkdakfimtveqkqrlq 564
Cdd:cd18795     1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 565 kyaysvrdsklrdilkdGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYS 644
Cdd:cd18795    65 -----------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELS 127
                         170       180
                  ....*....|....*....|....*..
gi 1370452148 645 ETDILQMIGRAGRPQFDTTATAVIMTR 671
Cdd:cd18795   128 PLEYLQMIGRAGRPGFDTRGEAIIMTK 154
PRK02362 PRK02362
ATP-dependent DNA helicase;
285-669 1.97e-51

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 192.09  E-value: 1.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 285 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEkFGPIGLNCKEL 364
Cdd:PRK02362   28 QAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIAR------GGKALYIVPLRALASEKFEEFER-FEELGVRVGIS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 365 TGDTVMDDLFeIQHAHIIMTTPEKWDSMTRK---W-RDNSLVqlvrlfLIDEVHIVKDENRGPTLEVVVSRMKTVQSVSQ 440
Cdd:PRK02362  101 TGDYDSRDEW-LGDNDIIVATSEKVDSLLRNgapWlDDITCV------VVDEVHLIDSANRGPTLEVTLAKLRRLNPDLQ 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 441 TlkntstaipmrfVAVSATIPNAEDIAEWLsDGERpavclkMDESHRPVKLQKVVL---GFPCSSNQTEFKF---DLTLN 514
Cdd:PRK02362  174 V------------VALSATIGNADELADWL-DAEL------VDSEWRPIDLREGVFyggAIHFDDSQREVEVpskDDTLN 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 515 YkiasVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVRDS-------KLRDILKDGAAYHH 587
Cdd:PRK02362  235 L----VLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVsdtetskDLADCVAKGAAFHH 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 588 AGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGL------FEEYSetdilQMIGRAGRPQFD 661
Cdd:PRK02362  311 AGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAgmqpipVLEYH-----QMAGRAGRPGLD 385

                  ....*...
gi 1370452148 662 TTATAVIM 669
Cdd:PRK02362  386 PYGEAVLL 393
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
285-669 5.65e-50

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 188.22  E-value: 5.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 285 QSKAFDDLLyTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEKFGP--IGLnck 362
Cdd:COG4581    30 QEEAILALE-AGRSVLVAAPTGSGKTLVAEFAIFLALAR------GRRSFYTAPIKALSNQKFFDLVERFGAenVGL--- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 363 eLTGDTVmddlfEIQHA-HIIMTTpEKWDSMTrkWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVsrmktvqsvsqt 441
Cdd:COG4581   100 -LTGDAS-----VNPDApIVVMTT-EILRNML--YREGADLEDVGVVVMDEFHYLADPDRGWVWEEPI------------ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 442 lkntsTAIP--MRFVAVSATIPNAEDIAEWLSD--GErpavCLKMDESHRPVKLQKVVLGFPCSSNQTEFKFDLTLNYKI 517
Cdd:COG4581   159 -----IHLParVQLVLLSATVGNAEEFAEWLTRvrGE----TAVVVSEERPVPLEFHYLVTPRLFPLFRVNPELLRPPSR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 518 ASVIQM--YSDQKPTLVFCATRKGVQQAASVLVkdAKFIMTVEQKQRLQKYA-------YSVRDSKLRDILKDGAAYHHA 588
Cdd:COG4581   230 HEVIEEldRGGLLPAIVFIFSRRGCDEAAQQLL--SARLTTKEERAEIREAIdefaedfSVLFGKTLSRLLRRGIAVHHA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 589 GMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVI 668
Cdd:COG4581   308 GMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLTAREFHQIAGRAGRRGIDTEGHVVV 387

                  .
gi 1370452148 669 M 669
Cdd:COG4581   388 L 388
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
284-466 8.87e-35

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: 130.05  E-value: 8.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 284 IQSKAFDdLLYTDRNFVICAPTGSGKTVVFELAItrlLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLN-CK 362
Cdd:pfam00270   3 IQAEAIP-AILEGRDVLVQAPTGSGKTLAFLLPA---LEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKvAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 363 ELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRdnsLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTvqsvsqtl 442
Cdd:pfam00270  79 LLGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-------- 147
                         170       180
                  ....*....|....*....|....*
gi 1370452148 443 kntstaiPMRFVAVSATIP-NAEDI 466
Cdd:pfam00270 148 -------KRQILLLSATLPrNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
276-470 4.75e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 106.42  E-value: 4.75e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  276 KEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQRFDDWKEKFG 355
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGK----GGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  356 PIGLN-CKELTGDTVMDDLFEIQH--AHIIMTTPEKWDSMTRKwrDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRM 432
Cdd:smart00487  80 SLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1370452148  433 KTVQsvsqtlkntstaipmRFVAVSATIPNAEDIAEWL 470
Cdd:smart00487 158 PKNV---------------QLLLLSATPPEEIENLLEL 180
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
301-676 1.92e-13

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 74.58  E-value: 1.92e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  301 ICAPTGSGKTVV-FELAITRLLME------VPLPWLNIKIVYMAPIKALCS--QR--------FDDWKEKFGPIGLNCKE 363
Cdd:PRK09751     1 VIAPTGSGKTLAaFLYALDRLFREggedtrEAHKRKTSRILYISPIKALGTdvQRnlqiplkgIADERRRRGETEVNLRV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  364 --LTGDTVMDDLFEI--QHAHIIMTTPEKWDSM-TRKWRDNslVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMktvqsv 438
Cdd:PRK09751    81 giRTGDTPAQERSKLtrNPPDILITTPESLYLMlTSRARET--LRGVETVIIDEVHAVAGSKRGAHLALSLERL------ 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  439 sQTLKNTstaiPMRFVAVSATIPNAEDIAEWLSdGERPAVCLKMDESHRPvKLQKVV-----LGFPCSSNQTEFKFDLTL 513
Cdd:PRK09751   153 -DALLHT----SAQRIGLSATVRSASDVAAFLG-GDRPVTVVNPPAMRHP-QIRIVVpvanmDDVSSVASGTGEDSHAGR 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  514 NYKI-----ASVIQMYSDQKPTLVFCATRkGVQQAASVLVKD---AKFIMTVEQKQRLQKYAYSVRDSKLRDILKDG--A 583
Cdd:PRK09751   226 EGSIwpyieTGILDEVLRHRSTIVFTNSR-GLAEKLTARLNElyaARLQRSPSIAVDAAHFESTSGATSNRVQSSDVfiA 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  584 AYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIK--STMHYAGGlfeeysetdiLQMIGRAGRpQFD 661
Cdd:PRK09751   305 RSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQvaTPLSVASG----------LQRIGRAGH-QVG 373
                          410
                   ....*....|....*
gi 1370452148  662 TTATAVIMTRlSTRD 676
Cdd:PRK09751   374 GVSKGLFFPR-TRRD 387
HELICc smart00490
helicase superfamily c-terminal domain;
579-658 9.81e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 64.16  E-value: 9.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  579 LKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIKSTmhyagglfeEYSETDILQMIGRAGR 657
Cdd:smart00490  10 LGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL---------PWSPASYIQRIGRAGR 80

