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Conserved domains on  [gi|1002988851|ref|WP_061433378|]
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MULTISPECIES: DEAD/DEAH box helicase [Microcystis]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11437332)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
24-441 1.25e-98

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


:

Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 308.49  E-value: 1.25e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  24 WLDFATWDDRIERFRILAIHYRPLVETLQ--EEGINFQDEAKAFNNLELIASFEREPYPHQTEALIAWK----KSQRRGV 97
Cdd:COG1061    25 RLELSLLRNLVEARRLAIKEGTREDGRRLpeEDTERELAEAEALEAGDEASGTSFELRPYQQEALEALLaaleRGGGRGL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  98 IVLPTAAGKTYLAQLALQS--TPRSTLIIVPTIDLMHQWYAQMLAAFPDAEVGllgGGSKDNSA-ILIATYQSAA--IYS 172
Cdd:COG1061   105 VVAPTGTGKTVLALALAAEllRGKRVLVLVPRRELLEQWAEELRRFLGDPLAG---GGKKDSDApITVATYQSLArrAHL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 173 ETLGNRYAFLIFDECHHLPSDFFRKIAEDSIAPYRLGLTATPDRGDGSHQDLDYLIGtIVYQKSPQDL-SGKALADHEII 251
Cdd:COG1061   182 DELGDRFGLVIIDEAHHAGAPSYRRILEAFPAAYRLGLTATPFRSDGREILLFLFDG-IVYEYSLKEAiEDGYLAPPEYY 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 252 QIKVKLSaKEQEKYQEaikirndflrrnnlslsgldgwqnfvmisarssegrramLAHRESKEISSGTQGKLRVLAELIC 331
Cdd:COG1061   261 GIRVDLT-DERAEYDA---------------------------------------LSERLREALAADAERKDKILRELLR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 332 EH-HPEPILIFTNDNATVYRISESFL-----IPAITHQTPVKERHEILTRFRQGEYKILVTSHVLNEGVDVPEAGIAIIL 405
Cdd:COG1061   301 EHpDDRKTLVFCSSVDHAEALAELLNeagirAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILL 380
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1002988851 406 SGTGSTREYIQRLGRVLRKgqQEDKR-AILYEVIAEN 441
Cdd:COG1061   381 RPTGSPREFIQRLGRGLRP--APGKEdALVYDFVGND 415
 
Name Accession Description Interval E-value
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
24-441 1.25e-98

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 308.49  E-value: 1.25e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  24 WLDFATWDDRIERFRILAIHYRPLVETLQ--EEGINFQDEAKAFNNLELIASFEREPYPHQTEALIAWK----KSQRRGV 97
Cdd:COG1061    25 RLELSLLRNLVEARRLAIKEGTREDGRRLpeEDTERELAEAEALEAGDEASGTSFELRPYQQEALEALLaaleRGGGRGL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  98 IVLPTAAGKTYLAQLALQS--TPRSTLIIVPTIDLMHQWYAQMLAAFPDAEVGllgGGSKDNSA-ILIATYQSAA--IYS 172
Cdd:COG1061   105 VVAPTGTGKTVLALALAAEllRGKRVLVLVPRRELLEQWAEELRRFLGDPLAG---GGKKDSDApITVATYQSLArrAHL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 173 ETLGNRYAFLIFDECHHLPSDFFRKIAEDSIAPYRLGLTATPDRGDGSHQDLDYLIGtIVYQKSPQDL-SGKALADHEII 251
Cdd:COG1061   182 DELGDRFGLVIIDEAHHAGAPSYRRILEAFPAAYRLGLTATPFRSDGREILLFLFDG-IVYEYSLKEAiEDGYLAPPEYY 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 252 QIKVKLSaKEQEKYQEaikirndflrrnnlslsgldgwqnfvmisarssegrramLAHRESKEISSGTQGKLRVLAELIC 331
Cdd:COG1061   261 GIRVDLT-DERAEYDA---------------------------------------LSERLREALAADAERKDKILRELLR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 332 EH-HPEPILIFTNDNATVYRISESFL-----IPAITHQTPVKERHEILTRFRQGEYKILVTSHVLNEGVDVPEAGIAIIL 405
Cdd:COG1061   301 EHpDDRKTLVFCSSVDHAEALAELLNeagirAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILL 380
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1002988851 406 SGTGSTREYIQRLGRVLRKgqQEDKR-AILYEVIAEN 441
Cdd:COG1061   381 RPTGSPREFIQRLGRGLRP--APGKEdALVYDFVGND 415
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
308-438 3.93e-55

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 181.68  E-value: 3.93e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 308 AHRESKEISSGTQGKLRVLAELICEHHP-EPILIFTNDNATVYRISESFLIPAITHQTPVKERHEILTRFRQGEYKILVT 386
Cdd:cd18789    21 AHRKRRLLAAMNPNKLRALEELLKRHEQgDKIIVFTDNVEALYRYAKRLLKPFITGETPQSEREEILQNFREGEYNTLVV 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002988851 387 SHVLNEGVDVPEAGIAIILSGT-GSTREYIQRLGRVLRKGQQEDKRAILYEVI 438
Cdd:cd18789   101 SKVGDEGIDLPEANVAIQISGHgGSRRQEAQRLGRILRPKKGGGKNAFFYSLV 153
ResIII pfam04851
Type III restriction enzyme, res subunit;
77-216 1.34e-31

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 119.31  E-value: 1.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  77 EPYPHQTEALIAWKKS----QRRGVIVLPTAAGKTYLA-----QLALQSTPRSTLIIVPTIDLMHQWYAQMLAAFPDA-- 145
Cdd:pfam04851   3 ELRPYQIEAIENLLESikngQKRGLIVMATGSGKTLTAakliaRLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYve 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 146 EVGLLGGGSKD----NSAILIATYQSAAI-----YSETLGNRYAFLIFDECHHLPSDFFRKIAEDSIAPYRLGLTATPDR 216
Cdd:pfam04851  83 IGEIISGDKKDesvdDNKIVVTTIQSLYKalelaSLELLPDFFDVIIIDEAHRSGASSYRNILEYFKPAFLLGLTATPER 162
DEXDc smart00487
DEAD-like helicases superfamily;
70-214 1.59e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.95  E-value: 1.59e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851   70 LIASFEREPYPHQTEALIAWKKSQRRGVIVLPTAAGKT-----YLAQLALQSTPRSTLIIVPTIDLMHQWYAQMLAAFPD 144
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTlaallPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  145 A---EVGLLGGGS---------KDNSAILIATYQSAAIYSE---TLGNRYAFLIFDECHHLPSDFFRKIAEDSI-----A 204
Cdd:smart00487  81 LglkVVGLYGGDSkreqlrkleSGKTDILVTTPGRLLDLLEndkLSLSNVDLVILDEAHRLLDGGFGDQLEKLLkllpkN 160
                          170
                   ....*....|
gi 1002988851  205 PYRLGLTATP 214
Cdd:smart00487 161 VQLLLLSATP 170
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
94-471 1.19e-20

