ID A0A411PDN0_9GAMM Unreviewed; 706 AA.
AC A0A411PDN0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ECO:0000313|EMBL:QBF81631.1};
GN ORFNames=EXU30_02185 {ECO:0000313|EMBL:QBF81631.1};
OS Shewanella maritima.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=2520507 {ECO:0000313|EMBL:QBF81631.1, ECO:0000313|Proteomes:UP000291106};
RN [1] {ECO:0000313|EMBL:QBF81631.1, ECO:0000313|Proteomes:UP000291106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D4-2 {ECO:0000313|EMBL:QBF81631.1,
RC ECO:0000313|Proteomes:UP000291106};
RA Baek K.;
RT "Shewanella sp. D4-2 isolated from Dokdo Island.";
RL Submitted (FEB-2019) 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}.
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DR EMBL; CP036200; QBF81631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411PDN0; -.
DR KEGG; smai:EXU30_02185; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000291106; Chromosome.
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; 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 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, ECO:0000313|EMBL:QBF81631.1};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01487}.
FT DOMAIN 629..676
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 202..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ SEQUENCE 706 AA; 77924 MW; D37B5A17088B6A32 CRC64;
MLVTQAPIKQ LLQHWQQQGL LTPLDRHFAL ELTRLQSRNE EVDADTQQQQ ESLQLLICAL
LSQRLSSQHT CLVINSINLE NPLGENLFSA STNTPSCQIS VNHQQLEQLI SEFSFVGQSG
DNKPLILELG RLYLNKYHYF ETQVAAKLLA LSQSHFQLDI ASTRRDLDIL FPVDSSSPTQ
GFNWQKIATA TALTQALAVI TGGPGTGKTT TVTKLLLLLL SQQSLTMKLV APTGKAAARL
TESIKGSKAR LKGKLGDNQR LIDALNAIPE EASTLHRLLG VIPHSHRFRH HADNPLRLDL
LVIDEASMVD LPMMHKIVSA LPANARLILL GDQDQLASVE AGAVLADICL GLRNTQVNQS
FNGESQGQIN DAWAMRYSAN QAKLIAELTG EDVSQYQVAQ QNSFGDSLCM LRHSHRFVGD
AGIGKLATAV NQADVRQIRQ VIRRNYPELV WFQHQINDAN AIAASDNAGK SELLEFACSA
YQPYLDMIGH NQNVFSSLAL SEGATDQAVN EHAANEQPAI YTSEQIIDSY NQFRLLCAMR
SGQYGVDGIN ASMTLALQQK QLLKPQQEFY LGRPIIIQSN DYNLGLFNGD IGLILQDDAN
PSRLMAHFIQ ADGSILKVLP ARLPKHDTCF AMTVHKSQGS EFDCVAFVLP AMPTTSQWQL
LTKELVYTAI TRAKSYFYCL GTAKVFERAS TNITLRSSGL GERLWG
//