                   .
gi 1370452148  658 P 658
Cdd:smart00490  81 A 81
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
516-657 7.52e-10

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: 56.84  E-value: 7.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 516 KIASVIQMYSDQKP--TLVFCATRKGVqqaasvlvkDAKFImtveqkqrLQKYAYSVrdsklrdilkdgaAYHHAGMELS 593
Cdd:pfam00271   2 KLEALLELLKKERGgkVLIFSQTKKTL---------EAELL--------LEKEGIKV-------------ARLHGDLSQE 51
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370452148 594 DRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIkstmhyagglFE-EYSETDILQMIGRAGR 657
Cdd:pfam00271  52 EREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN----------YDlPWNPASYIQRIGRAGR 107
 
Name Accession Description Interval E-value
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
280-488 2.67e-130

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: 386.71  E-value: 2.67e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 280 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEV-PLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIG 358
Cdd:cd18023     1 YFNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKERnPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 359 LNCKELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDN-SLVQLVRLFLIDEVHIVKdENRGPTLEVVVSRMKTVQS 437
Cdd:cd18023    81 LSCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIK-ENRGATLEVVVSRMKTLSS 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370452148 438 VSQTlkNTSTAIPMRFVAVSATIPNAEDIAEWLSDGerPAVCLKMDESHRP 488
Cdd:cd18023   160 SSEL--RGSTVRPMRFVAVSATIPNIEDLAEWLGDN--PAGCFSFGESFRP 206
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
264-785 6.86e-101

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 322.23  E-value: 6.86e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 264 VTEIP-AKFRSIFKEFPY--FNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIK 340
Cdd:COG1204     3 VAELPlEKVIEFLKERGIeeLYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLN------GGKALYIVPLR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 341 ALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRK---WRDNslvqlVRLFLIDEVHIVK 417
Cdd:COG1204    77 ALASEKYREFKRDFEELGIKVGVSTGDYDSDDE-WLGRYDILVATPEKLDSLLRNgpsWLRD-----VDLVVVDEAHLID 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 418 DENRGPTLEVVVSRMKTVqsvsqtlkntstAIPMRFVAVSATIPNAEDIAEWLsdgERPAVclkmDESHRPVKLQKVVLg 497
Cdd:COG1204   151 DESRGPTLEVLLARLRRL------------NPEAQIVALSATIGNAEEIAEWL---DAELV----KSDWRPVPLNEGVL- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 498 fpcSSNQTEF--KFDLTLNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVR---- 571
Cdd:COG1204   211 ---YDGVLRFddGSRRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLevse 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 572 ----DSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTmHYAGGlfEEYSETD 647
Cdd:COG1204   288 ethtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDT-KRGGM--VPIPVLE 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 648 ILQMIGRAGRPQFDTTATAVIMTR-LSTRDKYIQMLACRDT--VESSLH--RHLIEHLNAEIVLHTITDVNIAVEWIRST 722
Cdd:COG1204   365 FKQMAGRAGRPGYDPYGEAILVAKsSDEADELFERYILGEPepIRSKLAneSALRTHLLALIASGFANSREELLDFLENT 444
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370452148 723 LLYIRAlknpshygfasglNKDGIEAKLQElclkNLNDLSSLDLIKMDEGvNFKPTvSAGHRV 785
Cdd:COG1204   445 FYAYQY-------------DKGDLEEVVDD----ALEFLLENGFIEEDGD-RLRAT-KLGKLV 488
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
280-474 4.21e-69

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: 225.60  E-value: 4.21e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 280 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVplpwlNIKIVYMAPIKALCSQRFDDWKEKFGPIGL 359
Cdd:cd17921     1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALATS-----GGKAVYIAPTRALVNQKEADLRERFGPLGK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 360 NCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRKWRDNsLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVQsvs 439
Cdd:cd17921    76 NVGLLTGDPSVNKL-LLAEADILVATPEKLDLLLRNGGER-LIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRIN--- 150
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1370452148 440 qtlkntstaIPMRFVAVSATIPNAEDIAEWLSDGE 474
Cdd:cd17921   151 ---------KNARFVGLSATLPNAEDLAEWLGVED 176
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
487-671 3.81e-60

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: 200.47  E-value: 3.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 487 RPVKLQKVVLGFPCSSNQTEFKFDLT--LNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVkdakfimtveqkqrlq 564
Cdd:cd18795     1 RPVPLEEYVLGFNGLGIKLRVDVMNKfdSDIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA---------------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 565 kyaysvrdsklrdilkdGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYS 644
Cdd:cd18795    65 -----------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRELS 127
                         170       180
                  ....*....|....*....|....*..
gi 1370452148 645 ETDILQMIGRAGRPQFDTTATAVIMTR 671
Cdd:cd18795   128 PLEYLQMIGRAGRPGFDTRGEAIIMTK 154
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
278-470 8.78e-60

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: 200.95  E-value: 8.78e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 278 FPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQRFDDWKEKFGP- 356
Cdd:cd18021     1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNP----KGRAVYIAPMQELVDARYKDWRAKFGPl 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 357 IGLNCKELTGDTVMdDLFEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDENrGPTLEVVVSRMKTVQ 436
Cdd:cd18021    77 LGKKVVKLTGETST-DLKLLAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLIGGEN-GPVYEVVVSRMRYIS 154
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1370452148 437 svSQTLKntstaiPMRFVAVSATIPNAEDIAEWL 470
Cdd:cd18021   155 --SQLEK------PIRIVGLSSSLANARDVGEWL 180
DEXHc_ASCC3_2 cd18022
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
280-470 3.30e-58

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: 196.44  E-value: 3.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 280 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQRFDDWKEKF-GPIG 358
Cdd:cd18022     1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAFNKYP----GSKVVYIAPLKALVRERVDDWKKRFeEKLG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 359 LNCKELTGDtVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDEnRGPTLEVVVSRMKTVQSV 438
Cdd:cd18022    77 KKVVELTGD-VTPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGSD-RGPVLEVIVSRMNYISSQ 154
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1370452148 439 sqtlkntsTAIPMRFVAVSATIPNAEDIAEWL 470
Cdd:cd18022   155 --------TEKPVRLVGLSTALANAGDLANWL 178
PRK02362 PRK02362
ATP-dependent DNA helicase;
285-669 1.97e-51

