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Conserved domains on  [gi|1127884947|emb|CCP51220|]
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putative helicase [Brucella phage Tb]

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];
2-337 5.96e-68

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


:

Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 230.30  E-value: 5.96e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   2 PCMVEAPTGAGKSVIIAEIARIIYemTGKRILVTAPSAELVIQNRAKFiATGYPASmySASAGKKSTRHHVVFGTP--LT 79
Cdd:COG1061   102 RGLVVAPTGTGKTVLALALAAELL--RGKRVLVLVPRRELLEQWAEEL-RRFLGDP--LAGGGKKDSDAPITVATYqsLA 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947  80 IKSNIKAFQKNFAMVICDEC-DLITPTLKKIIEGMqegnPNLRVVGTTATPmrmregyiFREwpdgrinDDSQSLNPFYH 158
Cdd:COG1061   177 RRAHLDELGDRFGLVIIDEAhHAGAPSYRRILEAF----PAAYRLGLTATP--------FRS-------DGREILLFLFD 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 159 KCVYRIEARHLIEQGYLTKPVIGQIN------ASRYDTSGlqlnrmgnytpESLDKAFVGMGRKTAAIVADIVSQTRNRN 232
Cdd:COG1061   238 GIVYEYSLKEAIEDGYLAPPEYYGIRvdltdeRAEYDALS-----------ERLREALAADAERKDKILRELLREHPDDR 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 233 AVLIFAATVKHAEEVMASLPP--EISAIITGDT--KDRKAILDKVSRGKIKYVVNVGVLTVGVDLPIVDTIALMRQSESV 308
Cdd:COG1061   307 KTLVFCSSVDHAEALAELLNEagIRAAVVTGDTpkKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSP 386
                         330       340
                  ....*....|....*....|....*....
gi 1127884947 309 RLLQQIIGRGLRLYPNKTECLILDFCLNH 337
Cdd:COG1061   387 REFIQRLGRGLRPAPGKEDALVYDFVGND 415
DZR super family cl25536
Double zinc ribbon; This family consists of a pair of zinc ribbon domains.
415-456 1.19e-03

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: 36.97  E-value: 1.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1127884947 415 RCFGYVPVGAGRVERCGYRWSGKDCPACGEKNDIAARYCYVC 456
Cdd:pfam12773   3 NCGHPNPPGAKFCPACGTPLKPDRCPNCGAPVPPNARFCPYC 44
 
Name Accession Description Interval E-value
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
2-337 5.96e-68

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 230.30  E-value: 5.96e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   2 PCMVEAPTGAGKSVIIAEIARIIYemTGKRILVTAPSAELVIQNRAKFiATGYPASmySASAGKKSTRHHVVFGTP--LT 79
Cdd:COG1061   102 RGLVVAPTGTGKTVLALALAAELL--RGKRVLVLVPRRELLEQWAEEL-RRFLGDP--LAGGGKKDSDAPITVATYqsLA 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947  80 IKSNIKAFQKNFAMVICDEC-DLITPTLKKIIEGMqegnPNLRVVGTTATPmrmregyiFREwpdgrinDDSQSLNPFYH 158
Cdd:COG1061   177 RRAHLDELGDRFGLVIIDEAhHAGAPSYRRILEAF----PAAYRLGLTATP--------FRS-------DGREILLFLFD 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 159 KCVYRIEARHLIEQGYLTKPVIGQIN------ASRYDTSGlqlnrmgnytpESLDKAFVGMGRKTAAIVADIVSQTRNRN 232
Cdd:COG1061   238 GIVYEYSLKEAIEDGYLAPPEYYGIRvdltdeRAEYDALS-----------ERLREALAADAERKDKILRELLREHPDDR 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 233 AVLIFAATVKHAEEVMASLPP--EISAIITGDT--KDRKAILDKVSRGKIKYVVNVGVLTVGVDLPIVDTIALMRQSESV 308
Cdd:COG1061   307 KTLVFCSSVDHAEALAELLNEagIRAAVVTGDTpkKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSP 386
                         330       340
                  ....*....|....*....|....*....
gi 1127884947 309 RLLQQIIGRGLRLYPNKTECLILDFCLNH 337
Cdd:COG1061   387 REFIQRLGRGLRPAPGKEDALVYDFVGND 415
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
235-334 9.08e-26

