(data stored in ACNUC7421 zone)

SWISSPROT: C1ARQ0_RHOOB

ID   C1ARQ0_RHOOB            Unreviewed;       846 AA.
AC   C1ARQ0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 62.
DE   RecName: Full=UvrABC system protein A {ECO:0000256|SAAS:SAAS00385002};
GN   OrderedLocusNames=ROP_04800 {ECO:0000313|EMBL:BAH48727.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48727.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48727.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48727.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC       processing of DNA lesions. UvrA is an ATPase and a DNA-binding
CC       protein. A damage recognition complex composed of 2 UvrA and 2
CC       UvrB subunits scans DNA for abnormalities. When the presence of a
CC       lesion has been verified by UvrB, the UvrA molecules dissociate.
CC       {ECO:0000256|SAAS:SAAS00571360}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC       lesions. {ECO:0000256|SAAS:SAAS00571359}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00385027}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA
CC       family. {ECO:0000256|SAAS:SAAS00571366}.
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DR   EMBL; AP011115; BAH48727.1; -; Genomic_DNA.
DR   RefSeq; WP_012687734.1; NC_012522.1.
DR   STRING; 632772.ROP_04800; -.
DR   EnsemblBacteria; BAH48727; BAH48727; ROP_04800.
DR   KEGG; rop:ROP_04800; -.
DR   PATRIC; fig|632772.20.peg.533; -.
DR   eggNOG; ENOG4105C5U; Bacteria.
DR   eggNOG; COG0178; LUCA.
DR   HOGENOM; HOG000050449; -.
DR   KO; K03701; -.
DR   OMA; GAWQGKN; -.
DR   OrthoDB; POG091H00GY; -.
DR   BioCyc; ROPA632772:GH0Q-479-MONOMER; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0009381; F:excinuclease ABC activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004602; UvrA.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 4.
DR   TIGRFAMs; TIGR00630; uvra; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1ARQ0.
DR   SWISS-2DPAGE; C1ARQ0.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434,
KW   ECO:0000256|SAAS:SAAS00089089};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00089055};
KW   DNA damage {ECO:0000256|SAAS:SAAS00088992};
KW   DNA excision {ECO:0000256|SAAS:SAAS00088971};
KW   DNA repair {ECO:0000256|SAAS:SAAS00461409};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00088984};
KW   Excision nuclease {ECO:0000256|SAAS:SAAS00089033};
KW   Heme {ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00433,
KW   ECO:0000256|SAAS:SAAS00088968};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434,
KW   ECO:0000256|SAAS:SAAS00089112};
KW   Repeat {ECO:0000256|SAAS:SAAS00088976};
KW   Zinc {ECO:0000256|SAAS:SAAS00089006};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS00088978}.
FT   DOMAIN      138    283       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
FT   DOMAIN      487    832       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   NP_BIND     520    527       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00434}.
SQ   SEQUENCE   846 AA;  89687 MW;  31F876A69A4D769F CRC64;
     MPTPDPGPPA EPSPAREFAG IEVFDASEHN LAHVDVFIPR DCIVAFTGVS GSGKSSLAFG
     TIYAEAQRRF LESVTPYARR LMDQVGAPRV GDITGLPPAV ALQQARGHTS ARSSVGTLTH
     ISNVLRMLFS RAGTYPPDAA ELDSNAFSPN TPEGGCPTCH GLGRTHDVDV DALVPDPSRS
     IRDGAVAAWP GAWLGKNYRD ILDTLGIDVD RPWSELPAHQ REWILTTDEQ PTVTVSPIRD
     PGKMVRDYQG TFSSARTYVL HTFATTKSAT QRAKVSRYLL SRPCSACDGK RLRPEALAVR
     FAGLDIADAT ALPMSELATA LDAAVGSRDA AADDATDRAS EALVDNLLGR LRGLSELGLG
     YLSLGRSTTT LSPGELQRLR LATQLQSGLF GVLYVLDEPS AGLHPADTEA LVAAVRRLRA
     AGNSVFVIEH NLDIVRAADW IVDVGPDAGE HGGRVLYSGT VDGLAETPES VTRRYLFEPR
     EHRPEPAQPS RWIELSGITM HNLRDLTVRI PLGVLTAVTG VSGSGKSTLV SRVLTDVVAQ
     HLGVDDEPGP DTVGDDADST AVLADGRDTT ASTVVSSHGL GHIDRLVRVD QTPIGRTPRS
     NLATYTGLFD VIRKLFAAHP TARERGYSPG RFSFNVTGGR CDECEGAGAI TIGMLFLPEA
     SAPCPVCAGA RYNTETLEIL VDGRSIADVL AMTADEAGDF LNHVPAAKKS LDMLVEVGLG
     YLRLGQSATT LSGGEAQRVK LASELQRIRS GHTLYVLDEP TTGLHPADVD RLMVVLRRLV
     AAKNTVVLVE HDMSVIAAAD WMIDLGPGGG DNGGRVIASG QPVTVAATAD SATAAHLGRH
     LAPANG
//

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