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 192.09  E-value: 1.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 285 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEkFGPIGLNCKEL 364
Cdd:PRK02362   28 QAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIAR------GGKALYIVPLRALASEKFEEFER-FEELGVRVGIS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 365 TGDTVMDDLFeIQHAHIIMTTPEKWDSMTRK---W-RDNSLVqlvrlfLIDEVHIVKDENRGPTLEVVVSRMKTVQSVSQ 440
Cdd:PRK02362  101 TGDYDSRDEW-LGDNDIIVATSEKVDSLLRNgapWlDDITCV------VVDEVHLIDSANRGPTLEVTLAKLRRLNPDLQ 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 441 TlkntstaipmrfVAVSATIPNAEDIAEWLsDGERpavclkMDESHRPVKLQKVVL---GFPCSSNQTEFKF---DLTLN 514
Cdd:PRK02362  174 V------------VALSATIGNADELADWL-DAEL------VDSEWRPIDLREGVFyggAIHFDDSQREVEVpskDDTLN 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 515 YkiasVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVRDS-------KLRDILKDGAAYHH 587
Cdd:PRK02362  235 L----VLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVsdtetskDLADCVAKGAAFHH 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 588 AGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGL------FEEYSetdilQMIGRAGRPQFD 661
Cdd:PRK02362  311 AGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGAgmqpipVLEYH-----QMAGRAGRPGLD 385

                  ....*...
gi 1370452148 662 TTATAVIM 669
Cdd:PRK02362  386 PYGEAVLL 393
PRK00254 PRK00254
ski2-like helicase; Provisional
285-671 9.62e-51

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 190.03  E-value: 9.62e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 285 QSKAFDDLLYTDRNFVICAPTGSGKTVVFELAIT-RLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEkFGPIGLNCKE 363
Cdd:PRK00254   28 QAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVnKLLRE------GGKAVYLVPLKALAEEKYREFKD-WEKLGLRVAM 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 364 LTGDTVMDDLFeIQHAHIIMTTPEKWDSMTRkwRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVQSVsqtlk 443
Cdd:PRK00254  101 TTGDYDSTDEW-LGKYDIIIATAEKFDSLLR--HGSSWIKDVKLVVADEIHLIGSYDRGATLEMILTHMLGRAQI----- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 444 ntstaipmrfVAVSATIPNAEDIAEWLSdgerpAVCLKMDesHRPVKLQKVV--LGFPCSSNQTEFKFDLTLNykiASVI 521
Cdd:PRK00254  173 ----------LGLSATVGNAEELAEWLN-----AELVVSD--WRPVKLRKGVfyQGFLFWEDGKIERFPNSWE---SLVY 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 522 QMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVRDS----KLRDILKDGAAYHHAGMELSDRKV 597
Cdd:PRK00254  233 DAVKKGKGALVFVNTRRSAEKEALELAKKIKRFLTKPELRALKELADSLEENptneKLKKALRGGVAFHHAGLGRTERVL 312
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370452148 598 VEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVIMTR 671
Cdd:PRK00254  313 IEDAFREGLIKVITATPTLSAGINLPAFRVIIRDTKRYSNFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVAT 386
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
285-669 5.65e-50

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 188.22  E-value: 5.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 285 QSKAFDDLLyTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKEKFGP--IGLnck 362
Cdd:COG4581    30 QEEAILALE-AGRSVLVAAPTGSGKTLVAEFAIFLALAR------GRRSFYTAPIKALSNQKFFDLVERFGAenVGL--- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 363 eLTGDTVmddlfEIQHA-HIIMTTpEKWDSMTrkWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVsrmktvqsvsqt 441
Cdd:COG4581   100 -LTGDAS-----VNPDApIVVMTT-EILRNML--YREGADLEDVGVVVMDEFHYLADPDRGWVWEEPI------------ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 442 lkntsTAIP--MRFVAVSATIPNAEDIAEWLSD--GErpavCLKMDESHRPVKLQKVVLGFPCSSNQTEFKFDLTLNYKI 517
Cdd:COG4581   159 -----IHLParVQLVLLSATVGNAEEFAEWLTRvrGE----TAVVVSEERPVPLEFHYLVTPRLFPLFRVNPELLRPPSR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 518 ASVIQM--YSDQKPTLVFCATRKGVQQAASVLVkdAKFIMTVEQKQRLQKYA-------YSVRDSKLRDILKDGAAYHHA 588
Cdd:COG4581   230 HEVIEEldRGGLLPAIVFIFSRRGCDEAAQQLL--SARLTTKEERAEIREAIdefaedfSVLFGKTLSRLLRRGIAVHHA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 589 GMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVI 668
Cdd:COG4581   308 GMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVFTKLSKFDGERHRPLTAREFHQIAGRAGRRGIDTEGHVVV 387

                  .
gi 1370452148 669 M 669
Cdd:COG4581   388 L 388
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
264-470 3.77e-49

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: 172.55  E-value: 3.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 264 VTEIPAKFRSIFKEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNI-----KIVYMAP 338
Cdd:cd18019     1 IEELPDWAQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPDGTInldafKIVYIAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 339 IKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKD 418
Cdd:cd18019    81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKE-QISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370452148 419 EnRGPTLEVVVSRmkTVQSVSQTLKntstaiPMRFVAVSATIPNAEDIAEWL 470
Cdd:cd18019   160 D-RGPVLESIVAR--TIRQIEQTQE------YVRLVGLSATLPNYEDVATFL 202
PRK01172 PRK01172
ATP-dependent DNA helicase;
297-668 7.89e-43

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 166.21  E-value: 7.89e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 297 RNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKeKFGPIGLNCKELTGDtvMDDLFE- 375
Cdd:PRK01172   38 ENVIVSVPTAAGKTLIAYSAIYETFLA------GLKSIYIVPLRSLAMEKYEELS-RLRSLGMRVKISIGD--YDDPPDf 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 376 IQHAHIIMTTPEKWDSMTRkwRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVqsvsqtlkNTSTaipmRFVA 455
Cdd:PRK01172  109 IKRYDVVILTSEKADSLIH--HDPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSARYV--------NPDA----RILA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 456 VSATIPNAEDIAEWLSdgerpAVCLKmdESHRPVKLQKVVLGFPCSSNQTEFKFDLTLNYKIASVIQmysDQKPTLVFCA 535
Cdd:PRK01172  175 LSATVSNANELAQWLN-----ASLIK--SNFRPVPLKLGILYRKRLILDGYERSQVDINSLIKETVN---DGGQVLVFVS 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 536 TRKGVQQAASVLVK----DAKFIMTVEQKqrlqkyaySVRDSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLF 611
Cdd:PRK01172  245 SRKNAEDYAEMLIQhfpeFNDFKVSSENN--------NVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIV 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370452148 612 TTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVI 668
Cdd:PRK01172  317 ATPTLAAGVNLPARLVIVRDITRYGNGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYI 373
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
282-470 1.18e-41