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: 9.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 235 LIFAATVKHAEEV----------MASLPPEISAIITGDtkdRKAILDKVSRGKIKYVVNVGVLTVGVDLPIVDTIALMRQ 304
Cdd:cd18799    10 LIFCVSIEHAEFMaeafneagidAVALNSDYSDRERGD---EALILLFFGELKPPILVTVDLLTTGVDIPEVDNVVFLRP 86
                          90       100       110
                  ....*....|....*....|....*....|
gi 1127884947 305 SESVRLLQQIIGRGLRLYPNKTECLILDFC 334
Cdd:cd18799    87 TESRTLFLQMLGRGLRLHEGKDFFTILDFI 116
DEXDc smart00487
DEAD-like helicases superfamily;
3-129 5.73e-15

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 73.68  E-value: 5.73e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947    3 CMVEAPTGAGKSVIIAE-IARIIYEMTGKRILVTAPSAELVIQ--NRAKFIATGYP---------ASMYSASAGKKSTRH 70
Cdd:smart00487  27 VILAAPTGSGKTLAALLpALEALKRGKGGRVLVLVPTRELAEQwaEELKKLGPSLGlkvvglyggDSKREQLRKLESGKT 106
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1127884947   71 HVVFGTPLTIKSNIKA---FQKNFAMVICDECDLI-----TPTLKKIIEGMqegNPNLRVVGTTATP 129
Cdd:smart00487 107 DILVTTPGRLLDLLENdklSLSNVDLVILDEAHRLldggfGDQLEKLLKLL---PKNVQLLLLSATP 170
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
3-129 2.47e-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: 65.34  E-value: 2.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   3 CMVEAPTGAGKSVI--IAEIARIIYEMTGKRILVTAPSAELVIQ--NRAKFIATGYPASMYSASAGKKSTRH-------H 71
Cdd:pfam00270  17 VLVQAPTGSGKTLAflLPALEALDKLDNGPQALVLAPTRELAEQiyEELKKLGKGLGLKVASLLGGDSRKEQleklkgpD 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1127884947  72 VVFGTP---LTIKSNIKAFqKNFAMVICDECDLIT-----PTLKKIIEGMqegNPNLRVVGTTATP 129
Cdd:pfam00270  97 ILVGTPgrlLDLLQERKLL-KNLKLLVLDEAHRLLdmgfgPDLEEILRRL---PKKRQILLLSATL 158
uvsW PHA02558
UvsW helicase; Provisional
3-334 1.54e-10

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 63.49  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   3 CMVEAPTGAGKSVIIAEIARIIYEMTGKRILVTAPSAELVIQNRAKFIATGYPAS--MYSASAGK-KSTRHHVVFGTPLT 79
Cdd:PHA02558  132 RLLNLPTSAGKSLIQYLLSRYYLENYEGKVLIIVPTTSLVTQMIDDFVDYRLFPReaMHKIYSGTaKDTDAPIVVSTWQS 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947  80 IKSNIKAFQKNFAMVICDECDLITPT-LKKIIEGMqeGNPNLRvVGTTATPmrmregyifrewPDGRINddSQSLNPFYH 158
Cdd:PHA02558  212 AVKQPKEWFDQFGMVIVDECHLFTGKsLTSIITKL--DNCKFK-FGLTGSL------------RDGKAN--ILQYVGLFG 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 159 KCVYRIEARHLIEQGYLTKPvigQINAsrydtsgLQLnrmgNYTPESLDKAfvgMGRKTAAIVADIVSQTRnRNA----- 233
Cdd:PHA02558  275 DIFKPVTTSQLMEEGQVTDL---KINS-------IFL----RYPDEDRVKL---KGEDYQEEIKYITSHTK-RNKwianl 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 234 ----------VLIFAATVKHAEEV--MASLPPEISAIITGDTK--DRKAILDKVSRGK-IKYVVNVGVLTVGVDLPIVDT 298
Cdd:PHA02558  337 alklakkgenTFVMFKYVEHGKPLyeMLKKVYDKVYYVSGEVDteDRNEMKKIAEGGKgIIIVASYGVFSTGISIKNLHH 416
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1127884947 299 IALMRQSES-VRLLQQiIGRGLRLYPNKTECLILDFC 334
Cdd:PHA02558  417 VIFAHPSKSkIIVLQS-IGRVLRKHGSKSIATVWDII 452
DZR pfam12773
Double zinc ribbon; This family consists of a pair of zinc ribbon domains.
415-456 1.19e-03

