ID UVRC_SHESH Reviewed; 609 AA.
AC A8FW40;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=UvrABC system protein C {ECO:0000255|HAMAP-Rule:MF_00203};
DE Short=Protein UvrC {ECO:0000255|HAMAP-Rule:MF_00203};
DE AltName: Full=Excinuclease ABC subunit C {ECO:0000255|HAMAP-Rule:MF_00203};
GN Name=uvrC {ECO:0000255|HAMAP-Rule:MF_00203}; OrderedLocusNames=Ssed_2454;
OS Shewanella sediminis (strain HAW-EB3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=425104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella sediminis HAW-EB3.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC processing of DNA lesions. UvrC both incises the 5' and 3' sides of the
CC lesion. The N-terminal half is responsible for the 3' incision and the
CC C-terminal half is responsible for the 5' incision. {ECO:0000255|HAMAP-
CC Rule:MF_00203}.
CC -!- SUBUNIT: Interacts with UvrB in an incision complex.
CC {ECO:0000255|HAMAP-Rule:MF_00203}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00203}.
CC -!- SIMILARITY: Belongs to the UvrC family. {ECO:0000255|HAMAP-
CC Rule:MF_00203}.
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DR EMBL; CP000821; ABV37063.1; -; Genomic_DNA.
DR RefSeq; WP_012142798.1; NC_009831.1.
DR AlphaFoldDB; A8FW40; -.
DR SMR; A8FW40; -.
DR STRING; 425104.Ssed_2454; -.
DR KEGG; sse:Ssed_2454; -.
DR eggNOG; COG0322; Bacteria.
DR HOGENOM; CLU_014841_3_0_6; -.
DR OrthoDB; 9804933at2; -.
DR Proteomes; UP000002015; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd10434; GIY-YIG_UvrC_Cho; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.1440.10; GIY-YIG endonuclease; 1.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR Gene3D; 3.30.420.340; UvrC, RNAse H endonuclease domain; 1.
DR HAMAP; MF_00203; UvrC; 1.
DR InterPro; IPR000305; GIY-YIG_endonuc.
DR InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR InterPro; IPR047296; GIY-YIG_UvrC_Cho.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR001943; UVR_dom.
DR InterPro; IPR036876; UVR_dom_sf.
DR InterPro; IPR004791; UvrC.
DR InterPro; IPR001162; UvrC_RNase_H_dom.
DR InterPro; IPR038476; UvrC_RNase_H_dom_sf.
DR NCBIfam; TIGR00194; uvrC; 1.
DR PANTHER; PTHR30562:SF1; UVRABC SYSTEM PROTEIN C; 1.
DR PANTHER; PTHR30562; UVRC/OXIDOREDUCTASE; 1.
DR Pfam; PF01541; GIY-YIG; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF02151; UVR; 1.
DR Pfam; PF08459; UvrC_RNaseH_dom; 1.
DR SMART; SM00465; GIYc; 1.
DR SMART; SM00278; HhH1; 2.
DR SUPFAM; SSF46600; C-terminal UvrC-binding domain of UvrB; 1.
DR SUPFAM; SSF82771; GIY-YIG endonuclease; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR PROSITE; PS50164; GIY_YIG; 1.
DR PROSITE; PS50151; UVR; 1.
DR PROSITE; PS50165; UVRC; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA damage; DNA excision; DNA repair; Excision nuclease;
KW Reference proteome; SOS response.
FT CHAIN 1..609
FT /note="UvrABC system protein C"
FT /id="PRO_1000077842"
FT DOMAIN 16..94
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT DOMAIN 203..238
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ SEQUENCE 609 AA; 68531 MW; F5FBE3B56E84AAC3 CRC64;
MPSTFDSKLF LKTVSSSPGV YRMYDEEGTV IYVGKAKDLK KRLSSYFRVN LPNVKTQALV
SHIANIDVTV THSETDALIL ENDYIKQYMP RYNVLLRDDK SYPYILLSDH KHPRLAYHRG
PKRDKGSYFG PYPNGGAVRE SLHLLQKIFP IRQCDDLYYK SRSRPCLQYQ IGRCSAPCVN
KVSDEEYAVQ VKLASLFLKG KDLQVMTELV SKMEASALAL EYEQAASYRD QIAALRRVAE
QQEVSNTSGD MDVIGAYYAS GVACFHLLFI REGKIFGSRS YYPSVPAETE LDEVLSAFMI
QFYLNSDSQR TVPKEILLSH GFDDLPELER AIQTALEKKV EIKTNVRSER ANFLRLAVTN
ATNAVNTRLS HKNTVEQRFL LLEEALEVST LIQRMECFDI SHTMGESTVA SCVVFDREGP
NKADYRRYNI NGITPGDDYA AMKQAITRRF DKIDKNGKIP DLLFIDGGTG QLRIAQKIVD
EKFVDIDKTP MLIGVAKGEG RKPGLETLIY GENEQSFTIP ADSGALHLIQ HIRDESHRFA
ITGHRNKRQK TRNTSTLESI AGVGPKRRKA LLQYLGGIQE VKGASVAELA KVPGISLEMA
QTIHDSLRG
//
