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Conserved domains on  [gi|857272675|gb|AKO59210|]
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putative helicase [Brucella phage 11sa_141]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11437466)

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];
1-334 6.99e-68

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


:

Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 229.91  E-value: 6.99e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   1 MVEAPTGAGKSVIIAEIARIIYemTGKRILVTAPSAELVIQNRAKFiATGYPASmySASAGKKSTRHHVVFGTP--LTIK 78
Cdd:COG1061  104 LVVAPTGTGKTVLALALAAELL--RGKRVLVLVPRRELLEQWAEEL-RRFLGDP--LAGGGKKDSDAPITVATYqsLARR 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675  79 SNIKAFQKNFAMVICDEC-DLITPTLKKIIEGMqegnPNLRVVGTTATPmrmregyiFREwpdgrinDDSQSLNPFYHKC 157
Cdd:COG1061  179 AHLDELGDRFGLVIIDEAhHAGAPSYRRILEAF----PAAYRLGLTATP--------FRS-------DGREILLFLFDGI 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 158 VYRIEARHLIEQGYLTKPVIGQIN------ASRYDTSGlqlnrmgnytpESLDKAFVGMGRKTAAIVADIVSQTRNRNAV 231
Cdd:COG1061  240 VYEYSLKEAIEDGYLAPPEYYGIRvdltdeRAEYDALS-----------ERLREALAADAERKDKILRELLREHPDDRKT 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 232 LIFAATVKHAEEVMASLPP--EISAIITGDT--KDRKAILDKVSRGKIKYVVNVGVLTVGVDLPIVDTIALMRQSESVRL 307
Cdd:COG1061  309 LVFCSSVDHAEALAELLNEagIRAAVVTGDTpkKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPRE 388
                        330       340
                 ....*....|....*....|....*..
gi 857272675 308 LQQIIGRGLRLYPNKTECLILDFCLNH 334
Cdd:COG1061  389 FIQRLGRGLRPAPGKEDALVYDFVGND 415
DZR super family cl25536
Double zinc ribbon; This family consists of a pair of zinc ribbon domains.
412-453 8.88e-04

Double zinc ribbon; This family consists of a pair of zinc ribbon domains.


The actual alignment was detected with superfamily member pfam12773:

Pssm-ID: 432773 [Multi-domain]  Cd Length: 45  Bit Score: 37.35  E-value: 8.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 857272675  412 RCFGYVPVGAGRVERCGYRWSGKDCPACGEKNDIAARYCYVC 453
Cdd:pfam12773   3 NCGHPNPPGAKFCPACGTPLKPDRCPNCGAPVPPNARFCPYC 44
 
Name Accession Description Interval E-value
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
1-334 6.99e-68

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 229.91  E-value: 6.99e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   1 MVEAPTGAGKSVIIAEIARIIYemTGKRILVTAPSAELVIQNRAKFiATGYPASmySASAGKKSTRHHVVFGTP--LTIK 78
Cdd:COG1061  104 LVVAPTGTGKTVLALALAAELL--RGKRVLVLVPRRELLEQWAEEL-RRFLGDP--LAGGGKKDSDAPITVATYqsLARR 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675  79 SNIKAFQKNFAMVICDEC-DLITPTLKKIIEGMqegnPNLRVVGTTATPmrmregyiFREwpdgrinDDSQSLNPFYHKC 157
Cdd:COG1061  179 AHLDELGDRFGLVIIDEAhHAGAPSYRRILEAF----PAAYRLGLTATP--------FRS-------DGREILLFLFDGI 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 158 VYRIEARHLIEQGYLTKPVIGQIN------ASRYDTSGlqlnrmgnytpESLDKAFVGMGRKTAAIVADIVSQTRNRNAV 231
Cdd:COG1061  240 VYEYSLKEAIEDGYLAPPEYYGIRvdltdeRAEYDALS-----------ERLREALAADAERKDKILRELLREHPDDRKT 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 232 LIFAATVKHAEEVMASLPP--EISAIITGDT--KDRKAILDKVSRGKIKYVVNVGVLTVGVDLPIVDTIALMRQSESVRL 307
Cdd:COG1061  309 LVFCSSVDHAEALAELLNEagIRAAVVTGDTpkKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPRE 388
                        330       340
                 ....*....|....*....|....*..
gi 857272675 308 LQQIIGRGLRLYPNKTECLILDFCLNH 334
Cdd:COG1061  389 FIQRLGRGLRPAPGKEDALVYDFVGND 415
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
232-331 1.02e-25

