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Database: UniProt
Entry: A0A257FLS6_9BURK
LinkDB: A0A257FLS6_9BURK
Original site: A0A257FLS6_9BURK 
ID   A0A257FLS6_9BURK        Unreviewed;       506 AA.
AC   A0A257FLS6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:OYU26569.1};
GN   ORFNames=CFE41_15320 {ECO:0000313|EMBL:OYU26569.1};
OS   Burkholderiales bacterium PBB2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=2015564 {ECO:0000313|EMBL:OYU26569.1, ECO:0000313|Proteomes:UP000215624};
RN   [1] {ECO:0000313|EMBL:OYU26569.1, ECO:0000313|Proteomes:UP000215624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBB2 {ECO:0000313|EMBL:OYU26569.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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 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:OYU26569.1}.
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DR   EMBL; NKIM01000024; OYU26569.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257FLS6; -.
DR   Proteomes; UP000215624; 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:OYU26569.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215624}.
FT   DOMAIN          13..142
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          453..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..474
FT                   /note="Basic and acidic residues"
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"
FT   BINDING         274
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ   SEQUENCE   506 AA;  56990 MW;  FD79D84A8A791FFA CRC64;
     MRPLTASSHP FTPTALVWFK RDLRLLDHAP LVESTQFERA AALLLIEPEW LQSPECEARH
     VEFLLACAEA LQQDLARIGL PLIVRVGSAV AVLEQLRQEL GFSHLLSHEE TGTGWSYVRD
     IEVSRWCRAC GVAWQEWPQT GVVRRLKSRS GWAALWAQRM DAAPLPRPLG FKPWLDPRPV
     PLPGLQDLGF APSTVPATPA GERAAWQTLG SFLEGRGRDY RSALSSPLTA AEGCSRLSAH
     LAFGTISMRL LHQATERRIA STEDRSLAYG LRGFSSRLRW HCHFMQKLED EPALEWRNLA
     RAVDGLRPGE SALLEGADRE RFQAWCEGRT GYPMVDACMR QLRATGWLNF RMRAMLVSFA
     AYHLWLHWRE PGLFLARQFL DFEPGIHWSQ MQMQSGTTGI NTLRIYSPAK QAREHDPLGE
     YQRRWLPELG TAAYPAPIVD ERAALARAKE ALYGQRRSPE AQAEAERIQD KHGSRKSGLP
     STARPSRASA RREAPSAAEQ AQQSLF
//
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