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Database: UniProt
Entry: A0A1I7I9L1_9BACT
LinkDB: A0A1I7I9L1_9BACT
Original site: A0A1I7I9L1_9BACT 
ID   A0A1I7I9L1_9BACT        Unreviewed;       609 AA.
AC   A0A1I7I9L1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN04487941_2035 {ECO:0000313|EMBL:SFU69642.1};
OS   Pontibacter akesuensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=388950 {ECO:0000313|EMBL:SFU69642.1, ECO:0000313|Proteomes:UP000182491};
RN   [1] {ECO:0000313|Proteomes:UP000182491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18820 {ECO:0000313|Proteomes:UP000182491};
RA   Varghese N.;
RL   Submitted (OCT-2016) 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; FPCA01000002; SFU69642.1; -; Genomic_DNA.
DR   RefSeq; WP_068837577.1; NZ_FPCA01000002.1.
DR   AlphaFoldDB; A0A1I7I9L1; -.
DR   STRING; 388950.GCA_001611675_01507; -.
DR   OrthoDB; 9804933at2; -.
DR   Proteomes; UP000182491; 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; 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; 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; PF08459; UvrC_RNaseH_dom; 1.
DR   SMART; SM00465; GIYc; 1.
DR   SUPFAM; SSF82771; GIY-YIG endonuclease; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR   PROSITE; PS50164; GIY_YIG; 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:UP000182491};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00203}.
FT   DOMAIN          16..94
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000259|PROSITE:PS50164"
FT   DOMAIN          269..480
FT                   /note="UvrC family homology region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50165"
SQ   SEQUENCE   609 AA;  69568 MW;  D240471B978D63A3 CRC64;
     MPANEKLKEK ISHLPHKPGI YKFFDEKGII YVGKAIDIRK RVSSYFNRSA QHNRKTLKLV
     SQIKDIEFTI VDTEADAFLL ENNLIKQYQP KYNILLKDGK TYPYICIINE RFPRVITTRN
     KINDGSRYFG PYPTGTAMYV VLDLIRTLYP LRTCTYNLSP ENVAAGKFKV CLEYHIGNCK
     GPCEALVDET EYNANIAQIK NILSGNLSVA KSYFKEHMAA AAADFQYELA HKYKQKLDML
     EDFQVKSTVV SNTITNVDVF TITSNEECAF INYLKVMNGS IILTQSLEIQ KKLDEDDAEI
     LASVIVQLRQ EFESTSREVI TNIELSLPLD SITITYPQIG DKKKLLSLSL KNALYLRKER
     EGRKEKNKDL SEQRELRVLE TMKKDLRLTE LPRQIECFDN SNFQGDNPVA SMVCFKNGKP
     SKKDYRHYNI KTVIGPNDFE SMYEIVTRRY RRLLNENQPL PQLIIIDGGK GQLSMAVKAL
     KDLDIYGKIA VVGIAKRLEE IFYPGDSMPL YIDKKSESLK LIQRLRNEAH RFAITFHRSK
     RDAGTLKTGL TDIKGIGPST ADALLQKYRS VKKVRELSMA ELADEVGPAK AAIVYAYLHP
     VSEEENPMN
//
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