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Conserved domains on  [gi|112984084|ref|NP_001037718|]
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ATP-dependent DNA helicase PIF1 [Rattus norvegicus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 13209511)

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
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
203-500 1.62e-109

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


The actual alignment was detected with superfamily member pfam05970:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 361  Bit Score: 333.96  E-value: 1.62e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  203 LSEEQAAVLRMVL------KGQSIFFTGSAGTGKSYLLKHILGSLPPTG--TVATASTGVAACHI-GGTTLHAFAGIGSG 273
Cdd:pfam05970   1 LNDEQKKVFDAIIesvinnKGGVFFVYGYGGTGKTFLWKAIITSLRSEGkiVLAVASSGVAALLLpGGRTAHSRFGIPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  274 QAPLAQCvALAHRPGVRQGWLNCQRLVIDEISMVEADFFDKLEAVARAVRQQK--KPFGGIQLIICGDFLQLPPVT-KGS 350
Cdd:pfam05970  81 IDELSTC-KIKRGSKLAELLEKTSLIVWDEAPMTHRHCFEALDRTLRDILSETddKPFGGKTVVLGGDFRQILPVIpKGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  351 QHPRFCF---QAKSWRKCVpvTLELTEVWRQAD-----------QTFISLLKAVRLGRCSDEVTRQ-------------- 402
Cdd:pfam05970 160 RPEIVNAsitNSYLWKHVK--VLELTKNMRLLAdsldqteakelQDFSDWLLAIGDGKINDENEREqlidipidillntg 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  403 ---LRATAAHKVGRdgIIA-----------TRLCTHQDDVALTNEKRLKELPGDVHSFEAIDS--------------DPE 454
Cdd:pfam05970 238 gdpIEAIVSEVYPD--ILQnstdpnyleerAILCPTNEDVDEINNYRLSQLPGEEKEYLSSDSisksdndseidalyPTE 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 112984084  455 LSRTLDAQCPVGRVLQLKLGAQVMLVKNLAVSRGLVNGARGVVVGF 500
Cdd:pfam05970 316 FLNSLNANGLPNHVLKLKVGAPVMLLRNLDQSRGLCNGTRLIVTQL 361
SF1_C_RecD cd18809
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ...
544-589 1.37e-15

C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350196 [Multi-domain]  Cd Length: 80  Bit Score: 71.82  E-value: 1.37e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 112984084 544 LAWAMSIHKSQGMSLDCVEISLGRV---FASGQAYVALSRARSLQGLRV 589
Cdd:cd18809   32 QAYAMTIHKSQGSEFDRVIVVLPTShpmLSRGLLYTALTRARKLLTLVG 80
 
Name Accession Description Interval E-value
PIF1 pfam05970
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits ...
203-500 1.62e-109

PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits telomerase activity and is cell cycle regulated. This family includes a large number of largely uncharacterized plant proteins. This family includes a P-loop motif that is involved in nucleotide binding.


Pssm-ID: 428699 [Multi-domain]  Cd Length: 361  Bit Score: 333.96  E-value: 1.62e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  203 LSEEQAAVLRMVL------KGQSIFFTGSAGTGKSYLLKHILGSLPPTG--TVATASTGVAACHI-GGTTLHAFAGIGSG 273
Cdd:pfam05970   1 LNDEQKKVFDAIIesvinnKGGVFFVYGYGGTGKTFLWKAIITSLRSEGkiVLAVASSGVAALLLpGGRTAHSRFGIPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  274 QAPLAQCvALAHRPGVRQGWLNCQRLVIDEISMVEADFFDKLEAVARAVRQQK--KPFGGIQLIICGDFLQLPPVT-KGS 350
Cdd:pfam05970  81 IDELSTC-KIKRGSKLAELLEKTSLIVWDEAPMTHRHCFEALDRTLRDILSETddKPFGGKTVVLGGDFRQILPVIpKGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  351 QHPRFCF---QAKSWRKCVpvTLELTEVWRQAD-----------QTFISLLKAVRLGRCSDEVTRQ-------------- 402
Cdd:pfam05970 160 RPEIVNAsitNSYLWKHVK--VLELTKNMRLLAdsldqteakelQDFSDWLLAIGDGKINDENEREqlidipidillntg 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  403 ---LRATAAHKVGRdgIIA-----------TRLCTHQDDVALTNEKRLKELPGDVHSFEAIDS--------------DPE 454
Cdd:pfam05970 238 gdpIEAIVSEVYPD--ILQnstdpnyleerAILCPTNEDVDEINNYRLSQLPGEEKEYLSSDSisksdndseidalyPTE 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 112984084  455 LSRTLDAQCPVGRVLQLKLGAQVMLVKNLAVSRGLVNGARGVVVGF 500
Cdd:pfam05970 316 FLNSLNANGLPNHVLKLKVGAPVMLLRNLDQSRGLCNGTRLIVTQL 361
DEXSc_Pif1_like cd18037
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ...
206-377 3.01e-87

DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350795 [Multi-domain]  Cd Length: 183  Bit Score: 269.89  E-value: 3.01e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 206 EQAAVLRMVLKGQSIFFTGSAGTGKSYLLKHILGSLP--PTGTVATASTGVAACHIGGTTLHAFAGIGSGQAPLAQCVAL 283
Cdd:cd18037    1 EQRRVLDLVLDGKNVFFTGSAGTGKSYLLRRIIRALPsrPKRVAVTASTGIAACNIGGTTLHSFAGIGLGSEPAEDLLER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 284 AHR-PGVRQGWLNCQRLVIDEISMVEADFFDKLEAVARAVRQQKKPFGGIQLIICGDFLQLPPVTKGSQHPRF------- 355
Cdd:cd18037   81 VKRsPYLVQRWRKCDVLIIDEISMLDADLFDKLDRVAREVRGSDKPFGGIQLILCGDFLQLPPVTKNSERQAFffrgdqq 160
                        170       180
                 ....*....|....*....|...
gi 112984084 356 -CFQAKSWRKCVPVTLELTEVWR 377
Cdd:cd18037  161 fCFEAKSWERCIFLTVELTKVFR 183
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
197-584 1.15e-48

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 177.86  E-value: 1.15e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 197 PSSKPKLSEEQAAVLRMVLKGQSIFF-TGSAGTGKSYLLKHILGSLPPTG--TVATASTGVAA------CHIGGTTLHAF 267
Cdd:COG0507  119 PRAGITLSDEQREAVALALTTRRVSVlTGGAGTGKTTTLRALLAALEALGlrVALAAPTGKAAkrlsesTGIEARTIHRL 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 268 AGIGSGQAPLaqcvalahRPGVRQGWLNCQRLVIDEISMVEADFFDKLeavARAVRQqkkpfGGIQLIICGDFLQLPPVT 347
Cdd:COG0507  199 LGLRPDSGRF--------RHNRDNPLTPADLLVVDEASMVDTRLMAAL---LEALPR-----AGARLILVGDPDQLPSVG 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 348 KGSqhprfCFQAKSWRKCVPVTlELTEVWRQADQT-FISLLKAVRLGRCSDEVTRQLRA--------------------T 406
Cdd:COG0507  263 AGA-----VLRDLIESGTVPVV-ELTEVYRQADDSrIIELAHAIREGDAPEALNARYADvvfveaedaeeaaeaivelyA 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 407 AAHKVGRDGIIatrLCTHQDDVALTNEKRLKELPGdvhsfeaidsdpelSRTLDAQCPVGRVLQLKLGAQVMLVKNlAVS 486
Cdd:COG0507  337 DRPAGGEDIQV---LAPTNAGVDALNQAIREALNP--------------AGELERELAEDGELELYVGDRVMFTRN-DYD 398
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 487 RGLVNGARGVVVGFESEGRGLpRVRFlcgitevirtDRW-TVQVTGGQYLSrqqlpLQLAWAMSIHKSQGMSLDCVEISL 565
Cdd:COG0507  399 LGVFNGDIGTVLSIDEDEGRL-TVRF----------DGReIVTYDPSELDQ-----LELAYAITVHKSQGSTFDRVILVL 462
                        410       420
                 ....*....|....*....|...
gi 112984084 566 G----RVFASGQAYVALSRARSL 584
Cdd:COG0507  463 PsehsPLLSRELLYTALTRAREL 485
SF1_C_RecD cd18809
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ...
544-589 1.37e-15