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


Pssm-ID: 432773 [Multi-domain]  Cd Length: 45  Bit Score: 36.97  E-value: 1.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1127884947 415 RCFGYVPVGAGRVERCGYRWSGKDCPACGEKNDIAARYCYVC 456
Cdd:pfam12773   3 NCGHPNPPGAKFCPACGTPLKPDRCPNCGAPVPPNARFCPYC 44
 
Name Accession Description Interval E-value
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
2-337 5.96e-68

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 230.30  E-value: 5.96e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   2 PCMVEAPTGAGKSVIIAEIARIIYemTGKRILVTAPSAELVIQNRAKFiATGYPASmySASAGKKSTRHHVVFGTP--LT 79
Cdd:COG1061   102 RGLVVAPTGTGKTVLALALAAELL--RGKRVLVLVPRRELLEQWAEEL-RRFLGDP--LAGGGKKDSDAPITVATYqsLA 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947  80 IKSNIKAFQKNFAMVICDEC-DLITPTLKKIIEGMqegnPNLRVVGTTATPmrmregyiFREwpdgrinDDSQSLNPFYH 158
Cdd:COG1061   177 RRAHLDELGDRFGLVIIDEAhHAGAPSYRRILEAF----PAAYRLGLTATP--------FRS-------DGREILLFLFD 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 159 KCVYRIEARHLIEQGYLTKPVIGQIN------ASRYDTSGlqlnrmgnytpESLDKAFVGMGRKTAAIVADIVSQTRNRN 232
Cdd:COG1061   238 GIVYEYSLKEAIEDGYLAPPEYYGIRvdltdeRAEYDALS-----------ERLREALAADAERKDKILRELLREHPDDR 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 233 AVLIFAATVKHAEEVMASLPP--EISAIITGDT--KDRKAILDKVSRGKIKYVVNVGVLTVGVDLPIVDTIALMRQSESV 308
Cdd:COG1061   307 KTLVFCSSVDHAEALAELLNEagIRAAVVTGDTpkKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSP 386
                         330       340
                  ....*....|....*....|....*....
gi 1127884947 309 RLLQQIIGRGLRLYPNKTECLILDFCLNH 337
Cdd:COG1061   387 REFIQRLGRGLRPAPGKEDALVYDFVGND 415
SF2_C_EcoAI-like cd18799
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ...
235-334 9.08e-26

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: 9.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 235 LIFAATVKHAEEV----------MASLPPEISAIITGDtkdRKAILDKVSRGKIKYVVNVGVLTVGVDLPIVDTIALMRQ 304
Cdd:cd18799    10 LIFCVSIEHAEFMaeafneagidAVALNSDYSDRERGD---EALILLFFGELKPPILVTVDLLTTGVDIPEVDNVVFLRP 86
                          90       100       110
                  ....*....|....*....|....*....|
gi 1127884947 305 SESVRLLQQIIGRGLRLYPNKTECLILDFC 334
Cdd:cd18799    87 TESRTLFLQMLGRGLRLHEGKDFFTILDFI 116
DEXDc smart00487
DEAD-like helicases superfamily;
3-129 5.73e-15

