ID A0A1N6S925_9ACTN Unreviewed; 668 AA.
AC A0A1N6S925;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN05444858_102153 {ECO:0000313|EMBL:SIQ37581.1};
OS Micromonospora avicenniae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1198245 {ECO:0000313|EMBL:SIQ37581.1, ECO:0000313|Proteomes:UP000186004};
RN [1] {ECO:0000313|EMBL:SIQ37581.1, ECO:0000313|Proteomes:UP000186004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45758 {ECO:0000313|EMBL:SIQ37581.1,
RC ECO:0000313|Proteomes:UP000186004};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTNF01000002; SIQ37581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6S925; -.
DR STRING; 1198245.SAMN05444858_102153; -.
DR Proteomes; UP000186004; 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:UP000186004};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00203}.
FT DOMAIN 24..103
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT DOMAIN 216..251
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 267..538
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 74137 MW; DB65D35B9949F380 CRC64;
MPRTTLAGVA DPSTYRPAPG TIPESPGVYR FRDGTGRVIY VGKAKNLRSR LNSYFGDLWN
LHDRTRQMVT TAESVDWITV GTEVEALQQE FTWIKQYDPR FNVRYRDDKS YPYLAVTLDE
EYPRLQVMRG AKRKGVRYFG PYSHAWAIRE TLDLLLRVFP ARTCSAGVFK RAGQVGRPCL
LGYIGKCSAP CVGTVSAEQH RAIVDGFCDF MAGRTDTMVR KLEREMADAS EQLEFERAAR
VRDDIAALRR AMEKQTVVLG DGTDADVVAF ADDPLEAAVQ VFHVRDGRVR GQRGWVVEKT
EELTTGDLVH HFCTQVYGGE HGEADVPREL LVPELPGDAD ALADWLSSHR GSRVVLRVPQ
RGDKRALMET VERNAKDALA RHKLRRAGDL TTRSKALDEI SEALGMRTSP LRIECFDISQ
IQGTDVVASM VVFEDGLPRK SEYRRFIIRG ATDDLSAMSE VLRRRFARYL DSRAETGEAG
VESADDLEVP GDSAGVDEPR VGALVDPTTG RPRKFAYPPQ LVVVDGGPPQ VAAAAQALAE
LGIDDVALCG LAKRLEEVWL PDDEFPVVLP RSSEALYLLQ RVRDEAHRFA ITFHRQRRSK
RMTQSALDSV PGLGEVRRKA LLRHFGSLKR LSAATVEEIT EVPGVGRRTA EAILTALGGE
SAKASSTD
//