C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350196 [Multi-domain]  Cd Length: 80  Bit Score: 71.82  E-value: 1.37e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 112984084 544 LAWAMSIHKSQGMSLDCVEISLGRV---FASGQAYVALSRARSLQGLRV 589
Cdd:cd18809   32 QAYAMTIHKSQGSEFDRVIVVLPTShpmLSRGLLYTALTRARKLLTLVG 80
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
183-582 2.07e-14

exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273631 [Multi-domain]  Cd Length: 582  Bit Score: 76.34  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  183 EAPRWPLPVKKLRMPSSKPKLSEEQAAVLRMVLKGQSIFFTGSAGTGKSYLLKHILGSL---------------PPTGTV 247
Cdd:TIGR01447 125 EARKRTAPSAILENLFPLLNEQNWRKTAVALALKSNFSLITGGPGTGKTTTVARLLLALvkqspkqgklrialaAPTGKA 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  248 AT---------------ASTGVAACHIGGTTLHAFAGIGSGQAPLAQCvalahrpgvRQGWLNCQRLVIDEISMVEADFF 312
Cdd:TIGR01447 205 AArlaeslrkavknlaaAEALIAALPSEAVTIHRLLGIKPDTKRFRHH---------ERNPLPLDVLVVDEASMVDLPLM 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  313 DKLeavARAVRqqkkpfGGIQLIICGDFLQLPPVTKGSQHPRFCFQAKSWRKCVPVTLELTEVWRQ---ADQTF------ 383
Cdd:TIGR01447 276 AKL---LKALP------PNTKLILLGDKNQLPSVEAGAVLGDLCELASIGKSILYALCKKINSKTRnplSDNVCflktsh 346
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  384 -------ISLL-KAVRLGRC----SDEVTRQLRATAAHKVGRDGIIATRlcthqdDVALTNEKRLKELPGDVHSFEAIDS 451
Cdd:TIGR01447 347 rfgkdsgIGQLaKAINSGDIeavlNNLRSGQLIEFEFLNSKEDAIERLK------NLYVKYRTFLQKLAALSDAKEILET 420
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  452 DPELsRTLDA--QCPVGrVLQLK--------------------LGAQVMLVKNlAVSRGLVNGARGVVVGfesEGRGLPR 509
Cdd:TIGR01447 421 FDRL-RLLTAlrDGPFG-VLGLNrrieqelqekyfdpdeegwyIGRPIMVTEN-DYTLGLFNGDIGVLLR---DPDGILT 494
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 112984084  510 VRFL-CGITEVIRTDRWTVQVTggqylsrqqlplqlAWAMSIHKSQGMSLDCVEISL----GRVFASGQAYVALSRAR 582
Cdd:TIGR01447 495 VWFHfADGSKAVLPSRLPNYET--------------AFAMTVHKSQGSEFDHVILILpngnSPVLTRELLYTGITRAK 558
PHA03311 PHA03311
helicase-primase subunit BBLF4; Provisional
547-583 1.12e-04

helicase-primase subunit BBLF4; Provisional


Pssm-ID: 223040  Cd Length: 782  Bit Score: 45.28  E-value: 1.12e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 112984084 547 AMSIHKSQGMSLDCVEISlgrvFASG------QAYVALSRARS 583
Cdd:PHA03311 706 AMTIAKSQGLSLDKVAIC----FGNHknlklsHVYVAMSRVTS 744
Herpes_Helicase pfam02689
Helicase; This family consists of Helicases from the Herpes viruses. Helicases are responsible ...
547-594 2.82e-04

Helicase; This family consists of Helicases from the Herpes viruses. Helicases are responsible for the unwinding of DNA and are essential for replication and completion of the viral life cycle.


Pssm-ID: 280797  Cd Length: 809  Bit Score: 43.93  E-value: 2.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 112984084  547 AMSIHKSQGMSLDCVEISLG--RVFASGQAYVALSRARSLQGLrVLDFDP 594
Cdd:pfam02689 733 AMTIAKSQGLSLDKVAICFGnhPNLKLSHVYVAMSRATDPNHL-VMNVNP 781
 
Name Accession Description Interval E-value
PIF1 pfam05970
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits ...
203-500 1.62e-109

PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits telomerase activity and is cell cycle regulated. This family includes a large number of largely uncharacterized plant proteins. This family includes a P-loop motif that is involved in nucleotide binding.


