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Database: UniProt
Entry: A0A1J4PSB9_9ACTN
LinkDB: A0A1J4PSB9_9ACTN
Original site: A0A1J4PSB9_9ACTN 
ID   A0A1J4PSB9_9ACTN        Unreviewed;       458 AA.
AC   A0A1J4PSB9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:OIK23649.1};
GN   ORFNames=VT52_031255 {ECO:0000313|EMBL:OIK23649.1};
OS   Streptomyces malaysiense.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1428626 {ECO:0000313|EMBL:OIK23649.1, ECO:0000313|Proteomes:UP000034838};
RN   [1] {ECO:0000313|Proteomes:UP000034838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC136T {ECO:0000313|Proteomes:UP000034838};
RA   Lee L.H., Chan K.-G.;
RT   "Genome sequencing of Streptomyces sp. MUSC136T.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OIK23649.1, ECO:0000313|Proteomes:UP000034838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC136T {ECO:0000313|Proteomes:UP000034838};
RA   Lee L.-H., Ser H.-L.;
RT   "Genome sequence of Streptomyces malaysiense MUSC 136.";
RL   Submitted (OCT-2016) 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:OIK23649.1}.
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DR   EMBL; LBDA02000094; OIK23649.1; -; Genomic_DNA.
DR   RefSeq; WP_046420563.1; NZ_LBDA02000094.1.
DR   AlphaFoldDB; A0A1J4PSB9; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000034838; 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:OIK23649.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034838}.
FT   DOMAIN          2..131
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         218
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         230..234
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         363..365
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ   SEQUENCE   458 AA;  50751 MW;  24FE1A0556B5E6A1 CRC64;
     MSVSLVLFTS DLRLHDHPPL RAGLAAADQV VPLFVRDRAV EAAGFATPNR TAFLADCLAD
     LDASLRERGG RLVVRSGDLV SQVCGTAAEA GADEVHLAAA HSAFATRRED LLRRALEADG
     RRLFVHDAVT VAVPPGEVTP VGSDHFAVFT PYYRRWSQVG LRAPLAAPRR VPVPDGVQGE
     ALPAREDVTG VSPALPDGGE REGRKRVSAY WRRGLDAYDD TRDDLAADAT SRFSAHLHFG
     TLSPVELVQR ARRHGGPGAD SLVRQLAWRD FHRQVLAARP AVARADYRTK GDRWRTGQAA
     RADAEAWREG RTGYPVIDAA MRQLRHEGWM HNRARLLTAS FLAKTLYVDW RTGAEHFLHW
     LVDGDIANNQ LNWQWVAGTG TDTRPNRVLN PVAQARRYDP DGGYVRRWVP ELADVADRFV
     HEPWKLPGAE RAALDYPDPV VGLSEGLDRF RKARDRGR
//
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