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: 101.87  E-value: 1.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 232 LIFAATVKHAEEV----------MASLPPEISAIITGDtkdRKAILDKVSRGKIKYVVNVGVLTVGVDLPIVDTIALMRQ 301
Cdd:cd18799   10 LIFCVSIEHAEFMaeafneagidAVALNSDYSDRERGD---EALILLFFGELKPPILVTVDLLTTGVDIPEVDNVVFLRP 86
                         90       100       110
                 ....*....|....*....|....*....|
gi 857272675 302 SESVRLLQQIIGRGLRLYPNKTECLILDFC 331
Cdd:cd18799   87 TESRTLFLQMLGRGLRLHEGKDFFTILDFI 116
DEXDc smart00487
DEAD-like helicases superfamily;
1-126 1.42e-14

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 72.52  E-value: 1.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675     1 MVEAPTGAGKSVIIAE-IARIIYEMTGKRILVTAPSAELVIQ--NRAKFIATGYP---------ASMYSASAGKKSTRHH 68
Cdd:smart00487  28 ILAAPTGSGKTLAALLpALEALKRGKGGRVLVLVPTRELAEQwaEELKKLGPSLGlkvvglyggDSKREQLRKLESGKTD 107
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 857272675    69 VVFGTPLTIKSNIKA---FQKNFAMVICDECDLI-----TPTLKKIIEGMqegNPNLRVVGTTATP 126
Cdd:smart00487 108 ILVTTPGRLLDLLENdklSLSNVDLVILDEAHRLldggfGDQLEKLLKLL---PKNVQLLLLSATP 170
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
1-126 4.29e-12

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: 64.57  E-value: 4.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675    1 MVEAPTGAGKSVI--IAEIARIIYEMTGKRILVTAPSAELVIQ--NRAKFIATGYPASMYSASAGKKSTRH-------HV 69
Cdd:pfam00270  18 LVQAPTGSGKTLAflLPALEALDKLDNGPQALVLAPTRELAEQiyEELKKLGKGLGLKVASLLGGDSRKEQleklkgpDI 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 857272675   70 VFGTP---LTIKSNIKAFqKNFAMVICDECDLIT-----PTLKKIIEGMqegNPNLRVVGTTATP 126
Cdd:pfam00270  98 LVGTPgrlLDLLQERKLL-KNLKLLVLDEAHRLLdmgfgPDLEEILRRL---PKKRQILLLSATL 158
uvsW PHA02558
UvsW helicase; Provisional
1-331 4.78e-10

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 61.95  E-value: 4.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   1 MVEAPTGAGKSVIIAEIARIIYEMTGKRILVTAPSAELVIQNRAKFIATGYPAS--MYSASAGK-KSTRHHVVFGTPLTI 77
Cdd:PHA02558 133 LLNLPTSAGKSLIQYLLSRYYLENYEGKVLIIVPTTSLVTQMIDDFVDYRLFPReaMHKIYSGTaKDTDAPIVVSTWQSA 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675  78 KSNIKAFQKNFAMVICDECDLITPT-LKKIIEGMqeGNPNLRvVGTTATPmrmregyifrewPDGRINddSQSLNPFYHK 156
Cdd:PHA02558 213 VKQPKEWFDQFGMVIVDECHLFTGKsLTSIITKL--DNCKFK-FGLTGSL------------RDGKAN--ILQYVGLFGD 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 157 CVYRIEARHLIEQGYLTKPvigQINAsrydtsgLQLnrmgNYTPESLDKAfvgMGRKTAAIVADIVSQTRnRNA------ 230
Cdd:PHA02558 276 IFKPVTTSQLMEEGQVTDL---KINS-------IFL----RYPDEDRVKL---KGEDYQEEIKYITSHTK-RNKwianla 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 231 ---------VLIFAATVKHAEEV--MASLPPEISAIITGDTK--DRKAILDKVSRGK-IKYVVNVGVLTVGVDLPIVDTI 296
Cdd:PHA02558 338 lklakkgenTFVMFKYVEHGKPLyeMLKKVYDKVYYVSGEVDteDRNEMKKIAEGGKgIIIVASYGVFSTGISIKNLHHV 417
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 857272675 297 ALMRQSES-VRLLQQiIGRGLRLYPNKTECLILDFC 331
Cdd:PHA02558 418 IFAHPSKSkIIVLQS-IGRVLRKHGSKSIATVWDII 452
DZR pfam12773
Double zinc ribbon; This family consists of a pair of zinc ribbon domains.
412-453 8.88e-04

Double zinc ribbon; This family consists of a pair of zinc ribbon domains.