Pssm-ID: 428699 [Multi-domain]  Cd Length: 361  Bit Score: 333.96  E-value: 1.62e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  203 LSEEQAAVLRMVL------KGQSIFFTGSAGTGKSYLLKHILGSLPPTG--TVATASTGVAACHI-GGTTLHAFAGIGSG 273
Cdd:pfam05970   1 LNDEQKKVFDAIIesvinnKGGVFFVYGYGGTGKTFLWKAIITSLRSEGkiVLAVASSGVAALLLpGGRTAHSRFGIPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  274 QAPLAQCvALAHRPGVRQGWLNCQRLVIDEISMVEADFFDKLEAVARAVRQQK--KPFGGIQLIICGDFLQLPPVT-KGS 350
Cdd:pfam05970  81 IDELSTC-KIKRGSKLAELLEKTSLIVWDEAPMTHRHCFEALDRTLRDILSETddKPFGGKTVVLGGDFRQILPVIpKGS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  351 QHPRFCF---QAKSWRKCVpvTLELTEVWRQAD-----------QTFISLLKAVRLGRCSDEVTRQ-------------- 402
Cdd:pfam05970 160 RPEIVNAsitNSYLWKHVK--VLELTKNMRLLAdsldqteakelQDFSDWLLAIGDGKINDENEREqlidipidillntg 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  403 ---LRATAAHKVGRdgIIA-----------TRLCTHQDDVALTNEKRLKELPGDVHSFEAIDS--------------DPE 454
Cdd:pfam05970 238 gdpIEAIVSEVYPD--ILQnstdpnyleerAILCPTNEDVDEINNYRLSQLPGEEKEYLSSDSisksdndseidalyPTE 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 112984084  455 LSRTLDAQCPVGRVLQLKLGAQVMLVKNLAVSRGLVNGARGVVVGF 500
Cdd:pfam05970 316 FLNSLNANGLPNHVLKLKVGAPVMLLRNLDQSRGLCNGTRLIVTQL 361
DEXSc_Pif1_like cd18037
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ...
206-377 3.01e-87

DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350795 [Multi-domain]  Cd Length: 183  Bit Score: 269.89  E-value: 3.01e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 206 EQAAVLRMVLKGQSIFFTGSAGTGKSYLLKHILGSLP--PTGTVATASTGVAACHIGGTTLHAFAGIGSGQAPLAQCVAL 283
Cdd:cd18037    1 EQRRVLDLVLDGKNVFFTGSAGTGKSYLLRRIIRALPsrPKRVAVTASTGIAACNIGGTTLHSFAGIGLGSEPAEDLLER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 284 AHR-PGVRQGWLNCQRLVIDEISMVEADFFDKLEAVARAVRQQKKPFGGIQLIICGDFLQLPPVTKGSQHPRF------- 355
Cdd:cd18037   81 VKRsPYLVQRWRKCDVLIIDEISMLDADLFDKLDRVAREVRGSDKPFGGIQLILCGDFLQLPPVTKNSERQAFffrgdqq 160
                        170       180
                 ....*....|....*....|...
gi 112984084 356 -CFQAKSWRKCVPVTLELTEVWR 377
Cdd:cd18037  161 fCFEAKSWERCIFLTVELTKVFR 183
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
197-584 1.15e-48