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 95.63  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  94 RRGVIVLPTAAGKTYLAQLALQSTPRSTLIIVPTIDLMHQWYAQ--MLAAFPDAEVGLLGGGSKD----NSAILIATY-- 165
Cdd:TIGR00603 274 RSGIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWKQQfkMWSTIDDSQICRFTSDAKErfhgEAGVVVSTYsm 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 166 ---------QSAAIYSETLGNRYAFLIFDECHHLPSDFFRKIAEDSIAPYRLGLTATPDRGDGSHQDLDYLIGTIVYQKS 236
Cdd:TIGR00603 354 vahtgkrsyESEKVMEWLTNREWGLILLDEVHVVPAAMFRRVLTIVQAHCKLGLTATLVREDDKITDLNFLIGPKLYEAN 433
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 237 PQDLSGKA-LADHEIIQIKVKLSAkeqEKYQEAIKIRNdflrRNNLSLsgldgwqnFVMisarssegrramlahreskei 315
Cdd:TIGR00603 434 WMELQKKGfIANVQCAEVWCPMTP---EFYREYLRENS----RKRMLL--------YVM--------------------- 477
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 316 ssgTQGKLRVLAELICEHHP--EPILIFTnDNatVYRISESFL---IPAITHQTPVKERHEILTRFRQGE-YKILVTSHV 389
Cdd:TIGR00603 478 ---NPNKFRACQFLIRFHEQrgDKIIVFS-DN--VFALKEYAIklgKPFIYGPTSQQERMQILQNFQHNPkVNTIFLSKV 551
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 390 LNEGVDVPEAGIAI-ILSGTGSTREYIQRLGRVLRKGQQEDKR---AILYEVIAENTTEEKTSQRRRG------------ 453
Cdd:TIGR00603 552 GDTSIDLPEANVLIqISSHYGSRRQEAQRLGRILRAKKGSDAEeynAFFYSLVSKDTQEMYYSTKRQRflvdqgysfkvi 631
                         410       420
                  ....*....|....*....|....
gi 1002988851 454 ------EQKNKTSYKTGNRQLELL 471
Cdd:TIGR00603 632 thlpgmDNESNLAYSSKEEQLELL 655
uvsW PHA02558
UvsW helicase; Provisional
42-438 2.19e-17

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 84.68  E-value: 2.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  42 IHYRPLVETLQEegINFQDEAKAFNNLELIASFER-EPYPHQTEALIAWKKsQRRGVIVLPTAAGKTYLAQLA----LQS 116
Cdd:PHA02558   80 IWVDPRIEENED--ISREDFDEWVSSLEIYSGNKKiEPHWYQYDAVYEGLK-NNRRLLNLPTSAGKSLIQYLLsryyLEN 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 117 TPRSTLIIVPTIDLMHQWYAQML--AAFPDAEV-GLLGGGSKDNSA-ILIATYQSAAIYSETLGNRYAFLIFDECHHLPS 192
Cdd:PHA02558  157 YEGKVLIIVPTTSLVTQMIDDFVdyRLFPREAMhKIYSGTAKDTDApIVVSTWQSAVKQPKEWFDQFGMVIVDECHLFTG 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 193 DFFRKIAEDSI-APYRLGLTATPDRGDGSHQDLDYLIGTIVYQKSPQDLSGKA-LADHEIIQIKVKLSAKEQEK-----Y 265
Cdd:PHA02558  237 KSLTSIITKLDnCKFKFGLTGSLRDGKANILQYVGLFGDIFKPVTTSQLMEEGqVTDLKINSIFLRYPDEDRVKlkgedY 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 266 QEAIKIRNDFLRRN----NLSLSGLDGWQN-FVMIsarssegrramlahresKEISSGtqgklRVLAELICEHHPEpili 340
Cdd:PHA02558  317 QEEIKYITSHTKRNkwiaNLALKLAKKGENtFVMF-----------------KYVEHG-----KPLYEMLKKVYDK---- 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 341 ftndnatVYRISESflipaithqTPVKERHEILTRFRQGEYKILVTSH-VLNEGVDVPEAGIAIILSGTGSTREYIQRLG 419
Cdd:PHA02558  371 -------VYYVSGE---------VDTEDRNEMKKIAEGGKGIIIVASYgVFSTGISIKNLHHVIFAHPSKSKIIVLQSIG 434
                         410
                  ....*....|....*....
gi 1002988851 420 RVLRKGQQEDKrAILYEVI 438
Cdd:PHA02558  435 RVLRKHGSKSI-ATVWDII 452
 
Name Accession Description Interval E-value
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
24-441 1.25e-98

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 308.49  E-value: 1.25e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  24 WLDFATWDDRIERFRILAIHYRPLVETLQ--EEGINFQDEAKAFNNLELIASFEREPYPHQTEALIAWK----KSQRRGV 97
Cdd:COG1061    25 RLELSLLRNLVEARRLAIKEGTREDGRRLpeEDTERELAEAEALEAGDEASGTSFELRPYQQEALEALLaaleRGGGRGL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  98 IVLPTAAGKTYLAQLALQS--TPRSTLIIVPTIDLMHQWYAQMLAAFPDAEVGllgGGSKDNSA-ILIATYQSAA--IYS 172
Cdd:COG1061   105 VVAPTGTGKTVLALALAAEllRGKRVLVLVPRRELLEQWAEELRRFLGDPLAG---GGKKDSDApITVATYQSLArrAHL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 173 ETLGNRYAFLIFDECHHLPSDFFRKIAEDSIAPYRLGLTATPDRGDGSHQDLDYLIGtIVYQKSPQDL-SGKALADHEII 251
Cdd:COG1061   182 DELGDRFGLVIIDEAHHAGAPSYRRILEAFPAAYRLGLTATPFRSDGREILLFLFDG-IVYEYSLKEAiEDGYLAPPEYY 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 252 QIKVKLSaKEQEKYQEaikirndflrrnnlslsgldgwqnfvmisarssegrramLAHRESKEISSGTQGKLRVLAELIC 331
Cdd:COG1061   261 GIRVDLT-DERAEYDA---------------------------------------LSERLREALAADAERKDKILRELLR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 332 EH-HPEPILIFTNDNATVYRISESFL-----IPAITHQTPVKERHEILTRFRQGEYKILVTSHVLNEGVDVPEAGIAIIL 405
Cdd:COG1061   301 EHpDDRKTLVFCSSVDHAEALAELLNeagirAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILL 380
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1002988851 406 SGTGSTREYIQRLGRVLRKgqQEDKR-AILYEVIAEN 441
Cdd:COG1061   381 RPTGSPREFIQRLGRGLRP--APGKEdALVYDFVGND 415
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
308-438 3.93e-55

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 181.68  E-value: 3.93e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 308 AHRESKEISSGTQGKLRVLAELICEHHP-EPILIFTNDNATVYRISESFLIPAITHQTPVKERHEILTRFRQGEYKILVT 386
Cdd:cd18789    21 AHRKRRLLAAMNPNKLRALEELLKRHEQgDKIIVFTDNVEALYRYAKRLLKPFITGETPQSEREEILQNFREGEYNTLVV 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002988851 387 SHVLNEGVDVPEAGIAIILSGT-GSTREYIQRLGRVLRKGQQEDKRAILYEVI 438
Cdd:cd18789   101 SKVGDEGIDLPEANVAIQISGHgGSRRQEAQRLGRILRPKKGGGKNAFFYSLV 153
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
78-214 1.08e-47

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: 161.70  E-value: 1.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  78 PYPHQTEAL--IAWKKSQRRGVIVLPTAAGKTYLA-QLALQSTPRSTLIIVPTIDLMHQWYAQMLAAFPDAEVGLLGGGS 154
Cdd:cd17926     1 LRPYQEEALeaWLAHKNNRRGILVLPTGSGKTLTAlALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDSSIGLIGGGK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002988851 155 KD---NSAILIATYQSAAIYSET---LGNRYAFLIFDECHHLPSDFFRKIAEDSIAPYRLGLTATP 214
Cdd:cd17926    81 KKdfdDANVVVATYQSLSNLAEEekdLFDQFGLLIVDEAHHLPAKTFSEILKELNAKYRLGLTATP 146
ResIII pfam04851
Type III restriction enzyme, res subunit;
77-216 1.34e-31

