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Conserved domains on  [gi|1698318692|ref|XP_029686652|]
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probable ATP-dependent DNA helicase HFM1 isoform X3 [Takifugu rubripes]

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 ...
 303-509 3.32e-107

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: 338.56  E-value: 3.32e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  303 FNYVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQ-NSEPWNEVKAVYMAPIKALCSQCFENWNKKFGPLGL 381
Cdd:cd18023      2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKErNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  382 TCKELTGDTEIDDFFEIQDSHIILTTPEKWDSMTRKWKDH-CLLQQVRLFLIDEVHVIKDaTRGATLEVVVSRMKAVNAY 460
Cdd:cd18023     82 SCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIKE-NRGATLEVVVSRMKTLSSS 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1698318692  461 RAAqNQGTSGTMRIVAVSATIPNISDIADWLSHEslPATYLDMDESHRP 509
Cdd:cd18023    161 SEL-RGSTVRPMRFVAVSATIPNIEDLAEWLGDN--PAGCFSFGESFRP 206
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
287-830 1.96e-100

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


:

Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 332.63  E-value: 1.96e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  287 VSEIP--KFRSVFSEFPF--FNYVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSepwnevKAVYMAPIK 362
Cdd:COG1204      3 VAELPleKVIEFLKERGIeeLYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------KALYIVPLR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  363 ALCSQCFENWNKKFGPLGLTCKELTGDTEIDDFfEIQDSHIILTTPEKWDSMTRK---WkdhclLQQVRLFLIDEVHVIK 439
Cdd:COG1204     77 ALASEKYREFKRDFEELGIKVGVSTGDYDSDDE-WLGRYDILVATPEKLDSLLRNgpsW-----LRDVDLVVVDEAHLID 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  440 DATRGATLEVVVSRMKAVNAyraaqnqgtsgTMRIVAVSATIPNISDIADWLSHESLPATYldmdeshRPVMLRKVVLgf 519
Cdd:COG1204    151 DESRGPTLEVLLARLRRLNP-----------EAQIVALSATIGNAEEIAEWLDAELVKSDW-------RPVPLNEGVL-- 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  520 pcpqNQTEFKFD----LSLNYKMANIIQTYSDQKPALVFCSTRKGAQQAATVLAKDARFIMSIEHNQRLMKYANSIL--- 592
Cdd:COG1204    211 ----YDGVLRFDdgsrRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLevs 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  593 -----DSKLRELVMLGVGYHHAGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLPAHLVVIKSTMQyvaGSCEEYSDA 667
Cdd:COG1204    287 eethtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKR---GGMVPIPVL 363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  668 DMLQMIGRAGRPQFDTTATAVIMTKiqSKDKYMNLMNG-----VEIIESSLHS--HLVEHLNAEIVLQTISDVNMALDWI 740
Cdd:COG1204    364 EFKQMAGRAGRPGYDPYGEAILVAK--SSDEADELFERyilgePEPIRSKLANesALRTHLLALIASGFANSREELLDFL 441

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  741 RSTFLYIRALKNpshygfppsldrcGIEAKLQElclrNLNSLSSIGLIDMDEDiNIKPTETGKLMARYCIAFDTMNLFSK 820
Cdd:COG1204    442 ENTFYAYQYDKG-------------DLEEVVDD----ALEFLLENGFIEEDGD-RLRATKLGKLVSRLYIDPLTAAELVD 503

                          570
                   ....*....|..
gi 1698318692  821 VAG--TENLSDL 830
Cdd:COG1204    504 GLRkaDEEFTDL 515
Sec63 smart00973
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ...
 798-1114 2.69e-58

Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl domain) protein in which it was found. This protein is required for assembly of functional endoplasmic reticulum translocons. Other yeast proteins containing this domain include pre-mRNA splicing helicase BRR2, HFM1 protein and putative helicases.


:

Pssm-ID: 214946  Cd Length: 314  Bit Score: 204.13  E-value: 2.69e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   798 PTETGKLMARYCIAFDTMNLFSKVA-GTENLSDLIELLSRSKEFSNIQLRVNEKRALNTLNRDknrltIRFPFQGKIKTT 876
Cdd:smart00973    1 PTELGRIASYYYISYETIETFNQSLkPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKR-----VPIPVKEGIIDS 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   877 EM-KVNCLIQAQLGSLSIQEFGLSQDTARIFRTGTRISRCLSEFLSHgpKTGFSALLNSLILAKCFRAKLWENSPYVSKQ 955
Cdd:smart00973   76 PHaKVNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALS--KGWLRTALNALDLSQMVVQRLWEDSDSPLKQ 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   956 LEK--IGQTLSTAMVNAGLTTFSKIEQTNPRELELIVNRHPPFGNQIRDSVVHLPKYEVILEQLPRYSCaaAEMVVKVNL 1033
Cdd:smart00973  154 LPHflIEDVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEVEAEVLPITRD--LTLRVELEI 231

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  1034 KNQAELLTKKTAPDYHYVSLIIGNSD-NVVVFQQKLTSSMLLKSGSWSKKIEVAKASKG-EEISVNLISSEYVGLDIQQK 1111
Cdd:smart00973  232 TPVFAWDLPRHKGKSESWWLVVGDSDtNELLAIKRVTLRKKKKSNEVKLDFTVPLSEPGpENYTVYLISDSYLGCDQEVS 311


                    ...
gi 1698318692  1112 INV 1114
Cdd:smart00973  312 FSL 314
 
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 ...
 303-509 3.32e-107

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: 338.56  E-value: 3.32e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  303 FNYVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQ-NSEPWNEVKAVYMAPIKALCSQCFENWNKKFGPLGL 381
Cdd:cd18023      2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKErNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  382 TCKELTGDTEIDDFFEIQDSHIILTTPEKWDSMTRKWKDH-CLLQQVRLFLIDEVHVIKDaTRGATLEVVVSRMKAVNAY 460
Cdd:cd18023     82 SCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIKE-NRGATLEVVVSRMKTLSSS 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1698318692  461 RAAqNQGTSGTMRIVAVSATIPNISDIADWLSHEslPATYLDMDESHRP 509
Cdd:cd18023    161 SEL-RGSTVRPMRFVAVSATIPNIEDLAEWLGDN--PAGCFSFGESFRP 206
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
287-830 1.96e-100

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 332.63  E-value: 1.96e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  287 VSEIP--KFRSVFSEFPF--FNYVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSepwnevKAVYMAPIK 362
Cdd:COG1204      3 VAELPleKVIEFLKERGIeeLYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------KALYIVPLR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  363 ALCSQCFENWNKKFGPLGLTCKELTGDTEIDDFfEIQDSHIILTTPEKWDSMTRK---WkdhclLQQVRLFLIDEVHVIK 439
Cdd:COG1204     77 ALASEKYREFKRDFEELGIKVGVSTGDYDSDDE-WLGRYDILVATPEKLDSLLRNgpsW-----LRDVDLVVVDEAHLID 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  440 DATRGATLEVVVSRMKAVNAyraaqnqgtsgTMRIVAVSATIPNISDIADWLSHESLPATYldmdeshRPVMLRKVVLgf 519
Cdd:COG1204    151 DESRGPTLEVLLARLRRLNP-----------EAQIVALSATIGNAEEIAEWLDAELVKSDW-------RPVPLNEGVL-- 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  520 pcpqNQTEFKFD----LSLNYKMANIIQTYSDQKPALVFCSTRKGAQQAATVLAKDARFIMSIEHNQRLMKYANSIL--- 592
Cdd:COG1204    211 ----YDGVLRFDdgsrRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLevs 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  593 -----DSKLRELVMLGVGYHHAGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLPAHLVVIKSTMQyvaGSCEEYSDA 667
Cdd:COG1204    287 eethtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKR---GGMVPIPVL 363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  668 DMLQMIGRAGRPQFDTTATAVIMTKiqSKDKYMNLMNG-----VEIIESSLHS--HLVEHLNAEIVLQTISDVNMALDWI 740
Cdd:COG1204    364 EFKQMAGRAGRPGYDPYGEAILVAK--SSDEADELFERyilgePEPIRSKLANesALRTHLLALIASGFANSREELLDFL 441

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  741 RSTFLYIRALKNpshygfppsldrcGIEAKLQElclrNLNSLSSIGLIDMDEDiNIKPTETGKLMARYCIAFDTMNLFSK 820
Cdd:COG1204    442 ENTFYAYQYDKG-------------DLEEVVDD----ALEFLLENGFIEEDGD-RLRATKLGKLVSRLYIDPLTAAELVD 503

                          570
                   ....*....|..
gi 1698318692  821 VAG--TENLSDL 830
Cdd:COG1204    504 GLRkaDEEFTDL 515
Sec63 smart00973
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ...
 798-1114 2.69e-58

Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl domain) protein in which it was found. This protein is required for assembly of functional endoplasmic reticulum translocons. Other yeast proteins containing this domain include pre-mRNA splicing helicase BRR2, HFM1 protein and putative helicases.


Pssm-ID: 214946  Cd Length: 314  Bit Score: 204.13  E-value: 2.69e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   798 PTETGKLMARYCIAFDTMNLFSKVA-GTENLSDLIELLSRSKEFSNIQLRVNEKRALNTLNRDknrltIRFPFQGKIKTT 876
Cdd:smart00973    1 PTELGRIASYYYISYETIETFNQSLkPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKR-----VPIPVKEGIIDS 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   877 EM-KVNCLIQAQLGSLSIQEFGLSQDTARIFRTGTRISRCLSEFLSHgpKTGFSALLNSLILAKCFRAKLWENSPYVSKQ 955
Cdd:smart00973   76 PHaKVNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALS--KGWLRTALNALDLSQMVVQRLWEDSDSPLKQ 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   956 LEK--IGQTLSTAMVNAGLTTFSKIEQTNPRELELIVNRHPPFGNQIRDSVVHLPKYEVILEQLPRYSCaaAEMVVKVNL 1033
Cdd:smart00973  154 LPHflIEDVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEVEAEVLPITRD--LTLRVELEI 231

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  1034 KNQAELLTKKTAPDYHYVSLIIGNSD-NVVVFQQKLTSSMLLKSGSWSKKIEVAKASKG-EEISVNLISSEYVGLDIQQK 1111
Cdd:smart00973  232 TPVFAWDLPRHKGKSESWWLVVGDSDtNELLAIKRVTLRKKKKSNEVKLDFTVPLSEPGpENYTVYLISDSYLGCDQEVS 311


                    ...
gi 1698318692  1112 INV 1114
Cdd:smart00973  312 FSL 314
PRK02362 PRK02362
ATP-dependent DNA helicase;
307-807 5.55e-56

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 209.04  E-value: 5.55e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  307 QSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSepwnevKAVYMAPIKALCSQCFENWnKKFGPLGLTCKEL 386
Cdd:PRK02362    28 QAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIARGG------KALYIVPLRALASEKFEEF-ERFEELGVRVGIS 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  387 TGDTEIDDFFeIQDSHIILTTPEKWDSMTRK---WkdhclLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAVNAyraa 463
Cdd:PRK02362   101 TGDYDSRDEW-LGDNDIIVATSEKVDSLLRNgapW-----LDDITCVVVDEVHLIDSANRGPTLEVTLAKLRRLNP---- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  464 qnqgtsgTMRIVAVSATIPNISDIADWLSHESLpatyldmDESHRPVMLRKVVL---GFPCPQNQTEFKF-----DLSLn 535
Cdd:PRK02362   171 -------DLQVVALSATIGNADELADWLDAELV-------DSEWRPIDLREGVFyggAIHFDDSQREVEVpskddTLNL- 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  536 ykmanIIQTYSDQKPALVFCSTRKGAQQAATVLAKDARFIMSIEHNQRLMKYANSILDS-------KLRELVMLGVGYHH 608
Cdd:PRK02362   236 -----VLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVsdtetskDLADCVAKGAAFHH 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  609 AGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLPAHLVVIKSTMQYVAG------SCEEYSdadmlQMIGRAGRPQFD 682
Cdd:PRK02362   311 AGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGagmqpiPVLEYH-----QMAGRAGRPGLD 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  683 TTATAVIMTKIQSK-----DKYmnLMNGVEIIESSLHSH--LVEHLNAEIVLQTISDVNMALDWIRSTFLyirALKNPSH 755
Cdd:PRK02362   386 PYGEAVLLAKSYDEldelfERY--IWADPEDVRSKLATEpaLRTHVLSTIASGFARTRDGLLEFLEATFY---ATQTDDT 460

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1698318692  756 YGFPPSLDRCgieaklqelclrnLNSLSSIGLIDMDEDiNIKPTETGKLMAR 807
Cdd:PRK02362   461 GRLERVVDDV-------------LDFLERNGMIEEDGE-TLEATELGHLVSR 498
Sec63 pfam02889
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ...
 798-1113 3.13e-54

Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of functional endoplasmic reticulum translocons.


