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Database: UniProt
Entry: A0A399SWP3_9BACT
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ID   A0A399SWP3_9BACT        Unreviewed;       430 AA.
AC   A0A399SWP3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:RIJ47908.1};
GN   ORFNames=D1614_12335 {ECO:0000313|EMBL:RIJ47908.1};
OS   Maribellus luteus.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Maribellus.
OX   NCBI_TaxID=2305463 {ECO:0000313|EMBL:RIJ47908.1, ECO:0000313|Proteomes:UP000265926};
RN   [1] {ECO:0000313|EMBL:RIJ47908.1, ECO:0000313|Proteomes:UP000265926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XSD2 {ECO:0000313|EMBL:RIJ47908.1,
RC   ECO:0000313|Proteomes:UP000265926};
RA   Zhou L.Y.;
RT   "Pallidiluteibacterium maritimus gen. nov., sp. nov., isolated from coastal
RT   sediment.";
RL   Submitted (AUG-2018) 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:RIJ47908.1}.
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DR   EMBL; QWGR01000006; RIJ47908.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399SWP3; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000265926; 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; PS00691; DNA_PHOTOLYASES_1_2; 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:RIJ47908.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265926}.
FT   DOMAIN          5..134
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         211
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         223..227
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         251
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         254..261
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            285
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            338
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            361
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   430 AA;  50782 MW;  68D59C23128F8F41 CRC64;
     MIKEMNAVFW FRRDLRLEDN TALAKALSGT LKVIPLFIFD TNILDELPPD DARITFIYRQ
     LEKINAELKR HGSGLLIKHG DPQEVWKEMI QQFPVKEVYF NKDYEPYAIR RDEQVKTFLA
     AANIPVFSLK DQVVFEESEV MKPDGECYTV FTPYKSRWLQ QLKTQGLPAF QNTKWENFEK
     KNFDFPSLEA IGFSENPMPV KDANFSVIGN YEQTRNLPAL EGTSNLSVHL RFGTVSIRDI
     VRKVYDKFPV FLSELIWREF FMQILFHYPR VVHHNFRAKY DGIQWRNNEK EFERWCRGET
     GYPMVDAGMR ELNETGYMHN RVRMVTASFL CKHLLIDWRW GEAYFAKKLL DYELSSNNGN
     WQWAAGTGCD AAPYFRIFNP AEQQKKFDKK LDYVKRWIPE LNSFNYPTPM VEHTFARQRA
     LAAYQQGIIK
//
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