ID A0A0M9X5X3_9ACTN Unreviewed; 695 AA.
AC A0A0M9X5X3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=ADK41_35180 {ECO:0000313|EMBL:KOT29148.1};
OS Streptomyces caelestis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36816 {ECO:0000313|EMBL:KOT29148.1, ECO:0000313|Proteomes:UP000037773};
RN [1] {ECO:0000313|EMBL:KOT29148.1, ECO:0000313|Proteomes:UP000037773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24567 {ECO:0000313|EMBL:KOT29148.1,
RC ECO:0000313|Proteomes:UP000037773};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOT29148.1}.
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DR EMBL; LGCN01000251; KOT29148.1; -; Genomic_DNA.
DR RefSeq; WP_030820884.1; NZ_LGCN01000251.1.
DR AlphaFoldDB; A0A0M9X5X3; -.
DR PATRIC; fig|36816.3.peg.7643; -.
DR OrthoDB; 9804933at2; -.
DR Proteomes; UP000037773; 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:UP000037773};
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..528
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
FT REGION 470..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 77490 MW; 2287D909DFCBF01D CRC64;
MADPSSYRPK PGEIPDSPGV YRFRDEHRRV IYVGKAKSLR QRLANYFQDL AGLHPRTRSM
VTTAASVEWT VVSTEVEALQ LEYSWIKEYD PRFNVKYRDD KSYPYLAVTM NEEFPRVQVM
RGHKKKGVRY FGPYTHAWAI RDTVDLLLRV FPVRTCSAGV FKNAARTGRP CLLGYIDKCS
APCVDRISAE DHRGLAEEFS DFMTGRTGAY LRRLERRMAQ AAEEMEYERA ARLRDDIAAL
KKAMEKSAVV LADATDADLI AVAEDELEAA VQIFHVRGGR VRGQRGWVTD KVEEITTGAL
VEHALQQLYG EETGDAVPRE VLVPALPDPV EPVQQWLTGR RGSGVSLRIP QRGDKRALME
TVERNAQQAL VLHKTKRASD LTTRSRALEE ITDALELDSA PLRIECYDIS HLQGDDVVAS
MVVFEDGLAR RSEYRRFQIK GFAGQDDVRS MHEVITRRFR RYLAEKERTG EWADGGEPGA
EDSSAGLAEP PVTTLTEDEG RPRRFAYPPQ LVVVDGGAPQ VAAAQRALDE LGIDDIAVCG
LAKRLEEVWL PGETDPVVLP RTSEGLYLLQ RVRDEAHRFA ITYQRAKRAK RFRAGPLDEV
PGLGETRKQA LIKHFGSVKR LRSATIDQIC EVPGIGRKTA ETIVAALDRA APAAPAVNTA
TGEIMDDTEE PGQTTGSPGE PVSTGAPDER RGQDR
//