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 119.31  E-value: 1.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  77 EPYPHQTEALIAWKKS----QRRGVIVLPTAAGKTYLA-----QLALQSTPRSTLIIVPTIDLMHQWYAQMLAAFPDA-- 145
Cdd:pfam04851   3 ELRPYQIEAIENLLESikngQKRGLIVMATGSGKTLTAakliaRLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYve 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 146 EVGLLGGGSKD----NSAILIATYQSAAI-----YSETLGNRYAFLIFDECHHLPSDFFRKIAEDSIAPYRLGLTATPDR 216
Cdd:pfam04851  83 IGEIISGDKKDesvdDNKIVVTTIQSLYKalelaSLELLPDFFDVIIIDEAHRSGASSYRNILEYFKPAFLLGLTATPER 162
XPB_DRD pfam18458
Xeroderma pigmentosum group B helicase damage recognition domain; This domain is found in the ...
6-62 3.86e-27

Xeroderma pigmentosum group B helicase damage recognition domain; This domain is found in the N-terminal region of xeroderma pigmentosum group B (XPB) helicase present in Archaeoglobus fulgidus. XPB is essential for transcription, nucleotide excision repair, and TFIIH functional assembly. The domain is a damage recognition domain (DRD) which allows XPB to unwind damaged DNA as needed for nucleotide excision repair.


Pssm-ID: 465776  Cd Length: 57  Bit Score: 103.38  E-value: 3.86e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002988851   6 LKYERGTLILHPPPKGKKWLDFATWDDRIERFRILAIHYRPLVETLQEEGINFQDEA 62
Cdd:pfam18458   1 LRYDRGTLILHGPPPGKAWLPFATWDDRVEKYRAPAYRYRDLVEALRAAGIEFEDRA 57
DEXDc smart00487
DEAD-like helicases superfamily;
70-214 1.59e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 97.95  E-value: 1.59e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851   70 LIASFEREPYPHQTEALIAWKKSQRRGVIVLPTAAGKT-----YLAQLALQSTPRSTLIIVPTIDLMHQWYAQMLAAFPD 144
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTlaallPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  145 A---EVGLLGGGS---------KDNSAILIATYQSAAIYSE---TLGNRYAFLIFDECHHLPSDFFRKIAEDSI-----A 204
Cdd:smart00487  81 LglkVVGLYGGDSkreqlrkleSGKTDILVTTPGRLLDLLEndkLSLSNVDLVILDEAHRLLDGGFGDQLEKLLkllpkN 160
                          170
                   ....*....|
gi 1002988851  205 PYRLGLTATP 214
Cdd:smart00487 161 VQLLLLSATP 170
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
321-425 2.49e-21

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 88.81  E-value: 2.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 321 GKLRVLAELICEHHPEPILIFTNDNATV----YRISESFLIPAITHQTPVKERHEILTRFRQGEYKILVTSHVLNEGVDV 396
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLeaelLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
                          90       100
                  ....*....|....*....|....*....
gi 1002988851 397 PEAGIAIILSGTGSTREYIQRLGRVLRKG 425
Cdd:pfam00271  81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
78-221 4.55e-21

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 89.93  E-value: 4.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  78 PYPHQTEAL----IAWKKSQRRGVIVLPTAAGKTYLA-----QLALQSTPRSTLIIVPTIDLMHQWYAQMLAAFPDAEVG 148
Cdd:cd18032     1 PRYYQQEAIealeEAREKGQRRALLVMATGTGKTYTAaflikRLLEANRKKRILFLAHREELLEQAERSFKEVLPDGSFG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002988851 149 LLGGGSKDNSA--ILIATYQS--AAIYSETLG-NRYAFLIFDECHHLPSDFFRKIAEDSIAPYRLGLTATPDRGDGSH 221
Cdd:cd18032    81 NLKGGKKKPDDarVVFATVQTlnKRKRLEKFPpDYFDLIIIDEAHHAIASSYRKILEYFEPAFLLGLTATPERTDGLD 158
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
94-471 1.19e-20

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 95.63  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  94 RRGVIVLPTAAGKTYLAQLALQSTPRSTLIIVPTIDLMHQWYAQ--MLAAFPDAEVGLLGGGSKD----NSAILIATY-- 165
Cdd:TIGR00603 274 RSGIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWKQQfkMWSTIDDSQICRFTSDAKErfhgEAGVVVSTYsm 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 166 ---------QSAAIYSETLGNRYAFLIFDECHHLPSDFFRKIAEDSIAPYRLGLTATPDRGDGSHQDLDYLIGTIVYQKS 236
Cdd:TIGR00603 354 vahtgkrsyESEKVMEWLTNREWGLILLDEVHVVPAAMFRRVLTIVQAHCKLGLTATLVREDDKITDLNFLIGPKLYEAN 433
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 237 PQDLSGKA-LADHEIIQIKVKLSAkeqEKYQEAIKIRNdflrRNNLSLsgldgwqnFVMisarssegrramlahreskei 315
Cdd:TIGR00603 434 WMELQKKGfIANVQCAEVWCPMTP---EFYREYLRENS----RKRMLL--------YVM--------------------- 477
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 316 ssgTQGKLRVLAELICEHHP--EPILIFTnDNatVYRISESFL---IPAITHQTPVKERHEILTRFRQGE-YKILVTSHV 389
Cdd:TIGR00603 478 ---NPNKFRACQFLIRFHEQrgDKIIVFS-DN--VFALKEYAIklgKPFIYGPTSQQERMQILQNFQHNPkVNTIFLSKV 551
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 390 LNEGVDVPEAGIAI-ILSGTGSTREYIQRLGRVLRKGQQEDKR---AILYEVIAENTTEEKTSQRRRG------------ 453
Cdd:TIGR00603 552 GDTSIDLPEANVLIqISSHYGSRRQEAQRLGRILRAKKGSDAEeynAFFYSLVSKDTQEMYYSTKRQRflvdqgysfkvi 631
                         410       420
                  ....*....|....*....|....
gi 1002988851 454 ------EQKNKTSYKTGNRQLELL 471
Cdd:TIGR00603 632 thlpgmDNESNLAYSSKEEQLELL 655
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
80-219 6.87e-18

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 81.19  E-value: 6.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  80 PHQTEALIA-WKKSQ-RRGVIVLPTAAGKTYLAQLALQSTPRSTLIIVPTIDLMHQWYAQMLA--AFPDAEVGLLGGGSK 155
Cdd:cd18029    11 PYQEKALSKmFGNGRaRSGVIVLPCGAGKTLVGITAACTIKKSTLVLCTSAVSVEQWRRQFLDwtTIDDEQIGRFTSDKK 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002988851 156 D---NSAILIATYQ-----------SAAIYSETLGNRYAFLIFDECHHLPSDFFRKIAEDSIAPYRLGLTATPDRGDG 219
Cdd:cd18029    91 EifpEAGVTVSTYSmlantrkrspeSEKFMEFITEREWGLIILDEVHVVPAPMFRRVLTLQKAHCKLGLTATLVREDD 168
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
98-477 1.43e-17