Pssm-ID: 460740  Cd Length: 307  Bit Score: 192.03  E-value: 3.13e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  798 PTETGKLMARYCIAFDTMNLF-SKVAGTENLSDLIELLSRSKEFSNIQLRVNEKRALNTLNrDKnrltIRFPFQGKIKTT 876
Cdd:pfam02889    1 PTDLGRIASHYYISYETIETFnQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLL-EK----VPIPVKGDIEDP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  877 EMKVNCLIQAQLGSLSIQEFGLSQDTARIFRTGTRISRCLSEFLSHgpKTGFSALLNSLILAKCFRAKLWeNSPYVSKQL 956
Cdd:pfam02889   76 HAKVNILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLS--KGWLSAALTALDLCKMIEQRMW-DSDSPLRQF 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  957 EKIGQTLSTAMVNAGLTTFSKIEQTNPRELELIVNRHPPFGNQIRDSVVHLPKYEvILEQLPRYSCAAAEMVVKVNLKNQ 1036
Cdd:pfam02889  153 PGIPPELIKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIE-IEAEVQPITRSVLRVEVTITPDFP 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692 1037 AElltKKTAPDYHYVSLIIGNSDNVVVFQQKLTsSMLLKSGSWSKKIEVA---KASKGEEISVNLISSEYVGLDIQQKIN 1113
Cdd:pfam02889  232 WD---KRVHGKSEGFWLVVGDSDGNEILHIERF-TLTKRTLAGEHKLEFTvppSDPGPPQLFVRLISDSWLGADQEVPIS 307
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
 508-692 5.23e-53

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: 182.75  E-value: 5.23e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  508 RPVMLRKVVLGFP----CPQNQTEFKFDLslNYKMANIIQTYSDQKPALVFCSTRKGAQQAATVLAkdarfimsiehnqr 583
Cdd:cd18795      1 RPVPLEEYVLGFNglgiKLRVDVMNKFDS--DIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA-------------- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  584 lmkyansildsklrelvmlGVGYHHAGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLPAHLVVIKSTMQYVAGSCEE 663
Cdd:cd18795     65 -------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRE 125

                          170       180
                   ....*....|....*....|....*....
gi 1698318692  664 YSDADMLQMIGRAGRPQFDTTATAVIMTK 692
Cdd:cd18795    126 LSPLEYLQMIGRAGRPGFDTRGEAIIMTK 154
PRK01172 PRK01172
ATP-dependent DNA helicase;
318-695 1.13e-46

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 179.69  E-value: 1.13e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  318 GKNFVACAPTGSGKTVLFELAIIRLLMQNsepwneVKAVYMAPIKALCSQCFENWNKkFGPLGLTCKELTGDTEIDDFFe 397
Cdd:PRK01172    37 GENVIVSVPTAAGKTLIAYSAIYETFLAG------LKSIYIVPLRSLAMEKYEELSR-LRSLGMRVKISIGDYDDPPDF- 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  398 IQDSHIILTTPEKWDSMTRKwkDHCLLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAVNAyraaqnqgtsgTMRIVAV 477
Cdd:PRK01172   109 IKRYDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSARYVNP-----------DARILAL 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  478 SATIPNISDIADWLSHESLPATYldmdeshRPVMLRKVVLGFPCPQNQTEFKFDLSLNYKMANIIQtysDQKPALVFCST 557
Cdd:PRK01172   176 SATVSNANELAQWLNASLIKSNF-------RPVPLKLGILYRKRLILDGYERSQVDINSLIKETVN---DGGQVLVFVSS 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  558 RKGAQQAATVLAKdarfIMSIEHNQRLMKYANSILDSKLRELVMLGVGYHHAGVDLSDRKLIEMAFTQADLPVLFTTRTL 637
Cdd:PRK01172   246 RKNAEDYAEMLIQ----HFPEFNDFKVSSENNNVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTL 321

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1698318692  638 AMGVNLPAHLVVIKSTMQYVAGSCEEYSDADMLQMIGRAGRPQFDTTATAVIMTKIQS 695
Cdd:PRK01172   322 AAGVNLPARLVIVRDITRYGNGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYIYAASPA 379
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 306-487 4.91e-37

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: 137.37  E-value: 4.91e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDdVLYTGKNFVACAPTGSGKTVLFELAIIRLLmqnSEPWNEVKAVYMAPIKALCSQCFENWNKKFGPLGLT-CK 384
Cdd:pfam00270    3 IQAEAIP-AILEGRDVLVQAPTGSGKTLAFLLPALEAL---DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKvAS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  385 ELTGDTEIDDFFEIQDSHIILTTPEKWDSMTRKWKdhcLLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAvnayraaq 464
Cdd:pfam00270   79 LLGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-------- 147

                          170       180
                   ....*....|....*....|....
gi 1698318692  465 nqgtsgTMRIVAVSATIP-NISDI 487
Cdd:pfam00270  148 ------KRQILLLSATLPrNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
298-483 1.03e-28

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 114.90  E-value: 1.03e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   298 SEFPFFNYVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEPwnevKAVYMAPIKALCSQCFENWNKKFG 377
Cdd:smart00487    4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGG----RVLVLVPTRELAEQWAEELKKLGP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   378 PLGL-TCKELTGDTEIDDFFEIQ--DSHIILTTPEKWDSMTRkwKDHCLLQQVRLFLIDEVHVIKDATRGATLEVVVSRM 454
Cdd:smart00487   80 SLGLkVVGLYGGDSKREQLRKLEsgKTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157

                           170       180
                    ....*....|....*....|....*....
gi 1698318692   455 KAVNayraaqnqgtsgtmRIVAVSATIPN 483
Cdd:smart00487  158 PKNV--------------QLLLLSATPPE 172
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
306-707 1.21e-24

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


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 111.91  E-value: 1.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNsepwnEVKAVYMAPIKALCSQCFENWNKKFGPlGLTCKE 385
Cdd:COG1202    213 VQSLAVENGLLEGKDQLVVSATATGKTLIGELAGIKNALEG-----KGKMLFLVPLVALANQKYEDFKDRYGD-GLDVSI 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  386 LTGDTEIDDFFE--IQDSHIILTTPEKWDSMTRKWKDhclLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAVnaYRAA 463
Cdd:COG1202    287 RVGASRIRDDGTrfDPNADIIVGTYEGIDHALRTGRD---LGDIGTVVIDEVHMLEDPERGHRLDGLIARLKYY--CPGA 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  464 QnqgtsgtmrIVAVSATIPNISDIAdwlshESLPATYLDMDEshRPVML-RKVVLgfpCPQNQ----------TEFKFDL 532
Cdd:COG1202    362 Q---------WIYLSATVGNPEELA-----KKLGAKLVEYEE--RPVPLeRHLTF---ADGREkiriinklvkREFDTKS 422

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  533 SLNYKMANIIQTYSdqkpalvfcstRKGAQQAATVLAKDARfimsiehnqrlmkyansildsklrelvmlgvgYHHAGVD 612
Cdd:COG1202    423 SKGYRGQTIIFTNS-----------RRRCHEIARALGYKAA--------------------------------PYHAGLD 459

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  613 LSDRKLIEMAFTQADLPVLFTTRTLAMGVNLPAHLVVIKS--------TMQyvagsceEYSdadmlQMIGRAGRPQFDTT 684
Cdd:COG1202    460 YGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSlamgiewlSVQ-------EFH-----QMLGRAGRPDYHDR 527

                          410       420
                   ....*....|....*....|...
gi 1698318692  685 ATAVIMTKIQSkdKYMNLMNGVE 707
Cdd:COG1202    528 GKVYLLVEPGK--SYHRSMEMTE 548
HELICc smart00490
helicase superfamily c-terminal domain;
591-679 2.85e-12

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 63.77  E-value: 2.85e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   591 ILDSKLRELVmLGVGYHHAGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLP-AHLVVIKSTmqyvagsceEYSDADM 669
Cdd:smart00490    2 ELAELLKELG-IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL---------PWSPASY 71

                            90
                    ....*....|
gi 1698318692   670 LQMIGRAGRP 679
Cdd:smart00490   72 IQRIGRAGRA 81
DEXH_lig_assoc TIGR04121
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ...
 325-516 8.15e-12

DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.


Pssm-ID: 274994 [Multi-domain]  Cd Length: 804  Bit Score: 70.27  E-value: 8.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  325 APTGSGKTV-LFELAIIRLLMQNSEPWNEVKAVYMAPIKALCSQCFENWNKKFGPLGLTCK-EL-TGDTEIDDFFEIQDS 401
Cdd:TIGR04121   35 APTGSGKTLaGFLPSLIDLAGPEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGLPIRvETrTGDTSSSERARQRKK 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  402 --HIILTTPEKWdSMTRKWKDHC-LLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAVNAyraaqnqgtsgTMRIVAVS 478
Cdd:TIGR04121  115 ppDILLTTPESL-ALLLSYPDAArLFKDLRCVVVDEWHELAGSKRGDQLELALARLRRLAP-----------GLRRWGLS 182

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1698318692  479 ATIPNISDIADWLSHESLPATYLDMDESHRPVMLRKVV 516
Cdd:TIGR04121  183 ATIGNLEEARRVLLGVGGAPAVLVRGKLPKAIEVISLL 220
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 575-678 1.56e-08

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: 53.75  E-value: 1.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  575 IMSIEHNQRLMKYANSI--LDSK-LRELVMLGVGYHHAGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLP-AHLVVI 650
Cdd:pfam00271    9 LLKKERGGKVLIFSQTKktLEAElLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN 88

                           90       100
                   ....*....|....*....|....*...
gi 1698318692  651 kstmqyvagSCEEYSDADMLQMIGRAGR 678
Cdd:pfam00271   89 ---------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 ...
 303-509 3.32e-107

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: 338.56  E-value: 3.32e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  303 FNYVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQ-NSEPWNEVKAVYMAPIKALCSQCFENWNKKFGPLGL 381
Cdd:cd18023      2 FNRIQSEVFPDLLYSDKNFVVSAPTGSGKTVLFELAILRLLKErNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  382 TCKELTGDTEIDDFFEIQDSHIILTTPEKWDSMTRKWKDH-CLLQQVRLFLIDEVHVIKDaTRGATLEVVVSRMKAVNAY 460
Cdd:cd18023     82 SCAELTGDTEMDDTFEIQDADIILTTPEKWDSMTRRWRDNgNLVQLVALVLIDEVHIIKE-NRGATLEVVVSRMKTLSSS 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1698318692  461 RAAqNQGTSGTMRIVAVSATIPNISDIADWLSHEslPATYLDMDESHRP 509
Cdd:cd18023    161 SEL-RGSTVRPMRFVAVSATIPNIEDLAEWLGDN--PAGCFSFGESFRP 206
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
287-830 1.96e-100

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 332.63  E-value: 1.96e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  287 VSEIP--KFRSVFSEFPF--FNYVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSepwnevKAVYMAPIK 362
Cdd:COG1204      3 VAELPleKVIEFLKERGIeeLYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNGG------KALYIVPLR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  363 ALCSQCFENWNKKFGPLGLTCKELTGDTEIDDFfEIQDSHIILTTPEKWDSMTRK---WkdhclLQQVRLFLIDEVHVIK 439
Cdd:COG1204     77 ALASEKYREFKRDFEELGIKVGVSTGDYDSDDE-WLGRYDILVATPEKLDSLLRNgpsW-----LRDVDLVVVDEAHLID 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  440 DATRGATLEVVVSRMKAVNAyraaqnqgtsgTMRIVAVSATIPNISDIADWLSHESLPATYldmdeshRPVMLRKVVLgf 519
Cdd:COG1204    151 DESRGPTLEVLLARLRRLNP-----------EAQIVALSATIGNAEEIAEWLDAELVKSDW-------RPVPLNEGVL-- 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  520 pcpqNQTEFKFD----LSLNYKMANIIQTYSDQKPALVFCSTRKGAQQAATVLAKDARFIMSIEHNQRLMKYANSIL--- 592
Cdd:COG1204    211 ----YDGVLRFDdgsrRSKDPTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRLTPEEREELEELAEELLevs 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  593 -----DSKLRELVMLGVGYHHAGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLPAHLVVIKSTMQyvaGSCEEYSDA 667
Cdd:COG1204    287 eethtNEKLADCLEKGVAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLPARRVIIRDTKR---GGMVPIPVL 363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  668 DMLQMIGRAGRPQFDTTATAVIMTKiqSKDKYMNLMNG-----VEIIESSLHS--HLVEHLNAEIVLQTISDVNMALDWI 740
Cdd:COG1204    364 EFKQMAGRAGRPGYDPYGEAILVAK--SSDEADELFERyilgePEPIRSKLANesALRTHLLALIASGFANSREELLDFL 441

