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Database: UniProt
Entry: D2EPJ2_9STRE
LinkDB: D2EPJ2_9STRE
Original site: D2EPJ2_9STRE 
ID   D2EPJ2_9STRE            Unreviewed;       615 AA.
AC   D2EPJ2;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   24-JAN-2024, entry version 66.
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:EFA25006.1};
GN   ORFNames=HMPREF0850_00880 {ECO:0000313|EMBL:EFA25006.1};
OS   Streptococcus sp. M143.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=563037 {ECO:0000313|EMBL:EFA25006.1, ECO:0000313|Proteomes:UP000002766};
RN   [1] {ECO:0000313|EMBL:EFA25006.1, ECO:0000313|Proteomes:UP000002766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M143 {ECO:0000313|EMBL:EFA25006.1,
RC   ECO:0000313|Proteomes:UP000002766};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S.,
RA   Surette M.G., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Streptococcus sp. strain M143.";
RL   Submitted (OCT-2009) 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; GG730097; EFA25006.1; -; Genomic_DNA.
DR   RefSeq; WP_001061175.1; NZ_GG730097.1.
DR   AlphaFoldDB; D2EPJ2; -.
DR   eggNOG; COG0322; Bacteria.
DR   HOGENOM; CLU_014841_3_2_9; -.
DR   OrthoDB; 9804933at2; -.
DR   Proteomes; UP000002766; 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; 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   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}; Hydrolase {ECO:0000313|EMBL:EFA25006.1};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00203}.
FT   DOMAIN          14..91
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000259|PROSITE:PS50164"
FT   DOMAIN          196..231
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   DOMAIN          247..466
FT                   /note="UvrC family homology region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50165"
SQ   SEQUENCE   615 AA;  70598 MW;  39044BC1FADE3454 CRC64;
     MNNLIKSKLE LLPTSPGCYI HKDKNGTIIY VGKAKNLRNR VRSYFRGSHD TKTEALVSEI
     VDFEFIVTES NIEALLLEIN LIKENQPKYN IMLKDDKSYP FIKITNERYP RLIITRQVKK
     DGGLYFGPYP DVGAANEIKR LLDRIFPFRK CTNPPSKVCF YYHIGQCMAH TICKKDEAYF
     KSMAQEVSDF LKGQDDKIID DLKSKMAVAA QSMEFERAAE YRNLIQAIGT LRTKQRVMAK
     DLQNRDVFGY YVDKGWMCVQ VFFVRQGKLI ERDVNLFPYY NDPDEDFLTY VGQFYQEKSH
     LVPNEVLIPQ DIDEEAVKAL VDTKILKPQR GEKKQLVNLA IKNARVSLEQ KFNLLEKSVE
     KTQGAIENLG RLLQIPTPVR IESFDNSNIM GTSPVSAMVV FVNGKPSKKD YRKYKIKTVV
     GPDDYASMRE VIRRRYGRVQ REGLTPPDLI VIDGGQGQVN IAKQVIQEEL GLDIPIAGLQ
     KNDKHQTHEL LFGDPLEVVE LSRNSQEFFL LQRIQDEVHR FAITFHRQLR SKNSFSSQLD
     GIDGLGPKRK QNLMKHFKSL TKIKEASVDE IVEVGVPRTV AEAVQRKLNP QGEVELAQVA
     EERVDYQTKG DYDEP
//
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