ID A0A1E7RMA5_9GAMM Unreviewed; 623 AA.
AC A0A1E7RMA5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=BIY45_12030 {ECO:0000313|EMBL:OEZ00338.1};
OS Stenotrophomonas sp. BIIR7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=1904462 {ECO:0000313|EMBL:OEZ00338.1, ECO:0000313|Proteomes:UP000175905};
RN [1] {ECO:0000313|EMBL:OEZ00338.1, ECO:0000313|Proteomes:UP000175905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIIR7 {ECO:0000313|EMBL:OEZ00338.1,
RC ECO:0000313|Proteomes:UP000175905};
RA Sanchez-Castro I., Ruiz-Fresneda M.A., Bakkali M., Kampfer P., Busse H.J.,
RA Lopez-Fernandez M., Martinez-Rodriguez P., Merroun M.L.;
RT "Stenotrophomonas bentonitica sp. nov., isolated from bentonite
RT formations.";
RL Submitted (SEP-2016) 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:OEZ00338.1}.
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DR EMBL; MKCZ01000052; OEZ00338.1; -; Genomic_DNA.
DR RefSeq; WP_070208305.1; NZ_MKCZ01000052.1.
DR AlphaFoldDB; A0A1E7RMA5; -.
DR STRING; 1904462.BIY45_12030; -.
DR GeneID; 84662376; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000175905; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006344; RecD.
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; PF13538; UvrD_C_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000175905}.
FT DOMAIN 165..325
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 173..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ SEQUENCE 623 AA; 66479 MW; EDD2822585E2EFA3 CRC64;
MSLLAALLQQ GTLRTLDHAL AQSLRRLQPD TPDAVLAAAA LASLAVAQGH AGLDPQQPRR
LVDADLDWPL PGDWIAQLRA SPWVDTPARD DHAAADAPLV LEHGLLYLRR YREYERRLAL
GLQRIASQPL PAHDPAALAP LFAQLFPQAL EGIDHQARAA AVALRHPLVL VTGGPGTGKT
TTIARLLVLL AAQAQQADAA LPRVALAAPT GRAAERMAES LRLALQRLRL VGVAAELAEA
LPTTGATLHR LLGVIPDSPR FRHHADNPLP FDVVVVDEAS MIDLPLMTKL VEAVANGTRL
ILLGDPDQLP SVEAGDVLSA VLQASGDGLG TQADDAAALR PLLAPAALQP LAAPLPFAGR
RVQLQRGYRQ SDALDLAPLA AAVRVGDSAR ALELLRHGQL AGVHFHEDQV DPLQQHRQTL
LAHWRGLGEA ADPAQALAQA GQLRLLTALR EGPQGARGLN ERIEAALAGS ARPGGGPRYF
HGRLLLITEN SYRHRLFNGD IGLCLRSSEG AVLAWFPGDS PEHPRAFHPA ALPAHESAFA
MTVHKAQGSE FDEVWLQLPR RDNRVLSREL VYTGMTRARR ALHVLGSAEV VQEALARHAS
RLSGLAVRLG AGSKAPTQGD LFG
//