Pssm-ID: 432773 [Multi-domain]  Cd Length: 45  Bit Score: 37.35  E-value: 8.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 857272675  412 RCFGYVPVGAGRVERCGYRWSGKDCPACGEKNDIAARYCYVC 453
Cdd:pfam12773   3 NCGHPNPPGAKFCPACGTPLKPDRCPNCGAPVPPNARFCPYC 44
 
Name Accession Description Interval E-value
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
1-334 6.99e-68

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 229.91  E-value: 6.99e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   1 MVEAPTGAGKSVIIAEIARIIYemTGKRILVTAPSAELVIQNRAKFiATGYPASmySASAGKKSTRHHVVFGTP--LTIK 78
Cdd:COG1061  104 LVVAPTGTGKTVLALALAAELL--RGKRVLVLVPRRELLEQWAEEL-RRFLGDP--LAGGGKKDSDAPITVATYqsLARR 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675  79 SNIKAFQKNFAMVICDEC-DLITPTLKKIIEGMqegnPNLRVVGTTATPmrmregyiFREwpdgrinDDSQSLNPFYHKC 157
Cdd:COG1061  179 AHLDELGDRFGLVIIDEAhHAGAPSYRRILEAF----PAAYRLGLTATP--------FRS-------DGREILLFLFDGI 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 158 VYRIEARHLIEQGYLTKPVIGQIN------ASRYDTSGlqlnrmgnytpESLDKAFVGMGRKTAAIVADIVSQTRNRNAV 231
Cdd:COG1061  240 VYEYSLKEAIEDGYLAPPEYYGIRvdltdeRAEYDALS-----------ERLREALAADAERKDKILRELLREHPDDRKT 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 232 LIFAATVKHAEEVMASLPP--EISAIITGDT--KDRKAILDKVSRGKIKYVVNVGVLTVGVDLPIVDTIALMRQSESVRL 307
Cdd:COG1061  309 LVFCSSVDHAEALAELLNEagIRAAVVTGDTpkKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPRE 388
                        330       340
                 ....*....|....*....|....*..
gi 857272675 308 LQQIIGRGLRLYPNKTECLILDFCLNH 334
Cdd:COG1061  389 FIQRLGRGLRPAPGKEDALVYDFVGND 415
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
232-331 1.02e-25

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: 101.87  E-value: 1.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 232 LIFAATVKHAEEV----------MASLPPEISAIITGDtkdRKAILDKVSRGKIKYVVNVGVLTVGVDLPIVDTIALMRQ 301
Cdd:cd18799   10 LIFCVSIEHAEFMaeafneagidAVALNSDYSDRERGD---EALILLFFGELKPPILVTVDLLTTGVDIPEVDNVVFLRP 86
                         90       100       110
                 ....*....|....*....|....*....|
gi 857272675 302 SESVRLLQQIIGRGLRLYPNKTECLILDFC 331
Cdd:cd18799   87 TESRTLFLQMLGRGLRLHEGKDFFTILDFI 116
DEXDc smart00487
DEAD-like helicases superfamily;
1-126 1.42e-14

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 72.52  E-value: 1.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675     1 MVEAPTGAGKSVIIAE-IARIIYEMTGKRILVTAPSAELVIQ--NRAKFIATGYP---------ASMYSASAGKKSTRHH 68
Cdd:smart00487  28 ILAAPTGSGKTLAALLpALEALKRGKGGRVLVLVPTRELAEQwaEELKKLGPSLGlkvvglyggDSKREQLRKLESGKTD 107
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 857272675    69 VVFGTPLTIKSNIKA---FQKNFAMVICDECDLI-----TPTLKKIIEGMqegNPNLRVVGTTATP 126
Cdd:smart00487 108 ILVTTPGRLLDLLENdklSLSNVDLVILDEAHRLldggfGDQLEKLLKLL---PKNVQLLLLSATP 170
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
1-126 1.23e-12

