ID A0A1V3Q319_9GAMM Unreviewed; 686 AA.
AC A0A1V3Q319;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=RecBCD enzyme subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01487};
DE AltName: Full=Exonuclease V subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE Short=ExoV subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
GN Name=recD {ECO:0000256|HAMAP-Rule:MF_01487};
GN ORFNames=B0E48_07310 {ECO:0000313|EMBL:OOG57262.1};
OS Rhodanobacter sp. C03.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1945858 {ECO:0000313|EMBL:OOG57262.1, ECO:0000313|Proteomes:UP000189128};
RN [1] {ECO:0000313|EMBL:OOG57262.1, ECO:0000313|Proteomes:UP000189128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C03 {ECO:0000313|EMBL:OOG57262.1,
RC ECO:0000313|Proteomes:UP000189128};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for
CC recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly
CC rapid and processive ATP-dependent bidirectional helicase activity.
CC Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator)
CC sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the
CC Chi site. The properties and activities of the enzyme are changed at
CC Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and
CC facilitates RecA-binding to the ssDNA for homologous DNA recombination
CC and repair. Holoenzyme degrades any linearized DNA that is unable to
CC undergo homologous recombination. In the holoenzyme this subunit has
CC ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre-
CC assembled RecBC greatly stimulates nuclease activity and augments
CC holoenzyme processivity. Negatively regulates the RecA-loading ability
CC of RecBCD. {ECO:0000256|HAMAP-Rule:MF_01487}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage (in the presence of ATP) in either
CC 5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC phosphooligonucleotides.; EC=3.1.11.5; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01487};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01487}.
CC -!- SIMILARITY: Belongs to the RecD family. {ECO:0000256|HAMAP-
CC Rule:MF_01487}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OOG57262.1}.
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DR EMBL; MUNT01000005; OOG57262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3Q319; -.
DR STRING; 1945858.B0E48_07310; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000189128; Unassembled WGS sequence.
DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR CDD; cd17933; DEXSc_RecD-like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 1.10.10.1020; RecBCD complex, subunit RecD, N-terminal domain; 1.
DR HAMAP; MF_01487; RecD; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006344; RecD.
DR InterPro; IPR049550; RecD_N.
DR InterPro; IPR041851; RecD_N_sf.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR NCBIfam; TIGR01447; recD; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF21185; RecD_N; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01487}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01487};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01487};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01487};
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01487};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01487};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01487}.
FT DOMAIN 10..118
FT /note="RecBCD enzyme subunit RecD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21185"
FT DOMAIN 612..657
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ SEQUENCE 686 AA; 74276 MW; B2E707393649C03F CRC64;
MSHDAVFELL DQAVATQRLR PLDIALARFL AERDGDTAPG LLWLAALLSR QLADGHLCLD
LEALPALADE QDWPSGWRPL LRAITENPAA LSSSPLVADG HSGHPAAAPL VLDGTRLYLR
RYWNHERQVA AAIRVRLTLP QAVPEQLADE LTRLFPTPCR SDFSRDAPGV SQTESIAAEA
APTNSTPDWP KIACALAACG AFTVITGGPG TGKTTTVVRL LGLLQTLQLR QHARPLRIRL
AAPTGKAAAR LNASIAAQIA QLDVDDATRA AIPAEVVTLH RLLGARPDTR RFRHDRGNPL
HLDLLVVDEA SMIDLEMMSA VLAALPPTAR LILLGDKDQL SSVEAGAVLG DLCRRAETGH
YSASTADWLC ETTGSDIRAF VCADAQPLDQ QLAMLRHSHR FGDSSGIGQL ARAVNAGDTD
RVHALLATPS TDLAWLPVSQ RMQLAELAID GGNVHLSVND GSTIHHERAV GYRHYLELLR
RERPASAIDA AAHDHWARDV LQAFNRFQLL CALRQGPHGV EGLNQLIADA LHAQGLIESS
HGWYEGRPIM LTRNDYSLGL ANGDVGICLR LPDERGHLCL SVAFLASATA GSTSSTRIRH
VVPARLGEVA TVYAMTVHKS QGSEFEHTAL VLPTEASNVL TRELLYTGIT RARRWFSLLG
SEAIVDLATR QRTRRYSGLA ERLSSN
//
