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Database: UniProt
Entry: A0A1C6RF69_9ACTN
LinkDB: A0A1C6RF69_9ACTN
Original site: A0A1C6RF69_9ACTN 
ID   A0A1C6RF69_9ACTN        Unreviewed;       685 AA.
AC   A0A1C6RF69;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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   ORFNames=GA0070616_0780 {ECO:0000313|EMBL:SCL15616.1};
OS   Micromonospora nigra.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=145857 {ECO:0000313|EMBL:SCL15616.1, ECO:0000313|Proteomes:UP000199699};
RN   [1] {ECO:0000313|EMBL:SCL15616.1, ECO:0000313|Proteomes:UP000199699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43818 {ECO:0000313|EMBL:SCL15616.1,
RC   ECO:0000313|Proteomes:UP000199699};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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: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}.
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DR   EMBL; FMHT01000003; SCL15616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6RF69; -.
DR   STRING; 145857.GA0070616_0780; -.
DR   OrthoDB; 9804933at2; -.
DR   Proteomes; UP000199699; 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:UP000199699};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00203}.
FT   DOMAIN          16..95
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000259|PROSITE:PS50164"
FT   DOMAIN          208..243
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   DOMAIN          259..533
FT                   /note="UvrC family homology region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50165"
FT   REGION          472..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   685 AA;  75621 MW;  F273C934456B036F CRC64;
     MADPSTYRPA SGTIPESPGV YRFRDGTGRV IYVGKAKNLR SRLNSYFADP WGLHQRTQQM
     VTTAESVDWV TVGTEVEALQ LEYTWIKQYD PRFNVRYRDD KSYPYLAVTL DEDYPRLQVM
     RGAKRKGVRY FGPYSHAWAI RETLDLLLRV FPARTCSAGV FKRAGQVGRP CLLGYIGKCS
     APCVGSVSAE RHREIVDDFC DFMAGRTDSM VRKLEREMLQ ASEQLEFERA ARLRDDVAAL
     RRAMEKQTVV LGDGTDADVV AFADDPLEAS VQVFRVRDGR VRGQRGWVVE KTEELTTGDL
     VHHFCTQVYG GEHGEADVPR ELLVPELPAD ADALADWLSG RRGSRVSLRV PQRGDKRALL
     ETVERNAKDA LARHKLKRAG DLTTRGKALD EITEALGMRT APLRIECFDI SQIQGTDVVA
     SMVVFEDGLP RKGEYRRFII RGATDDLSAM SEVLRRRFAR YLDARAETGE AGVEAADDLD
     APSRGGPEAG ADEPRVGVLV DPTTGRPRKF AYPPQLVVVD GGAPQVAAAA QALAELGIDD
     VALCGLAKRL EEVWLPDDDF PVILPRASEG LYLLQRVRDE AHRFAITFHR QRRSKRMTTS
     ALDDVPGLGE MRRKALLRHF GSLKRLSAAT VEEITEVPGV GRRTAEAILA ALDTDSTPAD
     PATPADSATP ATPANPVIPA PPAGE
//
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