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Database: UniProt
Entry: A5KY33_VIBBS
LinkDB: A5KY33_VIBBS
Original site: A5KY33_VIBBS 
ID   A5KY33_VIBBS            Unreviewed;       497 AA.
AC   A5KY33;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Deoxyribodipyrimidine photolyase, putative {ECO:0000313|EMBL:EDK29604.1};
GN   ORFNames=VSWAT3_18633 {ECO:0000313|EMBL:EDK29604.1};
OS   Vibrionales bacterium (strain SWAT-3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales.
OX   NCBI_TaxID=391574 {ECO:0000313|EMBL:EDK29604.1, ECO:0000313|Proteomes:UP000004912};
RN   [1] {ECO:0000313|EMBL:EDK29604.1, ECO:0000313|Proteomes:UP000004912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SWAT-3 {ECO:0000313|EMBL:EDK29604.1,
RC   ECO:0000313|Proteomes:UP000004912};
RA   Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (APR-2007) 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:EDK29604.1}.
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DR   EMBL; AAZW01000008; EDK29604.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5KY33; -.
DR   Proteomes; UP000004912; 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:EDK29604.1}.
FT   DOMAIN          3..133
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          477..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         213
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ   SEQUENCE   497 AA;  58302 MW;  22881068F0C8960D CRC64;
     MQTINVVWLK RDLRLTDHAP LQHALSDQYP TILLYIFEPM LLNNAHYSER HWRFVWQSLQ
     CMNQSLKAYG HQVSILHGSA VDCFEAIQSR YHIKNLFSHQ EIGLNCTFER DRELSTWFTE
     HNIPWQEFAQ GAVVRGSKDR VGWDKHWNSV MRAPIEESLF TAESLHTLDP EELELAMEPP
     QAWLTKVNGI QTGGSALAWA TLHDFFDRRG RDYYRSISSP EASRHACTRL SPYLAWGNIS
     LREVYQHLLG HWQVAGFRRS LIALSSRLHW HCHFMQKFES ECAMEYRCIN HAYEALLQKE
     TVKDPTHLQA WKIGMTGVPL VDACMRCLHH TGYINFRMRS MLVSFLTHHM NMDWRDGVTH
     LAQMFLDFEP GIHYPQFQMQ AGVTGINTIR IYNPTKQAQE HDSDGDFIRK WVPELSDIPT
     PLLFEPWKMT PMEVMMHELE PDFPYLNPVV DLEVSAKEAR VRLWSWRKLT EVKQERSRIL
     SRHVRPPKKQ SKTTRAS
//
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