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  741 RSTFLYIRALKNpshygfppsldrcGIEAKLQElclrNLNSLSSIGLIDMDEDiNIKPTETGKLMARYCIAFDTMNLFSK 820
Cdd:COG1204    442 ENTFYAYQYDKG-------------DLEEVVDD----ALEFLLENGFIEEDGD-RLRATKLGKLVSRLYIDPLTAAELVD 503

                          570
                   ....*....|..
gi 1698318692  821 VAG--TENLSDL 830
Cdd:COG1204    504 GLRkaDEEFTDL 515
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 302-496 4.33e-60

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: 204.03  E-value: 4.33e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  302 FFNYVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQnsepwNEVKAVYMAPIKALCSQCFENWNKKFGPLGL 381
Cdd:cd17921      1 LLNPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAILRALAT-----SGGKAVYIAPTRALVNQKEADLRERFGPLGK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  382 TCKELTGDTEIDDfFEIQDSHIILTTPEKWDSMTRKWKdHCLLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAVNayr 461
Cdd:cd17921     76 NVGLLTGDPSVNK-LLLAEADILVATPEKLDLLLRNGG-ERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRIN--- 150

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1698318692  462 aaqnqgtsGTMRIVAVSATIPNISDIADWLSHESL 496
Cdd:cd17921    151 --------KNARFVGLSATLPNAEDLAEWLGVEDL 177
Sec63 smart00973
Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl ...
 798-1114 2.69e-58

Sec63 Brl domain; This domain was named after the yeast Sec63 (or NPL1) (also known as the Brl domain) protein in which it was found. This protein is required for assembly of functional endoplasmic reticulum translocons. Other yeast proteins containing this domain include pre-mRNA splicing helicase BRR2, HFM1 protein and putative helicases.


Pssm-ID: 214946  Cd Length: 314  Bit Score: 204.13  E-value: 2.69e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   798 PTETGKLMARYCIAFDTMNLFSKVA-GTENLSDLIELLSRSKEFSNIQLRVNEKRALNTLNRDknrltIRFPFQGKIKTT 876
Cdd:smart00973    1 PTELGRIASYYYISYETIETFNQSLkPTTTLKDILEILSRASEFKEIPVRHNEKKELNELNKR-----VPIPVKEGIIDS 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   877 EM-KVNCLIQAQLGSLSIQEFGLSQDTARIFRTGTRISRCLSEFLSHgpKTGFSALLNSLILAKCFRAKLWENSPYVSKQ 955
Cdd:smart00973   76 PHaKVNLLLQAHLSRLPLPDFDLVSDLKYILQNAPRILRALVDIALS--KGWLRTALNALDLSQMVVQRLWEDSDSPLKQ 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   956 LEK--IGQTLSTAMVNAGLTTFSKIEQTNPRELELIVNRHPPFGNQIRDSVVHLPKYEVILEQLPRYSCaaAEMVVKVNL 1033
Cdd:smart00973  154 LPHflIEDVYDKLELKDGSRSFELLLDMNAAELGEFLNRLPPNGRLIYELLRRFPKIEVEAEVLPITRD--LTLRVELEI 231

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  1034 KNQAELLTKKTAPDYHYVSLIIGNSD-NVVVFQQKLTSSMLLKSGSWSKKIEVAKASKG-EEISVNLISSEYVGLDIQQK 1111
Cdd:smart00973  232 TPVFAWDLPRHKGKSESWWLVVGDSDtNELLAIKRVTLRKKKKSNEVKLDFTVPLSEPGpENYTVYLISDSYLGCDQEVS 311


                    ...
gi 1698318692  1112 INV 1114
Cdd:smart00973  312 FSL 314
PRK02362 PRK02362
ATP-dependent DNA helicase;
307-807 5.55e-56

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 209.04  E-value: 5.55e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  307 QSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSepwnevKAVYMAPIKALCSQCFENWnKKFGPLGLTCKEL 386
Cdd:PRK02362    28 QAEAVEAGLLDGKNLLAAIPTASGKTLIAELAMLKAIARGG------KALYIVPLRALASEKFEEF-ERFEELGVRVGIS 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  387 TGDTEIDDFFeIQDSHIILTTPEKWDSMTRK---WkdhclLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAVNAyraa 463
Cdd:PRK02362   101 TGDYDSRDEW-LGDNDIIVATSEKVDSLLRNgapW-----LDDITCVVVDEVHLIDSANRGPTLEVTLAKLRRLNP---- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  464 qnqgtsgTMRIVAVSATIPNISDIADWLSHESLpatyldmDESHRPVMLRKVVL---GFPCPQNQTEFKF-----DLSLn 535
Cdd:PRK02362   171 -------DLQVVALSATIGNADELADWLDAELV-------DSEWRPIDLREGVFyggAIHFDDSQREVEVpskddTLNL- 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  536 ykmanIIQTYSDQKPALVFCSTRKGAQQAATVLAKDARFIMSIEHNQRLMKYANSILDS-------KLRELVMLGVGYHH 608
Cdd:PRK02362   236 -----VLDTLEEGGQCLVFVSSRRNAEGFAKRAASALKKTLTAAERAELAELAEEIREVsdtetskDLADCVAKGAAFHH 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  609 AGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLPAHLVVIKSTMQYVAG------SCEEYSdadmlQMIGRAGRPQFD 682
Cdd:PRK02362   311 AGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIRDYRRYDGGagmqpiPVLEYH-----QMAGRAGRPGLD 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  683 TTATAVIMTKIQSK-----DKYmnLMNGVEIIESSLHSH--LVEHLNAEIVLQTISDVNMALDWIRSTFLyirALKNPSH 755
Cdd:PRK02362   386 PYGEAVLLAKSYDEldelfERY--IWADPEDVRSKLATEpaLRTHVLSTIASGFARTRDGLLEFLEATFY---ATQTDDT 460

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1698318692  756 YGFPPSLDRCgieaklqelclrnLNSLSSIGLIDMDEDiNIKPTETGKLMAR 807
Cdd:PRK02362   461 GRLERVVDDV-------------LDFLERNGMIEEDGE-TLEATELGHLVSR 498
PRK00254 PRK00254
ski2-like helicase; Provisional
 268-986 2.05e-54

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 203.90  E-value: 2.05e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  268 MTPQPLRIKDRsdsgilrpVSEIPKFRSVFSEFPffnyVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAII-RLLMQN 346
Cdd:PRK00254     1 MKVDELRVDER--------IKRVLKERGIEELYP----PQAEALKSGVLEGKNLVLAIPTASGKTLVAEIVMVnKLLREG 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  347 SepwnevKAVYMAPIKALCS---QCFENWNKkfgpLGLTCKELTGDTE-IDDFFEIQDshIILTTPEKWDSMTR---KWk 419
Cdd:PRK00254    69 G------KAVYLVPLKALAEekyREFKDWEK----LGLRVAMTTGDYDsTDEWLGKYD--IIIATAEKFDSLLRhgsSW- 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  420 dhclLQQVRLFLIDEVHVIKDATRGATLEVVVSRMkavnayraaqnqgtSGTMRIVAVSATIPNISDIADWLSHESLPAT 499
Cdd:PRK00254   136 ----IKDVKLVVADEIHLIGSYDRGATLEMILTHM--------------LGRAQILGLSATVGNAEELAEWLNAELVVSD 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  500 YldmdeshRPVMLRKVV--LGFPCPQNQTEFKFDLSLNykmANIIQTYSDQKPALVFCSTRKGAQQAATVLAKDARFIMS 577
Cdd:PRK00254   198 W-------RPVKLRKGVfyQGFLFWEDGKIERFPNSWE---SLVYDAVKKGKGALVFVNTRRSAEKEALELAKKIKRFLT 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  578 IEHNQRLMKYANSILDS----KLRELVMLGVGYHHAGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLPAHLVVIKST 653
Cdd:PRK00254   268 KPELRALKELADSLEENptneKLKKALRGGVAFHHAGLGRTERVLIEDAFREGLIKVITATPTLSAGINLPAFRVIIRDT 347

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  654 MQYVAGSCEEYSDADMLQMIGRAGRPQFDTTATAVIMTKIQSKDKYMN-------------LMNgveiiESSLHSHLVeh 720
Cdd:PRK00254   348 KRYSNFGWEDIPVLEIQQMMGRAGRPKYDEVGEAIIVATTEEPSKLMEryifgkpeklfsmLSN-----ESAFRSQVL-- 420

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  721 lnAEIVLQTISDVNMALDWIRSTFlYIRALKNPSHygfppsldrcgIEAKLQELclrnLNSLSSIGLIDMDEDINIKPTE 800
Cdd:PRK00254   421 --ALITNFGVSNFKELVNFLERTF-YAHQRKDLYS-----------LEEKAKEI----VYFLLENEFIDIDLEDRFIPLP 482

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  801 TGKLMARYCIAFDTMNLFS----KVAGTENLSDLIELLSRSKEFSNIQLRVNEKRALNTLNRD-KNRLTIRFP------- 868
Cdd:PRK00254   483 LGIRTSQLYIDPLTAKKFKdafpKIEKNPNPLGIFQLIASTPDMTPLNYSRKEMEDLLDEAYEmEDRLYFNIPywedykf 562

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  869 --FQGKIKTTEMKVNCLIQAQLGSLsIQEFGLSQ-DTARIFRTGTRISRCLSEFLS-HGPKTGFSALLNSLIL--AKCFR 942
Cdd:PRK00254   563 qkFLRAFKTAKVLLDWINEVPEGEI-VETYNIDPgDLYRILELADWLMYSLIELYKlFEPKQEVLDYLETLHLrvKHGVR 641

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....
gi 1698318692  943 AKLWEnspyvSKQLEKIGQTLSTAMVNAGLTTFSKIEQTNPREL 986
Cdd:PRK00254   642 EELLE-----LMRLPMIGRKRARALYNAGFRSIEDIVNAKPSEL 680
Sec63 pfam02889
Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of ...
 798-1113 3.13e-54

Sec63 Brl domain; This domain (also known as the Brl domain) is required for assembly of functional endoplasmic reticulum translocons.


Pssm-ID: 460740  Cd Length: 307  Bit Score: 192.03  E-value: 3.13e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  798 PTETGKLMARYCIAFDTMNLF-SKVAGTENLSDLIELLSRSKEFSNIQLRVNEKRALNTLNrDKnrltIRFPFQGKIKTT 876
Cdd:pfam02889    1 PTDLGRIASHYYISYETIETFnQSLKPNTTLADLLRILSSASEFEQIPVRQEEKKELKKLL-EK----VPIPVKGDIEDP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  877 EMKVNCLIQAQLGSLSIQEFGLSQDTARIFRTGTRISRCLSEFLSHgpKTGFSALLNSLILAKCFRAKLWeNSPYVSKQL 956
Cdd:pfam02889   76 HAKVNILLQAYISRLKLPGFALVSDMNYILQNAGRILRALFEILLS--KGWLSAALTALDLCKMIEQRMW-DSDSPLRQF 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  957 EKIGQTLSTAMVNAGLTTFSKIEQTNPRELELIVNRHPPFGNQIRDSVVHLPKYEvILEQLPRYSCAAAEMVVKVNLKNQ 1036
Cdd:pfam02889  153 PGIPPELIKKLEKKGVESVRDILELDDAEELGELIRNPKMGKDIAQFVNRFPKIE-IEAEVQPITRSVLRVEVTITPDFP 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692 1037 AElltKKTAPDYHYVSLIIGNSDNVVVFQQKLTsSMLLKSGSWSKKIEVA---KASKGEEISVNLISSEYVGLDIQQKIN 1113
Cdd:pfam02889  232 WD---KRVHGKSEGFWLVVGDSDGNEILHIERF-TLTKRTLAGEHKLEFTvppSDPGPPQLFVRLISDSWLGADQEVPIS 307
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
 508-692 5.23e-53

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: 182.75  E-value: 5.23e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  508 RPVMLRKVVLGFP----CPQNQTEFKFDLslNYKMANIIQTYSDQKPALVFCSTRKGAQQAATVLAkdarfimsiehnqr 583
Cdd:cd18795      1 RPVPLEEYVLGFNglgiKLRVDVMNKFDS--DIIVLLKIETVSEGKPVLVFCSSRKECEKTAKDLA-------------- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  584 lmkyansildsklrelvmlGVGYHHAGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLPAHLVVIKSTMQYVAGSCEE 663
Cdd:cd18795     65 -------------------GIAFHHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLPARTVIIKGTQRYDGKGYRE 125

