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Database: UniProt
Entry: A0A119CUM9_THIDE
LinkDB: A0A119CUM9_THIDE
Original site: A0A119CUM9_THIDE 
ID   A0A119CUM9_THIDE        Unreviewed;       579 AA.
AC   A0A119CUM9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=UvrABC system protein C {ECO:0000256|HAMAP-Rule:MF_00203};
DE            Short=Protein UvrC {ECO:0000256|HAMAP-Rule:MF_00203};
DE   AltName: Full=Excinuclease ABC subunit C {ECO:0000256|HAMAP-Rule:MF_00203};
GN   Name=uvrC {ECO:0000256|HAMAP-Rule:MF_00203,
GN   ECO:0000313|EMBL:KVW93437.1};
GN   ORFNames=ABW22_14265 {ECO:0000313|EMBL:KVW93437.1};
OS   Thiobacillus denitrificans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW93437.1, ECO:0000313|Proteomes:UP000064243};
RN   [1] {ECO:0000313|EMBL:KVW93437.1, ECO:0000313|Proteomes:UP000064243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RG {ECO:0000313|EMBL:KVW93437.1,
RC   ECO:0000313|Proteomes:UP000064243};
RX   PubMed=26712544;
RA   Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA   van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT   "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT   Chemoautotroph.";
RL   Appl. Environ. Microbiol. 82:1486-1495(2015).
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:0000256|HAMAP-
CC       Rule:MF_00203}.
CC   -!- SUBUNIT: Interacts with UvrB in an incision complex.
CC       {ECO:0000256|HAMAP-Rule:MF_00203}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00203}.
CC   -!- SIMILARITY: Belongs to the UvrC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00203}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KVW93437.1}.
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DR   EMBL; LDUG01000048; KVW93437.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A119CUM9; -.
DR   STRING; 1123392.GCA_000376425_01447; -.
DR   PATRIC; fig|36861.3.peg.2671; -.
DR   eggNOG; COG0322; Bacteria.
DR   Proteomes; UP000064243; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00203};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00203};
KW   DNA excision {ECO:0000256|ARBA:ARBA00022769, ECO:0000256|HAMAP-
KW   Rule:MF_00203};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00203};
KW   Excision nuclease {ECO:0000256|ARBA:ARBA00022881, ECO:0000256|HAMAP-
KW   Rule:MF_00203}; Reference proteome {ECO:0000313|Proteomes:UP000064243};
KW   SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW   Rule:MF_00203}.
FT   DOMAIN          1..72
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000259|PROSITE:PS50164"
FT   DOMAIN          181..216
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   DOMAIN          233..454
FT                   /note="UvrC family homology region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50165"
SQ   SEQUENCE   579 AA;  63830 MW;  FE847A90CBF0AF1E CRC64;
     MIDAAGAVLY IGKAKDLKKR VTSYFQKTDQ SPRIRLMLKS VDHIDTTVTR TEAEALLLEN
     NLIKGLKPRF NILFRDDKSY PYLLLTGHRF PRLAYFRGTP KKHDQTFGPY PNSYAVRESI
     QLLQKVFQLR TCEDTVFANR SRPCLLHQIK RCSAPCVKLI TPEAYARDVG AAAQLLHGEA
     SALTELITEQ MNAAAKNLNF ETAAHLRDRL RMLATVREKQ FVDTTGGEAD ADVVAVAEAG
     GVIAVNLTMI RGGRHLGDRS FFPQHGEGAT PAEALEAFIG QHYLEHPIPA RILISETIET
     DALEALLTEQ AGKKVTLLHR VTGERKVWIG MAQANARLSA ARRSADRANQ SQRLAALRDT
     LDLPTLNRIE CFDISHTMGE ATVASCVVYE GDDLKKSDYR RYNISGITPG DDYAAMRAAL
     TKRFHKSIEE NGVLPDLLLI DGGKGQISSA VEAMTELGLG DVLLLGVAKG EARKPGLETL
     IFADGRELKL AKDHPGFHLI QQVRDEAHRF AITGHRAKRG KARVQSTLED IAGIGPKRRK
     QLLEHFGGLQ GVRDAGVDAL ATVNGISREL AETLYNALH
//
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