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 85.94  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  98 IVLPTAAGKTYLAQLA----LQSTPRSTLIIVPTIDLMHQWYAQMLAAF--PDAEVGLLGGGSK--------DNSAILIA 163
Cdd:COG1111    22 VVLPTGLGKTAVALLViaerLHKKGGKVLFLAPTKPLVEQHAEFFKEALniPEDEIVVFTGEVSpekrkelwEKARIIVA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 164 TYQSaaIYSETLGNRY-----AFLIFDECHHLPSDF-----FRKIAEDSIAPYRLGLTATPdrgdGSHQD-LDYLIGTI- 231
Cdd:COG1111   102 TPQV--IENDLIAGRIdlddvSLLIFDEAHRAVGNYayvyiAERYHEDAKDPLILGMTASP----GSDEEkIEEVCENLg 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 232 ---VYQKSPQDLSGKA-LADHEIIQIKVKLSaKEQEK----YQEAIKIRNDFLRRN--------NLSLSGLDGWQNFVM- 294
Cdd:COG1111   176 ienVEVRTEEDPDVAPyVHDTEVEWIRVELP-EELKEirdlLNEVLDDRLKKLKELgvivstspDLSKKDLLALQKKLQr 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 295 -ISARSSEGRRAMLAH----------------------------RESKEISSGTQG------------------------ 321
Cdd:COG1111   255 rIREDDSEGYRAISILaealklrhalelletqgveallrylerlEEEARSSGGSKAskrlvsdprfrkamrlaeeadieh 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 322 -KLRVLAELICEH---HPEP-ILIFTNDNATVYRISEsFL----IPAITH-------------QtpvKERHEILTRFRQG 379
Cdd:COG1111   335 pKLSKLREILKEQlgtNPDSrIIVFTQYRDTAEMIVE-FLsepgIKAGRFvgqaskegdkgltQ---KEQIEILERFRAG 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 380 EYKILVTSHVLNEGVDVPEAGIAIILSGTGSTREYIQRLGRVlrkGQQEDKRAILYevIAENTTEE---KTSQRRrgEQK 456
Cdd:COG1111   411 EFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRT---GRKREGRVVVL--IAKGTRDEayyWSSRRK--EKK 483
                         490       500
                  ....*....|....*....|.
gi 1002988851 457 NKTSYKTGNRQLELLPSAPKK 477
Cdd:COG1111   484 MKSILKKLKKLLDKQEKEKLK 504
uvsW PHA02558
UvsW helicase; Provisional
42-438 2.19e-17

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 84.68  E-value: 2.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  42 IHYRPLVETLQEegINFQDEAKAFNNLELIASFER-EPYPHQTEALIAWKKsQRRGVIVLPTAAGKTYLAQLA----LQS 116
Cdd:PHA02558   80 IWVDPRIEENED--ISREDFDEWVSSLEIYSGNKKiEPHWYQYDAVYEGLK-NNRRLLNLPTSAGKSLIQYLLsryyLEN 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 117 TPRSTLIIVPTIDLMHQWYAQML--AAFPDAEV-GLLGGGSKDNSA-ILIATYQSAAIYSETLGNRYAFLIFDECHHLPS 192
Cdd:PHA02558  157 YEGKVLIIVPTTSLVTQMIDDFVdyRLFPREAMhKIYSGTAKDTDApIVVSTWQSAVKQPKEWFDQFGMVIVDECHLFTG 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 193 DFFRKIAEDSI-APYRLGLTATPDRGDGSHQDLDYLIGTIVYQKSPQDLSGKA-LADHEIIQIKVKLSAKEQEK-----Y 265
Cdd:PHA02558  237 KSLTSIITKLDnCKFKFGLTGSLRDGKANILQYVGLFGDIFKPVTTSQLMEEGqVTDLKINSIFLRYPDEDRVKlkgedY 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 266 QEAIKIRNDFLRRN----NLSLSGLDGWQN-FVMIsarssegrramlahresKEISSGtqgklRVLAELICEHHPEpili 340
Cdd:PHA02558  317 QEEIKYITSHTKRNkwiaNLALKLAKKGENtFVMF-----------------KYVEHG-----KPLYEMLKKVYDK---- 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 341 ftndnatVYRISESflipaithqTPVKERHEILTRFRQGEYKILVTSH-VLNEGVDVPEAGIAIILSGTGSTREYIQRLG 419
Cdd:PHA02558  371 -------VYYVSGE---------VDTEDRNEMKKIAEGGKGIIIVASYgVFSTGISIKNLHHVIFAHPSKSKIIVLQSIG 434
                         410
                  ....*....|....*....
gi 1002988851 420 RVLRKGQQEDKrAILYEVI 438
Cdd:PHA02558  435 RVLRKHGSKSI-ATVWDII 452
HELICc smart00490
helicase superfamily c-terminal domain;
363-425 1.51e-15

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 71.47  E-value: 1.51e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002988851  363 QTPVKERHEILTRFRQGEYKILVTSHVLNEGVDVPEAGIAIILSGTGSTREYIQRLGRVLRKG 425
Cdd:smart00490  20 GLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
PRK13766 PRK13766
Hef nuclease; Provisional
98-500 2.62e-15

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 78.76  E-value: 2.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  98 IVLPTAAGKTYLAQLA----LQSTPRSTLIIVPTIDLMHQ---WYAQMLAAFPDAEVGLLGGGSKD-------NSAILIA 163
Cdd:PRK13766   34 VVLPTGLGKTAIALLViaerLHKKGGKVLILAPTKPLVEQhaeFFRKFLNIPEEKIVVFTGEVSPEkraelweKAKVIVA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 164 TYQsaAIYSETLGNRY-----AFLIFDECHHLPSDF--------FRKIAEDsiaPYRLGLTATPdrgdGSHQD-----LD 225
Cdd:PRK13766  114 TPQ--VIENDLIAGRIsledvSLLIFDEAHRAVGNYayvyiaerYHEDAKN---PLVLGLTASP----GSDEEkikevCE 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 226 YL-IGTIVYqKSPQDLSGKA-LADHEIIQIKVKLSAKEQEKY---QEAIKIRNDFLR--------RNNLSLSGLDGWQN- 291
Cdd:PRK13766  185 NLgIEHVEV-RTEDDPDVKPyVHKVKIEWVRVELPEELKEIRdllNEALKDRLKKLKelgvivsiSPDVSKKELLGLQKk 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 292 -FVMISARSSEGRRAMLAHRESKEISSG-----TQG-------------------------------------------- 321
Cdd:PRK13766  264 lQQEIANDDSEGYEAISILAEAMKLRHAvelleTQGvealrrylerlreearssggskaskrlvedprfrkavrkakeld 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 322 ----KLRVLAELICE---HHPEP-ILIFTNDNATVYRISESFLIPAITHQTPV-------------KERHEILTRFRQGE 380
Cdd:PRK13766  344 iehpKLEKLREIVKEqlgKNPDSrIIVFTQYRDTAEKIVDLLEKEGIKAVRFVgqaskdgdkgmsqKEQIEILDKFRAGE 423
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 381 YKILVTSHVLNEGVDVPEAGIAIILSGTGSTREYIQRLGRVlrkGQQEDKRAILyeVIAENTTEEK---TSQRRRGEQKN 457
Cdd:PRK13766  424 FNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRT---GRQEEGRVVV--LIAKGTRDEAyywSSRRKEKKMKE 498
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1002988851 458 --KTSYKTGNRQLELLPSAPKKSFSFPKAAESSTPWVSSPESEEE 500
Cdd:PRK13766  499 elKNLKGILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEE 543
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
72-446 9.65e-15