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 73.68  E-value: 5.73e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947    3 CMVEAPTGAGKSVIIAE-IARIIYEMTGKRILVTAPSAELVIQ--NRAKFIATGYP---------ASMYSASAGKKSTRH 70
Cdd:smart00487  27 VILAAPTGSGKTLAALLpALEALKRGKGGRVLVLVPTRELAEQwaEELKKLGPSLGlkvvglyggDSKREQLRKLESGKT 106
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1127884947   71 HVVFGTPLTIKSNIKA---FQKNFAMVICDECDLI-----TPTLKKIIEGMqegNPNLRVVGTTATP 129
Cdd:smart00487 107 DILVTTPGRLLDLLENdklSLSNVDLVILDEAHRLldggfGDQLEKLLKLL---PKNVQLLLLSATP 170
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
4-129 1.24e-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: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   4 MVEAPTGAGKSVIIAEIARIIYEmtgKRILVTAPSAELVIQNRAKFIATGYPASMYSASAGKK--STRHHVVFGTPLTIK 81
Cdd:cd17926    22 ILVLPTGSGKTLTALALIAYLKE---LRTLIVVPTDALLDQWKERFEDFLGDSSIGLIGGGKKkdFDDANVVVATYQSLS 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1127884947  82 S---NIKAFQKNFAMVICDECDLIT-PTLKKIIEGMQEGnpnlRVVGTTATP 129
Cdd:cd17926    99 NlaeEEKDLFDQFGLLIVDEAHHLPaKTFSEILKELNAK----YRLGLTATP 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
3-129 2.47e-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: 65.34  E-value: 2.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   3 CMVEAPTGAGKSVI--IAEIARIIYEMTGKRILVTAPSAELVIQ--NRAKFIATGYPASMYSASAGKKSTRH-------H 71
Cdd:pfam00270  17 VLVQAPTGSGKTLAflLPALEALDKLDNGPQALVLAPTRELAEQiyEELKKLGKGLGLKVASLLGGDSRKEQleklkgpD 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1127884947  72 VVFGTP---LTIKSNIKAFqKNFAMVICDECDLIT-----PTLKKIIEGMqegNPNLRVVGTTATP 129
Cdd:pfam00270  97 ILVGTPgrlLDLLQERKLL-KNLKLLVLDEAHRLLdmgfgPDLEEILRRL---PKKRQILLLSATL 158
HsdR COG4096
Type I site-specific restriction endonuclease, part of a restriction-modification system ...
199-338 5.79e-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: 68.71  E-value: 5.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 199 GNYTPESLDKAFVGMGRkTAAIVADIVSQ----TRNRNA-VLIFAATVKHAE-------EVMASLPPEISAIITGDTKDR 266
Cdd:COG4096   390 REYEAKDFNRKVVNEDT-TRKVLEELMEYldkpGGDRLGkTIIFAKNDDHADrivqalrELYPELGGDFVKKITGDDDYG 468
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1127884947 267 KAILDKVSRGKiKY---VVNVGVLTVGVDLPIVDTIALMRQSESVRLLQQIIGRGLRL----YPNKTECLILDFCLNHE 338
Cdd:COG4096   469 KSLIDNFKNPE-KYpriAVTVDMLDTGIDVPEVVNLVFMRPVKSRIKFEQMIGRGTRLcpdlFPGKTHFTIFDFVGNTE 546
uvsW PHA02558
UvsW helicase; Provisional
3-334 1.54e-10