                          170       180
                   ....*....|....*....|....*....
gi 1698318692  664 YSDADMLQMIGRAGRPQFDTTATAVIMTK 692
Cdd:cd18795    126 LSPLEYLQMIGRAGRPGFDTRGEAIIMTK 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 ...
 300-491 5.44e-52

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: 181.30  E-value: 5.44e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  300 FPFFNYVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEPwnevKAVYMAPIKALCSQCFENWNKKFGP- 378
Cdd:cd18021      1 FKFFNPIQTQVFNSLYNTDDNVFVGAPTGSGKTVCAELALLRHWRQNPKG----RAVYIAPMQELVDARYKDWRAKFGPl 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  379 LGLTCKELTGDTEIDDFFeIQDSHIILTTPEKWDSMTRKWKDHCLLQQVRLFLIDEVHVIkDATRGATLEVVVSRMKavn 458
Cdd:cd18021     77 LGKKVVKLTGETSTDLKL-LAKSDVILATPEQWDVLSRRWKQRKNVQSVELFIADELHLI-GGENGPVYEVVVSRMR--- 151

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1698318692  459 aYRAAQnqgTSGTMRIVAVSATIPNISDIADWL 491
Cdd:cd18021    152 -YISSQ---LEKPIRIVGLSSSLANARDVGEWL 180
PRK01172 PRK01172
ATP-dependent DNA helicase;
318-695 1.13e-46

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 179.69  E-value: 1.13e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  318 GKNFVACAPTGSGKTVLFELAIIRLLMQNsepwneVKAVYMAPIKALCSQCFENWNKkFGPLGLTCKELTGDTEIDDFFe 397
Cdd:PRK01172    37 GENVIVSVPTAAGKTLIAYSAIYETFLAG------LKSIYIVPLRSLAMEKYEELSR-LRSLGMRVKISIGDYDDPPDF- 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  398 IQDSHIILTTPEKWDSMTRKwkDHCLLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAVNAyraaqnqgtsgTMRIVAV 477
Cdd:PRK01172   109 IKRYDVVILTSEKADSLIHH--DPYIINDVGLIVADEIHIIGDEDRGPTLETVLSSARYVNP-----------DARILAL 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  478 SATIPNISDIADWLSHESLPATYldmdeshRPVMLRKVVLGFPCPQNQTEFKFDLSLNYKMANIIQtysDQKPALVFCST 557
Cdd:PRK01172   176 SATVSNANELAQWLNASLIKSNF-------RPVPLKLGILYRKRLILDGYERSQVDINSLIKETVN---DGGQVLVFVSS 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  558 RKGAQQAATVLAKdarfIMSIEHNQRLMKYANSILDSKLRELVMLGVGYHHAGVDLSDRKLIEMAFTQADLPVLFTTRTL 637
Cdd:PRK01172   246 RKNAEDYAEMLIQ----HFPEFNDFKVSSENNNVYDDSLNEMLPHGVAFHHAGLSNEQRRFIEEMFRNRYIKVIVATPTL 321

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1698318692  638 AMGVNLPAHLVVIKSTMQYVAGSCEEYSDADMLQMIGRAGRPQFDTTATAVIMTKIQS 695
Cdd:PRK01172   322 AAGVNLPARLVIVRDITRYGNGGIRYLSNMEIKQMIGRAGRPGYDQYGIGYIYAASPA 379
DEXHc_ASCC3_2 cd18022
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
 302-491 5.78e-45

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: 161.00  E-value: 5.78e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  302 FFNYVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLmqNSEPwnEVKAVYMAPIKALCSQCFENWNKKF-GPLG 380
Cdd:cd18022      1 HFNPIQTQVFHTLYHTDNNVLLGAPTGSGKTIAAELAMFRAF--NKYP--GSKVVYIAPLKALVRERVDDWKKRFeEKLG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  381 LTCKELTGDTeIDDFFEIQDSHIILTTPEKWDSMTRKWKDHCLLQQVRLFLIDEVHVIKDaTRGATLEVVVSRMKavnaY 460
Cdd:cd18022     77 KKVVELTGDV-TPDMKALADADIIITTPEKWDGISRSWQTREYVQQVSLIIIDEIHLLGS-DRGPVLEVIVSRMN----Y 150

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1698318692  461 RAAQnqgTSGTMRIVAVSATIPNISDIADWL 491
Cdd:cd18022    151 ISSQ---TEKPVRLVGLSTALANAGDLANWL 178
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
 304-491 9.89e-44

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: 157.98  E-value: 9.89e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  304 NYVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEPW-----NEVKAVYMAPIKALCSQCFENWNKKFGP 378
Cdd:cd18020      3 NRIQSLVFPVAYKTNENMLICAPTGAGKTNIAMLTILHEIRQHVNQGgvikkDDFKIVYIAPMKALAAEMVEKFSKRLAP 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  379 LGLTCKELTGDTEIDDfFEIQDSHIILTTPEKWDSMTRKW-KDHCLLQQVRLFLIDEVHVIKDaTRGATLEVVVSRMKav 457
Cdd:cd18020     83 LGIKVKELTGDMQLTK-KEIAETQIIVTTPEKWDVVTRKSsGDVALSQLVRLLIIDEVHLLHD-DRGPVIESLVARTL-- 158

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1698318692  458 nayraAQNQGTSGTMRIVAVSATIPNISDIADWL 491
Cdd:cd18020    159 -----RQVESTQSMIRIVGLSATLPNYLDVADFL 187
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
 303-494 1.07e-41

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: 151.33  E-value: 1.07e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  303 FNYVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSepwnevKAVYMAPIKALCSQCFENWnKKFGPLGLT 382
Cdd:cd18028      2 LYPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG------KALYLVPLRALASEKYEEF-KKLEEIGLK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  383 CKELTGDTEIDDFFeIQDSHIILTTPEKWDSMTRKWKDhcLLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAVNayra 462
Cdd:cd18028     75 VGISTGDYDEDDEW-LGDYDIIVATYEKFDSLLRHSPS--WLRDVGVVVVDEIHLISDEERGPTLESIVARLRRLN---- 147

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1698318692  463 aqnqgtsGTMRIVAVSATIPNISDIADWLSHE 494
Cdd:cd18028    148 -------PNTQIIGLSATIGNPDELAEWLNAE 172
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
 287-491 1.56e-41

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: 152.14  E-value: 1.56e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  287 VSEIPKF-RSVFSEFPFFNYVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEP-----WNEVKAVYMAP 360
Cdd:cd18019      1 IEELPDWaQPAFEGFKSLNRIQSKLFPAAFETDENLLLCAPTGAGKTNVALLTILREIGKHRNPdgtinLDAFKIVYIAP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  361 IKALCSQCFENWNKKFGPLGLTCKELTGDTEIDDFfEIQDSHIILTTPEKWDSMTRKWKDHCLLQQVRLFLIDEVHVIKD 440
Cdd:cd18019     81 MKALVQEMVGNFSKRLAPYGITVAELTGDQQLTKE-QISETQIIVTTPEKWDIITRKSGDRTYTQLVRLIIIDEIHLLHD 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1698318692  441 aTRGATLEVVVSRmkavnAYRaaQNQGTSGTMRIVAVSATIPNISDIADWL 491
Cdd:cd18019    160 -DRGPVLESIVAR-----TIR--QIEQTQEYVRLVGLSATLPNYEDVATFL 202
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
268-690 1.99e-39

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 158.56  E-value: 1.99e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  268 MTPQPLRIKDRSDSgILRPVSEIPkfrsvFSEFPFfnyvQSKALDDVLyTGKNFVACAPTGSGKTVLFELAIIRLLMQNs 347
Cdd:COG4581      1 MTLSPARADARLEA-LADFAEERG-----FELDPF----QEEAILALE-AGRSVLVAAPTGSGKTLVAEFAIFLALARG- 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  348 epwneVKAVYMAPIKALCSQCFENWNKKFGP--LGLtckeLTGDTEIDDffeiQDSHIILTTpEKWDSMTRKWKDHclLQ 425
Cdd:COG4581     69 -----RRSFYTAPIKALSNQKFFDLVERFGAenVGL----LTGDASVNP----DAPIVVMTT-EILRNMLYREGAD--LE 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  426 QVRLFLIDEVHVIKDATRGATLEVVVSRMKAvnayraaqnqgtsgTMRIVAVSATIPNISDIADWLShESLPATYLdMDE 505
Cdd:COG4581    133 DVGVVVMDEFHYLADPDRGWVWEEPIIHLPA--------------RVQLVLLSATVGNAEEFAEWLT-RVRGETAV-VVS 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  506 SHRPVMLRKVVL----GFPCPQNQTEFKFDLSLNYKMANIIQTysDQKPALVFCSTRKGAQQAATVLAKD---------- 571
Cdd:COG4581    197 EERPVPLEFHYLvtprLFPLFRVNPELLRPPSRHEVIEELDRG--GLLPAIVFIFSRRGCDEAAQQLLSArlttkeerae 274

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  572 -ARFIMSIEHNQRLMKYansildSKLRELVMLGVGYHHAGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLPAHLVVI 650
Cdd:COG4581    275 iREAIDEFAEDFSVLFG------KTLSRLLRRGIAVHHAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINMPARTVVF 348

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1698318692  651 KS-------TMQYVAGSceEYsdadmLQMIGRAGRPQFDTTATAVIM 690
Cdd:COG4581    349 TKlskfdgeRHRPLTAR--EF-----HQIAGRAGRRGIDTEGHVVVL 388
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 306-487 4.91e-37

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: 137.37  E-value: 4.91e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDdVLYTGKNFVACAPTGSGKTVLFELAIIRLLmqnSEPWNEVKAVYMAPIKALCSQCFENWNKKFGPLGLT-CK 384
Cdd:pfam00270    3 IQAEAIP-AILEGRDVLVQAPTGSGKTLAFLLPALEAL---DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKvAS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  385 ELTGDTEIDDFFEIQDSHIILTTPEKWDSMTRKWKdhcLLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAvnayraaq 464
Cdd:pfam00270   79 LLGGDSRKEQLEKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPK-------- 147

                          170       180
                   ....*....|....*....|....
gi 1698318692  465 nqgtsgTMRIVAVSATIP-NISDI 487
Cdd:pfam00270  148 ------KRQILLLSATLPrNLEDL 165
DEXDc smart00487
DEAD-like helicases superfamily;
298-483 1.03e-28

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 114.90  E-value: 1.03e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   298 SEFPFFNYVQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEPwnevKAVYMAPIKALCSQCFENWNKKFG 377
Cdd:smart00487    4 FGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKGG----RVLVLVPTRELAEQWAEELKKLGP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   378 PLGL-TCKELTGDTEIDDFFEIQ--DSHIILTTPEKWDSMTRkwKDHCLLQQVRLFLIDEVHVIKDATRGATLEVVVSRM 454
Cdd:smart00487   80 SLGLkVVGLYGGDSKREQLRKLEsgKTDILVTTPGRLLDLLE--NDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL 157

                           170       180
                    ....*....|....*....|....*....
gi 1698318692   455 KAVNayraaqnqgtsgtmRIVAVSATIPN 483
Cdd:smart00487  158 PKNV--------------QLLLLSATPPE 172
COG1202 COG1202
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
306-707 1.21e-24

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


Pssm-ID: 440815 [Multi-domain]  Cd Length: 790  Bit Score: 111.91  E-value: 1.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNsepwnEVKAVYMAPIKALCSQCFENWNKKFGPlGLTCKE 385
Cdd:COG1202    213 VQSLAVENGLLEGKDQLVVSATATGKTLIGELAGIKNALEG-----KGKMLFLVPLVALANQKYEDFKDRYGD-GLDVSI 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  386 LTGDTEIDDFFE--IQDSHIILTTPEKWDSMTRKWKDhclLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAVnaYRAA 463
Cdd:COG1202    287 RVGASRIRDDGTrfDPNADIIVGTYEGIDHALRTGRD---LGDIGTVVIDEVHMLEDPERGHRLDGLIARLKYY--CPGA 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  464 QnqgtsgtmrIVAVSATIPNISDIAdwlshESLPATYLDMDEshRPVML-RKVVLgfpCPQNQ----------TEFKFDL 532
Cdd:COG1202    362 Q---------WIYLSATVGNPEELA-----KKLGAKLVEYEE--RPVPLeRHLTF---ADGREkiriinklvkREFDTKS 422