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 76.80  E-value: 9.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  72 ASFEREPYPHQTEAL--IAWKKSQRRGVIVlptA----AGKT-----YLAQLALQSTPRSTLIIVPTIdLMHQWYAQMLA 140
Cdd:COG0553   236 AGLKATLRPYQLEGAawLLFLRRLGLGGLL---AddmgLGKTiqalaLLLELKERGLARPVLIVAPTS-LVGNWQRELAK 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 141 AFPDAEVGLLGGGSK--------DNSAILIATYQSAAIYSETLGN-RYAFLIFDECHHLP------SDFFRKIAedsiAP 205
Cdd:COG0553   312 FAPGLRVLVLDGTRErakganpfEDADLVITSYGLLRRDIELLAAvDWDLVILDEAQHIKnpatkrAKAVRALK----AR 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 206 YRLGLTATPDRgdGSHQDL---------DYLiGTI-----VYQKSPQDLSGKALAD-HEIIQ------------------ 252
Cdd:COG0553   388 HRLALTGTPVE--NRLEELwslldflnpGLL-GSLkafreRFARPIEKGDEEALERlRRLLRpfllrrtkedvlkdlpek 464
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 253 ----IKVKLSAKEQEKYQEAIK-IRNDFLRRNNLSlsgldgwQNFVMISARSSegRRAMLAH-----RESKEISSGTqGK 322
Cdd:COG0553   465 teetLYVELTPEQRALYEAVLEyLRRELEGAEGIR-------RRGLILAALTR--LRQICSHpalllEEGAELSGRS-AK 534
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 323 LRVLAELICEH--HPEPILIFTNDNATVYRISEsFL------IPAITHQTPVKERHEILTRFRQGEYK--ILVTSHVLNE 392
Cdd:COG0553   535 LEALLELLEELlaEGEKVLVFSQFTDTLDLLEE-RLeergieYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGE 613
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002988851 393 GVDVPEAGIAIILSgtgstREY-----IQRLGRVLRKGQQEDkrAILYEVIAENTTEEK 446
Cdd:COG0553   614 GLNLTAADHVIHYD-----LWWnpaveEQAIDRAHRIGQTRD--VQVYKLVAEGTIEEK 665
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
96-213 3.19e-13

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: 67.04  E-value: 3.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  96 GVIVLPTAAGKTYLAQLA----LQSTPRSTLIIVPTIDLMHQWYAQMLAAF-PDAEVGLLGGGSK---------DNSAIL 161
Cdd:cd00046     4 VLITAPTGSGKTLAALLAalllLLKKGKKVLVLVPTKALALQTAERLRELFgPGIRVAVLVGGSSaeereknklGDADII 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002988851 162 IATYQSAAIYSETLG----NRYAFLIFDECHHLPSDFFRKIAEDSIA-------PYRLGLTAT 213
Cdd:cd00046    84 IATPDMLLNLLLREDrlflKDLKLIIVDEAHALLIDSRGALILDLAVrkaglknAQVILLSAT 146
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
339-424 1.63e-12

C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350186 [Multi-domain]  Cd Length: 116  Bit Score: 64.12  E-value: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 339 LIFTNDNATVYRISESFL-----IPAITHQTPVKER-HEILTRFRQGEYK--ILVTSHVLNEGVDVPEAGIAIILSGTGS 410
Cdd:cd18799    10 LIFCVSIEHAEFMAEAFNeagidAVALNSDYSDRERgDEALILLFFGELKppILVTVDLLTTGVDIPEVDNVVFLRPTES 89
                          90
                  ....*....|....
gi 1002988851 411 TREYIQRLGRVLRK 424
Cdd:cd18799    90 RTLFLQMLGRGLRL 103
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
77-224 1.21e-11

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: 63.82  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  77 EPYPHQTEALIAWKKsqRRGVIVLPTAAGKTYLA----------QLALQSTPRSTLIIVPTIDLMHQwYAQMLAAFPDAE 146
Cdd:cd18034     2 TPRSYQLELFEAALK--RNTIVVLPTGSGKTLIAvmlikemgelNRKEKNPKKRAVFLVPTVPLVAQ-QAEAIRSHTDLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 147 VGLL-GGGSKDNSA------------ILIATYQsaaIYSETLGNRYA------FLIFDECHHLPSDF-FRKIAED----- 201
Cdd:cd18034    79 VGEYsGEMGVDKWTkerwkeelekydVLVMTAQ---ILLDALRHGFLslsdinLLIFDECHHATGDHpYARIMKEfyhle 155
                         170       180
                  ....*....|....*....|....*
gi 1002988851 202 --SIAPYRLGLTATPDRGDGSHQDL 224
Cdd:cd18034   156 grTSRPRILGLTASPVNGKGDPKSV 180
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
79-216 1.43e-11

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: 62.65  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  79 YPHQTEALIAWKksQRRGVIVL-PTAAGKTYLAQLAL------QSTPRSTLIIVPTIDLMHQWYAQM--LAAFPDAEVGL 149
Cdd:pfam00270   1 TPIQAEAIPAIL--EGRDVLVQaPTGSGKTLAFLLPAlealdkLDNGPQALVLAPTRELAEQIYEELkkLGKGLGLKVAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 150 LGGGSK--------DNSAILIATYQSAAIYSETLG--NRYAFLIFDECHHLPSDFFRKIAEDSIA-----PYRLGLTATP 214
Cdd:pfam00270  79 LLGGDSrkeqleklKGPDILVGTPGRLLDLLQERKllKNLKLLVLDEAHRLLDMGFGPDLEEILRrlpkkRQILLLSATL 158

                  ..
gi 1002988851 215 DR 216
Cdd:pfam00270 159 PR 160
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
337-435 2.51e-11

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 59.25  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 337 PILIFTNDNATVYRISESFlipaithqtpvkerheiltrfrqgeyKILVTSHVLNEGVDVPEAGIAIILSGTGSTREYIQ 416
Cdd:cd18785     5 KIIVFTNSIEHAEEIASSL--------------------------EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQ 58
                          90
                  ....*....|....*....
gi 1002988851 417 RLGRVLRKGQQEDkRAILY 435
Cdd:cd18785    59 RVGRAGRGGKDEG-EVILF 76
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
78-214 4.27e-11

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 61.81  E-value: 4.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  78 PYPHQTEAL--IAWKKSQRRGVIVlptA----AGKT-----YLAQLALQS-TPRSTLIIVPTIdLMHQWYAQMLAAFPDA 145
Cdd:cd17919     1 LRPYQLEGLnfLLELYENGPGGIL---AdemgLGKTlqaiaFLAYLLKEGkERGPVLVVCPLS-VLENWEREFEKWTPDL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 146 EVGLLGGGSKDNSA-----------ILIATYQSAAIYSETLGN-RYAFLIFDECHHL---PSDFFRKIaeDSI-APYRLG 209
Cdd:cd17919    77 RVVVYHGSQRERAQirakekldkfdVVLTTYETLRRDKASLRKfRWDLVVVDEAHRLknpKSQLSKAL--KALrAKRRLL 154

                  ....*
gi 1002988851 210 LTATP 214
Cdd:cd17919   155 LTGTP 159
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
322-426 9.29e-11

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 59.44  E-value: 9.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 322 KLRVLAELICEHHPEPILIFTNDNATVYRISESFL---IPAIT-H-QTPVKERHEILTRFRQGEYKILVTSHVLNEGVDV 396
Cdd:cd18787    14 KLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEelgIKVAAlHgDLSQEERERALKKFRSGKVRVLVATDVAARGLDI 93
                          90       100       110
                  ....*....|....*....|....*....|
gi 1002988851 397 PEAGIAIILSGTGSTREYIQRLGRVLRKGQ 426
Cdd:cd18787    94 PGVDHVINYDLPRDAEDYVHRIGRTGRAGR 123
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
322-424 1.33e-08

