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Database: UniProt
Entry: A0A432WKJ2_9GAMM
LinkDB: A0A432WKJ2_9GAMM
Original site: A0A432WKJ2_9GAMM 
ID   A0A432WKJ2_9GAMM        Unreviewed;       479 AA.
AC   A0A432WKJ2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:RUO34268.1};
GN   ORFNames=CWE11_05945 {ECO:0000313|EMBL:RUO34268.1};
OS   Aliidiomarina sanyensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Aliidiomarina.
OX   NCBI_TaxID=1249555 {ECO:0000313|EMBL:RUO34268.1, ECO:0000313|Proteomes:UP000288405};
RN   [1] {ECO:0000313|EMBL:RUO34268.1, ECO:0000313|Proteomes:UP000288405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GYP-17 {ECO:0000313|EMBL:RUO34268.1,
RC   ECO:0000313|Proteomes:UP000288405};
RX   PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA   Liu Y., Lai Q., Shao Z.;
RT   "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT   Idiomarinaceae.";
RL   Front. Microbiol. 9:2453-2453(2018).
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:RUO34268.1}.
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DR   EMBL; PIPM01000004; RUO34268.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432WKJ2; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000288405; 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:RUO34268.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288405}.
FT   DOMAIN          1..128
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         206
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         256
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ   SEQUENCE   479 AA;  55770 MW;  6E1C698D2DAC6DA8 CRC64;
     MINIVWLKRD LRLTDHAPLA AAQAANKPFI ILFVVEDFLR NDPHYSDRHW RFMWQSLTEI
     NHQLAGRLTL TQGRLSDTLN NLHRTYRIGT IFSHEEIGIE STYARDRALK KWCIKRGVQW
     QEFPCGAVIR GLSDRSGWDQ HWRSVMNQPC PSVELTALSQ LFRADHLPPV SPPREWRQPV
     PEQQIGGAQH GWRELKEFMA GRGARYHQDI SKPAASRSSC SRISPYLAWG NLSIREVWQY
     ALQHHTQLPT RAWRAFSSRL HWRCHFLQKF ESGMDMEHEH FNPGYRAFPF RADVNVPKDL
     KAWEQGQTGI PLVDASMRCL NTTGYINFRM RAMLVSMLSH HLNIDWRLGA PHLARVFLDF
     EPGIHYPQLN MQAGVTGIHT IRIYNPVYQG QKQDPNGDFI RHWVPELASL PNGLLHQPWE
     MTPMEQTMHG VVLGRDYPEP LVNIAETHRA ARDRLWGFQQ KSEVQLHNPH LLARHTRRA
//
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