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  533 SLNYKMANIIQTYSdqkpalvfcstRKGAQQAATVLAKDARfimsiehnqrlmkyansildsklrelvmlgvgYHHAGVD 612
Cdd:COG1202    423 SKGYRGQTIIFTNS-----------RRRCHEIARALGYKAA--------------------------------PYHAGLD 459

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  613 LSDRKLIEMAFTQADLPVLFTTRTLAMGVNLPAHLVVIKS--------TMQyvagsceEYSdadmlQMIGRAGRPQFDTT 684
Cdd:COG1202    460 YGERKKVERRFADQELAAVVTTAALAAGVDFPASQVIFDSlamgiewlSVQ-------EFH-----QMLGRAGRPDYHDR 527

                          410       420
                   ....*....|....*....|...
gi 1698318692  685 ATAVIMTKIQSkdKYMNLMNGVE 707
Cdd:COG1202    528 GKVYLLVEPGK--SYHRSMEMTE 548
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
 307-678 1.00e-21

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: 102.22  E-value: 1.00e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  307 QSKALDdVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEPwnevKAVYMAPIKALCSQCFENWNK--KFGPLGLTCK 384
Cdd:COG1205     61 QAEAIE-AARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGA----TALYLYPTKALARDQLRRLRElaEALGLGVRVA 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  385 ELTGDTEIDDFFEIQD-SHIILTTPEKWD-SM---TRKWKDhcLLQQVRLFLIDEVHVIKDATrGATLEVVVSRMKavna 459
Cdd:COG1205    136 TYDGDTPPEERRWIREhPDIVLTNPDMLHyGLlphHTRWAR--FFRNLRYVVIDEAHTYRGVF-GSHVANVLRRLR---- 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  460 yRAAQNQGTSgtMRIVAVSATIPNISDIAdwlshESLpaTYLDM---DESHRPVMLRKVVLGFPCPQNQTEFKfdlSLNY 536
Cdd:COG1205    209 -RICRHYGSD--PQFILASATIGNPAEHA-----ERL--TGRPVtvvDEDGSPRGERTFVLWNPPLVDDGIRR---SALA 275

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  537 KMANIIQTYSDQK-PALVFCSTRKGAQQAATVLAKDARfimsiehnqrlmkyansilDSKLRELVMLgvgyHHAGVDLSD 615
Cdd:COG1205    276 EAARLLADLVREGlRTLVFTRSRRGAELLARYARRALR-------------------EPDLADRVAA----YRAGYLPEE 332

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698318692  616 RKLIEMAFTQADLPVLFTTRTLAMGVNLPaHL-VVIkstmqyVAGsceeY--SDADMLQMIGRAGR 678
Cdd:COG1205    333 RREIERGLRSGELLGVVSTNALELGIDIG-GLdAVV------LAG----YpgTRASFWQQAGRAGR 387
SEC63 smart00611
Domain of unknown function in Sec63p, Brr2p and other proteins;
796-1115 5.25e-20

Domain of unknown function in Sec63p, Brr2p and other proteins;


Pssm-ID: 214744  Cd Length: 312  Bit Score: 92.71  E-value: 5.25e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   796 IKPTETGKLMARYCIAFDTMNLFSKvAGTENLS--DLIELLSRSKEFSNIQLRVNEKRALNTLNrdkNRLTIRFPFQgKI 873
Cdd:smart00611    2 IWPTDLGRIASYYYISYTTIRTFNE-LLKPKMTtkDLLRILSMSSEFDQIPVRHEEDLLLEELA---EKLPIRLENP-SL 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   874 KTTEMKVNCLIQAQLGSLSIQEFGLSQDTARIFRTGTRISRCLSEFLSHgpKTGFSALLNSLILAKCFRAKLWENSPYVs 953
Cdd:smart00611   77 DDPHVKANLLLQAHLSRLKLPSFALESDTVYVLQNAGRLLQAMVDIALE--RGWLSTALNALNLSQMIIQALWPTDSPL- 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   954 KQLEKIGQTLSTAMVNAGLTTFSKIEQTNPRELELIVNRHPPFGNQIRDSVVHLPKYEVILEQLPR-YSCAAAEMVVKVN 1032
Cdd:smart00611  154 LQLPHLPEEILKRLEKKKVLSLEDLLELEDEERGELLGLLDAEGERVYKVLSRLPKLNIEISLEPItRTVLGVEVTLTVD 233

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  1033 LKNQaELLTKKTAPDYhyvsLIIGNSD-NVVVFQQKLtsSMLLKSGSWSKKIE-VAKASKG-EEISVNLISSEYVGLDIQ 1109
Cdd:smart00611  234 LTWD-DEIHGKQEGWW----LVIGDSDgNELLHIERF--SLNKKNVSEEVKLDfTAPATEGnYQYTLRLVSDSYLGCDQE 306


                    ....*.
gi 1698318692  1110 QKINVH 1115
Cdd:smart00611  307 YPLSFD 312
DEXHc_POLQ-like cd18026
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ...
 311-491 1.21e-17

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: 83.03  E-value: 1.21e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  311 LDDVLyTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEpwnevKAVYMAPIKALCSQCFENWNKKFGPLGLTCKELTGDT 390
Cdd:cd18026     27 LPGLL-EGRNLVYSLPTSGGKTLVAEILMLKRLLERRK-----KALFVLPYVSIVQEKVDALSPLFEELGFRVEGYAGNK 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  391 EIDDFFEIQDSHIILTTPEKWDSMTRKWKDHCLLQQVRLFLIDEVHVIKDATRGATLEVVVSRMkavnAYRAaqnqgtSG 470
Cdd:cd18026    101 GRSPPKRRKSLSVAVCTIEKANSLVNSLIEEGRLDELGLVVVDELHMLGDGHRGALLELLLTKL----LYAA------QK 170

                          170       180
                   ....*....|....*....|.
gi 1698318692  471 TMRIVAVSATIPNISDIADWL 491
Cdd:cd18026    171 NIQIVGMSATLPNLEELASWL 191
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
 318-491 4.06e-17

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: 80.32  E-value: 4.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  318 GKNFVACAPTGSGKTVLFELAIIRLLMQnsEPWNEVKAVYMAPIKALCSQCFENWNKkfgPLGLTCKEL-----TGDT-- 390
Cdd:cd17922      1 GRNVLIAAPTGSGKTEAAFLPALSSLAD--EPEKGVQVLYISPLKALINDQERRLEE---PLDEIDLEIpvavrHGDTsq 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  391 EIDDFFEIQDSHIILTTPEKWDSM-TRKWKDHcLLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAVnayraaqnqgTS 469
Cdd:cd17922     76 SEKAKQLKNPPGILITTPESLELLlVNKKLRE-LFAGLRYVVVDEIHALLGSKRGVQLELLLERLRKL----------TG 144

                          170       180
                   ....*....|....*....|..
gi 1698318692  470 GTMRIVAVSATIPNISDIADWL 491
Cdd:cd17922    145 RPLRRIGLSATLGNLEEAAAFL 166
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
 318-488 5.98e-17

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: 80.32  E-value: 5.98e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  318 GKNFVACAPTGSGKTVLFELAIIRLLMQNSepwnEVKAVYMAPIKALC-SQ--CFENWNKKFGPlGLTCKELTGDTEIDD 394
Cdd:cd17923     15 GRSVVVTTGTASGKSLCYQLPILEALLRDP----GSRALYLYPTKALAqDQlrSLRELLEQLGL-GIRVATYDGDTPREE 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  395 FFEIQDS--HIILTTPEKWD-SMTR---KWKDhcLLQQVRLFLIDEVHVIKDAtRGATLEVVVSRMKavnayRAAQNQGT 468
Cdd:cd17923     90 RRAIIRNppRILLTNPDMLHyALLPhhdRWAR--FLRNLRYVVLDEAHTYRGV-FGSHVALLLRRLR-----RLCRRYGA 161

                          170       180
                   ....*....|....*....|
gi 1698318692  469 SgtMRIVAVSATIPNISDIA 488
Cdd:cd17923    162 D--PQFILTSATIGNPAEHA 179
DEXHc_SKIV2L cd18027
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ...
 291-491 2.78e-16

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: 78.46  E-value: 2.78e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  291 PKFRSVFSEFPFfnyvQSKALDDVLYTGKNFVAcAPTGSGKTVLFELAIIrlLMQNsepwNEVKAVYMAPIKALCSQCFE 370
Cdd:cd18027      1 PAFKWPFELDVF----QKQAILHLEAGDSVFVA-AHTSAGKTVVAEYAIA--LAQK----HMTRTIYTSPIKALSNQKFR 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  371 NWNKKFGPLGLtckeLTGDTEIDdffeiQDSHIILTTPEKWDSMTRKWKDhcLLQQVRLFLIDEVHVIKDATRGATLEVV 450
Cdd:cd18027     70 DFKNTFGDVGL----ITGDVQLN-----PEASCLIMTTEILRSMLYNGSD--VIRDLEWVIFDEVHYINDAERGVVWEEV 138

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1698318692  451 VSRMKAvnayraaqnqgtsgTMRIVAVSATIPNISDIADWL 491
Cdd:cd18027    139 LIMLPD--------------HVSIILLSATVPNTVEFADWI 165
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
294-679 2.24e-14

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 78.14  E-value: 2.24e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  294 RSVFSEFPFFNYvQSKALDDVLYT----GKNFVACAPTGSGKTVLFELAIIRLLmqnsepwNEVKAVYMAPIKALCSQcf 369
Cdd:COG1061     73 EASGTSFELRPY-QQEALEALLAAlergGGRGLVVAPTGTGKTVLALALAAELL-------RGKRVLVLVPRRELLEQ-- 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  370 enWNKKFgplgltcKELTGDTEIDDFFEIQDSHIILTTpekWDSMTRKWKDHCLLQQVRLFLIDEVHVIkdatRGATLEV 449
Cdd:COG1061    143 --WAEEL-------RRFLGDPLAGGGKKDSDAPITVAT---YQSLARRAHLDELGDRFGLVIIDEAHHA----GAPSYRR 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  450 VVSRMKAVnayraaqnqgtsgtmRIVAVSATiPNISD----IADWLSHESLPATYLDMDESH--RPVMLRKVVLGFPCPQ 523
Cdd:COG1061    207 ILEAFPAA---------------YRLGLTAT-PFRSDgreiLLFLFDGIVYEYSLKEAIEDGylAPPEYYGIRVDLTDER 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  524 NQTEfKFDLSLNYKMAN-----------IIQTYSDQKPALVFCStrkgaqqaatvlakdarfimSIEHNQRLMKYansil 592
Cdd:COG1061    271 AEYD-ALSERLREALAAdaerkdkilreLLREHPDDRKTLVFCS--------------------SVDHAEALAEL----- 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  593 dskLRELvmlgvGYH----HAGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLPA--HLVVIKSTMqyvagsceeySD 666
Cdd:COG1061    325 ---LNEA-----GIRaavvTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRldVAILLRPTG----------SP 386

                          410
                   ....*....|...
gi 1698318692  667 ADMLQMIGRAGRP 679
Cdd:COG1061    387 REFIQRLGRGLRP 399
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 318-448 5.90e-14

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 70.51  E-value: 5.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  318 GKNFVACAPTGSGKTVLFELAIIRLLMQnsepwNEVKAVYMAPIKALCSQCFENWnKKFGPLGLTCKELTGDT--EIDDF 395
Cdd:cd00046      1 GENVLITAPTGSGKTLAALLAALLLLLK-----KGKKVLVLVPTKALALQTAERL-RELFGPGIRVAVLVGGSsaEEREK 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1698318692  396 FEIQDSHIILTTPEK-WDSMTRKWKDHclLQQVRLFLIDEVHVIKDATRGATLE 448
Cdd:cd00046     75 NKLGDADIIIATPDMlLNLLLREDRLF--LKDLKLIIVDEAHALLIDSRGALIL 126
DEXHc_Mtr4-like cd18024
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ...
 325-493 8.67e-14

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: 71.71  E-value: 8.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  325 APTGSGKTVLFELAIIRLLMQNSepwnevKAVYMAPIKALCSQCFENWNKKFGPLGLtckeLTGDTEIDdffeiQDSHII 404
Cdd:cd18024     54 AHTSAGKTVVAEYAIAQSLRDKQ------RVIYTSPIKALSNQKYRELQEEFGDVGL----MTGDVTIN-----PNASCL 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  405 LTTPEKWDSMTrkWKDHCLLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAvnayraaqnqgtsgTMRIVAVSATIPNI 484
Cdd:cd18024    119 VMTTEILRSML--YRGSEIMREVAWVIFDEIHYMRDKERGVVWEETIILLPD--------------KVRYVFLSATIPNA 182