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: 65.40  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   1 MVEAPTGAGKSVIIAEIARIIYEmtgKRILVTAPSAELVIQNRAKFIATGYPASMYSASAGKK--STRHHVVFGTPLTIK 78
Cdd:cd17926   22 ILVLPTGSGKTLTALALIAYLKE---LRTLIVVPTDALLDQWKERFEDFLGDSSIGLIGGGKKkdFDDANVVVATYQSLS 98
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 857272675  79 S---NIKAFQKNFAMVICDECDLIT-PTLKKIIEGMQEGnpnlRVVGTTATP 126
Cdd:cd17926   99 NlaeEEKDLFDQFGLLIVDEAHHLPaKTFSEILKELNAK----YRLGLTATP 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
1-126 4.29e-12

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: 64.57  E-value: 4.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675    1 MVEAPTGAGKSVI--IAEIARIIYEMTGKRILVTAPSAELVIQ--NRAKFIATGYPASMYSASAGKKSTRH-------HV 69
Cdd:pfam00270  18 LVQAPTGSGKTLAflLPALEALDKLDNGPQALVLAPTRELAEQiyEELKKLGKGLGLKVASLLGGDSRKEQleklkgpDI 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 857272675   70 VFGTP---LTIKSNIKAFqKNFAMVICDECDLIT-----PTLKKIIEGMqegNPNLRVVGTTATP 126
Cdd:pfam00270  98 LVGTPgrlLDLLQERKLL-KNLKLLVLDEAHRLLdmgfgPDLEEILRRL---PKKRQILLLSATL 158
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
196-335 6.82e-12

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


Pssm-ID: 443272 [Multi-domain]  Cd Length: 806  Bit Score: 68.33  E-value: 6.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 196 GNYTPESLDKAFVGMGRkTAAIVADIVSQ----TRNRNA-VLIFAATVKHAE-------EVMASLPPEISAIITGDTKDR 263
Cdd:COG4096  390 REYEAKDFNRKVVNEDT-TRKVLEELMEYldkpGGDRLGkTIIFAKNDDHADrivqalrELYPELGGDFVKKITGDDDYG 468
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 857272675 264 KAILDKVSRGKiKY---VVNVGVLTVGVDLPIVDTIALMRQSESVRLLQQIIGRGLRL----YPNKTECLILDFCLNHE 335
Cdd:COG4096  469 KSLIDNFKNPE-KYpriAVTVDMLDTGIDVPEVVNLVFMRPVKSRIKFEQMIGRGTRLcpdlFPGKTHFTIFDFVGNTE 546
uvsW PHA02558
UvsW helicase; Provisional
1-331 4.78e-10

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 61.95  E-value: 4.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   1 MVEAPTGAGKSVIIAEIARIIYEMTGKRILVTAPSAELVIQNRAKFIATGYPAS--MYSASAGK-KSTRHHVVFGTPLTI 77
Cdd:PHA02558 133 LLNLPTSAGKSLIQYLLSRYYLENYEGKVLIIVPTTSLVTQMIDDFVDYRLFPReaMHKIYSGTaKDTDAPIVVSTWQSA 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675  78 KSNIKAFQKNFAMVICDECDLITPT-LKKIIEGMqeGNPNLRvVGTTATPmrmregyifrewPDGRINddSQSLNPFYHK 156
Cdd:PHA02558 213 VKQPKEWFDQFGMVIVDECHLFTGKsLTSIITKL--DNCKFK-FGLTGSL------------RDGKAN--ILQYVGLFGD 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 157 CVYRIEARHLIEQGYLTKPvigQINAsrydtsgLQLnrmgNYTPESLDKAfvgMGRKTAAIVADIVSQTRnRNA------ 230
Cdd:PHA02558 276 IFKPVTTSQLMEEGQVTDL---KINS-------IFL----RYPDEDRVKL---KGEDYQEEIKYITSHTK-RNKwianla 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 231 ---------VLIFAATVKHAEEV--MASLPPEISAIITGDTK--DRKAILDKVSRGK-IKYVVNVGVLTVGVDLPIVDTI 296
Cdd:PHA02558 338 lklakkgenTFVMFKYVEHGKPLyeMLKKVYDKVYYVSGEVDteDRNEMKKIAEGGKgIIIVASYGVFSTGISIKNLHHV 417
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 857272675 297 ALMRQSES-VRLLQQiIGRGLRLYPNKTECLILDFC 331
Cdd:PHA02558 418 IFAHPSKSkIIVLQS-IGRVLRKHGSKSIATVWDII 452
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
216-317 6.68e-10