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: 151.04  E-value: 1.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 282 NYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLME--VPLPWL---NIKIVYMAPIKALCSQRFDDWKEKFGP 356
Cdd:cd18020     3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQhvNQGGVIkkdDFKIVYIAPMKALAAEMVEKFSKRLAP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 357 IGLNCKELTGDTVMDDLfEIQHAHIIMTTPEKWDSMTRKWR-DNSLVQLVRLFLIDEVHIVKDEnRGPTLEVVVSR-MKT 434
Cdd:cd18020    83 LGIKVKELTGDMQLTKK-EIAETQIIVTTPEKWDVVTRKSSgDVALSQLVRLLIIDEVHLLHDD-RGPVIESLVARtLRQ 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370452148 435 VQSvSQTLkntstaipMRFVAVSATIPNAEDIAEWL 470
Cdd:cd18020   161 VES-TQSM--------IRIVGLSATLPNYLDVADFL 187
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
280-470 2.60e-39

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: 143.63  E-value: 2.60e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 280 YFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKeKFGPIGL 359
Cdd:cd18028     1 ELYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLE------GGKALYLVPLRALASEKYEEFK-KLEEIGL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 360 NCKELTGDTVMDDLFeIQHAHIIMTTPEKWDSMTR-KWrdnSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVqsv 438
Cdd:cd18028    74 KVGISTGDYDEDDEW-LGDYDIIVATYEKFDSLLRhSP---SWLRDVGVVVVDEIHLISDEERGPTLESIVARLRRL--- 146
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1370452148 439 sqtlkNTSTaipmRFVAVSATIPNAEDIAEWL 470
Cdd:cd18028   147 -----NPNT----QIIGLSATIGNPDELAEWL 169
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
284-466 8.87e-35

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: 130.05  E-value: 8.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 284 IQSKAFDdLLYTDRNFVICAPTGSGKTVVFELAItrlLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLN-CK 362
Cdd:pfam00270   3 IQAEAIP-AILEGRDVLVQAPTGSGKTLAFLLPA---LEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKvAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 363 ELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRdnsLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTvqsvsqtl 442
Cdd:pfam00270  79 LLGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-------- 147
                         170       180
                  ....*....|....*....|....*
gi 1370452148 443 kntstaiPMRFVAVSATIP-NAEDI 466
Cdd:pfam00270 148 -------KRQILLLSATLPrNLEDL 165
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
267-660 1.35e-26

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


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 116.53  E-value: 1.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 267 IPAKFRSIFK-EFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELA-ITRLLMEvplpwlNIKIVYMAPIKALCS 344
Cdd:COG1202   195 LPPELKDLLEgRGEELLPVQSLAVENGLLEGKDQLVVSATATGKTLIGELAgIKNALEG------KGKMLFLVPLVALAN 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 345 QRFDDWKEKFGPiGLNCKELTG---------DTVMDdlfeiqhAHIIMTTPEKWDSMTRKWRDNSLVQLVrlfLIDEVHI 415
Cdd:COG1202   269 QKYEDFKDRYGD-GLDVSIRVGasrirddgtRFDPN-------ADIIVGTYEGIDHALRTGRDLGDIGTV---VIDEVHM 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 416 VKDENRGPTLEVVVSRMKTVQSVSQtlkntstaipmrFVAVSATIPNAEDIAEWLSdgerpavcLKMDE-SHRPVKLQKV 494
Cdd:COG1202   338 LEDPERGHRLDGLIARLKYYCPGAQ------------WIYLSATVGNPEELAKKLG--------AKLVEyEERPVPLERH 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 495 VLgFpcssNQTEFKFDLtlnykIASVIQMYSDQKP-------TLVFCATRKgvqqaasvlvkdakfimtveqkqrlqkya 567
Cdd:COG1202   398 LT-F----ADGREKIRI-----INKLVKREFDTKSskgyrgqTIIFTNSRR----------------------------- 438
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 568 ysvRDSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKS-TMhyaGGlfEEYSET 646
Cdd:COG1202   439 ---RCHEIARALGYKAAPYHAGLDYGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSlAM---GI--EWLSVQ 510
                         410
                  ....*....|....
gi 1370452148 647 DILQMIGRAGRPQF 660
Cdd:COG1202   511 EFHQMLGRAGRPDY 524
DEXDc smart00487
DEAD-like helicases superfamily;
276-470 4.75e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 106.42  E-value: 4.75e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  276 KEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQRFDDWKEKFG 355
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGK----GGRVLVLVPTRELAEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  356 PIGLN-CKELTGDTVMDDLFEIQH--AHIIMTTPEKWDSMTRKwrDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRM 432
Cdd:smart00487  80 SLGLKvVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLEN--DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1370452148  433 KTVQsvsqtlkntstaipmRFVAVSATIPNAEDIAEWL 470
Cdd:smart00487 158 PKNV---------------QLLLLSATPPEEIENLLEL 180
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
285-657 2.82e-22

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: 102.61  E-value: 2.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 285 QSKAFDdLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCS---QRFDDWKEKFGPiGLNC 361
Cdd:COG1205    61 QAEAIE-AARAGKNVVIATPTASGKSLAYLLPVLEALLEDP----GATALYLYPTKALARdqlRRLRELAEALGL-GVRV 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 362 KELTGDTVMDDLFEI-QHAHIIMTTPEKWD-SM---TRKWRdnSLVQLVRLFLIDEVHIVkdenRGptleV-------VV 429
Cdd:COG1205   135 ATYDGDTPPEERRWIrEHPDIVLTNPDMLHyGLlphHTRWA--RFFRNLRYVVIDEAHTY----RG----VfgshvanVL 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 430 SRMKTVqsvsqtLKNTSTAipMRFVAVSATIPNAEDIAEWLSDgeRPAVCLkmDESHRPVKLQKVVLGFPCSSNQTEFKF 509
Cdd:COG1205   205 RRLRRI------CRHYGSD--PQFILASATIGNPAEHAERLTG--RPVTVV--DEDGSPRGERTFVLWNPPLVDDGIRRS 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 510 DLTLNYKIASVIqMYSDQKpTLVFCATRKGVQQAASVLvkdakfimtveqKQRLQKYAYSVRdsklrdIlkdgAAYhHAG 589
Cdd:COG1205   273 ALAEAARLLADL-VREGLR-TLVFTRSRRGAELLARYA------------RRALREPDLADR------V----AAY-RAG 327
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370452148 590 MELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPA-HLVVIkstMHYAGglfeeySETDILQMIGRAGR 657
Cdd:COG1205   328 YLPEERREIERGLRSGELLGVVSTNALELGIDIGGlDAVVL---AGYPG------TRASFWQQAGRAGR 387
DEXHc_Mtr4-like cd18024
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ...
276-471 5.93e-20

