ID UVRC_PROMT Reviewed; 640 AA.
AC Q46L08;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=UvrABC system protein C {ECO:0000255|HAMAP-Rule:MF_00203};
DE Short=Protein UvrC {ECO:0000255|HAMAP-Rule:MF_00203};
DE AltName: Full=Excinuclease ABC subunit C {ECO:0000255|HAMAP-Rule:MF_00203};
GN Name=uvrC {ECO:0000255|HAMAP-Rule:MF_00203}; OrderedLocusNames=PMN2A_0328;
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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:0000255|HAMAP-
CC Rule:MF_00203}.
CC -!- SUBUNIT: Interacts with UvrB in an incision complex.
CC {ECO:0000255|HAMAP-Rule:MF_00203}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00203}.
CC -!- SIMILARITY: Belongs to the UvrC family. {ECO:0000255|HAMAP-
CC Rule:MF_00203}.
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DR EMBL; CP000095; AAZ57820.1; -; Genomic_DNA.
DR RefSeq; WP_011293862.1; NC_007335.2.
DR AlphaFoldDB; Q46L08; -.
DR SMR; Q46L08; -.
DR STRING; 59920.PMN2A_0328; -.
DR KEGG; pmn:PMN2A_0328; -.
DR HOGENOM; CLU_014841_3_2_3; -.
DR OrthoDB; 9804933at2; -.
DR PhylomeDB; Q46L08; -.
DR Proteomes; UP000002535; Chromosome.
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; 3.30.420.340; UvrC, RNAse H endonuclease domain; 1.
DR HAMAP; MF_00203; UvrC; 1.
DR InterPro; IPR041663; DisA/LigA_HHH.
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; PF12826; HHH_2; 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; DNA damage; DNA excision; DNA repair; Excision nuclease;
KW Reference proteome; SOS response.
FT CHAIN 1..640
FT /note="UvrABC system protein C"
FT /id="PRO_0000227460"
FT DOMAIN 22..101
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT DOMAIN 211..246
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ SEQUENCE 640 AA; 74128 MW; CB360445DC4378CC CRC64;
MELTPLIRDK SRLSDFLKDI PNDPGCYLMK DGEDRLLYVG KSKKLRNRVR SYFRSGNELS
PRISLMVRQV ADIELIVTDN ESEALTLESN LIKSHQPYFN VLLKDDKKYP YVCITWGDKY
PRIFLTRKRR QRQLKDKYYG PYVDVYLLRQ TLFSIKKLFP LRQRRIPLYK DRTCLNYSIG
RCPGVCQEEI SSEDYKNTLK RVEMIFQGRT DELRILLEKQ MISFSESLKF EEAGSVRDQL
KGIDRLYESQ KMIIPDSSVC RDIIAMASEE NISSVQIFQM RSGKLIGRLG YFSDNSNFNS
SQILQQVIEN HYSNVDPVEI PSEILVQHQL VNNILISDWL SEIKKQKVNI NVPKRSRKAE
IIKLVEKNAN LELQRIKQSQ DKNLVELDDL TNILDLENIP KRIECYDISH IQGSDAVASQ
VVFIDGIAAR QHYRRYKIKS PNIKIGHSDD FESMAEVITR RFRRWARFKE EGGDIDALLS
NESSVLDNLN LNDWPDLVVI DGGKGQLSSV VAALEGLKLD QNLNVISLAK KKEEVFIPKV
KQSLVTESNQ PGMLLLRRLR DEAHRFAITF HRQKRSQRMK RSQLNEIPGL GPQRIKLLLE
HFRSIEAIQM ATFSELSSTP GLGRSTAVVI RNYFHPDKNI
//