                   ....*....
gi 1698318692  485 SDIADWLSH 493
Cdd:cd18024    183 RQFAEWICK 191
ResIII pfam04851
Type III restriction enzyme, res subunit;
303-436 2.18e-12

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 66.54  E-value: 2.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  303 FNYVQSKALDDVL----YTGKNFVACAPTGSGKTVLFeLAIIRLLMQNSepwNEVKAVYMAPIKALCSQCFENWNKKFGP 378
Cdd:pfam04851    4 LRPYQIEAIENLLesikNGQKRGLIVMATGSGKTLTA-AKLIARLFKKG---PIKKVLFLVPRKDLLEQALEEFKKFLPN 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1698318692  379 LGLTCKELTGDTEIddfFEIQDSHIILTTPEKWDSMTRKWKDHCLLQQVRLFLIDEVH 436
Cdd:pfam04851   80 YVEIGEIISGDKKD---ESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAH 134
HELICc smart00490
helicase superfamily c-terminal domain;
591-679 2.85e-12

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 63.77  E-value: 2.85e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692   591 ILDSKLRELVmLGVGYHHAGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLP-AHLVVIKSTmqyvagsceEYSDADM 669
Cdd:smart00490    2 ELAELLKELG-IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPgVDLVIIYDL---------PWSPASY 71

                            90
                    ....*....|
gi 1698318692   670 LQMIGRAGRP 679
Cdd:smart00490   72 IQRIGRAGRA 81
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
 325-677 7.89e-12

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 70.72  E-value: 7.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  325 APTGSGKTVL-FELAIIRLLMQ------NSEPWNEVKAVYMAPIKALCSQCFENWN----------KKFGPLG--LTCKE 385
Cdd:PRK09751     3 APTGSGKTLAaFLYALDRLFREggedtrEAHKRKTSRILYISPIKALGTDVQRNLQiplkgiaderRRRGETEvnLRVGI 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  386 LTGDTEIDDFFEI--QDSHIILTTPEKWDSM-TRKWKDhcLLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAVNAYRA 462
Cdd:PRK09751    83 RTGDTPAQERSKLtrNPPDILITTPESLYLMlTSRARE--TLRGVETVIIDEVHAVAGSKRGAHLALSLERLDALLHTSA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  463 AQnqgtsgtmriVAVSATIPNISDIADWLSHESlPATYLDMDESHRPvMLRKVVlgfPC------PQNQTEFKFDLSLN- 535
Cdd:PRK09751   161 QR----------IGLSATVRSASDVAAFLGGDR-PVTVVNPPAMRHP-QIRIVV---PVanmddvSSVASGTGEDSHAGr 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  536 ------YKMANIIQTYSDQKPALVFCSTRKGAQQAATVL--AKDARFIMSIEHNQRLMKYANSILDSKLREL---VMLGV 604
Cdd:PRK09751   226 egsiwpYIETGILDEVLRHRSTIVFTNSRGLAEKLTARLneLYAARLQRSPSIAVDAAHFESTSGATSNRVQssdVFIAR 305

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1698318692  605 GyHHAGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLPAHLVVIKstmqyVAGSceeYSDADMLQMIGRAG 677
Cdd:PRK09751   306 S-HHGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQ-----VATP---LSVASGLQRIGRAG 369
DEXH_lig_assoc TIGR04121
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ...
 325-516 8.15e-12

DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.


Pssm-ID: 274994 [Multi-domain]  Cd Length: 804  Bit Score: 70.27  E-value: 8.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  325 APTGSGKTV-LFELAIIRLLMQNSEPWNEVKAVYMAPIKALCSQCFENWNKKFGPLGLTCK-EL-TGDTEIDDFFEIQDS 401
Cdd:TIGR04121   35 APTGSGKTLaGFLPSLIDLAGPEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGLPIRvETrTGDTSSSERARQRKK 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  402 --HIILTTPEKWdSMTRKWKDHC-LLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAVNAyraaqnqgtsgTMRIVAVS 478
Cdd:TIGR04121  115 ppDILLTTPESL-ALLLSYPDAArLFKDLRCVVVDEWHELAGSKRGDQLELALARLRRLAP-----------GLRRWGLS 182

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1698318692  479 ATIPNISDIADWLSHESLPATYLDMDESHRPVMLRKVV 516
Cdd:TIGR04121  183 ATIGNLEEARRVLLGVGGAPAVLVRGKLPKAIEVISLL 220
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
293-491 8.74e-11

Lhr-like helicase [Replication, recombination and repair];


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 66.66  E-value: 8.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  293 FRSVFSE-FPFfnyvQSKALDDVLyTGKNFVACAPTGSGKTV-LFeLAIIRLLMQNSEPW---NEVKAVYMAPIKALCSQ 367
Cdd:COG1201     18 FAARFGApTPP----QREAWPAIA-AGESTLLIAPTGSGKTLaAF-LPALDELARRPRPGelpDGLRVLYISPLKALAND 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  368 CFENWNKkfgPL-------GLTCKEL-----TGDTeiddffeiqDS-----------HIILTTPEkwdSMT-----RKWK 419
Cdd:COG1201     92 IERNLRA---PLeeigeaaGLPLPEIrvgvrTGDT---------PAserqrqrrrppHILITTPE---SLAllltsPDAR 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1698318692  420 DHclLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAVNAYRaaqnqgtsgtMRIVAVSATIPNISDIADWL 491
Cdd:COG1201    157 EL--LRGVRTVIVDEIHALAGSKRGVHLALSLERLRALAPRP----------LQRIGLSATVGPLEEVARFL 216
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 306-493 1.47e-10

DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 62.34  E-value: 1.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDDVLyTGKNFVACAPTGSGKTVLFELAIIRLlmqnsepwneVKAVYMAPIKALCSQ---CFENWNKKFGPLGLT 382
Cdd:cd17938     25 IQAEAIPLIL-GGGDVLMAAETGSGKTGAFCLPVLQI----------VVALILEPSRELAEQtynCIENFKKYLDNPKLR 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  383 CKELTGDTEIDDFFE--IQDSHIILTTPEKWDSMTRKWKDhcLLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKavnay 460
Cdd:cd17938     94 VALLIGGVKAREQLKrlESGVDIVVGTPGRLEDLIKTGKL--DLSSVRFFVLDEADRLLSQGNLETINRIYNRIP----- 166

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1698318692  461 raaqnQGTSGTMR--IVAVSATI--PNISDIADWLSH 493
Cdd:cd17938    167 -----KITSDGKRlqVIVCSATLhsFEVKKLADKIMH 198
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 318-490 1.66e-10

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: 62.22  E-value: 1.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  318 GKNFVACAPTGSGKTVLFELAII-RLLMQNSEPwnEVKAVYMAPIKALCSQCFENWNKKFGPLGLTCKELT-GDTEIDDF 395
Cdd:cd17957     27 GRDLLACAPTGSGKTLAFLIPILqKLGKPRKKK--GLRALILAPTRELASQIYRELLKLSKGTGLRIVLLSkSLEAKAKD 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  396 FEIQDSH--IILTTPEKW-DSMTRKWKDhclLQQVRLFLIDEVHVIKDAT-RGATLEVvvsrmkavnaYRAAQNQGTSGT 471
Cdd:cd17957    105 GPKSITKydILVSTPLRLvFLLKQGPID---LSSVEYLVLDEADKLFEPGfREQTDEI----------LAACTNPNLQRS 171

                          170
                   ....*....|....*....
gi 1698318692  472 MrivaVSATIPniSDIADW 490
Cdd:cd17957    172 L----FSATIP--SEVEEL 184
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 306-435 2.11e-10

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: 61.69  E-value: 2.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDDVLyTGKNFVACAPTGSGKTVLFELAII-RLLMQNSEPWNEVKAVYMAPIKALCSQCFENWNKKFGPLGLTCK 384
Cdd:cd00268     16 IQAQAIPLIL-SGRDVIGQAQTGSGKTLAFLLPILeKLLPEPKKKGRGPQALVLAPTRELAMQIAEVARKLGKGTGLKVA 94

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1698318692  385 ELTGDTEIDDFFEI--QDSHIILTTPEK-WDSMTRKwkdHCLLQQVRLFLIDEV 435
Cdd:cd00268     95 AIYGGAPIKKQIEAlkKGPDIVVGTPGRlLDLIERG---KLDLSNVKYLVLDEA 145
PRK13767 PRK13767
ATP-dependent helicase; Provisional
 267-677 3.12e-10

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 64.91  E-value: 3.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  267 PMTPQPLRIKDRSDSGILRP-VSEIpkFRSVFSEF-PffnyVQSKALDDVlYTGKNFVACAPTGSGKTVLFELAIIRLLM 344
Cdd:PRK13767     1 MIEYATKEYSDEEILDLLRPyVREW--FKEKFGTFtP----PQRYAIPLI-HEGKNVLISSPTGSGKTLAAFLAIIDELF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  345 QNSEPW---NEVKAVYMAPIKALCSQCFENW-------NKKFGPLGLTCKEL-----TGDTeidDFFEIQD-----SHII 404
Cdd:PRK13767    74 RLGREGeleDKVYCLYVSPLRALNNDIHRNLeeplteiREIAKERGEELPEIrvairTGDT---SSYEKQKmlkkpPHIL 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  405 LTTPEkwdSM-----TRKWKDhcLLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAVnayraaqnqgTSGTMRIVAVSA 479
Cdd:PRK13767   151 ITTPE---SLaillnSPKFRE--KLRTVKWVIVDEIHSLAENKRGVHLSLSLERLEEL----------AGGEFVRIGLSA 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  480 TIPNISDIADWLsheslpATYLDmDESHRPV------MLRKVVLGFPCPQ----NQTEFKFDLSLNYKMANIIQtysDQK 549
Cdd:PRK13767   216 TIEPLEEVAKFL------VGYED-DGEPRDCeivdarFVKPFDIKVISPVddliHTPAEEISEALYETLHELIK---EHR 285

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  550 PALVFCSTRKGAQQAATVLAKdarfimsiehnqrlmKYANSILDSKlrelvmlgVGYHHAgvDLS-DRKL-IEMAFTQAD 627
Cdd:PRK13767   286 TTLIFTNTRSGAERVLYNLRK---------------RFPEEYDEDN--------IGAHHS--SLSrEVRLeVEEKLKRGE 340

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1698318692  628 LPVLFTTRTLAMGVNLPaH--LVVIKSTMQYVAGsceeysdadMLQMIGRAG 677
Cdd:PRK13767   341 LKVVVSSTSLELGIDIG-YidLVVLLGSPKSVSR---------LLQRIGRAG 382
DEXHc_DDX60 cd18025
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ...
 313-492 1.77e-09

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: 58.92  E-value: 1.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  313 DVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNsepwNEVKAVYMAPIKALCSQ----CFENWNKKFGPLGLT-CKELT 387
Cdd:cd18025     11 DIVDRRESALIVAPTSSGKTFISYYCMEKVLRES----DDGVVVYVAPTKALVNQvvaeVYARFSKKYPPSGKSlWGVFT 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  388 GDTEIDDffeIQDSHIILTTPEKWDSM-----TRKWKDHCllqqvRLFLIDEVHVIKDATRGATLEVVVSRMKAvnayra 462
Cdd:cd18025     87 RDYRHNN---PMNCQVLITVPECLEILllsphNASWVPRI-----KYVIFDEIHSIGQSEDGAVWEQLLLLIPC------ 152

                          170       180       190
                   ....*....|....*....|....*....|
gi 1698318692  463 aqnqgtsgtmRIVAVSATIPNISDIADWLS 492
Cdd:cd18025    153 ----------PFLALSATIGNPQKFHEWLQ 172
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 575-678 1.56e-08

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: 53.75  E-value: 1.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  575 IMSIEHNQRLMKYANSI--LDSK-LRELVMLGVGYHHAGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLP-AHLVVI 650
Cdd:pfam00271    9 LLKKERGGKVLIFSQTKktLEAElLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPdVDLVIN 88

                           90       100
                   ....*....|....*....|....*...
gi 1698318692  651 kstmqyvagSCEEYSDADMLQMIGRAGR 678
Cdd:pfam00271   89 ---------YDLPWNPASYIQRIGRAGR 107
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
 318-436 3.22e-08

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: 55.52  E-value: 3.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  318 GKNFVACAPTGSGKTvLFELAIIRLLMQNSEPWNEVKAVYMAPIKALCSQCFENWNKKFGPLGLTCKELTGDTEIDDFFE 397
Cdd:cd17927     17 GKNTIICLPTGSGKT-FVAVLICEHHLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENVSVE 95