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: 89.04  E-value: 5.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 276 KEFPY-FNYIQSKAFDDLlytDRN--FVICAPTGSGKTVVFELAITRLLMEvplpwlNIKIVYMAPIKALCSQRFDDWKE 352
Cdd:cd18024    27 RTYPFtLDPFQKTAIACI---ERNesVLVSAHTSAGKTVVAEYAIAQSLRD------KQRVIYTSPIKALSNQKYRELQE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 353 KFGPIGLnckeLTGDTVMDDLFEIqhahIIMTTpEKWDSMTrkWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEvvvsrm 432
Cdd:cd18024    98 EFGDVGL----MTGDVTINPNASC----LVMTT-EILRSML--YRGSEIMREVAWVIFDEIHYMRDKERGVVWE------ 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1370452148 433 KTVQSVSQTlkntstaipMRFVAVSATIPNAEDIAEWLS 471
Cdd:cd18024   161 ETIILLPDK---------VRYVFLSATIPNARQFAEWIC 190
DEXHc_SKIV2L cd18027
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ...
285-470 5.14e-18

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: 82.70  E-value: 5.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 285 QSKAFDDLLYTDRNFViCAPTGSGKTVVFELAITRLLMEVplpwlnIKIVYMAPIKALCSQRFDDWKEKFGPIGLnckeL 364
Cdd:cd18027    13 QKQAILHLEAGDSVFV-AAHTSAGKTVVAEYAIALAQKHM------TRTIYTSPIKALSNQKFRDFKNTFGDVGL----I 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 365 TGDTVMDDlfeiQHAHIIMTTpEKWDSMTrkWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKtvQSVSqtlkn 444
Cdd:cd18027    82 TGDVQLNP----EASCLIMTT-EILRSML--YNGSDVIRDLEWVIFDEVHYINDAERGVVWEEVLIMLP--DHVS----- 147
                         170       180
                  ....*....|....*....|....*.
gi 1370452148 445 tstaipmrFVAVSATIPNAEDIAEWL 470
Cdd:cd18027   148 --------IILLSATVPNTVEFADWI 165
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
285-658 1.77e-17

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 86.62  E-value: 1.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 285 QSKAFDDLLYT----DRNFVICAPTGSGKTVVFELAITRLLmevplpwLNIKIVYMAPIKALCSQrfddWKEKFgpigln 360
Cdd:COG1061    85 QQEALEALLAAlergGGRGLVVAPTGTGKTVLALALAAELL-------RGKRVLVLVPRRELLEQ----WAEEL------ 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 361 cKELTGDTVMDDLFEIQHAHIIMTTpekWDSMTRKWRDNSLVQLVRLFLIDEVHIVkdenRGPTLEVVVSRMKtvqsvsq 440
Cdd:COG1061   148 -RRFLGDPLAGGGKKDSDAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHA----GAPSYRRILEAFP------- 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 441 tlkntstaiPMRFVAVSATiPNAED---IAEWLSDGERPAVCLK--MDESH-RPVKLQKVVLGFpcSSNQTEF-KFDLTL 513
Cdd:COG1061   213 ---------AAYRLGLTAT-PFRSDgreILLFLFDGIVYEYSLKeaIEDGYlAPPEYYGIRVDL--TDERAEYdALSERL 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 514 NYKIAS-----------VIQMYSDQKPTLVFCATrkgvqqaasvlVKDAKFIMtveqkQRLQKYAYSvrdsklrdilkdg 582
Cdd:COG1061   281 REALAAdaerkdkilreLLREHPDDRKTLVFCSS-----------VDHAEALA-----ELLNEAGIR------------- 331
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370452148 583 AAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPA--HLVVIKSTMhyagglfeeySETDILQMIGRAGRP 658
Cdd:COG1061   332 AAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPTG----------SPREFIQRLGRGLRP 399
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
296-470 6.55e-15

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: 73.00  E-value: 6.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 296 DRNFVICAPTGSGKTVVFELAITRLLMEVPLPwlNIKIVYMAPIKALCSQRFDDWKEKfgpigLNCKEL-------TGDT 368
Cdd:cd17922     1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEK--GVQVLYISPLKALINDQERRLEEP-----LDEIDLeipvavrHGDT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 369 -------VMDDLfeiqhAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVqsvsqt 441
Cdd:cd17922    74 sqsekakQLKNP-----PGILITTPESLELLLVNKKLRELFAGLRYVVVDEIHALLGSKRGVQLELLLERLRKL------ 142
                         170       180
                  ....*....|....*....|....*....
gi 1370452148 442 lkntsTAIPMRFVAVSATIPNAEDIAEWL 470
Cdd:cd17922   143 -----TGRPLRRIGLSATLGNLEEAAAFL 166
DEXHc_POLQ-like cd18026
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ...
289-470 5.92e-14

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: 71.48  E-value: 5.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 289 FDDLLYTDRNFVICAPTGSGKTVVFELAITRLLmevplpWLNIKIV-YMAPIKALCSQRFDDWKEKFGPIGLNCKELTGD 367
Cdd:cd18026    26 SLPGLLEGRNLVYSLPTSGGKTLVAEILMLKRL------LERRKKAlFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 368 --TVMDDLFEiqHAHIIMTTPEKWDSMTrkwrdNSLVQLVRLFLI-----DEVHIVKDENRGPTLEVVVSRMktvqsvsq 440
Cdd:cd18026   100 kgRSPPKRRK--SLSVAVCTIEKANSLV-----NSLIEEGRLDELglvvvDELHMLGDGHRGALLELLLTKL-------- 164
                         170       180       190
                  ....*....|....*....|....*....|
gi 1370452148 441 TLKNTSTaipMRFVAVSATIPNAEDIAEWL 470
Cdd:cd18026   165 LYAAQKN---IQIVGMSATLPNLEELASWL 191
DEXHc_DDX60 cd18025
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ...
291-475 1.58e-13

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: 69.70  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 291 DLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALCSQ-------RFDdwkEKFGPIGLN-CK 362
Cdd:cd18025    11 DIVDRRESALIVAPTSSGKTFISYYCMEKVLRESD----DGVVVYVAPTKALVNQvvaevyaRFS---KKYPPSGKSlWG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 363 ELTGDTVMDDlfeIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEvvvsrmktvqsvsQTL 442
Cdd:cd18025    84 VFTRDYRHNN---PMNCQVLITVPECLEILLLSPHNASWVPRIKYVIFDEIHSIGQSEDGAVWE-------------QLL 147
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1370452148 443 kntsTAIPMRFVAVSATIPNAEDIAEWLSDGER 475
Cdd:cd18025   148 ----LLIPCPFLALSATIGNPQKFHEWLQSVQR 176
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
285-468 1.89e-13

