ID A0A1H0N9F1_9MICC Unreviewed; 668 AA.
AC A0A1H0N9F1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN04487914_10112 {ECO:0000313|EMBL:SDO89291.1};
OS Arthrobacter sp. ok909.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1761746 {ECO:0000313|EMBL:SDO89291.1, ECO:0000313|Proteomes:UP000199538};
RN [1] {ECO:0000313|EMBL:SDO89291.1, ECO:0000313|Proteomes:UP000199538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK909 {ECO:0000313|EMBL:SDO89291.1,
RC ECO:0000313|Proteomes:UP000199538};
RA de Groot N.N.;
RL Submitted (OCT-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; FNJS01000001; SDO89291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0N9F1; -.
DR STRING; 1761746.SAMN04487914_10112; -.
DR Proteomes; UP000199538; 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}; SOS response {ECO:0000256|HAMAP-Rule:MF_00203}.
FT DOMAIN 16..95
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT DOMAIN 207..242
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 258..526
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
SQ SEQUENCE 668 AA; 73143 MW; 91E18466648D57DA CRC64;
MADPASYRPQ TGEIPTNPGV YRFRDPHGRV IYVGKAKNLR SRLNSYFANP AGLMPKTYAM
VHTASSVEWT VVGSELESLQ LEYTWIKEFT PRFNVMFRDD KSYPYLAVTM GEKYPRVQVL
RGDRRKGTRY FGPYTAGAIR DTMDTLLRVF PVRSCSAGVL KRAEASGRPC LLGYIDKCSA
PCVGRISAED HRALAEDFCS FMGGEAKPFV NRLEREMAAA VAELDYERAA RLRDDIVAMK
KVFERNAVVL AEGTDADVFA LHEDELEAAV QVFHVRGGRI RGQRGWVVEK VEDSTTPELV
EHLLQQVYGE EAGVQGRLPR EVLVPAEPSN AAELAQWLSG LRGARVDIRV PQRGDKAALM
STVRDNAEHA LKLHKSRRAG DLTMRSQALQ ELQEALDLPV ALLRIECFDI SHVQGTNVVG
SMVVVEDGLP KKSDYRKFAV TGAAATDDTA AMHDVLTRRF RHYLDEKREQ AAAAAKPAHQ
AALEAATAAA VADSTTPAPR SKFAYPPNLV VVDGGKPQVN AAARALAELG IEDVYVVGLA
KRLEEVWLPD SDFPVILPRA SAGLYLLQRI RDEAHRFAIS FHRQKRGKAM TVSALDGVPG
LGESKRKALL AEFGSVKGIK AATQEELTGA KGIGPSLAAA IVRHFTADGE EAATVPAINM
TTGEILET
//