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1698318692  398 --IQDSHIILTTPEKWDSmTRKWKDHCLLQQVRLFLIDEVH 436
Cdd:cd17927     96 qiVESSDVIIVTPQILVN-DLKSGTIVSLSDFSLLVFDECH 135
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
306-571 1.90e-07

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 55.15  E-value: 1.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDDVLyTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEpwNEVKAVYMAPIKALCSQCFENWnKKFG-PLGLTCK 384
Cdd:COG0513     28 IQAQAIPLIL-AGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP--RAPQALILAPTRELALQVAEEL-RKLAkYLGLRVA 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  385 ELTGDTEIDDffEIQD----SHIILTTPEK-WDSMTRKwkdHCLLQQVRLFLIDEVhvikDatrgatlevvvsRM----- 454
Cdd:COG0513    104 TVYGGVSIGR--QIRAlkrgVDIVVATPGRlLDLIERG---ALDLSGVETLVLDEA----D------------RMldmgf 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  455 -KAVNayraaqnqgtsgtmRIVA----------VSATIPN-ISDIADWLSHEslPATyLDMDESHRPVMLRKVVLgFPCP 522
Cdd:COG0513    163 iEDIE--------------RILKllpkerqtllFSATMPPeIRKLAKRYLKN--PVR-IEVAPENATAETIEQRY-YLVD 224

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1698318692  523 QNQtefKFDLslnykMANIIQTYSDQKpALVFCSTRKGAQQAATVLAKD 571
Cdd:COG0513    225 KRD---KLEL-----LRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKR 264
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
 306-408 6.24e-07

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: 51.54  E-value: 6.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDDVLyTGKNFVACAPTGSGKTVLFELAIIRLLmQNSEPWNEVKAVYMAPIKALCSQCFeNWNKKFGP-LGLTCK 384
Cdd:cd17959     27 IQRKTIPLIL-DGRDVVAMARTGSGKTAAFLIPMIEKL-KAHSPTVGARALILSPTRELALQTL-KVTKELGKfTDLRTA 103

                           90       100
                   ....*....|....*....|....*.
gi 1698318692  385 ELTGDTEIDDFFEIQDSH--IILTTP 408
Cdd:cd17959    104 LLVGGDSLEEQFEALASNpdIIIATP 129
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
 319-480 1.66e-06

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: 50.01  E-value: 1.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  319 KNFVACAPTGSGKTVlfelaIIRLLMQNSEPW-NEVKAVYMAPIKALCSQCFENWNKKFGPLGLTCKELTGDTEIDDFFE 397
Cdd:cd18033     17 QNTLVALPTGLGKTF-----IAAVVMLNYYRWfPKGKIVFMAPTKPLVSQQIEACYKITGIPSSQTAELTGSVPPTKRAE 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  398 IQDS-HIILTTPEKWDSMTRkwKDHCLLQQVRLFLIDEVHvikDATRGATLEVVVSRMKAVNAYraaqnqgtsgtMRIVA 476
Cdd:cd18033     92 LWASkRVFFLTPQTLENDLK--EGDCDPKSIVCLVIDEAH---RATGNYAYCQVVRELMRYNSH-----------FRILA 155


                   ....
gi 1698318692  477 VSAT 480
Cdd:cd18033    156 LTAT 159
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
 318-436 5.57e-06

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: 49.01  E-value: 5.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  318 GKNFVACAPTGSGKTVLFELAIIRLLMQNSEPWNEVKAVYMAPIKALCSQCFENWNKKFGPlGLTCKELTGDTEIDDFF- 396
Cdd:cd18036     17 GKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEKGRVVVLVNKVPLVEQQLEKFFKYFRK-GYKVTGLSGDSSHKVSFg 95

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1698318692  397 -EIQDSHIILTTPEKWDSMTRKWK--DHCLLQQVRLFLIDEVH 436
Cdd:cd18036     96 qIVKASDVIICTPQILINNLLSGReeERVYLSDFSLLIFDECH 138
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
 306-712 5.77e-06

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 50.94  E-value: 5.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDDVLyTGKNFVACAPTGSGKTVLFELAII----RLLMQNSEPWNEVKAVYMAPIKALCSQCfENWNKKFGPlGL 381
Cdd:PLN00206   147 IQMQAIPAAL-SGRSLLVSADTGSGKTASFLVPIIsrccTIRSGHPSEQRNPLAMVLTPTRELCVQV-EDQAKVLGK-GL 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  382 TCKE---LTGDTEIDDFFEIQDS-HIILTTPEKWDSMTRKwkdHCL-LQQVRLFLIDEVHVIKDatRGAtlevvvsRMKA 456
Cdd:PLN00206   224 PFKTalvVGGDAMPQQLYRIQQGvELIVGTPGRLIDLLSK---HDIeLDNVSVLVLDEVDCMLE--RGF-------RDQV 291

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  457 VNAYRA-AQNQgtsgtmrIVAVSATI-PNISDIADWLSHESLpatYLDMDESHRPVMLRKVVLGFPCPQNQTEFKFDlsl 534
Cdd:PLN00206   292 MQIFQAlSQPQ-------VLLFSATVsPEVEKFASSLAKDII---LISIGNPNRPNKAVKQLAIWVETKQKKQKLFD--- 358

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  535 nykmanIIQTYSD-QKPALVFCSTRKGAQ---QAATVLAK-DARFImsieHNQRLMKyansildsklrelvmlgvgyhha 609
Cdd:PLN00206   359 ------ILKSKQHfKPPAVVFVSSRLGADllaNAITVVTGlKALSI----HGEKSMK----------------------- 405

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  610 gvdlsDRKLIEMAFTQADLPVLFTTRTLAMGVNLpahLVVIKSTMQYVAGSCEEYsdadmLQMIGRAGRpqFDTTATAVI 689
Cdd:PLN00206   406 -----ERREVMKSFLVGEVPVIVATGVLGRGVDL---LRVRQVIIFDMPNTIKEY-----IHQIGRASR--MGEKGTAIV 470

                          410       420
                   ....*....|....*....|...
gi 1698318692  690 MTKIQSKDKYMNLmngVEIIESS 712
Cdd:PLN00206   471 FVNEEDRNLFPEL---VALLKSS 490
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 306-489 1.13e-05

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 48.52  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDdVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSE----PWNEVKAVYMAPIKALCSQCFENWNKKFGPLGL 381
Cdd:cd17948     16 VQKQGIP-SILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLlaegPFNAPRGLVITPSRELAEQIGSVAQSLTEGLGL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  382 TCKELTGDTEIDDF--FEIQDSHIILTTPEKWDSMTrkWKDHCLLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKaVNA 459
Cdd:cd17948     95 KVKVITGGRTKRQIrnPHFEEVDILVATPGALSKLL--TSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLRRFP-LAS 171

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1698318692  460 YRAAQNQGTSGTMRIVAVSATIPN-----ISDIAD 489
Cdd:cd17948    172 RRSENTDGLDPGTQLVLVSATMPSgvgevLSKVID 206
DEADc_DDX47 cd17954
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ...
 306-434 1.62e-05

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: 47.31  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDDVLyTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEPWNevkAVYMAPIKALCSQCFENWNKKFGPLGLTCKE 385
Cdd:cd17954     26 IQEEAIPVAL-QGRDIIGLAETGSGKTAAFALPILQALLENPQRFF---ALVLAPTRELAQQISEQFEALGSSIGLKSAV 101

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1698318692  386 LTG--DTEIDDFFEIQDSHIILTTPEK-WDSM--TRKWKdhclLQQVRLFLIDE 434
Cdd:cd17954    102 LVGgmDMMAQAIALAKKPHVIVATPGRlVDHLenTKGFS----LKSLKFLVMDE 151
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
 300-408 1.65e-05

DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 47.57  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  300 FPFFNYVQSKALDDVLyTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEPW--NEVKAVYMAPIKALCSQCFENWNK--K 375
Cdd:cd17960     10 FTSMTPVQAATIPLFL-SNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLkkGQVGALIISPTRELATQIYEVLQSflE 88

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1698318692  376 FGPLGLTCKELTGDTEI---DDFFEIQDSHIILTTP 408
Cdd:cd17960     89 HHLPKLKCQLLIGGTNVeedVKKFKRNGPNILVGTP 124
DEADc_DDX3_DDX4 cd17967
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ...
 306-376 4.62e-05

DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350725 [Multi-domain]  Cd Length: 221  Bit Score: 46.33  E-value: 4.62e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698318692  306 VQSKALDDVLyTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEPWN-------EVKAVYMAPIKALCSQCFENwNKKF 376
Cdd:cd17967     26 VQKYAIPIIL-AGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSVgrgrrkaYPSALILAPTRELAIQIYEE-ARKF 101
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
 306-367 5.24e-05

DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 46.04  E-value: 5.24e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1698318692  306 VQSKALDDVLyTGKNFVACAPTGSGKTVLFELAII-RLLMQNSEPWNE--VKAVYMAPIKALCSQ 367
Cdd:cd17961     20 IQSKAIPLAL-EGKDILARARTGSGKTAAYALPIIqKILKAKAESGEEqgTRALILVPTRELAQQ 83
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 220-434 5.49e-05

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 47.60  E-value: 5.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  220 LAVSPPSPR---HHFSPLPPTGSSAASSRPLQQAALAKTQDKGTKRAFVPPMTPQPLRIKDRsdsgILRPVSEIPKFRSV 296
Cdd:PRK01297    17 PAPAPPSPAaapAPPPPAKTAAPATKAAAPAAAAPRAEKPKKDKPRRERKPKPASLWKLEDF----VVEPQEGKTRFHDF 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  297 FSE-----------FPFFNYVQSKALDDVLyTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEP----WNEVKAVYMAPI 361
Cdd:PRK01297    93 NLApelmhaihdlgFPYCTPIQAQVLGYTL-AGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPkeryMGEPRALIIAPT 171

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698318692  362 KALCSQCFENWNKKFGPLGLTCKELTGDTEIDDFFEIQDSH---IILTTPEKWDSMTRKWKDHclLQQVRLFLIDE 434
Cdd:PRK01297   172 RELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARfcdILVATPGRLLDFNQRGEVH--LDMVEVMVLDE 245
DEADc_DDX46 cd17953
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ...
 306-408 6.00e-05

DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350711 [Multi-domain]  Cd Length: 222  Bit Score: 46.22  E-value: 6.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDDVLyTGKNFVACAPTGSGKTVLFELAIIRLLMQN--SEPWNEVKAVYMAPIKALCSQCFENWNKKFGPLGLTC 383
Cdd:cd17953     38 IQAQALPAIM-SGRDVIGIAKTGSGKTLAFLLPMFRHIKDQrpVKPGEGPIGLIMAPTRELALQIYVECKKFSKALGLRV 116

                           90       100
                   ....*....|....*....|....*....
gi 1698318692  384 KELTGDTEIDDffEIQD----SHIILTTP 408
Cdd:cd17953    117 VCVYGGSGISE--QIAElkrgAEIVVCTP 143
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
 317-409 1.63e-04

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: 44.43  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  317 TGKNFVACAPTGSGKTvLFELAIIRLLMQNSEPWNEVKAVYMAPIKALCSQCFENWNKKFGPLGLTCKELTGDTEIDDFF 396
Cdd:cd18073     16 KGKNTIICAPTGCGKT-FVSLLICEHHLKKFPQGQKGKVVFFATKVPVYEQQKSVFSKYFERHGYRVTGISGATAENVPV 94

                           90
                   ....*....|....*
gi 1698318692  397 E--IQDSHIILTTPE 409
Cdd:cd18073     95 EqiIENNDIIILTPQ 109
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
 306-408 1.91e-04

DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 44.50  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDDVLYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEPW--NEVKAVYMAPIKALCSQCFENWNKKFGPL-GLT 382
Cdd:cd17964     20 VQQKTLKPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGrrSGVSALIISPTRELALQIAAEAKKLLQGLrKLR 99

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1698318692  383 CKELTGDTEIDdfFEIQD-----SHIILTTP 408
Cdd:cd17964    100 VQSAVGGTSRR--AELNRlrrgrPDILVATP 128
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
 306-370 2.14e-04

