(data stored in SCRATCH zone)

SWISSPROT: C1AT14_RHOOB

ID   C1AT14_RHOOB            Unreviewed;       997 AA.
AC   C1AT14;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 67.
DE   RecName: Full=UvrABC system protein A {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00385002};
DE            Short=UvrA protein {ECO:0000256|HAMAP-Rule:MF_00205};
DE   AltName: Full=Excinuclease ABC subunit A {ECO:0000256|HAMAP-Rule:MF_00205};
GN   Name=uvrA {ECO:0000256|HAMAP-Rule:MF_00205,
GN   ECO:0000313|EMBL:BAH48946.1};
GN   OrderedLocusNames=ROP_06990 {ECO:0000313|EMBL:BAH48946.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48946.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48946.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48946.1,
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|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00571360}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC       lesions. {ECO:0000256|HAMAP-Rule:MF_00205,
CC       ECO:0000256|SAAS:SAAS00571359}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00205,
CC       ECO:0000256|SAAS:SAAS00385027}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA
CC       family. {ECO:0000256|HAMAP-Rule:MF_00205,
CC       ECO:0000256|SAAS:SAAS00571366}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00205}.
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DR   EMBL; AP011115; BAH48946.1; -; Genomic_DNA.
DR   STRING; 632772.ROP_06990; -.
DR   EnsemblBacteria; BAH48946; BAH48946; ROP_06990.
DR   KEGG; rop:ROP_06990; -.
DR   PATRIC; fig|632772.20.peg.760; -.
DR   eggNOG; ENOG4105C5U; Bacteria.
DR   eggNOG; COG0178; LUCA.
DR   HOGENOM; HOG000050448; -.
DR   KO; K03701; -.
DR   OMA; VIEMNFL; -.
DR   OrthoDB; POG091H00GY; -.
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-HAMAP.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00205; UvrA; 1.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004602; UvrA.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SUPFAM; SSF52540; SSF52540; 3.
DR   TIGRFAMs; TIGR00630; uvra; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1AT14.
DR   SWISS-2DPAGE; C1AT14.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|PROSITE-
KW   ProRule:PRU00434, ECO:0000256|SAAS:SAAS00089089};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00089055};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00088992};
KW   DNA excision {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00088971};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00461409};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00088984};
KW   Excision nuclease {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00089033};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00088968};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|PROSITE-ProRule:PRU00434, ECO:0000256|SAAS:SAAS00089112};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00088976};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00205};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00089006};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00205,
KW   ECO:0000256|SAAS:SAAS00088978}.
FT   DOMAIN      619    947       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   NP_BIND      32     39       ATP. {ECO:0000256|HAMAP-Rule:MF_00205}.
FT   NP_BIND     651    658       ATP. {ECO:0000256|HAMAP-Rule:MF_00205,
FT                                ECO:0000256|PROSITE-ProRule:PRU00434}.
FT   ZN_FING     750    776       C4-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00205}.
SQ   SEQUENCE   997 AA;  109044 MW;  F55D81771B88C95D CRC64;
     MADRLIVRGA REHNLRGVDL DLPRDSLIVF TGLSGSGKSS LAFDTIFAEG QRRYVESLSA
     YARQFLGQMD KPDVDFIEGL SPAVSIDQKS TNRNPRSTVG TITEVYDYLR LLYARAGTAH
     CPVCGEQIAR QTPQQIVDQV LEMEEGTRFQ VLAPVVRTRK GEFVDLFDQL NMQGYSRVRV
     DGVVYPLSEP PKLKKQEKHD IEVVVDRLTV KAGSKQRLTD SVETALRLAE GIVVLDFVDR
     EENAADRERR FSEKLACPNG HALSIDDLEP RSFSFNSPYG ACPECTGLGI RKEVDPDLVV
     PDPELSLGDG AIAPWSMGQS SEYFGRLLSG LGDILGFDMK TPWNKLPAKA RRAILEGSEE
     QVHVRYKNRY GRTRSYYAEF EGVMPFLHRR LEQTESDQMK ERYDGYMRDT PCPACGGARL
     RPEILSVTIA NEKFGMKSIA EVCELSISDC ADFLNSLTLG SREEAIAGQV LKEVQARLGF
     LLDVGLEYLS LARAAGTLSG GEAQRIRLAT QIGSGLVGVL YVLDEPSIGL HQRDNRRLIE
     TLTRLRDLGN TLIVVEHDED TIRTSDWVVD IGPLAGEHGG KVVHSGPYQE LLDCEESLTG
     AYLSGRSHIE IPAIRRPVDR KRQVTVVGAR EHNLGGIDVS FPLGVLTSVT GVSGSGKSTL
     VNDILATVMA NKLNGARQVP GRHTRINGLD QLDKLVQVDQ SPIGRTPRSN AATYTGVFDK
     IRTLFAATTE SKVRGYQPGR FSFNVKGGRC EACSGDGTLK IEMNFLPDVY VPCEVCHGAR
     YNRETLEVHY KGKTIAEVLD MPIEEAAEFF EPITSIHRYL KTLVEVGLGY VRLGQPAPTL
     SGGEAQRVKL AAELQKRSTG RTVYILDEPT TGLHFEDIRK LLGVVNGLVD KGNTVIVIEH
     NLDVIKTSDW VVDMGPEGGS GGGTVVAQGT PEDVAQVPES YTGRFLENVL AVPAPVAAKP
     KAAKSSPTRK SASAKKTAAA TAATPRKRAP KKAAAVS
//

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