ID A0A0H5DQN8_9BACT Unreviewed; 611 AA.
AC A0A0H5DQN8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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:CRX37899.1};
GN ORFNames=ELAC_0544 {ECO:0000313|EMBL:CRX37899.1};
OS Estrella lausannensis.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Criblamydiaceae;
OC Estrella.
OX NCBI_TaxID=483423 {ECO:0000313|EMBL:CRX37899.1, ECO:0000313|Proteomes:UP000220251};
RN [1] {ECO:0000313|Proteomes:UP000220251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIB-30 {ECO:0000313|Proteomes:UP000220251};
RA Bertelli C.;
RL Submitted (JUN-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}.
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DR EMBL; CWGJ01000009; CRX37899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H5DQN8; -.
DR OrthoDB; 9804933at2; -.
DR Proteomes; UP000220251; 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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000220251};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00203}.
FT DOMAIN 12..91
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT DOMAIN 203..238
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 285..476
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
FT COILED 206..245
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 611 AA; 69532 MW; 88B4402EA11CC7B4 CRC64;
MVDDKVLERL PEKTGVYIMK SGEDVVLYVG KAKNLKERVK QYFIPGRDGR PQVPFLTLKV
RHIDTMITSS EKEALILENT LIKQYQPKYN VLLRDDKSFA ALKIKIKHEW PSVELVRSRG
SHKKDGLYFG PYPSAFSARM TLDLIKKIFP LRQCSDSELA SRTRPCILHA MGRCIAPCVG
LCTKEEYDDL VQKVVQFLKG SDKEIIQKLK AEMLRLSDAL EFEKAQSVKN ILDHIEKTLE
QQRVEKIHGK DMDAVGIYRE GDEGILVRMI YRQGRLVSAA THSFSKIAEE DADLISSFLL
QSYEEPHAMP REVLVPVEMA DAAALSEILA AKKGGLCEVL FPQKGDKKAI LDIALENAIA
KFRQVKDQKE LSERALMEIK ETFHLKSYPK KIECFDISNF QGSAIVGALV AFTDGEKDTS
RYRKFKIKLT EEPDDYLSMY EVLTRRFKKA KEENNLPDLI LVDGGKGHLN VALKVLKELD
IITVDVISLA KEESRHDKGI RAEKVFLPNI KDPLYLKTHS KILFFLQKIR DEAHRFALSF
MHQRKSKSLV QSELDAIAGI GPKKKRALLR KFGSVKKIRE AAAEELLATP GVHRKDVEAI
RLFLQSDKQP Q
//