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 56.45  E-value: 6.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675  216 AIVADIVSQTRNRNaVLIFAATVKHAEEVMASLPPEISAI-ITGDT--KDRKAILDKVSRGKIKYVVNVGVLTVGVDLPI 292
Cdd:pfam00271   4 EALLELLKKERGGK-VLIFSQTKKTLEAELLLEKEGIKVArLHGDLsqEEREEILEDFRKGKIDVLVATDVAERGLDLPD 82
                          90       100
                  ....*....|....*....|....*
gi 857272675  293 VDTIALMRQSESVRLLQQIIGRGLR 317
Cdd:pfam00271  83 VDLVINYDLPWNPASYIQRIGRAGR 107
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
2-125 3.15e-09

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: 55.87  E-value: 3.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   2 VEAPTGAGKSVIIAEIARIIYEMTGKRILVTAPSAELVIQNRA---KFIATGYPASMYSAS------AGKKSTRHHVVFG 72
Cdd:cd00046    6 ITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAErlrELFGPGIRVAVLVGGssaeerEKNKLGDADIIIA 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 857272675  73 TPLTIKSNIKA----FQKNFAMVICDECDLITPTLKKIIEGMQ----EGNPNLRVVGTTAT 125
Cdd:cd00046   86 TPDMLLNLLLRedrlFLKDLKLIIVDEAHALLIDSRGALILDLavrkAGLKNAQVILLSAT 146
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
1-136 3.41e-09

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: 56.03  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   1 MVEAPTGAGKSVIIAE-IARIIYEMTGKRILVTAPSAELVIQNRAKFIATGYPASMYSASAGKKSTR-HHVVFGTPLTIK 78
Cdd:cd18032   24 LLVMATGTGKTYTAAFlIKRLLEANRKKRILFLAHREELLEQAERSFKEVLPDGSFGNLKGGKKKPDdARVVFATVQTLN 103
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 857272675  79 SNIK--AFQKN-FAMVICDECD-LITPTLKKIIEgmqEGNPNlRVVGTTATPMRMREGYIFR 136
Cdd:cd18032  104 KRKRleKFPPDyFDLIIIDEAHhAIASSYRKILE---YFEPA-FLLGLTATPERTDGLDTYE 161
ResIII pfam04851
Type III restriction enzyme, res subunit;
1-128 3.78e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 55.76  E-value: 3.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675    1 MVEAPTGAGKSVIIAEIARIIYEMTG-KRILVTAPSAELVIQNRAKF--IATGYPASMYSASAGKKSTRHH---VVFGTP 74
Cdd:pfam04851  27 LIVMATGSGKTLTAAKLIARLFKKGPiKKVLFLVPRKDLLEQALEEFkkFLPNYVEIGEIISGDKKDESVDdnkIVVTTI 106
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   75 LTIKSNIKAFQK-----NFAMVICDEC-DLITPTLKKIIegmqEGNPNLRVVGTTATPMR 128
Cdd:pfam04851 107 QSLYKALELASLellpdFFDVIIIDEAhRSGASSYRNIL----EYFKPAFLLGLTATPER 162
HELICc smart00490
helicase superfamily c-terminal domain;
254-317 3.77e-08

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 50.67  E-value: 3.77e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 857272675   254 AIITGDT--KDRKAILDKVSRGKIKYVVNVGVLTVGVDLPIVDTIALMRQSESVRLLQQIIGRGLR 317
Cdd:smart00490  15 ARLHGGLsqEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
232-329 1.14e-07

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 54.96  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675  232 LIFAATVKHAEEVMASLPPEISAI-----------ITGDT-KDRKAILdkvsRGK----IKYVVNVGVLTVGVDLPIVDT 295
Cdd:PRK11448  702 LIFAATDAHADMVVRLLKEAFKKKygqveddavikITGSIdKPDQLIR----RFKnerlPNIVVTVDLLTTGIDVPSICN 777
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 857272675  296 IALMRQSESVRLLQQIIGRGLRLYP--NKTECLILD 329
Cdd:PRK11448  778 LVFLRRVRSRILYEQMLGRATRLCPeiGKTHFRIFD 813
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
1-314 1.34e-06