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 53.51  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 322 KLRVLAELICEH-------HPEPILIFTNdnatvYRISESFLIPAITHQTPV--------------------KERHEILT 374
Cdd:cd18801    10 KLEKLEEIVKEHfkkkqegSDTRVIIFSE-----FRDSAEEIVNFLSKIRPGiratrfigqasgksskgmsqKEQKEVIE 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002988851 375 RFRQGEYKILVTSHVLNEGVDVPEAGIAIILSGTGSTREYIQRLGRVLRK 424
Cdd:cd18801    85 QFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRK 134
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
368-456 1.76e-08

C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 53.79  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 368 ERHEILTRFRQGEYKILVTSHVLNEGVDVPEAGIAIILSGTG-----STREYIQRLGRVLRkgqQEDKRAILYeviAENT 442
Cdd:cd18790    65 ERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDADKegflrSETSLIQTIGRAAR---NVNGKVILY---ADKI 138
                          90
                  ....*....|....*....
gi 1002988851 443 TE--EKT---SQRRRGEQK 456
Cdd:cd18790   139 TDsmQKAieeTERRREIQM 157
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
322-420 2.19e-08

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 52.98  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 322 KLRVLAELICEHHPEPI----LIFTNDNATVY--------------RISESFLI------PAITHQTPVKERHEILTRFR 377
Cdd:cd18802     8 KLQKLIEILREYFPKTPdfrgIIFVERRATAVvlsrllkehpstlaFIRCGFLIgrgnssQRKRSLMTQRKQKETLDKFR 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1002988851 378 QGEYKILVTSHVLNEGVDVPEAGIAIILSGTGSTREYIQRLGR 420
Cdd:cd18802    88 DGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR 130
DEXHc_UvsW cd18031
DEXH-box helicase domain of bacteriophage UvsW; Bacteriophage UvsW is part of the WXY system ...
78-214 6.67e-08

DEXH-box helicase domain of bacteriophage UvsW; Bacteriophage UvsW is part of the WXY system that repairs DNA damage by a process that involves homologous recombination. UvsW 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: 350789 [Multi-domain]  Cd Length: 161  Bit Score: 52.05  E-value: 6.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  78 PYPHQTEALIAWKKSQRRgVIVLPTAAGKTYLAQLA----LQSTPRSTLIIVPTIDLMHQWYAQML--AAFPDAEVGLLG 151
Cdd:cd18031     1 PHWYQKDAVFEGLVNRRR-ILNLPTSAGRSLIQALLaryyLENYEGKILIIVPTTALTTQMADDFVdyRLFSHAMIKKIG 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 152 GGSKDNSA------ILIATYQSAAIYSETLGNRYAFLIFDECHHLPSDFFRKIAED-SIAPYRLGLTATP 214
Cdd:cd18031    80 GGASKDDKykndapVVVGTWQTVVKQPKEWFSQFGMMMNDECHLATGKSISSIISGlNNCMFKFGLSGSL 149
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
86-214 9.70e-08

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 52.13  E-value: 9.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  86 LIAWKKSQRRGVIVLPTAAGKTYLAQLA----LQSTPRSTLIIVPTIDLMHQWYAQM--LAAFPDAEVGLLGGGSKDNSA 159
Cdd:cd18035     9 LIAAVALNGNTLIVLPTGLGKTIIAILVaadrLTKKGGKVLILAPSRPLVEQHAENLkrVLNIPDKITSLTGEVKPEERA 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002988851 160 -------ILIATYQSaaIYSETLGNRY-----AFLIFDECHHLPSDF--------FRKIAEDsiaPYRLGLTATP 214
Cdd:cd18035    89 erwdaskIIVATPQV--IENDLLAGRItlddvSLLIFDEAHHAVGNYayvyiahrYKREANN---PLILGLTASP 158
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
332-439 1.35e-07

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 54.02  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 332 EHHPEPILIFTNDnatvyRISESFLIPAITHQT-----------PVKERHEILTRFRQGEYKILVTSHVLNEGVDVPEAG 400
Cdd:PLN00206  364 QHFKPPAVVFVSS-----RLGADLLANAITVVTglkalsihgekSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVR 438
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1002988851 401 IAIILSGTGSTREYIQRLGRVLRKGQQ--------EDKRAILYEVIA 439
Cdd:PLN00206  439 QVIIFDMPNTIKEYIHQIGRASRMGEKgtaivfvnEEDRNLFPELVA 485
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
68-190 1.85e-07

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 53.75  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  68 LELIASFEREP----YPHQTEALIAWKKSQRRGVIVLPTAAGKTYLAQLALQSTPRS---TLIIVPTIDLMHQWYAQMLA 140
Cdd:COG1204     9 EKVIEFLKERGieelYPPQAEALEAGLLEGKNLVVSAPTASGKTLIAELAILKALLNggkALYIVPLRALASEKYREFKR 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002988851 141 AFPDA--EVGLLGGGSKDNSA------ILIATYQSAAIYsetLGNRYAFL------IFDECHHL 190
Cdd:COG1204    89 DFEELgiKVGVSTGDYDSDDEwlgrydILVATPEKLDSL---LRNGPSWLrdvdlvVVDEAHLI 149
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
79-188 1.89e-07

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: 51.11  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  79 YPHQTEALIAWKKSQRRGVIVLPTAAGKTYLAQLA----LQSTPRSTLIIVPTIDLMHQWYA---QMLAAFPDAEVGLLG 151
Cdd:cd17921     3 NPIQREALRALYLSGDSVLVSAPTSSGKTLIAELAilraLATSGGKAVYIAPTRALVNQKEAdlrERFGPLGKNVGLLTG 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1002988851 152 GGSKD-----NSAILIATYQSAAIYSETLGNRYAF----LIFDECH 188
Cdd:cd17921    83 DPSVNklllaEADILVATPEKLDLLLRNGGERLIQdvrlVVVDEAH 128
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
77-219 2.35e-07

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 51.32  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  77 EPYPHQTEALIAWKKSqRRGVIVLPTAAGKTYLAQLAL---------QSTPRSTLIIVPTIDLMHQWYAQMLAAFPDA-E 146
Cdd:cd18036     2 ELRNYQLELVLPALRG-KNTIICAPTGSGKTRVAVYICrhhlekrrsAGEKGRVVVLVNKVPLVEQQLEKFFKYFRKGyK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 147 VGLLGGGSKDNSA----------------ILIATYQSAAIYSETLGNRYAFLIFDECHHLPSD------FFR----KIAE 200
Cdd:cd18036    81 VTGLSGDSSHKVSfgqivkasdviictpqILINNLLSGREEERVYLSDFSLLIFDECHHTQKEhpynkiMRMyldkKLSS 160
                         170
                  ....*....|....*....
gi 1002988851 201 DSIAPYRLGLTATPDRGDG 219
Cdd:cd18036   161 QGPLPQILGLTASPGVGGA 179
ERCC3_RAD25_C pfam16203
ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 ...
358-452 7.92e-07

ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 and XPB helicases.


