(data stored in SCRATCH zone)

SWISSPROT: A1SDB1_NOCSJ

ID   A1SDB1_NOCSJ            Unreviewed;      1113 AA.
AC   A1SDB1;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   10-APR-2019, entry version 70.
DE   RecName: Full=RecBCD enzyme subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE            EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01486};
DE   AltName: Full=Exonuclease V subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE            Short=ExoV subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
DE   AltName: Full=Helicase/nuclease RecBCD subunit RecC {ECO:0000256|HAMAP-Rule:MF_01486};
GN   Name=recC {ECO:0000256|HAMAP-Rule:MF_01486};
GN   OrderedLocusNames=Noca_0251 {ECO:0000313|EMBL:ABL79796.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL79796.1, 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:ABL79796.1, 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 recognizes the wild-
CC       type Chi sequence, and when added to isolated RecB increases its
CC       ATP-dependent helicase processivity. {ECO:0000256|HAMAP-
CC       Rule:MF_01486}.
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_01486};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits
CC       contribute to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01486}.
CC   -!- SIMILARITY: Belongs to the RecC family. {ECO:0000256|HAMAP-
CC       Rule:MF_01486}.
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DR   EMBL; CP000509; ABL79796.1; -; Genomic_DNA.
DR   RefSeq; WP_011753747.1; NC_008699.1.
DR   STRING; 196162.Noca_0251; -.
DR   EnsemblBacteria; ABL79796; ABL79796; Noca_0251.
DR   KEGG; nca:Noca_0251; -.
DR   eggNOG; ENOG4105DSY; Bacteria.
DR   eggNOG; COG1330; LUCA.
DR   HOGENOM; HOG000043415; -.
DR   KO; K03583; -.
DR   OMA; PHIRAVF; -.
DR   OrthoDB; 1320159at2; -.
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   Gene3D; 1.10.10.160; -; 1.
DR   HAMAP; MF_01486; RecC; 1.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006697; RecC.
DR   InterPro; IPR041500; RecC_C.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   Pfam; PF17946; RecC_C; 1.
DR   PIRSF; PIRSF000980; RecC; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR01450; recC; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1SDB1.
DR   SWISS-2DPAGE; A1SDB1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01486,
KW   ECO:0000256|SAAS:SAAS00992480};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000640};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01486};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01486};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01486,
KW   ECO:0000256|SAAS:SAAS00992482};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01486};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01486,
KW   ECO:0000256|SAAS:SAAS00992489, ECO:0000313|EMBL:ABL79796.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01486,
KW   ECO:0000256|SAAS:SAAS00992512, ECO:0000313|EMBL:ABL79796.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01486};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01486,
KW   ECO:0000256|SAAS:SAAS00992504};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640}.
FT   DOMAIN      811   1035       RecC_C. {ECO:0000259|Pfam:PF17946}.
SQ   SEQUENCE   1113 AA;  121323 MW;  8CAC4816CD3D5D23 CRC64;
     MTLQIHRASR TDVLADALGD LLRTPLADPF AEEVVVVPAK GVERWLTQRL SHRLGAGPRG
     DDGVCAGVRF LNPRSLVSLL LGRERDDPWD PERLVWPLLA TIDESLGERE FATLGRHLGH
     GVDGADGELR RNRRYSVALR LAHLFASYAL QRPSLVTAWR EGRDGEHGGE QGLPPDLAWQ
     PELWRRLIAQ VDAPPPDVRH AQTCAALQAG GDGLPLPDRL SLFGHTRIPV TEVALLKALG
     EHRDVHLFLP QPSPVLWDDL ADLGGPGGVV PRAADDSVER VGHPLLASLG RDARELRRLL
     DGVSSEEVRP PAGTPTGSTT DPVTLLGWLQ HDLRANHAPS YDERSTRELD PDDHSLQVHA
     CHGPARQVDV LREVLVGLLE DDPTLEPRDV LVMCPDIETY APLISAGFGL ATTDGHPAHR
     LRVKLADRAL TSTNPLLAVA GDLLDLAGGR VTASDVLDLA GTDPVRRRFG FTDDELDRVS
     RWVARAGVRW GLDEESRAAF RMERFPHNTW RTGLDRILLG VAMSGDDHHH LGRGLPLDDV
     ASSEIDLAGR LAELVARVDR TLTVLAGART VADWATGLRD GVRSLVDVAA DDAWQVPQFE
     RELGRAAASS HEGGLELRLA DVRAMLESRL AGRPTRANFR TGSLTVATMV PMRSVPHRVV
     CLVGLDDGVF PRAGAVDGDD VLGRHPLTGE RDVRSEDRQL LLDAVLAATE HLVITYSGAD
     EQSGASLPPA VPLGEILDAA DRTTNAPVRD RVLTRHPLQP YDARNFTRER PFSFDTAALA
     GARSARGVRR EPPPLLDGPL PPRLALDGRA ADVSLQDLRD FLGHPVRAFL RGRLDVATPF
     EPDDLADAIP VSLDSLEKWQ IGDRLLRQLL AGQDPVAVLT AEQLAGTLPP RGLGTLALHE
     VAEECQRLWS RTADLRDGER RSVDVDVDLR DGRRLTGTVP GVYGSRVVSL GYSRLNARQR
     LHAWVDLLAL SATYPDQHWT AHAVGKDRAG PKRALCGPLD HRAVGWLRDL VDLRDRGLCA
     PLPVPVKTGA AWADAHAREL MGQDHPPVEA ARREWETDPH NQFGITGEDA DPYHQRVYGP
     AAPVEALLDA GLGEHAWAIW EPLLTGGERV GPL
//

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