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: 69.54  E-value: 1.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 285 QSKAFDdLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPlpwlNIKIVYMAPIKALC-SQ--RFDDWKEKFGPiGLNC 361
Cdd:cd17923     5 QAEAIE-AARAGRSVVVTTGTASGKSLCYQLPILEALLRDP----GSRALYLYPTKALAqDQlrSLRELLEQLGL-GIRV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 362 KELTGDTVMDDLFEI--QHAHIIMTTPEKWD-SMTR---KWRdnSLVQLVRLFLIDEVHIVkdenRGP---TLEVVVSRM 432
Cdd:cd17923    79 ATYDGDTPREERRAIirNPPRILLTNPDMLHyALLPhhdRWA--RFLRNLRYVVLDEAHTY----RGVfgsHVALLLRRL 152
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370452148 433 KtvqsvsQTLKNTSTAIpmRFVAVSATIPNAEDIAE 468
Cdd:cd17923   153 R------RLCRRYGADP--QFILTSATIGNPAEHAR 180
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
301-676 1.92e-13

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 74.58  E-value: 1.92e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  301 ICAPTGSGKTVV-FELAITRLLME------VPLPWLNIKIVYMAPIKALCS--QR--------FDDWKEKFGPIGLNCKE 363
Cdd:PRK09751     1 VIAPTGSGKTLAaFLYALDRLFREggedtrEAHKRKTSRILYISPIKALGTdvQRnlqiplkgIADERRRRGETEVNLRV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  364 --LTGDTVMDDLFEI--QHAHIIMTTPEKWDSM-TRKWRDNslVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMktvqsv 438
Cdd:PRK09751    81 giRTGDTPAQERSKLtrNPPDILITTPESLYLMlTSRARET--LRGVETVIIDEVHAVAGSKRGAHLALSLERL------ 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  439 sQTLKNTstaiPMRFVAVSATIPNAEDIAEWLSdGERPAVCLKMDESHRPvKLQKVV-----LGFPCSSNQTEFKFDLTL 513
Cdd:PRK09751   153 -DALLHT----SAQRIGLSATVRSASDVAAFLG-GDRPVTVVNPPAMRHP-QIRIVVpvanmDDVSSVASGTGEDSHAGR 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  514 NYKI-----ASVIQMYSDQKPTLVFCATRkGVQQAASVLVKD---AKFIMTVEQKQRLQKYAYSVRDSKLRDILKDG--A 583
Cdd:PRK09751   226 EGSIwpyieTGILDEVLRHRSTIVFTNSR-GLAEKLTARLNElyaARLQRSPSIAVDAAHFESTSGATSNRVQSSDVfiA 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  584 AYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIK--STMHYAGGlfeeysetdiLQMIGRAGRpQFD 661
Cdd:PRK09751   305 RSHHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQvaTPLSVASG----------LQRIGRAGH-QVG 373
                          410
                   ....*....|....*
gi 1370452148  662 TTATAVIMTRlSTRD 676
Cdd:PRK09751   374 GVSKGLFFPR-TRRD 387
HELICc smart00490
helicase superfamily c-terminal domain;
579-658 9.81e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 64.16  E-value: 9.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148  579 LKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIKSTmhyagglfeEYSETDILQMIGRAGR 657
Cdd:smart00490  10 LGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL---------PWSPASYIQRIGRAGR 80

                   .
gi 1370452148  658 P 658
Cdd:smart00490  81 A 81
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
298-438 2.79e-10

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: 59.34  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 298 NFVICAPTGSGKTVVFELAITRLLMEVPLpwlniKIVYMAPIKALCSQRFDDWKEKFGPiGLNCKELTGDTVM--DDLFE 375
Cdd:cd00046     3 NVLITAPTGSGKTLAALLAALLLLLKKGK-----KVLVLVPTKALALQTAERLRELFGP-GIRVAVLVGGSSAeeREKNK 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370452148 376 IQHAHIIMTTPEK-WDSMTRKWRdnsLVQL-VRLFLIDEVHIVKDENRGPTLE---VVVSRMKTVQSV 438
Cdd:cd00046    77 LGDADIIIATPDMlLNLLLREDR---LFLKdLKLIIVDEAHALLIDSRGALILdlaVRKAGLKNAQVI 141
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
516-657 7.52e-10

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: 56.84  E-value: 7.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 516 KIASVIQMYSDQKP--TLVFCATRKGVqqaasvlvkDAKFImtveqkqrLQKYAYSVrdsklrdilkdgaAYHHAGMELS 593
Cdd:pfam00271   2 KLEALLELLKKERGgkVLIFSQTKKTL---------EAELL--------LEKEGIKV-------------ARLHGDLSQE 51
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370452148 594 DRKVVEGAFTVGDLPVLFTTSTLAMGVNLP-AHLVVIkstmhyagglFE-EYSETDILQMIGRAGR 657
Cdd:pfam00271  52 EREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN----------YDlPWNPASYIQRIGRAGR 107
ResIII pfam04851
Type III restriction enzyme, res subunit;
274-414 1.89e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 57.30  E-value: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 274 IFKEFPYfnyiQSKAFDDLL----YTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPwlniKIVYMAPIKALCSQRFDD 349
Cdd:pfam04851   1 KLELRPY----QIEAIENLLesikNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK----KVLFLVPRKDLLEQALEE 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370452148 350 WKEKFGPIGLNCKELTGDTvmdDLFEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVH 414
Cdd:pfam04851  73 FKKFLPNYVEIGEIISGDK---KDESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
PRK13767 PRK13767
ATP-dependent helicase; Provisional
297-656 2.42e-07

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 54.51  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 297 RNFVICAPTGSGKTVVFELAI----TRLLMEVPLPwLNIKIVYMAPIKALCSqrfDDWKEKFGPIGLNCKELTGDTVmdD 372
Cdd:PRK13767   48 KNVLISSPTGSGKTLAAFLAIidelFRLGREGELE-DKVYCLYVSPLRALNN---DIHRNLEEPLTEIREIAKERGE--E 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 373 LFEIQHA-------------------HIIMTTPE---------KWdsmTRKWRDnslvqlVRLFLIDEVHIVKDENRGPT 424
Cdd:PRK13767  122 LPEIRVAirtgdtssyekqkmlkkppHILITTPEslaillnspKF---REKLRT------VKWVIVDEIHSLAENKRGVH 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 425 LEVVVSRmktvqsvsqtLKNTSTAIPMRfVAVSATIPNAEDIAEWL---SDGERPAVCLKMDESH-RPVKLqKVVLGFPC 500
Cdd:PRK13767  193 LSLSLER----------LEELAGGEFVR-IGLSATIEPLEEVAKFLvgyEDDGEPRDCEIVDARFvKPFDI-KVISPVDD 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 501 SSNQTEFKFDLTLNYKIASVIQmysDQKPTLVFCATRKGvqqAASVLVKdakfimtveQKQRLQKYAYSvrdsklrdilk 580
Cdd:PRK13767  261 LIHTPAEEISEALYETLHELIK---EHRTTLIFTNTRSG---AERVLYN---------LRKRFPEEYDE----------- 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370452148 581 DGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPaH--LVVIKSTmhyagglfeEYSETDILQMIGRAG 656
Cdd:PRK13767  315 DNIGAHHSSLSREVRLEVEEKLKRGELKVVVSSTSLELGIDIG-YidLVVLLGS---------PKSVSRLLQRIGRAG 382
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
527-657 3.48e-07