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 63.49  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   3 CMVEAPTGAGKSVIIAEIARIIYEMTGKRILVTAPSAELVIQNRAKFIATGYPAS--MYSASAGK-KSTRHHVVFGTPLT 79
Cdd:PHA02558  132 RLLNLPTSAGKSLIQYLLSRYYLENYEGKVLIIVPTTSLVTQMIDDFVDYRLFPReaMHKIYSGTaKDTDAPIVVSTWQS 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947  80 IKSNIKAFQKNFAMVICDECDLITPT-LKKIIEGMqeGNPNLRvVGTTATPmrmregyifrewPDGRINddSQSLNPFYH 158
Cdd:PHA02558  212 AVKQPKEWFDQFGMVIVDECHLFTGKsLTSIITKL--DNCKFK-FGLTGSL------------RDGKAN--ILQYVGLFG 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 159 KCVYRIEARHLIEQGYLTKPvigQINAsrydtsgLQLnrmgNYTPESLDKAfvgMGRKTAAIVADIVSQTRnRNA----- 233
Cdd:PHA02558  275 DIFKPVTTSQLMEEGQVTDL---KINS-------IFL----RYPDEDRVKL---KGEDYQEEIKYITSHTK-RNKwianl 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 234 ----------VLIFAATVKHAEEV--MASLPPEISAIITGDTK--DRKAILDKVSRGK-IKYVVNVGVLTVGVDLPIVDT 298
Cdd:PHA02558  337 alklakkgenTFVMFKYVEHGKPLyeMLKKVYDKVYYVSGEVDteDRNEMKKIAEGGKgIIIVASYGVFSTGISIKNLHH 416
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1127884947 299 IALMRQSES-VRLLQQiIGRGLRLYPNKTECLILDFC 334
Cdd:PHA02558  417 VIFAHPSKSkIIVLQS-IGRVLRKHGSKSIATVWDII 452
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
219-320 6.09e-10

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 56.84  E-value: 6.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 219 AIVADIVSQTRNRNaVLIFAATVKHAEEVMASLPPEISAI-ITGDT--KDRKAILDKVSRGKIKYVVNVGVLTVGVDLPI 295
Cdd:pfam00271   4 EALLELLKKERGGK-VLIFSQTKKTLEAELLLEKEGIKVArLHGDLsqEEREEILEDFRKGKIDVLVATDVAERGLDLPD 82
                          90       100
                  ....*....|....*....|....*
gi 1127884947 296 VDTIALMRQSESVRLLQQIIGRGLR 320
Cdd:pfam00271  83 VDLVINYDLPWNPASYIQRIGRAGR 107
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
5-128 3.17e-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: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   5 VEAPTGAGKSVIIAEIARIIYEMTGKRILVTAPSAELVIQNRA---KFIATGYPASMYSAS------AGKKSTRHHVVFG 75
Cdd:cd00046     6 ITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQTAErlrELFGPGIRVAVLVGGssaeerEKNKLGDADIIIA 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1127884947  76 TPLTIKSNIKA----FQKNFAMVICDECDLITPTLKKIIEGMQ----EGNPNLRVVGTTAT 128
Cdd:cd00046    86 TPDMLLNLLLRedrlFLKDLKLIIVDEAHALLIDSRGALILDLavrkAGLKNAQVILLSAT 146
ResIII pfam04851
Type III restriction enzyme, res subunit;
4-131 3.23e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 56.14  E-value: 3.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   4 MVEAPTGAGKSVIIAEIARIIYEMTG-KRILVTAPSAELVIQNRAKF--IATGYPASMYSASAGKKSTRHH---VVFGTP 77
Cdd:pfam04851  27 LIVMATGSGKTLTAAKLIARLFKKGPiKKVLFLVPRKDLLEQALEEFkkFLPNYVEIGEIISGDKKDESVDdnkIVVTTI 106
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947  78 LTIKSNIKAFQK-----NFAMVICDEC-DLITPTLKKIIegmqEGNPNLRVVGTTATPMR 131
Cdd:pfam04851 107 QSLYKALELASLellpdFFDVIIIDEAhRSGASSYRNIL----EYFKPAFLLGLTATPER 162
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
4-139 3.43e-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: 3.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   4 MVEAPTGAGKSVIIAE-IARIIYEMTGKRILVTAPSAELVIQNRAKFIATGYPASMYSASAGKKSTR-HHVVFGTPLTIK 81
Cdd:cd18032    24 LLVMATGTGKTYTAAFlIKRLLEANRKKRILFLAHREELLEQAERSFKEVLPDGSFGNLKGGKKKPDdARVVFATVQTLN 103
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1127884947  82 SNIK--AFQKN-FAMVICDECD-LITPTLKKIIEgmqEGNPNlRVVGTTATPMRMREGYIFR 139
Cdd:cd18032   104 KRKRleKFPPDyFDLIIIDEAHhAIASSYRKILE---YFEPA-FLLGLTATPERTDGLDTYE 161
HELICc smart00490
helicase superfamily c-terminal domain;
257-320 3.41e-08

