ID   A0A366WGD1_9GAMM        Unreviewed;       509 AA.
AC   A0A366WGD1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:RBW47252.1};
GN   ORFNames=DS885_04135 {ECO:0000313|EMBL:RBW47252.1};
OS   Psychromonas sp. B3M02.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=2267226 {ECO:0000313|EMBL:RBW47252.1, ECO:0000313|Proteomes:UP000252071};
RN   [1] {ECO:0000313|EMBL:RBW47252.1, ECO:0000313|Proteomes:UP000252071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B3M02 {ECO:0000313|EMBL:RBW47252.1,
RC   ECO:0000313|Proteomes:UP000252071};
RA   Enke T.N., Datta M.S., Schwartzman J.A., Cermak N., Schmitz D.A.,
RA   Barrere J., Cordero O.X.;
RT   "Modular assembly of carbohydrate-degrading microbial communities in the
RT   ocean.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC         Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|ARBA:ARBA00001932};
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 class-1 family.
CC       {ECO:0000256|ARBA:ARBA00005862}.
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:RBW47252.1}.
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DR   EMBL; QOCB01000029; RBW47252.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366WGD1; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000252071; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   Chromophore {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:RBW47252.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252071}.
FT   DOMAIN          11..140
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          490..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         220
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ   SEQUENCE   509 AA;  59492 MW;  EA3F6C7B3C75587C CRC64;
     MNKVLSKAQP AINVVWLKRD LRLSDHQPLA SAVESGLTLL FYVFEPCLVN DPHYDLRHWR
     FVWQSIQDLN RQLARFNTQV YLFYGDTQAG LESIQQQFNI KQLFSHEETG LLVTFKRDKQ
     IKAWCQRQQV QWHETPTGAV VRAKKDRQGW DTQWRKVING EFASPRLSEQ DLLTNDQIAA
     LPQASLPNTW LIPDPLMLTG GEQWAHKILN SFLAGRGKDY HFNIGKPLAS RKSCSRLSPY
     LAWGNISLKQ CYQAILQKRP ELGWKKPIDG LASRLHWHCH FIQKFESEHQ MQWQHVNKAY
     HHLHYPEQHC GLSIETRLSR WKNAQTGYPL VDACMLCLIK TGYINFRMRA MLVSFLCHHL
     LVDWRLGVTY LARLFLDFEP GIHYPQFQMQ SGVTGTNTIR VYNPVKQSQE KDPDGEFIKQ
     WLPQLSEIPK EIIHTPWVLS PMEQQLYQFV IGDTYPEPMV DIEETGKIAR DLLWGFRQRL
     DTRQEGKRIV AKHVRKRRST SSMSKQSNA
//