(data stored in ACNUC1104 zone)

SWISSPROT: A1SDB3_NOCSJ

ID   A1SDB3_NOCSJ            Unreviewed;       584 AA.
AC   A1SDB3;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 76.
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=Noca_0253 {ECO:0000313|EMBL:ABL79798.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL79798.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL79798.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C.,
RA   Copeland A., Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A.,
RA   Hammon N.M., Han S., Hauser L.J., Israni S., Kim E., Kyrpides N.,
RA   Land M.L., Lapidus A., Larimer F.W., Lucas S., Pitluck S.,
RA   Richardson P., Schmutz J., Tapia R., Thompson S., Tice H.N.,
RA   Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing
RT   actinomycete Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
CC   -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for
CC       recombinational DNA repair. Binds to DSBs and unwinds DNA via a
CC       highly rapid and processive ATP-dependent bidirectional helicase
CC       activity. Unwinds dsDNA until it encounters a Chi (crossover
CC       hotspot instigator) sequence from the 3' direction. Cuts ssDNA a
CC       few nucleotides 3' to the Chi site. The properties and activities
CC       of the enzyme are changed at Chi. The Chi-altered holoenzyme
CC       produces a long 3'-ssDNA overhang and facilitates RecA-binding to
CC       the ssDNA for homologous DNA recombination and repair. Holoenzyme
CC       degrades any linearized DNA that is unable to undergo homologous
CC       recombination. In the holoenzyme this subunit has ssDNA-dependent
CC       ATPase and 5'-3' helicase activity. When added to pre-assembled
CC       RecBC greatly stimulates nuclease activity and augments holoenzyme
CC       processivity. Negatively regulates the RecA-loading ability of
CC       RecBCD. {ECO:0000256|HAMAP-Rule:MF_01487}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage (in the presence of ATP) in
CC         either 5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC         phosphooligonucleotides.; EC=3.1.11.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01487};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits
CC       contribute 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; CP000509; ABL79798.1; -; Genomic_DNA.
DR   RefSeq; WP_011753749.1; NC_008699.1.
DR   STRING; 196162.Noca_0253; -.
DR   EnsemblBacteria; ABL79798; ABL79798; Noca_0253.
DR   KEGG; nca:Noca_0253; -.
DR   eggNOG; ENOG4107UQ3; Bacteria.
DR   eggNOG; ENOG410YQWW; LUCA.
DR   HOGENOM; HOG000258341; -.
DR   KO; K03581; -.
DR   OMA; MIDLEMM; -.
DR   OrthoDB; 961809at2; -.
DR   Proteomes; UP000000640; Chromosome.
DR   GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; 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   HAMAP; MF_01487; RecD; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006344; RecD.
DR   InterPro; IPR027785; UvrD-like_helicase_C.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01447; recD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1SDB3.
DR   SWISS-2DPAGE; A1SDB3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000640};
KW   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   ECO:0000313|EMBL:ABL79798.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01487,
KW   ECO:0000313|EMBL:ABL79798.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640}.
FT   DOMAIN      167    369       AAA. {ECO:0000259|SMART:SM00382}.
FT   NP_BIND     175    182       ATP. {ECO:0000256|HAMAP-Rule:MF_01487}.
SQ   SEQUENCE   584 AA;  63397 MW;  CE19912DDF35C425 CRC64;
     MTELFEPVDE HDWRIATGAT GLLATFNAAG VLTSSDVHVA TRIGVLGGET DERMLLAVAL
     TVRAVRRGSV CLDLAGVAAT APDLPWPDEW PVAGSPLVHA GVVRWDHELL YLDRYHRLER
     QVHDDLAARL ALAPPAVDEQ RLEAALARLG GGHFSEEQRA AVVAAVRRRT TILTGGPGTG
     KTTTVARLLA LLADQAAGRG SRLSIALAAP TGKAATRLQE AVVTELAAVA TAWPEAPALV
     GRLDGLTLHR LLGWRPDNAT RFRHDRANRL KYDVVVVDES SMVELTMMGR LLEALRPDSR
     LVLVGDPQQL TSVGAGAVLS DLVAGYEGRP DSPVAALSTN FRSEEDIKSL AAALRSGDAD
     EVIAVLRAPS EQVSWVETSD AAEVEAALRP DSLASARAVW AAARDEDAER ALAELDRYRL
     LCAHREGLYG VRRWNHLVER WLAEDPDVEI YDEWYVGRPL LVTSNDYALD VYNGESGVVV
     RQDQRRRVFV AGSERLKEFA PGRLEAVETM HAMTIHKSQG SQADRVSVLL PDEGSRLLTL
     ELFYTAITRA RHHVRVVGSE AAVRAAVDTR AQRATGLRAR LADG
//

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