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 51.05  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   1 MVEAPTGAGKSViIAEIArIIYEM-TGKRILVTAPSAELVIQNRAKF------------IATG-YPasmysaSAGKKSTR 66
Cdd:COG1204   42 VVSAPTASGKTL-IAELA-ILKALlNGGKALYIVPLRALASEKYREFkrdfeelgikvgVSTGdYD------SDDEWLGR 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675  67 HHVVFGTP---LTIKSNIKAFQKNFAMVICDECDLIT-----PTLKKIIEGMQEGNPNLRVVGTTAT------------- 125
Cdd:COG1204  114 YDILVATPeklDSLLRNGPSWLRDVDLVVVDEAHLIDdesrgPTLEVLLARLRRLNPEAQIVALSATignaeeiaewlda 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 126 --------PMRMREGYIFrewpDGRIN-DDSqslnpfYHKCVYRIE--ARHLIEQGyltkpviGQ----INaSRYDTSGL 190
Cdd:COG1204  194 elvksdwrPVPLNEGVLY----DGVLRfDDG------SRRSKDPTLalALDLLEEG-------GQvlvfVS-SRRDAESL 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 191 qLNRMGNYTPESLDKAFVGMGRKTAAIVADIVSQTRNRNAVlifAATVK------HaeevmASLPPEIsaiitgdtkdRK 264
Cdd:COG1204  256 -AKKLADELKRRLTPEEREELEELAEELLEVSEETHTNEKL---ADCLEkgvafhH-----AGLPSEL----------RR 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 857272675 265 AILDKVSRGKIKYVVNVGVLTVGVDLP----IVDTIALMRQSE-SVRLLQQIIGR 314
Cdd:COG1204  317 LVEDAFREGLIKVLVATPTLAAGVNLParrvIIRDTKRGGMVPiPVLEFKQMAGR 371
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
231-331 1.77e-06

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 45.77  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 231 VLIFAATVKHAEEVMASLppeiSAIITGDtkdrkaildkvsrgkikyvvnvgVLTVGVDLPIVDTIALMRQSESVRLLQQ 310
Cdd:cd18785    6 IIVFTNSIEHAEEIASSL----EILVATN-----------------------VLGEGIDVPSLDTVIFFDPPSSAASYIQ 58
                         90       100
                 ....*....|....*....|.
gi 857272675 311 IIGRGLRlyPNKTECLILDFC 331
Cdd:cd18785   59 RVGRAGR--GGKDEGEVILFV 77
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
5-127 5.38e-06

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: 47.26  E-value: 5.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   5 PTGAGKSVI----IAEIARIIYEMT--GKRILVTAPSAELVIQnRAKFIA--TGYPASMYSASAGKKS----------TR 66
Cdd:cd18034   24 PTGSGKTLIavmlIKEMGELNRKEKnpKKRAVFLVPTVPLVAQ-QAEAIRshTDLKVGEYSGEMGVDKwtkerwkeelEK 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 857272675  67 HHVVFGTP---LTIKSNIKAFQKNFAMVICDECDLIT---P--TLKKIIEGMQEGNPNLRVVGTTATPM 127
Cdd:cd18034  103 YDVLVMTAqilLDALRHGFLSLSDINLLIFDECHHATgdhPyaRIMKEFYHLEGRTSRPRILGLTASPV 171
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
1-143 7.50e-06

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: 46.56  E-value: 7.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   1 MVEAPTGAGKSvIIAEIARIIYEMTGKRILVTAPSAELVIQNRAKF-----------IATGypasMYSaSAGKKSTRHHV 69
Cdd:cd18028   21 LISIPTASGKT-LIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFkkleeiglkvgISTG----DYD-EDDEWLGDYDI 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675  70 VFGTPLTIKS---NIKAFQKNFAMVICDECDLIT-----PTLKKIIEGMQEGNPNLRVVGTTATPMRMREgyiFREWPDG 141
Cdd:cd18028   95 IVATYEKFDSllrHSPSWLRDVGVVVVDEIHLISdeergPTLESIVARLRRLNPNTQIIGLSATIGNPDE---LAEWLNA 171

                 ..
gi 857272675 142 RI 143
Cdd:cd18028  172 EL 173
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
1-125 9.80e-06