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: 44.11  E-value: 2.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698318692  306 VQSKALDDVLyTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEPWNE---VKAVYMAPIKALCSQCFE 370
Cdd:cd17949     17 IQKLAIPVLL-QGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVDRsdgTLALVLVPTRELALQIYE 83
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 319-436 4.90e-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: 43.02  E-value: 4.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  319 KNFVACAPTGSGKTVLFELAIIRLLMQNSEPWNEVK-AVYMAPIKALCSQCFE---NWnkkfgpLGLTCKELTGDTEIDD 394
Cdd:cd18034     17 RNTIVVLPTGSGKTLIAVMLIKEMGELNRKEKNPKKrAVFLVPTVPLVAQQAEairSH------TDLKVGEYSGEMGVDK 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1698318692  395 F------FEIQDSHIILTTPEKW-DSMTRKWKDhclLQQVRLFLIDEVH 436
Cdd:cd18034     91 WtkerwkEELEKYDVLVMTAQILlDALRHGFLS---LSDINLLIFDECH 136
DEADc_DDX49 cd17955
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ...
 306-408 5.26e-04

DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350713 [Multi-domain]  Cd Length: 204  Bit Score: 42.98  E-value: 5.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDDVLyTGKNFVACAPTGSGKTVLFELAIIRLLMQnsEPWNeVKAVYMAPIKALCSQCFENWNkKFG-PLGLTCK 384
Cdd:cd17955     25 IQKLCIPEIL-AGRDVIGGAKTGSGKTAAFALPILQRLSE--DPYG-IFALVLTPTRELAYQIAEQFR-ALGaPLGLRCC 99

                           90       100
                   ....*....|....*....|....*....
gi 1698318692  385 ELTGDTeidDFFE-----IQDSHIILTTP 408
Cdd:cd17955    100 VIVGGM---DMVKqalelSKRPHIVVATP 125
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
 292-440 6.04e-04

DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 42.91  E-value: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  292 KFRSVFSEFPffnyVQSKALDDVlYTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEPWNEVKA---VYMAPIKALCSQC 368
Cdd:cd17944      6 QARGVTYLFP----IQVKTFHPV-YSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKRGRApkvLVLAPTRELANQV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698318692  369 FENWNKKFGPLGLTCkeLTGDTEID-DFFEIQDS-HIILTTPEkwdsmtrKWKDHclLQQVRLFLIDEVHVIKD 440
Cdd:cd17944     81 TKDFKDITRKLSVAC--FYGGTPYQqQIFAIRNGiDILVGTPG-------RIKDH--LQNGRLDLTKLKHVVLD 143
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
 324-434 7.23e-04

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 43.00  E-value: 7.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  324 CAPTGSGKTVLFELAIIRLLMQNSEPwnEVKAVYMAPIKALCSQC---FENWNKKFgplGLTCKELTGDT-EIDDFFEIQ 399
Cdd:cd17956     42 SAPTGSGKTLAYVLPIVQALSKRVVP--RLRALIVVPTKELVQQVykvFESLCKGT---GLKVVSLSGQKsFKKEQKLLL 116

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1698318692  400 DSH---------IILTTPEKW-DSMTRkwKDHCLLQQVRLFLIDE 434
Cdd:cd17956    117 VDTsgrylsrvdILVATPGRLvDHLNS--TPGFTLKHLRFLVIDE 159
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
 548-678 8.84e-04

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: 41.04  E-value: 8.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  548 QKPALVFCSTRKGAQQAATVLAKDarfimsiehnqrlmkyansildsklrelvmlGV--GYHHAGVDLSDRKLIEMAFTQ 625
Cdd:cd18794     30 GGSGIIYCLSRKECEQVAARLQSK-------------------------------GIsaAAYHAGLEPSDRRDVQRKWLR 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1698318692  626 ADLPVLFTTRTLAMGVNLP-----AHLVVIKSTMQYVagsceeysdadmlQMIGRAGR 678
Cdd:cd18794     79 DKIQVIVATVAFGMGIDKPdvrfvIHYSLPKSMESYY-------------QESGRAGR 123
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
 318-484 1.06e-03

DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 41.89  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  318 GKNFVACAPTGSGKTvlfELAIIRLLmQNSEPWNEVKAVYMAPIKALCSQCFENWNKKFGPLG--LTCKELTGDTEID-- 393
Cdd:cd17930      1 PGLVILEAPTGSGKT---EAALLWAL-KLAARGGKRRIIYALPTRATINQMYERIREILGRLDdeDKVLLLHSKAALEll 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  394 ---------DFFEIQD---------SHIILTTP-------EKWDSMTRKWkdHCLLQQVrlFLIDEVHVIKDATRGATLE 448
Cdd:cd17930     77 esdeepdddPVEAVDWalllkrswlAPIVVTTIdqlleslLKYKHFERRL--HGLANSV--VVLDEVQAYDPEYMALLLK 152

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1698318692  449 VVVSRMKAVNAYraaqnqgtsgtmrIVAVSATIPNI 484
Cdd:cd17930    153 ALLELLGELGGP-------------VVLMTATLPAL 175
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 307-436 1.31e-03

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 40.75  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  307 QSKALDDVLYTGKNF--VACAPTGSGKTVLfELAIIRLLMqnsepwnEVKAVYMAPIKALCSQCFENWNKKFG--PLGLt 382
Cdd:cd17926      5 QEEALEAWLAHKNNRrgILVLPTGSGKTLT-ALALIAYLK-------ELRTLIVVPTDALLDQWKERFEDFLGdsSIGL- 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1698318692  383 ckeLTGDTEIDdffeIQDSHIILTTpekWDSMTRKWKDHCLLQQVRLFLI-DEVH 436
Cdd:cd17926     76 ---IGGGKKKD----FDDANVVVAT---YQSLSNLAEEEKDLFDQFGLLIvDEAH 120
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
319-436 1.76e-03

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 42.79  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  319 KNFVACAPTGSGKTVLFELAII-RLLMQNSepwnevKAVYMAPIKALCSQCFENWNKKFGPLGLTCKELTGDTEIDDFFE 397
Cdd:COG1111     18 KNTLVVLPTGLGKTAVALLVIAeRLHKKGG------KVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVFTGEVSPEKRKE 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1698318692  398 I-QDSHIILTTPE--KWDsMTRKWKDhclLQQVRLFLIDEVH 436
Cdd:COG1111     92 LwEKARIIVATPQviEND-LIAGRID---LDDVSLLIFDEAH 129
DEADc_DDX27 cd17947
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ...
 306-370 1.87e-03

DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ribosomal subunits protein 1 homolog, and probable ATP-dependent RNA helicase DDX27) is involved in the processing of 5.8S and 28S ribosomal RNAs. More specifically, the encoded protein localizes to the nucleolus, where it interacts with the PeBoW complex to ensure proper 3' end formation of 47S rRNA. DDX27 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350705 [Multi-domain]  Cd Length: 196  Bit Score: 41.09  E-value: 1.87e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1698318692  306 VQSKALDDVLyTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEPWNEVKAVYMAPIKALCSQCFE 370
Cdd:cd17947     16 IQAAAIPLAL-LGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAATRVLVLVPTRELAMQCFS 79
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
 607-678 1.93e-03

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 40.33  E-value: 1.93e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1698318692  607 HHAGVDLSDRKLIEMAFTQADLPVLFTTRTLAMGVNLPAhlvvIKSTMQYvaGSceEYSDADMLQMIGRAGR 678
Cdd:cd18796     74 HHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGD----VDLVIQI--GS--PKSVARLLQRLGRSGH 137
DEXQc_Suv3 cd17913
DEXQ-box helicase domain of Suv3; Suppressor of var1 3-like protein (Suv3) is a DNA/RNA ...
 326-444 2.40e-03

DEXQ-box helicase domain of Suv3; Suppressor of var1 3-like protein (Suv3) is a DNA/RNA unwinding enzyme belonging to the class of DexH-box helicases. It localizes predominantly in the mitochondria, where it forms an RNA-degrading complex called mitochondrial degradosome (mtEXO) with exonuclease PNP (polynucleotide phosphorylase), that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Suv3 plays a role in the RNA surveillance system in mitochondria; it regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. It also confers salinity and drought stress tolerance by maintaining both photosynthesis and antioxidant machinery, probably via an increase in plant hormone levels such as gibberellic acid (GA3), the cytokinin zeatin (Z), and indole-3-acetic acid (IAA). Suv3 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: 350671 [Multi-domain]  Cd Length: 142  Bit Score: 39.85  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  326 PTGSGKTvlfELAIIRLLmqNSEpwnevKAVYMAPIKALCSQCFENWNKKfgplGLTCKELTGDTEIddffEIQDSHIIL 405
Cdd:cd17913      9 PTNSGKT---YHALQRLK--SAK-----SGVYCGPLRLLAWEVYERLNAE----GVPCDLVTGQERR----EVEGATHVS 70

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1698318692  406 TTPEkwdsMTrkwkdhCLLQQVRLFLIDEVHVIKDATRG 444
Cdd:cd17913     71 CTVE----MA------SISEPYDVAVIDEIQMIGDPQRG 99
DEADc_DDX6 cd17940
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ...
 306-434 3.45e-03

DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, 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: 350698 [Multi-domain]  Cd Length: 201  Bit Score: 40.36  E-value: 3.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDDVLyTGKNFVACAPTGSGKTVLFelaIIRLLMQNSEPWNEVKAVYMAPIKALCSQCFENWnKKFGP-LGLTCK 384
Cdd:cd17940     25 IQEESIPIAL-SGRDILARAKNGTGKTGAY---LIPILEKIDPKKDVIQALILVPTRELALQTSQVC-KELGKhMGVKVM 99

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1698318692  385 ELTGDTEI-DDFFEIQDS-HIILTTPEK-WDSMTRKwkdHCLLQQVRLFLIDE 434
Cdd:cd17940    100 VTTGGTSLrDDIMRLYQTvHVLVGTPGRiLDLAKKG---VADLSHCKTLVLDE 149
DEADc_DDX20 cd17943
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ...
 306-482 3.76e-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: 40.33  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  306 VQSKALDdVLYTGKNFVACAPTGSGKTVLFE-LAIIRLLMQNSEPwnevKAVYMAPIKALCSQ---CFENWNKKFGplGL 381
Cdd:cd17943     16 IQLAAIP-LGLAGHDLIVQAKSGTGKTLVFVvIALESLDLERRHP----QVLILAPTREIAVQihdVFKKIGKKLE--GL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  382 TCKELTGDTEID-DFFEIQDSHIILTTPEKWDSMTRkwKDHCLLQQVRLFLIDEVHVIKDATRGATLEVVVSRMKAvnay 460
Cdd:cd17943     89 KCEVFIGGTPVKeDKKKLKGCHIAVGTPGRIKQLIE--LGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSLPK---- 162

                          170       180
                   ....*....|....*....|..
gi 1698318692  461 raaqnqgtsgTMRIVAVSATIP 482
Cdd:cd17943    163 ----------NKQVIAFSATYP 174
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
 306-371 5.45e-03

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 40.95  E-value: 5.45e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698318692  306 VQSKALDDVLyTGKNFVACAPTGSGKTVLFELAIIRLLMQNSEPWN---EVKAVYMAPIKALCSQCFEN 371
Cdd:PRK10590    27 IQQQAIPAVL-EGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrPVRALILTPTRELAAQIGEN 94
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
 317-494 5.85e-03

DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 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: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 39.84  E-value: 5.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  317 TGKNFVACAPTGSGKTVLFEL-AIIRLLMQNSEPwnevKAVYMAPIKALCSQcFENWNKKFG---PLGLTCKELTGDTEI 392
Cdd:cd17962     26 LGRDILASADTGSGKTAAFLLpVIIRCLTEHRNP----SALILTPTRELAVQ-IEDQAKELMkglPPMKTALLVGGLPLP 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698318692  393 DDFFEIQDS-HIILTTPEKWDSMTRKwkdHCL-LQQVRLFLIDEVH-VIKDATRGATLEVVvsrmkavnayraaqnQGTS 469
Cdd:cd17962    101 PQLYRLQQGvKVIIATPGRLLDILKQ---SSVeLDNIKIVVVDEADtMLKMGFQQQVLDIL---------------ENIS 162

                          170       180
                   ....*....|....*....|....*.
gi 1698318692  470 GTMRIVAVSATIP-NISDIADWLSHE 494
Cdd:cd17962    163 HDHQTILVSATIPrGIEQLAGQLLQN 188
DEADc_DDX4 cd18052
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ...
 318-369 7.25e-03

DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350810 [Multi-domain]  Cd Length: 264  Bit Score: 39.95  E-value: 7.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1698318692  318 GKNFVACAPTGSGKTVLFELAIIRLLMQN-------SEPwNEVKAVYMAPIKALCSQCF 369
Cdd:cd18052     80 GRDLMACAQTGSGKTAAFLLPVLTGMMKEgltassfSEV-QEPQALIVAPTRELANQIF 137
 
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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