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


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 53.61  E-value: 3.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 527 QKPTLVFCATRKGVQQAAsvlvkdakfimtveqkQRLQKYAYSVrdsklrdilkdgAAYHhAGMELSDRKVVEGAFTVGD 606
Cdd:COG0514   230 GGSGIVYCLSRKKVEELA----------------EWLREAGIRA------------AAYH-AGLDAEEREANQDRFLRDE 280
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370452148 607 LPVLFTTSTLAMGVNLP-----AHLVVIKSTmhyagglfEEYsetdiLQMIGRAGR 657
Cdd:COG0514   281 VDVIVATIAFGMGIDKPdvrfvIHYDLPKSI--------EAY-----YQEIGRAGR 323
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
527-657 5.43e-07

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 49.51  E-value: 5.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 527 QKPTLVFCATRKGVQQAAsvlvkdakfimtveqkQRLQKyaysvrdsklrdiLKDGAAYHHAGMELSDRKVVEGAFTVGD 606
Cdd:cd18794    30 GGSGIIYCLSRKECEQVA----------------ARLQS-------------KGISAAAYHAGLEPSDRRDVQRKWLRDK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370452148 607 LPVLFTTSTLAMGVNLP-----AHLVVIKSTMHYagglfeeysetdiLQMIGRAGR 657
Cdd:cd18794    81 IQVIVATVAFGMGIDKPdvrfvIHYSLPKSMESY-------------YQESGRAGR 123
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
296-414 7.04e-07

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: 50.51  E-value: 7.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 296 DRNFVICAPTGSGKTVVfelAItrLLMEVPLPWLNI----KIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMD 371
Cdd:cd17927    17 GKNTIICLPTGSGKTFV---AV--LICEHHLKKFPAgrkgKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSEN 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370452148 372 DLFE--IQHAHIIMTTPEKWDSMTRKWRDNSLvQLVRLFLIDEVH 414
Cdd:cd17927    92 VSVEqiVESSDVIIVTPQILVNDLKSGTIVSL-SDFSLLVFDECH 135
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
297-414 7.18e-07

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: 50.55  E-value: 7.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 297 RNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNIKIVYMAPIKALCSQ---RFDDWKEKfgpiGLNCKELTGDTVMDDL 373
Cdd:cd18036    18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVNKVPLVEQqleKFFKYFRK----GYKVTGLSGDSSHKVS 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370452148 374 F--EIQHAHIIMTTPEKWDSMTRKWRDNSLVQL--VRLFLIDEVH 414
Cdd:cd18036    94 FgqIVKASDVIICTPQILINNLLSGREEERVYLsdFSLLIFDECH 138
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
284-470 8.76e-07

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: 50.13  E-value: 8.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 284 IQSKAFDDLLyTDRNFVICAPTGSGKTVVFEL-AITRLLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCK 362
Cdd:cd00268    16 IQAQAIPLIL-SGRDVIGQAQTGSGKTLAFLLpILEKLLPEPKKKGRGPQALVLAPTRELAMQIAEVARKLGKGTGLKVA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 363 ELTGDTVMDDLFEI--QHAHIIMTTPEK-WDSMTRKWRDnslVQLVRLFLIDEVhivkDE--NRG--PTLEVVVSRM-KT 434
Cdd:cd00268    95 AIYGGAPIKKQIEAlkKGPDIVVGTPGRlLDLIERGKLD---LSNVKYLVLDEA----DRmlDMGfeEDVEKILSALpKD 167
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1370452148 435 VQSvsqtlkntstaipmrfVAVSATIPNA-EDIAEWL 470
Cdd:cd00268   168 RQT----------------LLFSATLPEEvKELAKKF 188
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
297-386 4.81e-06

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: 47.97  E-value: 4.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 297 RNFVICAPTGSGKTVVFELAItrlLMEVPLPWLN--IKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTG---DTVMD 371
Cdd:cd17957    28 RDLLACAPTGSGKTLAFLIPI---LQKLGKPRKKkgLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSKsleAKAKD 104
                          90
                  ....*....|....*
gi 1370452148 372 DLFEIQHAHIIMTTP 386
Cdd:cd17957   105 GPKSITKYDILVSTP 119
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
295-387 2.20e-05

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: 46.35  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 295 TDRNFVICAPTGSGKTVVfELAITRLLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTvmDDLF 374
Cdd:cd18073    16 KGKNTIICAPTGCGKTFV-SLLICEHHLKKFPQGQKGKVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGAT--AENV 92
                          90
                  ....*....|....*..
gi 1370452148 375 E----IQHAHIIMTTPE 387
Cdd:cd18073    93 PveqiIENNDIIILTPQ 109
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
303-386 1.03e-04

DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can shuttle between the nucleus and the cytoplasm, and has an RNA-independent ATPase activity. DX47 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: 350712 [Multi-domain]  Cd Length: 203  Bit Score: 44.23  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 303 APTGSGKTVVFELAITRLLMEVPLPWLnikIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTG--DTVMDDLFEIQHAH 380
Cdd:cd17954    44 AETGSGKTAAFALPILQALLENPQRFF---ALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGgmDMMAQAIALAKKPH 120

                  ....*.
gi 1370452148 381 IIMTTP 386
Cdd:cd17954   121 VIVATP 126
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
259-386 1.13e-04

DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 44.22  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 259 GSLKAVTEIPAKFRSIFKE-FPYFNYIQSKAFDDLLyTDRNFVICAPTGSGKTVVFELAITRLLmEVPLPWLNIKIVYMA 337
Cdd:cd17959     1 GGFQSMGLSPPLLRAIKKKgYKVPTPIQRKTIPLIL-DGRDVVAMARTGSGKTAAFLIPMIEKL-KAHSPTVGARALILS 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370452148 338 PIKALCSQRFDDWKE--KFgpIGLNCKELTGDTVMDDLFEIQHAH--IIMTTP 386
Cdd:cd17959    79 PTRELALQTLKVTKElgKF--TDLRTALLVGGDSLEEQFEALASNpdIIIATP 129
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
517-657 1.79e-04

