ID Q7MIA4_VIBVY Unreviewed; 704 AA.
AC Q7MIA4;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 109.
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 OrderedLocusNames=VV2613 {ECO:0000313|EMBL:BAC95377.1};
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC95377.1, ECO:0000313|Proteomes:UP000002675};
RN [1] {ECO:0000313|EMBL:BAC95377.1, ECO:0000313|Proteomes:UP000002675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016 {ECO:0000313|EMBL:BAC95377.1,
RC ECO:0000313|Proteomes:UP000002675};
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.Y., Wu K.M., Chang Y.C., Chang C.H., Tsai H.C., Liao T.L., Liu Y.M.,
RA Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T., Hor L.I.,
RA Tsai S.F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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; BA000037; BAC95377.1; -; Genomic_DNA.
DR RefSeq; WP_011151005.1; NC_005139.1.
DR AlphaFoldDB; Q7MIA4; -.
DR STRING; 672.VV93_v1c23280; -.
DR KEGG; vvy:VV2613; -.
DR PATRIC; fig|196600.6.peg.2615; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_1_2_6; -.
DR Proteomes; UP000002675; Chromosome I.
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; IPR041451; RecD-like_SH13.
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; PF18335; SH3_13; 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 14..123
FT /note="RecBCD enzyme subunit RecD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21185"
FT DOMAIN 549..610
FT /note="RecD-like DNA helicase SH3"
FT /evidence="ECO:0000259|Pfam:PF18335"
FT DOMAIN 631..678
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13538"
FT BINDING 254..261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ SEQUENCE 704 AA; 77138 MW; D63C9F7AFA62FA91 CRC64;
MMLNGSLQAT LSMLEQQAQQ GYLRLLDYQF ARFIGEQSQH SGLALLAAAV SAELGKGHIC
LPLLDELGQV CELASKIGLF GEAATELNAQ LQLIDWRALL QTSGLVGTQG EAVPLMFDGE
RVYLHRYWHY EVVLAQKLNQ LSHGIELNAS SAASLSALLD RLFARDYRFL FETLIAAQAS
GSTQVQRQQW VCDFLDVVEE HRLDWTAIEQ VLSQVSKVSD LNALDHLVPH AACINWQKVA
AAVALTRRFA VISGGPGTGK TTTVTKLLAA LIEQAGAQTP TIRLVAPTGK AAARLTESIG
KAVQSLAVEP SLKALIPTEA STLHRLLGAI PGSAEFRHHS QNPLHLDVLV VDEASMVDLS
MMYKVIDALP KHARLILLGD KDQLASVEAG AVLGDICAFS ASGYSAEQAA TLAKLTGYQA
LPKSASRLAP VADSLCMLQK SYRFDARSGI GQLAKAINAG SVAALESVWQ REFSDIARHP
LDASHYNHML QTLVSEYSHY LARIALTQQH LEPKERESSA ERAKAGLNLF HRCRLLCAVR
EGNFGVAGLN LRIERALAAR NLIKVKDEIW YHGRPVMVTR NDYALGLYNG DIGICMWDDT
DEDPRLKVYF ELADGSVKAV LPSRVPEHET AYAMTIHKSQ GSEFDFTLMI LPADFSPILT
RELIYTGITR AKKRLALYAD LQVLKRGMKI KTQRASGLPH RLGQ
//