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 177.86  E-value: 1.15e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 197 PSSKPKLSEEQAAVLRMVLKGQSIFF-TGSAGTGKSYLLKHILGSLPPTG--TVATASTGVAA------CHIGGTTLHAF 267
Cdd:COG0507  119 PRAGITLSDEQREAVALALTTRRVSVlTGGAGTGKTTTLRALLAALEALGlrVALAAPTGKAAkrlsesTGIEARTIHRL 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 268 AGIGSGQAPLaqcvalahRPGVRQGWLNCQRLVIDEISMVEADFFDKLeavARAVRQqkkpfGGIQLIICGDFLQLPPVT 347
Cdd:COG0507  199 LGLRPDSGRF--------RHNRDNPLTPADLLVVDEASMVDTRLMAAL---LEALPR-----AGARLILVGDPDQLPSVG 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 348 KGSqhprfCFQAKSWRKCVPVTlELTEVWRQADQT-FISLLKAVRLGRCSDEVTRQLRA--------------------T 406
Cdd:COG0507  263 AGA-----VLRDLIESGTVPVV-ELTEVYRQADDSrIIELAHAIREGDAPEALNARYADvvfveaedaeeaaeaivelyA 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 407 AAHKVGRDGIIatrLCTHQDDVALTNEKRLKELPGdvhsfeaidsdpelSRTLDAQCPVGRVLQLKLGAQVMLVKNlAVS 486
Cdd:COG0507  337 DRPAGGEDIQV---LAPTNAGVDALNQAIREALNP--------------AGELERELAEDGELELYVGDRVMFTRN-DYD 398
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 487 RGLVNGARGVVVGFESEGRGLpRVRFlcgitevirtDRW-TVQVTGGQYLSrqqlpLQLAWAMSIHKSQGMSLDCVEISL 565
Cdd:COG0507  399 LGVFNGDIGTVLSIDEDEGRL-TVRF----------DGReIVTYDPSELDQ-----LELAYAITVHKSQGSTFDRVILVL 462
                        410       420
                 ....*....|....*....|...
gi 112984084 566 G----RVFASGQAYVALSRARSL 584
Cdd:COG0507  463 PsehsPLLSRELLYTALTRAREL 485
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
206-376 9.90e-28

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD 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: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 109.18  E-value: 9.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 206 EQAAVLRMVLKGQSIFFTGSAGTGKSYLLKHILGSL--PPTGTVATASTGVAACHIG------GTTLHAFAGIGSGQAPL 277
Cdd:cd17933    1 EQKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAALeaEGKRVVLAAPTGKAAKRLSestgieASTIHRLLGINPGGGGF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084 278 AQCvalahrpgvRQGWLNCQRLVIDEISMVEADFFDKLEAVARAvrqqkkpfgGIQLIICGDFLQLPPVTKGSQhPRFCF 357
Cdd:cd17933   81 YYN---------EENPLDADLLIVDEASMVDTRLMAALLSAIPA---------GARLILVGDPDQLPSVGAGNV-LRDLI 141
                        170
                 ....*....|....*....
gi 112984084 358 QAKSwrkcVPVTlELTEVW 376
Cdd:cd17933  142 ASKG----VPTV-ELTEVF 155
SF1_C_RecD cd18809
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ...
544-589 1.37e-15

C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350196 [Multi-domain]  Cd Length: 80  Bit Score: 71.82  E-value: 1.37e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 112984084 544 LAWAMSIHKSQGMSLDCVEISLGRV---FASGQAYVALSRARSLQGLRV 589
Cdd:cd18809   32 QAYAMTIHKSQGSEFDRVIVVLPTShpmLSRGLLYTALTRARKLLTLVG 80
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
203-394 4.15e-15

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.


Pssm-ID: 433343 [Multi-domain]  Cd Length: 191  Bit Score: 74.14  E-value: 4.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  203 LSEEQAAVLRMVLKGQSIFF--TGSAGTGKSYLLKHILGSLPPTG--TVATASTGVAAchiggttlhafAGIGSGQAPLA 278
Cdd:pfam13604   2 LNAEQAAAVRALLTSGDRVAvlVGPAGTGKTTALKALREAWEAAGyrVIGLAPTGRAA-----------KVLGEELGIPA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  279 QCVA-LAHRPGVRQGWLNCQRLVIDEISMVeaDFFDkLEAVARAVRQQkkpfgGIQLIICGDFLQLPPVTKGSQHpRFCF 357
Cdd:pfam13604  71 DTIAkLLHRLGGRAGLDPGTLLIVDEAGMV--GTRQ-MARLLKLAEDA-----GARVILVGDPRQLPSVEAGGAF-RDLL 141
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 112984084  358 QAkswrkcVPVTLELTEVWRQADQTFISLLKAVRLGR 394
Cdd:pfam13604 142 AA------GIGTAELTEIVRQRDPWQRAASLALRDGD 172
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
183-582 2.07e-14

exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273631 [Multi-domain]  Cd Length: 582  Bit Score: 76.34  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  183 EAPRWPLPVKKLRMPSSKPKLSEEQAAVLRMVLKGQSIFFTGSAGTGKSYLLKHILGSL---------------PPTGTV 247
Cdd:TIGR01447 125 EARKRTAPSAILENLFPLLNEQNWRKTAVALALKSNFSLITGGPGTGKTTTVARLLLALvkqspkqgklrialaAPTGKA 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  248 AT---------------ASTGVAACHIGGTTLHAFAGIGSGQAPLAQCvalahrpgvRQGWLNCQRLVIDEISMVEADFF 312
Cdd:TIGR01447 205 AArlaeslrkavknlaaAEALIAALPSEAVTIHRLLGIKPDTKRFRHH---------ERNPLPLDVLVVDEASMVDLPLM 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  313 DKLeavARAVRqqkkpfGGIQLIICGDFLQLPPVTKGSQHPRFCFQAKSWRKCVPVTLELTEVWRQ---ADQTF------ 383
Cdd:TIGR01447 276 AKL---LKALP------PNTKLILLGDKNQLPSVEAGAVLGDLCELASIGKSILYALCKKINSKTRnplSDNVCflktsh 346
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  384 -------ISLL-KAVRLGRC----SDEVTRQLRATAAHKVGRDGIIATRlcthqdDVALTNEKRLKELPGDVHSFEAIDS 451
Cdd:TIGR01447 347 rfgkdsgIGQLaKAINSGDIeavlNNLRSGQLIEFEFLNSKEDAIERLK------NLYVKYRTFLQKLAALSDAKEILET 420
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  452 DPELsRTLDA--QCPVGrVLQLK--------------------LGAQVMLVKNlAVSRGLVNGARGVVVGfesEGRGLPR 509
Cdd:TIGR01447 421 FDRL-RLLTAlrDGPFG-VLGLNrrieqelqekyfdpdeegwyIGRPIMVTEN-DYTLGLFNGDIGVLLR---DPDGILT 494
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 112984084  510 VRFL-CGITEVIRTDRWTVQVTggqylsrqqlplqlAWAMSIHKSQGMSLDCVEISL----GRVFASGQAYVALSRAR 582
Cdd:TIGR01447 495 VWFHfADGSKAVLPSRLPNYET--------------AFAMTVHKSQGSEFDHVILILpngnSPVLTRELLYTGITRAK 558
TraA_Ti TIGR02768
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a ...
202-582 3.60e-10

Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a single strand exonuclease (N-terminus, MobA/MobL, pfam03389) as well as a helicase domain (central region, homologous to the corresponding region of the F-type relaxase TraI, TIGR02760). This protein likely fills the same role as TraI(F), nicking (at the oriT site) and unwinding the coiled plasmid prior to conjugative transfer.


Pssm-ID: 274289 [Multi-domain]  Cd Length: 744  Bit Score: 62.90  E-value: 3.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  202 KLSEEQAAVLRMVLKGQSI-FFTGSAGTGKSYLLKHILGSLPPTG--TVATASTGVAAchiggTTLHAFAGI-----GSG 273
Cdd:TIGR02768 352 RLSEEQYEAVRHVTGSGDIaVVVGRAGTGKSTMLKAAREAWEAAGyrVIGAALSGKAA-----EGLQAESGIesrtlASL 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  274 QAPLAQCVALAHRPGVrqgwlncqrLVIDEISMVEadfFDKLEAVARAVRQqkkpfGGIQLIICGDFLQLPPVTKGSqhp 353
Cdd:TIGR02768 427 EYAWANGRDLLSDKDV---------LVIDEAGMVG---SRQMARVLKEAEE-----AGAKVVLVGDPEQLQPIEAGA--- 486
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  354 rfCFQAKSWRKCvpvTLELTEVWRQAD--QTFISLLKAvrlgrcSDEVTRQLRATAAHkvGRDGIIATRLCTHQDDVALT 431
Cdd:TIGR02768 487 --AFRAIAERIG---YAELETIRRQREawARQASLELA------RGDVEKALAAYRDH--GHITIHDTREEAIEQVVADW 553
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  432 NEKRLKELPG-----------DVHSF-----EAIDSDPELSRTLDAQCPVGRvLQLKLGAQVMLVKNlAVSRGLVNGARG 495
Cdd:TIGR02768 554 KQDLREANPAgsqimlahtrkDVRALneaarEALIERGELGESILFQTARGE-RKFAAGDRIVFLEN-NRDLGVKNGMLG 631
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  496 VVvgfesegrglprvrflcgitEVIRTDRWTVQVTGGQYLS---RQQLPLQLAWAMSIHKSQGMSLDCVeislgRVFASG 572
Cdd:TIGR02768 632 TV--------------------EEIEDGRLVVQLDSGELVIipqAEYDALDHGYATTIHKSQGVTVDRA-----FVLASK 686
                         410
                  ....*....|....*
gi 112984084  573 Q-----AYVALSRAR 582
Cdd:TIGR02768 687 SmdrhlAYVAMTRHR 701
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
533-591 1.64e-09