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 51.06  E-value: 3.41e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1127884947  257 AIITGDT--KDRKAILDKVSRGKIKYVVNVGVLTVGVDLPIVDTIALMRQSESVRLLQQIIGRGLR 320
Cdd:smart00490  15 ARLHGGLsqEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
235-332 1.15e-07

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 54.96  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947  235 LIFAATVKHAEEVMASLPPEISAI-----------ITGDT-KDRKAILdkvsRGK----IKYVVNVGVLTVGVDLPIVDT 298
Cdd:PRK11448   702 LIFAATDAHADMVVRLLKEAFKKKygqveddavikITGSIdKPDQLIR----RFKnerlPNIVVTVDLLTTGIDVPSICN 777
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1127884947  299 IALMRQSESVRLLQQIIGRGLRLYP--NKTECLILD 332
Cdd:PRK11448   778 LVFLRRVRSRILYEQMLGRATRLCPeiGKTHFRIFD 813
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
4-317 1.35e-06

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


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 51.05  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   4 MVEAPTGAGKSViIAEIArIIYEM-TGKRILVTAPSAELVIQNRAKF------------IATG-YPasmysaSAGKKSTR 69
Cdd:COG1204    42 VVSAPTASGKTL-IAELA-ILKALlNGGKALYIVPLRALASEKYREFkrdfeelgikvgVSTGdYD------SDDEWLGR 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947  70 HHVVFGTP---LTIKSNIKAFQKNFAMVICDECDLIT-----PTLKKIIEGMQEGNPNLRVVGTTAT------------- 128
Cdd:COG1204   114 YDILVATPeklDSLLRNGPSWLRDVDLVVVDEAHLIDdesrgPTLEVLLARLRRLNPEAQIVALSATignaeeiaewlda 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 129 --------PMRMREGYIFrewpDGRIN-DDSqslnpfYHKCVYRIE--ARHLIEQGyltkpviGQ----INaSRYDTSGL 193
Cdd:COG1204   194 elvksdwrPVPLNEGVLY----DGVLRfDDG------SRRSKDPTLalALDLLEEG-------GQvlvfVS-SRRDAESL 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 194 qLNRMGNYTPESLDKAFVGMGRKTAAIVADIVSQTRNRNAVlifAATVK------HaeevmASLPPEIsaiitgdtkdRK 267
Cdd:COG1204   256 -AKKLADELKRRLTPEEREELEELAEELLEVSEETHTNEKL---ADCLEkgvafhH-----AGLPSEL----------RR 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1127884947 268 AILDKVSRGKIKYVVNVGVLTVGVDLP----IVDTIALMRQSE-SVRLLQQIIGR 317
Cdd:COG1204   317 LVEDAFREGLIKVLVATPTLAAGVNLParrvIIRDTKRGGMVPiPVLEFKQMAGR 371
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
234-334 1.61e-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: 46.16  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 234 VLIFAATVKHAEEVMASLppeiSAIITGDtkdrkaildkvsrgkikyvvnvgVLTVGVDLPIVDTIALMRQSESVRLLQQ 313
Cdd:cd18785     6 IIVFTNSIEHAEEIASSL----EILVATN-----------------------VLGEGIDVPSLDTVIFFDPPSSAASYIQ 58
                          90       100
                  ....*....|....*....|.
gi 1127884947 314 IIGRGLRlyPNKTECLILDFC 334
Cdd:cd18785    59 RVGRAGR--GGKDEGEVILFV 77
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
3-129 4.54e-06

