ID A0A176J4B5_9BACI Unreviewed; 319 AA.
AC A0A176J4B5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=UV DNA damage endonuclease {ECO:0000256|HAMAP-Rule:MF_00606};
DE Short=UV-endonuclease {ECO:0000256|HAMAP-Rule:MF_00606};
DE Short=UVED {ECO:0000256|HAMAP-Rule:MF_00606};
DE EC=3.-.-.- {ECO:0000256|HAMAP-Rule:MF_00606};
GN Name=uvsE {ECO:0000256|HAMAP-Rule:MF_00606,
GN ECO:0000313|EMBL:KZZ83798.1};
GN ORFNames=AS29_013665 {ECO:0000313|EMBL:KZZ83798.1};
OS Bacillus sp. SJS.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423321 {ECO:0000313|EMBL:KZZ83798.1, ECO:0000313|Proteomes:UP000028527};
RN [1] {ECO:0000313|EMBL:KZZ83798.1, ECO:0000313|Proteomes:UP000028527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJS {ECO:0000313|EMBL:KZZ83798.1,
RC ECO:0000313|Proteomes:UP000028527};
RA Newman J.D., Stropko S.J., Pipes S.E.;
RT "Bacillus sp. SJS genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component in a DNA repair pathway. Removal of UV LIGHT
CC damaged nucleotides. Recognizes pyrimidine dimers and cleave a
CC phosphodiester bond immediately 5' to the lesion.
CC {ECO:0000256|ARBA:ARBA00025029}.
CC -!- FUNCTION: Component in a DNA repair pathway. Removal of UV-light
CC damaged nucleotides. Recognizes pyrimidine dimers and cleave a
CC phosphodiester bond immediately 5' to the lesion. {ECO:0000256|HAMAP-
CC Rule:MF_00606}.
CC -!- SIMILARITY: Belongs to the uve1/UvsE family. {ECO:0000256|HAMAP-
CC Rule:MF_00606}.
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:KZZ83798.1}.
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DR EMBL; JAQV02000023; KZZ83798.1; -; Genomic_DNA.
DR RefSeq; WP_035407972.1; NZ_JAQV02000023.1.
DR AlphaFoldDB; A0A176J4B5; -.
DR STRING; 1423321.AS29_013665; -.
DR eggNOG; COG4294; Bacteria.
DR OrthoDB; 9782576at2; -.
DR Proteomes; UP000028527; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0006290; P:pyrimidine dimer repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009411; P:response to UV; IEA:InterPro.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR HAMAP; MF_00606; UV_endonuclease; 1.
DR InterPro; IPR004601; UvdE.
DR InterPro; IPR023520; UvdE_bac.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR NCBIfam; TIGR00629; uvde; 1.
DR PANTHER; PTHR31290; UV-DAMAGE ENDONUCLEASE; 1.
DR PANTHER; PTHR31290:SF5; UV-DAMAGE ENDONUCLEASE; 1.
DR Pfam; PF03851; UvdE; 1.
DR SUPFAM; SSF51658; Xylose isomerase-like; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00606};
KW DNA excision {ECO:0000256|ARBA:ARBA00022769, ECO:0000256|HAMAP-
KW Rule:MF_00606}; DNA repair {ECO:0000256|HAMAP-Rule:MF_00606};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00606}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00606};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00606};
KW Reference proteome {ECO:0000313|Proteomes:UP000028527}.
SQ SEQUENCE 319 AA; 36927 MW; 4F2D82411F3AC24A CRC64;
MKIRFGYVAN ALSLWDCSPS KTMTFARYQK LEESERKEAL CRVTKQNLEH TLRIIHYNIA
HEIHLYRFSS SLVPLATHPE VSWDFVAPFK DQFKEIGELV KKHKMRTSFH PSQYTLFTSD
RPSITENSVR DMEYHYAMLE AMGLEKEGLI NLHVGGAYGD KTASAERFFV NIQSLPAPVF
SRMTLENDDK TYTTEETLQV CEKGGTPLMF DYHHHQANKN EGDQKLEDLL PRFFDTWKQT
GLAPKIHISS PKSEKEYRSH SDYVDLEFIR PLLKMLKEFD VDVDVMIEAK MKDLALLKLI
EEISAIRGVK RVDGGSVVW
//
