ID A0A0A2UW59_9BACI Unreviewed; 486 AA.
AC A0A0A2UW59;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KGP90978.1};
GN ORFNames=N780_16995 {ECO:0000313|EMBL:KGP90978.1};
OS Pontibacillus chungwhensis BH030062.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385513 {ECO:0000313|EMBL:KGP90978.1, ECO:0000313|Proteomes:UP000030153};
RN [1] {ECO:0000313|EMBL:KGP90978.1, ECO:0000313|Proteomes:UP000030153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030062 {ECO:0000313|EMBL:KGP90978.1,
RC ECO:0000313|Proteomes:UP000030153};
RA Wang Q., Wang G.;
RT "Genome of Pontibacillus chungwhensis.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR602081-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR602081-1};
CC -!- SIMILARITY: Belongs to the DNA photolyase family.
CC {ECO:0000256|RuleBase:RU004182}.
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:KGP90978.1}.
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DR EMBL; AVBG01000008; KGP90978.1; -; Genomic_DNA.
DR RefSeq; WP_052115025.1; NZ_AVBG01000008.1.
DR AlphaFoldDB; A0A0A2UW59; -.
DR STRING; 1385513.N780_16995; -.
DR eggNOG; COG0415; Bacteria.
DR Proteomes; UP000030153; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR Gene3D; 1.25.40.80; -; 1.
DR Gene3D; 1.10.579.10; DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR InterPro; IPR036155; Crypto/Photolyase_N_sf.
DR InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR InterPro; IPR018394; DNA_photolyase_1_CS_C.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF9; CRYPTOCHROME-1; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|RuleBase:RU004182};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW 1}; Lyase {ECO:0000313|EMBL:KGP90978.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030153}.
FT DOMAIN 1..131
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 215
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 269
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 486 AA; 56434 MW; 487C115D6B08E371 CRC64;
MLHVVWYKRD LRIGDHRPLQ EAWREKEPIL PLYVAEPSIW QESELSIRHL QFVKESLEDL
QGAFERLGGS MFVTIAEMES VLGTIYESVG PFTLHAHEEN GTPVTYERDK RVRQWMKDRG
LLFHEYQHCG VVRGERSEEL FKKDWKEFIE TPVMNAPDSI LTLDQEILPS TITTNMDTLL
RFKIGGYRIK YGQQGGEGLA HETLESFLDG RFTRYKEELA NPLASTNTCS RLSPYLAFGN
ISMRQVVQLT KEAIEQCDKS DDKKQLKAFN SKLEEHCRSI QWIEDHPQFA CNSGNPTFDP
SRDVWQEGFE RWSRGETGFP IIDAAMRALI KTGWLNFRSR AMLLSFACHT LRMNWKEPAD
YLAGLFVDYE PGIHYKQVHL VVSPESMKRV CLYDPIKEGK KHDPEGRFVR QYVPELKHVP
DSYIHEPWKY DGFFHLDYYG PIVDVGKANR HVRARMADVE SSGDGLKKKE ADKEGNEQIV
FDLFTE
//