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: 47.81  E-value: 4.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   3 CMVEAPTGAGKSVIIAEIA----RIIYEMTGKRILVTAPSAELVIQN-RAKFIATGYPASMYSASAGKKST--------- 68
Cdd:cd17927    20 TIICLPTGSGKTFVAVLICehhlKKFPAGRKGKVVFLANKVPLVEQQkEVFRKHFERPGYKVTGLSGDTSEnvsveqive 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1127884947  69 RHHVVFGTPLTIKSNIKAFQK----NFAMVICDEC----------DLITPTLKKIIEGMqegNPNLRVVGTTATP 129
Cdd:cd17927   100 SSDVIIVTPQILVNDLKSGTIvslsDFSLLVFDEChnttknhpynEIMFRYLDQKLGSS---GPLPQILGLTASP 171
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
8-130 5.42e-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: 5.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   8 PTGAGKSVI----IAEIARIIYEMT--GKRILVTAPSAELVIQnRAKFIA--TGYPASMYSASAGKKS----------TR 69
Cdd:cd18034    24 PTGSGKTLIavmlIKEMGELNRKEKnpKKRAVFLVPTVPLVAQ-QAEAIRshTDLKVGEYSGEMGVDKwtkerwkeelEK 102
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1127884947  70 HHVVFGTP---LTIKSNIKAFQKNFAMVICDECDLIT---P--TLKKIIEGMQEGNPNLRVVGTTATPM 130
Cdd:cd18034   103 YDVLVMTAqilLDALRHGFLSLSDINLLIFDECHHATgdhPyaRIMKEFYHLEGRTSRPRILGLTASPV 171
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
3-99 5.47e-06

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: 47.12  E-value: 5.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   3 CMVEAPTGAGKSVIIAEIARIIYEMTGKRILVTAPSAELVIQNRAKFIATGYPASMYSASAGKKST--------RHHVVF 74
Cdd:cd18035    19 TLIVLPTGLGKTIIAILVAADRLTKKGGKVLILAPSRPLVEQHAENLKRVLNIPDKITSLTGEVKPeeraerwdASKIIV 98
                          90       100
                  ....*....|....*....|....*...
gi 1127884947  75 GTPLTIKSNIKAFQKN---FAMVICDEC 99
Cdd:cd18035    99 ATPQVIENDLLAGRITlddVSLLIFDEA 126
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
4-146 7.55e-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: 7.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   4 MVEAPTGAGKSvIIAEIARIIYEMTGKRILVTAPSAELVIQNRAKF-----------IATGypasMYSaSAGKKSTRHHV 72
Cdd:cd18028    21 LISIPTASGKT-LIAEMAMVNTLLEGGKALYLVPLRALASEKYEEFkkleeiglkvgISTG----DYD-EDDEWLGDYDI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947  73 VFGTPLTIKS---NIKAFQKNFAMVICDECDLIT-----PTLKKIIEGMQEGNPNLRVVGTTATPMRMREgyiFREWPDG 144
Cdd:cd18028    95 IVATYEKFDSllrHSPSWLRDVGVVVVDEIHLISdeergPTLESIVARLRRLNPNTQIIGLSATIGNPDE---LAEWLNA 171

                  ..
gi 1127884947 145 RI 146
Cdd:cd18028   172 EL 173
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
4-128 9.86e-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: 9.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   4 MVEAPTGAGKSViIAE--IARIIYEMtGKRILVTAPSAELVIQNRAKF------------IATGYPASMYSASAGKkstr 69
Cdd:cd17921    21 LVSAPTSSGKTL-IAElaILRALATS-GGKAVYIAPTRALVNQKEADLrerfgplgknvgLLTGDPSVNKLLLAEA---- 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1127884947  70 hHVVFGTP-----LTIKSNIKAFQKnFAMVICDECDLIT-----PTLKKIIEGMQEGNPNLRVVGTTAT 128
Cdd:cd17921    95 -DILVATPekldlLLRNGGERLIQD-VRLVVVDEAHLIGdgergVVLELLLSRLLRINKNARFVGLSAT 161
SF2_C_UvrB cd18790
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ...
215-320 3.99e-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: 44.54  E-value: 3.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947 215 RKTAAIVADIVSQTRNRNA----VLIFAATVKHAEEV----------MASLPPEIsaiitgDTKDRKAILDKVSRGKIKY 280
Cdd:cd18790     7 RPTEGQVDDLLGEIRKRVArgerVLVTTLTKRMAEDLteylqelgvkVRYLHSEI------DTLERVEIIRDLRLGEFDV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1127884947 281 VVNVGVLTVGVDLPIVDTIALMRQSE-----SVRLLQQIIGRGLR 320
Cdd:cd18790    81 LVGINLLREGLDLPEVSLVAILDADKegflrSETSLIQTIGRAAR 125
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
3-99 9.46e-05

