ID A0A3M2M042_9ACTN Unreviewed; 717 AA.
AC A0A3M2M042;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:RMI42937.1};
GN ORFNames=EBO15_18115 {ECO:0000313|EMBL:RMI42937.1};
OS Actinomadura harenae.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2483351 {ECO:0000313|EMBL:RMI42937.1, ECO:0000313|Proteomes:UP000282674};
RN [1] {ECO:0000313|EMBL:RMI42937.1, ECO:0000313|Proteomes:UP000282674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-Ht49 {ECO:0000313|EMBL:RMI42937.1,
RC ECO:0000313|Proteomes:UP000282674};
RA Hu J.;
RT "Isolation from soil.";
RL Submitted (OCT-2018) 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}.
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:RMI42937.1}.
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DR EMBL; RFFG01000029; RMI42937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2M042; -.
DR OrthoDB; 9804933at2; -.
DR Proteomes; UP000282674; 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 208..243
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 259..529
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
FT REGION 470..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 717 AA; 79560 MW; ED4B6818FC359876 CRC64;
MADPATYRPA PGTIPDEPGV YRFRDEHGRV IYVGKAKNLR SRLSSYFADF ATLHPRTQTM
VSTASRVDWT VVSTEVEALQ LEYSWIKEFD PRFNVKYRDD KSYPYLAVTL NEEFPRVQVM
RGAKRKGVRY FGPYSHAWAI RETVDQLLRV FPVRTCSAGV FKRQHQLDRP CLLGYIDKCS
APCVGRVTPE EHRDLAADFC DFMAGNTGRY IKRLERDMRE AATSMEYERA ARLRDDIRAL
ERALEKQTVV LADDTDLDMI AFAEDELEAA VQVFYIRGGR IRGQRGWVVD KVEAVTTPDL
VEQFLIQIYG DSDSVPREVY VPALPPDDEA MTELLAEQRG GPVRLRVPQR GDKKALLETV
QRNALEALKQ HKTRRASDLT TRSVALRELQ EALELDEAPL RVECYDVSNL QGTNVVASMV
VFEDGLARKS EYRRFTIKAV EGQDDVRSIH EVISRRFRRY LAESEKTGEL DVLGDGHDDD
GDASGTGAEP AAHGPIDPET GRPRRFAYPP NLVLVDGGPP QVAAAQRALD ELGVDDIAVV
GIAKRLEELW LPGDDDPVIL PRNSESMFLV QRIRDEAHRF AITFHRQKRS KSMTVSELDG
VPGLGPARRT ALVKHFGSVK RLKEATPEQI AEVPGIGLRT AETIAAALNG PGASAAARKD
APGNAPTAAP NDTARPEDTA RPDDGTRTTP DAAGAADGGT DSGTDNRGDA DNRGKRT
//