Pssm-ID: 406585  Cd Length: 248  Bit Score: 50.29  E-value: 7.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 358 PAITHQTPVKERHEILTRFRQG-EYKILVTSHVLNEGVDVPEAGIAI-ILSGTGSTREYIQRLGRVLR---KGQQEDKRA 432
Cdd:pfam16203  83 PYIYGGTSQAERMRILQNFKHNpNVNTIFLSKVGDTSIDLPEANVLIqISSHFGSRRQEAQRLGRILRakrRSNDEGFNA 162
                          90       100
                  ....*....|....*....|
gi 1002988851 433 ILYEVIAENTTEEKTSQRRR 452
Cdd:pfam16203 163 FFYSLVSKDTQEMYYSTKRQ 182
DEXHc_RecG cd17918
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ...
69-214 4.79e-06

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


Pssm-ID: 350676 [Multi-domain]  Cd Length: 180  Bit Score: 47.03  E-value: 4.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  69 ELIASFEREPYPHQTEALIAWKKSQRRG-----VIVLPTAAGKTYLAQLALQ---STPRSTLIIVPTIDLMHQWYAQMLA 140
Cdd:cd17918     7 ELCKSLPFSLTKDQAQAIKDIEKDLHSPepmdrLLSGDVGSGKTLVALGAALlayKNGKQVAILVPTEILAHQHYEEARK 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002988851 141 AFPDAEVGLLGGGSKDN----SAILIATyqSAAIYSETLGNRYAFLIFDECHHLPSDFFRKIAEDSiAPYRLGLTATP 214
Cdd:cd17918    87 FLPFINVELVTGGTKAQilsgISLLVGT--HALLHLDVKFKNLDLVIVDEQHRFGVAQREALYNLG-ATHFLEATATP 161
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
78-218 5.00e-06

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 47.28  E-value: 5.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  78 PYPHQTEAL---IAwkkSQRRGVIVlptA----AGKT-----YLAQLALQSTPRSTLIIVPTIdLMHQWYAQMLAAFPD- 144
Cdd:cd18011     1 PLPHQIDAVlraLR---KPPVRLLL---AdevgLGKTieaglIIKELLLRGDAKRVLILCPAS-LVEQWQDELQDKFGLp 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 145 ---------AEVGLLGGGSKDNSAILIATYQSAA--IYSETLGN--RYAFLIFDECHHL----------PSDFFRKIAEd 201
Cdd:cd18011    74 flildretaAQLRRLIGNPFEEFPIVIVSLDLLKrsEERRGLLLseEWDLVVVDEAHKLrnsgggketkRYKLGRLLAK- 152
                         170
                  ....*....|....*..
gi 1002988851 202 sIAPYRLGLTATPDRGD 218
Cdd:cd18011   153 -RARHVLLLTATPHNGK 168
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
322-398 9.12e-06

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


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 47.83  E-value: 9.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 322 KLRVLAELICEHHPEPILIFTNDNATVYRISESFL---IPAIT-H----QtpvKERHEILTRFRQGEYKILVTSHVLNEG 393
Cdd:COG0513   228 KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQkrgISAAAlHgdlsQ---GQRERALDAFRNGKIRVLVATDVAARG 304

                  ....*
gi 1002988851 394 VDVPE 398
Cdd:COG0513   305 IDIDD 309
PRK05298 PRK05298
excinuclease ABC subunit UvrB;
368-455 1.41e-05

excinuclease ABC subunit UvrB;


Pssm-ID: 235395 [Multi-domain]  Cd Length: 652  Bit Score: 47.73  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 368 ERHEILTRFRQGEYKILVTSHVLNEGVDVPEAGIAIILSG--TG---STREYIQRLGRVLRkgqQEDKRAILYeviAENT 442
Cdd:PRK05298  484 ERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDAdkEGflrSERSLIQTIGRAAR---NVNGKVILY---ADKI 557
                          90
                  ....*....|....*...
gi 1002988851 443 TE--EKT---SQRRRGEQ 455
Cdd:PRK05298  558 TDsmQKAideTERRREIQ 575
SF2_C_RecG cd18811
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ...
365-451 2.16e-05

C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350198 [Multi-domain]  Cd Length: 159  Bit Score: 44.64  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 365 PVKERHEILTRFRQGEYKILVTSHVLNEGVDVPEAGIAII-------LSGTGSTReyiqrlGRVLRKGQQEdkrailYEV 437
Cdd:cd18811    72 KSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIedaerfgLSQLHQLR------GRVGRGDHQS------YCL 139
                          90
                  ....*....|....
gi 1002988851 438 IAENTTEEKTSQRR 451
Cdd:cd18811   140 LVYKDPLTETAKQR 153
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
77-223 5.83e-05

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: 43.96  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  77 EPYPHQTEALIAWKKSqRRGVIVLPTAAGKTYLAQLA----LQSTPRS----TLIIVPTIDLMHQwyaQMLAAF-----P 143
Cdd:cd17927     2 KPRNYQLELAQPALKG-KNTIICLPTGSGKTFVAVLIcehhLKKFPAGrkgkVVFLANKVPLVEQ---QKEVFRkhferP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 144 DAEVGLLGGGSKDN---------SAILIATYQ-------SAAIYSETlgnRYAFLIFDECHHL----PSDFFRKIAEDSI 203
Cdd:cd17927    78 GYKVTGLSGDTSENvsveqivesSDVIIVTPQilvndlkSGTIVSLS---DFSLLVFDECHNTtknhPYNEIMFRYLDQK 154
                         170       180
                  ....*....|....*....|....*.
gi 1002988851 204 A------PYRLGLTATPDRGDGSHQD 223
Cdd:cd17927   155 LgssgplPQILGLTASPGVGGAKNTE 180
SF2_C_RecG_TRCF cd18792
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ...
359-451 1.38e-04

C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350179 [Multi-domain]  Cd Length: 160  Bit Score: 42.25  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 359 AITH-QTPVKERHEILTRFRQGEYKILVTSHVLNEGVDVPEAGIAIIlsgtgstrEYIQRL---------GRVLRKGQQe 428
Cdd:cd18792    64 ALLHgKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMII--------EDADRFglsqlhqlrGRVGRGKHQ- 134
                          90       100
                  ....*....|....*....|...
gi 1002988851 429 dkrAILYEVIAENTTEEKTSQRR 451
Cdd:cd18792   135 ---SYCYLLYPDPKKLTETAKKR 154
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
30-398 1.75e-04

Type I site-specific restriction endonuclease, part of a restriction-modification system [Defense mechanisms];


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 44.45  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  30 WDDR----IERfRILAIHyRPlvETLQEeginFQDEAKAFNNLELIA---SFEREPYPHQTEAlI-----AWKKSQRRGV 97
Cdd:COG4096   112 WDDRdpypRER-EVDGFP-SP--EELWE----LLKRRKGTARKRLATepyNDGIALRYYQIEA-IrrveeAIAKGQRRAL 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  98 IVLPTAAGKTYLA-QLA---LQSTP---------RSTLIivptidlmhqwyAQMLAAFPDAEVGL-----LGGGSKD--- 156
Cdd:COG4096   183 LVMATGTGKTRTAiALIyrlLKAGRakrilfladRNALV------------DQAKNAFKPFLPDLdaftkLYNKSKDidk 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 157 NSAILIATYQsaAIYSETLGNR------------YAFLIFDECHHlpSDF--FRKIAE--DSiapYRLGLTATPDRgDGS 220
Cdd:COG4096   251 SARVYFSTYQ--TMMNRIDGEEeepgyrqfppdfFDLIIIDECHR--GIYskWRAILDyfDA---LQIGLTATPKD-TID 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 221 HQDLDYLIGTIVYQKS-PQDLSGKALADHEIIQIKVKLSaKEQEKYQEAIKIRNDflRRNNLSLSGLDgwqnfvmisars 299
Cdd:COG4096   323 RNTYEYFNGNPVYTYSlEQAVADGFLVPYKVIRIDTKFD-REGIRYDAGEDLSDE--EGEEIELEELE------------ 387
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 300 segrramlahrESKEISSG-------TQGKLRVLAELICEHHPEPI-------LIFTNDNATVYRISESF--LIPA---- 359
Cdd:COG4096   388 -----------EDREYEAKdfnrkvvNEDTTRKVLEELMEYLDKPGgdrlgktIIFAKNDDHADRIVQALreLYPElggd 456
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1002988851 360 ----ITHQTPVKERHeiLTRFRQGEY--KILVTSHVLNEGVDVPE 398
Cdd:COG4096   457 fvkkITGDDDYGKSL--IDNFKNPEKypRIAVTVDMLDTGIDVPE 499
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
320-427 2.02e-04