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 45.49  E-value: 9.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   3 CMVEAPTGAGKSVIIAEIARIIYEMTGKRILVTAPSAELVIQNRAKFI-ATGYPASMYSASAGK----------KSTRhh 71
Cdd:COG1111    20 TLVVLPTGLGKTAVALLVIAERLHKKGGKVLFLAPTKPLVEQHAEFFKeALNIPEDEIVVFTGEvspekrkelwEKAR-- 97
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1127884947  72 VVFGTPLTIKSNIKA---FQKNFAMVICDEC 99
Cdd:COG1111    98 IIVATPQVIENDLIAgriDLDDVSLLIFDEA 128
DZR pfam12773
Double zinc ribbon; This family consists of a pair of zinc ribbon domains.
415-456 1.19e-03

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


Pssm-ID: 432773 [Multi-domain]  Cd Length: 45  Bit Score: 36.97  E-value: 1.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1127884947 415 RCFGYVPVGAGRVERCGYRWSGKDCPACGEKNDIAARYCYVC 456
Cdd:pfam12773   3 NCGHPNPPGAKFCPACGTPLKPDRCPNCGAPVPPNARFCPYC 44
DEXHc_UvsW cd18031
DEXH-box helicase domain of bacteriophage UvsW; Bacteriophage UvsW is part of the WXY system ...
4-129 2.16e-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: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   4 MVEAPTGAGKSVIIAEIARIIYEMTGKRILVTAPSAELVIQNRAKFIATG-YP-ASMYSASAGkkSTRHHVVFGTPLTIK 81
Cdd:cd18031    19 ILNLPTSAGRSLIQALLARYYLENYEGKILIIVPTTALTTQMADDFVDYRlFShAMIKKIGGG--ASKDDKYKNDAPVVV 96
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1127884947  82 SNIKA-------FQKNFAMVICDECDLITP-TLKKIIEGMqegNPNLRVVGTTATP 129
Cdd:cd18031    97 GTWQTvvkqpkeWFSQFGMMMNDECHLATGkSISSIISGL---NNCMFKFGLSGSL 149
DEXDc_ComFA cd17925
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon ...
1-100 3.41e-03

DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon protein 1) is part of the complex mediating the binding and uptake of single-stranded DNA. ComFA is required for DNA uptake but not for binding. It belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350683 [Multi-domain]  Cd Length: 143  Bit Score: 38.05  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   1 MPCMVEAPTGAGKS-VIIAEIARIIyeMTGKRILVTAPSAELVIQ----NRAKFiATGYPASMYSASAGKkstrhhvVFG 75
Cdd:cd17925    17 EDLLVWAVTGAGKTeMLFPAIAQAL--RQGGRVAIASPRIDVCLElaprLKAAF-PGAAIVLLHGGSEDQ-------YQR 86
                          90       100
                  ....*....|....*....|....*..
gi 1127884947  76 TPLTIKSNIKA--FQKNFAMVICDECD 100
Cdd:cd17925    87 SPLVIATTHQLlrFYRAFDLLIIDEVD 113
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
3-129 7.56e-03

DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 37.69  E-value: 7.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127884947   3 CMVEAPTGAGKSVIIAEIARIIYEM--TGKrILVTAPSAELVIQNR-AKFIATGYPASMYSASAG--KKSTRH------H 71
Cdd:cd18033    19 TLVALPTGLGKTFIAAVVMLNYYRWfpKGK-IVFMAPTKPLVSQQIeACYKITGIPSSQTAELTGsvPPTKRAelwaskR 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1127884947  72 VVFGTPLTIKSNIKAFQKNFAMVIC---DECDLITPTLK--KIIEGMQEGNPNLRVVGTTATP 129
Cdd:cd18033    98 VFFLTPQTLENDLKEGDCDPKSIVClviDEAHRATGNYAycQVVRELMRYNSHFRILALTATP 160
 
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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