C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 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: 350173 [Multi-domain]  Cd Length: 89  Bit Score: 55.14  E-value: 1.64e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112984084 533 QYLSRQQLPLQLAWAMSIHKSQGMSLDCVEISLGRVFA--SGQAYVALSRARslQGLRVLD 591
Cdd:cd18786   31 QGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTANSltPRRLYVALTRAR--KRLVIYD 89
AAA_19 pfam13245
AAA domain;
207-346 8.63e-08

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 51.45  E-value: 8.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112984084  207 QAAVLRMVLKGQSIFFTGSAGTGKSYLLKHILGSL-------------PPTGTVA---TASTGVAAchiggTTLHAFAGI 270
Cdd:pfam13245   1 QREAVRTALPSKVVLLTGGPGTGKTTTIRHIVALLvalggvsfpillaAPTGRAAkrlSERTGLPA-----STIHRLLGF 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112984084  271 GSGQAplaqcVALAHRPGvrqGWLNCQRLVIDEISMVEADFFDKL-EAVARavrqqkkpfgGIQLIICGDFLQLPPV 346
Cdd:pfam13245  76 DDLEA-----GGFLRDEE---EPLDGDLLIVDEFSMVDLPLAYRLlKALPD----------GAQLLLVGDPDQLPSV 134
PHA03311 PHA03311
helicase-primase subunit BBLF4; Provisional
547-583 1.12e-04

helicase-primase subunit BBLF4; Provisional


Pssm-ID: 223040  Cd Length: 782  Bit Score: 45.28  E-value: 1.12e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 112984084 547 AMSIHKSQGMSLDCVEISlgrvFASG------QAYVALSRARS 583
Cdd:PHA03311 706 AMTIAKSQGLSLDKVAIC----FGNHknlklsHVYVAMSRVTS 744
Herpes_Helicase pfam02689
Helicase; This family consists of Helicases from the Herpes viruses. Helicases are responsible ...
547-594 2.82e-04

Helicase; This family consists of Helicases from the Herpes viruses. Helicases are responsible for the unwinding of DNA and are essential for replication and completion of the viral life cycle.


Pssm-ID: 280797  Cd Length: 809  Bit Score: 43.93  E-value: 2.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 112984084  547 AMSIHKSQGMSLDCVEISLG--RVFASGQAYVALSRARSLQGLrVLDFDP 594
Cdd:pfam02689 733 AMTIAKSQGLSLDKVAICFGnhPNLKLSHVYVAMSRATDPNHL-VMNVNP 781
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
295-349 3.89e-03

DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to 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: 438708 [Multi-domain]  Cd Length: 121  Bit Score: 37.60  E-value: 3.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 112984084 295 NCQRLVIDEISMVEAdffdkLEAVARAVRQQKkpfggiqLIICGDFLQLPPVTKG 349
Cdd:cd17934   44 NVDVVIIDEASQITE-----PELLIALIRAKK-------VVLVGDPKQLPPVVQE 86
UvrD_C_2 pfam13538
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ...
544-582 6.76e-03

UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold.


Pssm-ID: 463913 [Multi-domain]  Cd Length: 52  Bit Score: 35.24  E-value: 6.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 112984084  544 LAWAMSIHKSQGMSLDCVEISLGRVFASGQA-------YVALSRAR 582
Cdd:pfam13538   1 LAYALTVHKAQGSEFPAVFLVDPDLTAHYHSmlrrrllYTAVTRAR 46
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
216-247 7.69e-03

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 38.25  E-value: 7.69e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 112984084 216 KGQSIFFTGSAGTGKSYLLKHILGSLPPT-GTV 247
Cdd:cd03261   25 RGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEV 57
 
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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