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 43.75  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 320 QGKLRVLAELICEHHPEPILIFTNDNATVYRISESFLIPAI-----THQTPVKERHEILTRFRQGEYKILVTSHVLNEGV 394
Cdd:PRK01297  320 SDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGInaaqlSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGI 399
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002988851 395 DVPeaGIAIILSGT--GSTREYIQRLGRVLRKGQQ 427
Cdd:PRK01297  400 HID--GISHVINFTlpEDPDDYVHRIGRTGRAGAS 432
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
79-214 2.33e-04

DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 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: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 42.31  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  79 YPHQTEAL-IAWKKSQRR--GVIVLPTAAGKT-----YLAQLALQSTP-RSTLIIVPTiDLMHQWYAQMLAAFPDAEVGL 149
Cdd:cd18000     2 FKYQQTGVqWLWELHCQRvgGILGDEMGLGKTiqiiaFLAALHHSKLGlGPSLIVCPA-TVLKQWVKEFHRWWPPFRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 150 L-----GGGSKDNS-----------------AILIATYQSAAIYSETLGNR-YAFLIFDECHhlpsdffrKI----AEDS 202
Cdd:cd18000    81 LhssgsGTGSEEKLgsierksqlirkvvgdgGILITTYEGFRKHKDLLLNHnWQYVILDEGH--------KIrnpdAEIT 152
                         170
                  ....*....|....*...
gi 1002988851 203 IA------PYRLGLTATP 214
Cdd:cd18000   153 LAckqlrtPHRLILSGTP 170
PTZ00424 PTZ00424
helicase 45; Provisional
367-427 3.49e-04

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 42.89  E-value: 3.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002988851 367 KERHEILTRFRQGEYKILVTSHVLNEGVDVPEAGIAIILSGTGSTREYIQRLGRVLRKGQQ 427
Cdd:PTZ00424  304 KDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRK 364
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
322-429 4.45e-04

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 43.02  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 322 KLRVLAELICEHHPEPILIFTNDNATVYRISES-----FLIPAITHQTPVKERHEILTRFRQGEYKILVTSHVLNEGVDV 396
Cdd:PRK04537  244 KQTLLLGLLSRSEGARTMVFVNTKAFVERVARTlerhgYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHI 323
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1002988851 397 PEAGIAIILSGTGSTREYIQRLGRVLRKGQQED 429
Cdd:PRK04537  324 DGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGD 356
ComFA COG4098
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ...
80-404 6.28e-04

Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];


Pssm-ID: 443274 [Multi-domain]  Cd Length: 451  Bit Score: 42.17  E-value: 6.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851  80 PHQTEA---LIAWKKSQRRGVIVLPTAAGKT----YLAQLALQSTPRsTLIIVPTIDLMHQWYAQMLAAFPDAEVGLLGG 152
Cdd:COG4098   113 PAQQKAsdeLLEAIKKKEEHLVWAVCGAGKTemlfPAIAEALKQGGR-VCIATPRVDVVLELAPRLQQAFPGVDIAALYG 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 153 GSKD---NSAILIAT-------YQsaaiysetlgnryAF--LIFDEChhlpsDFFrkiaedsiaPYR------------- 207
Cdd:COG4098   192 GSEEkyrYAQLVIATthqllrfYQ-------------AFdlLIIDEV-----DAF---------PYSgdpmlqyavkrar 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 208 ------LGLTATPDRgdgsHQDLDYLIGTIVYQKSPQDLSGKALAdheIIQIKVklsakeQEKYQEAikirndfLRRNNL 281
Cdd:COG4098   245 kpdgklIYLTATPSK----ALQRQVKRGKLKVVKLPARYHGHPLP---VPKFKW------LGNWKKR-------LRRGKL 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 282 SLSgLDGWqnfvmISARSSEGRRAML--AHRESKEissgtqgklrVLAELICEHHPEPILiftndnATVYriSESflipa 359
Cdd:COG4098   305 PRK-LLKW-----LKKRLKEGRQLLIfvPTIELLE----------QLVALLQKLFPEERI------AGVH--AED----- 355
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1002988851 360 ithqtpvKERHEILTRFRQGEYKILVTSHVLNEGVDVPEAGIAII 404
Cdd:COG4098   356 -------PERKEKVQAFRDGEIPILVTTTILERGVTFPNVDVAVL 393
PRK13767 PRK13767
ATP-dependent helicase; Provisional
307-420 9.66e-04

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 41.80  E-value: 9.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 307 LAHRESKEISSGTqgkLRVLAELICEHhpEPILIFTND-NAT---VY----RISESFLIPAIT--HQTPVKE-RHEILTR 375
Cdd:PRK13767  261 LIHTPAEEISEAL---YETLHELIKEH--RTTLIFTNTrSGAervLYnlrkRFPEEYDEDNIGahHSSLSREvRLEVEEK 335
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1002988851 376 FRQGEYKILVTSHVLNEGVDVPEAGIAIILSGTGSTREYIQRLGR 420
Cdd:PRK13767  336 LKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGR 380
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
321-429 1.91e-03

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. 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: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 38.61  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002988851 321 GKLRVLAELI--CEHHPEPILIFTNDNATVYRIsESFLIPA------ITHQTPVKERHEILTRFRQGEYK--ILVTSHVL 390
Cdd:cd18793    11 GKLEALLELLeeLREPGEKVLIFSQFTDTLDIL-EEALRERgikylrLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1002988851 391 NEGVDVPEAGIAII--LSGTgSTREyIQRLGRVLRKGQQED 429
Cdd:cd18793    90 GVGLNLTAANRVILydPWWN-PAVE-EQAIDRAHRIGQKKP 128
PRK10917 PRK10917
ATP-dependent DNA helicase RecG; Provisional
359-404 3.79e-03

ATP-dependent DNA helicase RecG; Provisional


Pssm-ID: 236794 [Multi-domain]  Cd Length: 681  Bit Score: 39.75  E-value: 3.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1002988851 359 AITH-QTPVKERHEILTRFRQGEYKILVTSHVLNEGVDVPEAGIAII 404
Cdd:PRK10917  509 GLLHgRMKPAEKDAVMAAFKAGEIDILVATTVIEVGVDVPNATVMVI 555
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
79-117 8.78e-03

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 37.31  E-value: 8.78e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1002988851  79 YPHQTEALIAWKKSQRRGVIVLPTAAGKTYLAQLALQST 117
Cdd:cd18028     3 YPPQAEAVRAGLLKGENLLISIPTASGKTLIAEMAMVNT 41
 
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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