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: 46.49  E-value: 9.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   1 MVEAPTGAGKSViIAE--IARIIYEMtGKRILVTAPSAELVIQNRAKF------------IATGYPASMYSASAGKkstr 66
Cdd:cd17921   21 LVSAPTSSGKTL-IAElaILRALATS-GGKAVYIAPTRALVNQKEADLrerfgplgknvgLLTGDPSVNKLLLAEA---- 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 857272675  67 hHVVFGTP-----LTIKSNIKAFQKnFAMVICDECDLIT-----PTLKKIIEGMQEGNPNLRVVGTTAT 125
Cdd:cd17921   95 -DILVATPekldlLLRNGGERLIQD-VRLVVVDEAHLIGdgergVVLELLLSRLLRINKNARFVGLSAT 161
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
1-126 1.86e-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: 45.89  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   1 MVEAPTGAGKSVIIAEIA----RIIYEMTGKRILVTAPSAELVIQN-RAKFIATGYPASMYSASAGKKST---------R 66
Cdd:cd17927   21 IICLPTGSGKTFVAVLICehhlKKFPAGRKGKVVFLANKVPLVEQQkEVFRKHFERPGYKVTGLSGDTSEnvsveqiveS 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 857272675  67 HHVVFGTPLTIKSNIKAFQK----NFAMVICDEC----------DLITPTLKKIIEGMqegNPNLRVVGTTATP 126
Cdd:cd17927  101 SDVIIVTPQILVNDLKSGTIvslsDFSLLVFDEChnttknhpynEIMFRYLDQKLGSS---GPLPQILGLTASP 171
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
1-96 3.04e-05

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: 44.81  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   1 MVEAPTGAGKSVIIAEIARIIYEMTGKRILVTAPSAELVIQNRAKFIATGYPASMYSASAGKKST--------RHHVVFG 72
Cdd:cd18035   20 LIVLPTGLGKTIIAILVAADRLTKKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITSLTGEVKPeeraerwdASKIIVA 99
                         90       100
                 ....*....|....*....|....*..
gi 857272675  73 TPLTIKSNIKAFQKN---FAMVICDEC 96
Cdd:cd18035  100 TPQVIENDLLAGRITlddVSLLIFDEA 126
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
212-317 4.65e-05

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


Pssm-ID: 350177 [Multi-domain]  Cd Length: 171  Bit Score: 44.16  E-value: 4.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675 212 RKTAAIVADIVSQTRNRNA----VLIFAATVKHAEEV----------MASLPPEIsaiitgDTKDRKAILDKVSRGKIKY 277
Cdd:cd18790    7 RPTEGQVDDLLGEIRKRVArgerVLVTTLTKRMAEDLteylqelgvkVRYLHSEI------DTLERVEIIRDLRLGEFDV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 857272675 278 VVNVGVLTVGVDLPIVDTIALMRQSE-----SVRLLQQIIGRGLR 317
Cdd:cd18790   81 LVGINLLREGLDLPEVSLVAILDADKegflrSETSLIQTIGRAAR 125
DZR pfam12773
Double zinc ribbon; This family consists of a pair of zinc ribbon domains.
412-453 8.88e-04

Double zinc ribbon; This family consists of a pair of zinc ribbon domains.


Pssm-ID: 432773 [Multi-domain]  Cd Length: 45  Bit Score: 37.35  E-value: 8.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 857272675  412 RCFGYVPVGAGRVERCGYRWSGKDCPACGEKNDIAARYCYVC 453
Cdd:pfam12773   3 NCGHPNPPGAKFCPACGTPLKPDRCPNCGAPVPPNARFCPYC 44
DEXHc_UvsW cd18031
DEXH-box helicase domain of bacteriophage UvsW; Bacteriophage UvsW is part of the WXY system ...
1-126 2.09e-03

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: 39.34  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857272675   1 MVEAPTGAGKSVIIAEIARIIYEMTGKRILVTAPSAELVIQNRAKFIatGYPASMYSA--SAGKKSTRHHVVFGTPLTIK 78
Cdd:cd18031   19 ILNLPTSAGRSLIQALLARYYLENYEGKILIIVPTTALTTQMADDFV--DYRLFSHAMikKIGGGASKDDKYKNDAPVVV 96
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 857272675  79 SNIKA-------FQKNFAMVICDECDLITP-TLKKIIEGMqegNPNLRVVGTTATP 126
Cdd:cd18031   97 GTWQTvvkqpkeWFSQFGMMMNDECHLATGkSISSIISGL---NNCMFKFGLSGSL 149
 
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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