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Database: UniProt
Entry: A0A075JDE1_9MICO
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Original site: A0A075JDE1_9MICO 
ID   A0A075JDE1_9MICO        Unreviewed;       466 AA.
AC   A0A075JDE1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:AIF39655.1};
GN   ORFNames=HX89_00040 {ECO:0000313|EMBL:AIF39655.1}, HX89_14180
GN   {ECO:0000313|EMBL:AIF41860.1};
OS   Dermacoccus nishinomiyaensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Dermacoccus.
OX   NCBI_TaxID=1274 {ECO:0000313|EMBL:AIF39655.1, ECO:0000313|Proteomes:UP000027986};
RN   [1] {ECO:0000313|EMBL:AIF39655.1, ECO:0000313|Proteomes:UP000027986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M25 {ECO:0000313|EMBL:AIF39655.1,
RC   ECO:0000313|Proteomes:UP000027986};
RA   Hong K.W., Chan K.G.;
RT   "Genome Sequencing of Dermacoccus nishinomiyaensis.";
RL   Submitted (JUL-2014) 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}.
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DR   EMBL; CP008889; AIF39655.1; -; Genomic_DNA.
DR   EMBL; CP008889; AIF41860.1; -; Genomic_DNA.
DR   RefSeq; WP_038566022.1; NZ_CP008889.1.
DR   AlphaFoldDB; A0A075JDE1; -.
DR   GeneID; 41842164; -.
DR   KEGG; dni:HX89_00040; -.
DR   KEGG; dni:HX89_14180; -.
DR   eggNOG; COG0415; Bacteria.
DR   HOGENOM; CLU_010348_2_2_11; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000027986; Chromosome.
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:AIF39655.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027986}.
FT   DOMAIN          1..150
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         249
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         261..265
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         292
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         393..395
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            326
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            380
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            403
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   466 AA;  52162 MW;  F24B3524D5D8445E CRC64;
     MTSLVWFRDD LRTFDHPALR AAVDHAVTSQ GSQGSQESDD GASSEPAGVV ALFVLDEESD
     GLRPLGGAVK WWLHHSLVAL REKLEALGIP LVLRRDAAHD VVLDVVETFD VDFVGWNRRY
     GGPERAVDAG IKEALAERDV EVHSYAANLL FEPWTISTGG GTPYRVFTPF WKACLSESEP
     REPLGAPSAL TPPSALVEQA GQASDDLDTW ALLPTKPDWS TGIARAWTPG EDAAHELLAD
     FLDDAVVHYA TQRDEPSKPA TSRLSPHLRF GEISPQAIWH AARRSGKDVE TFLSEVGWRE
     FAWHTLYENP DLHEVNLNRK FDAFPWPPLD EDALLAWEKG ETGVPLVDAG MRELWETGTM
     HNRVRMVVAS FLTKNLLIDW RIGEEWFWDT LVDADAASNP FNWQWVAGCG ADAAPYFRVF
     NPETQRKKFD PDERYVRRWG ADDGREPIVD LAQTRKAALA AYEQTK
//
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