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: 42.64  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 517 IASVIQMYSDQKPTLVFCATRKGVqqaasvlvkdakfimtveqkqrlQKYAYSVRDskLRDILKDG--AAYHHAGMELSD 594
Cdd:cd18796    28 YAEVIFLLERHKSTLVFTNTRSQA-----------------------ERLAQRLRE--LCPDRVPPdfIALHHGSLSREL 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370452148 595 RKVVEGAFTVGDLPVLFTTSTLAMGVNLPA-HLVV-IKSTmhyagglfeeYSETDILQMIGRAGR 657
Cdd:cd18796    83 REEVEAALKRGDLKVVVATSSLELGIDIGDvDLVIqIGSP----------KSVARLLQRLGRSGH 137
PRK11057 PRK11057
ATP-dependent DNA helicase RecQ; Provisional
528-657 2.41e-04

ATP-dependent DNA helicase RecQ; Provisional


Pssm-ID: 182933 [Multi-domain]  Cd Length: 607  Bit Score: 44.70  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 528 KPTLVFCATRKGVQQAASvlvkdakfimtveqkqRLQKYAYSVrdsklrdilkdgAAYHhAGMELSDRKVVEGAFTVGDL 607
Cdd:PRK11057  237 KSGIIYCNSRAKVEDTAA----------------RLQSRGISA------------AAYH-AGLDNDVRADVQEAFQRDDL 287
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370452148 608 PVLFTTSTLAMGVNLP-----AHLVVIKSTMHYagglfeeYSETdilqmiGRAGR 657
Cdd:PRK11057  288 QIVVATVAFGMGINKPnvrfvVHFDIPRNIESY-------YQET------GRAGR 329
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
296-387 2.82e-04

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 44.34  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 296 DRNFVICAPTGSGKTVVFELAITRLLMEVplpwlNIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLFE 375
Cdd:COG1111    17 RKNTLVVLPTGLGKTAVALLVIAERLHKK-----GGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKRKE 91
                          90
                  ....*....|...
gi 1370452148 376 I-QHAHIIMTTPE 387
Cdd:COG1111    92 LwEKARIIVATPQ 104
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
285-414 7.58e-04

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: 41.48  E-value: 7.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 285 QSKAFDDLLytDRNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNIKI-VYMAPIKALCSQRFDDWKEKFgpiGLNCKE 363
Cdd:cd18034     7 QLELFEAAL--KRNTIVVLPTGSGKTLIAVMLIKEMGELNRKEKNPKKRaVFLVPTVPLVAQQAEAIRSHT---DLKVGE 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370452148 364 LTGDTVMDD------LFEIQHAHIIMTTPEkwdsMTRKWRDNSLVQL--VRLFLIDEVH 414
Cdd:cd18034    82 YSGEMGVDKwtkerwKEELEKYDVLVMTAQ----ILLDALRHGFLSLsdINLLIFDECH 136
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
530-657 9.07e-04

C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 40.32  E-value: 9.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 530 TLVFCATRKgvqqAASVLVKDAKfimtveqkQRLQKYAYSVrdSKLrdilkdgAAYHhAGMELSDRKVVEGAFTVGDLPV 609
Cdd:cd18797    38 TIVFCRSRK----LAELLLRYLK--------ARLVEEGPLA--SKV-------ASYR-AGYLAEDRREIEAELFNGELLG 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1370452148 610 LFTTSTLAMGVNLPAHLVVIKSTmhYAGGLFEeysetdILQMIGRAGR 657
Cdd:cd18797    96 VVATNALELGIDIGGLDAVVLAG--YPGSLAS------LWQQAGRAGR 135
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
298-414 1.32e-03

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: 40.38  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 298 NFVICAPTGSGKTVvfelaITRLLMEVPLPWL-NIKIVYMAPIKALCSQRFDDWKeKFGPIGLN-CKELTGDTVMDD-LF 374
Cdd:cd18033    18 NTLVALPTGLGKTF-----IAAVVMLNYYRWFpKGKIVFMAPTKPLVSQQIEACY-KITGIPSSqTAELTGSVPPTKrAE 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370452148 375 EIQHAHIIMTTPEKWDS-MTRKWRD-NSLVQLVrlflIDEVH 414
Cdd:cd18033    92 LWASKRVFFLTPQTLENdLKEGDCDpKSIVCLV----IDEAH 129
SF2_C_suv3 cd18805
C-terminal helicase domain of ATP-dependent RNA helicase; The SUV3 (suppressor of Var 3) gene ...
609-657 1.75e-03

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: 39.46  E-value: 1.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370452148 609 VLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGR 657
Cdd:cd18805    73 VLVASDAIGMGLNLNIRRVIFSSLSKFDGNEMRPLSPSEVKQIAGRAGR 121
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
300-472 5.01e-03

DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350701 [Multi-domain]  Cd Length: 192  Bit Score: 38.78  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 300 VICAPTGSGKTVVFE-LAITRLLMEVplpwLNIKIVYMAPIKALCSQRFDDWKE--KFGPiGLNCKELTGDT-VMDDLFE 375
Cdd:cd17943    31 IVQAKSGTGKTLVFVvIALESLDLER----RHPQVLILAPTREIAVQIHDVFKKigKKLE-GLKCEVFIGGTpVKEDKKK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 376 IQHAHIIMTTPEKWDSMTRKwrdNSL-VQLVRLFLIDEVHIVKDENRGPTLEVVVSRMktvQSVSQTLkntstaipmrfv 454
Cdd:cd17943   106 LKGCHIAVGTPGRIKQLIEL---GALnVSHVRLFVLDEADKLMEGSFQKDVNWIFSSL---PKNKQVI------------ 167
                         170       180
                  ....*....|....*....|
gi 1370452148 455 AVSATIPN--AEDIAEWLSD 472
Cdd:cd17943   168 AFSATYPKnlDNLLARYMRK 187
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
284-348 7.58e-03

DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 38.72  E-value: 7.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370452148 284 IQSKAFDDLLyTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNIK---IVYMAPIKALCSQRFD 348
Cdd:cd17949    17 IQKLAIPVLL-QGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRSDgtlALVLVPTRELALQIYE 83
DEXHc_RecQ5 cd18014
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ...
272-416 8.92e-03

DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) 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.


Pssm-ID: 350772 [Multi-domain]  Cd Length: 205  Bit Score: 38.22  E-value: 8.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452148 272 RSIFKEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAitrllmevPLPWLNIKIVYmAPIKALCSQRFDDWK 351
Cdd:cd18014     5 KKVFGHSDFKSPLQEKATMAVVKGNKDVFVCMPTGAGKSLCYQLP--------ALLAKGITIVI-SPLIALIQDQVDHLK 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370452148 352 E-KFGPIGLNCKELTG--DTVMDDL-FEIQHAHIIMTTPEKWDSMTRKWRDNSLVQ--LVRLFLIDEVHIV 416
Cdd:cd18014    76 TlKIRVDSLNSKLSAQerKRIIADLeSEKPQTKFLYITPEMAATSSFQPLLSSLVSrnLLSYLVVDEAHCV 146
 
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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