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Database: UniProt
Entry: Q47SJ5_THEFY
LinkDB: Q47SJ5_THEFY
Original site: Q47SJ5_THEFY 
ID   Q47SJ5_THEFY            Unreviewed;       419 AA.
AC   Q47SJ5;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   SubName: Full=Deoxyribodipyrimidine photo-lyase type I {ECO:0000313|EMBL:AAZ54572.1};
DE            EC=4.1.99.3 {ECO:0000313|EMBL:AAZ54572.1};
GN   OrderedLocusNames=Tfu_0534 {ECO:0000313|EMBL:AAZ54572.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54572.1};
RN   [1] {ECO:0000313|EMBL:AAZ54572.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YX {ECO:0000313|EMBL:AAZ54572.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Thermobifida fusca YX.";
RL   Submitted (JUL-2005) 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; CP000088; AAZ54572.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47SJ5; -.
DR   STRING; 269800.Tfu_0534; -.
DR   KEGG; tfu:Tfu_0534; -.
DR   eggNOG; COG0415; Bacteria.
DR   HOGENOM; CLU_010348_2_2_11; -.
DR   OrthoDB; 9772484at2; -.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
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:AAZ54572.1}.
FT   DOMAIN          2..129
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         346..348
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            280
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            333
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            356
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   419 AA;  46534 MW;  4430FFDA6826FDFF CRC64;
     MSTTVVLFTR DLRVSDHPAL HAAVTEADRV VPLFVVDPAL VRVSARNRIA YLLEALAELR
     GLLRERGGEL VVRQGDTVAE TVRIVAEAGA QAVYLSADVS AAAVRRARQL TEAVRAAGAH
     VRTFPGVTVV PPGALRPAHG DHYQIFTPYL NAWRAAQWRS PRPAPERVRL PEGLVPGPLP
     GAELIRLGTG VLAPQREQGG PRTARERIRA WLAQPNQDSR FGCHLHFGCL SPLEVALVAR
     EHPRGALLLR QLALRDFHHQ VLQAFPRLPR ADYRPRPIQW RDDDSAFAAW CSGRTGVPIV
     DAGMRQLLWE GYVPGRIRML TATYLTQVLR IHWKRGADHF YSLLVDGDVA NNYGNWQQIA
     GTGGVPRPAR RINLYRQAER YDPSGDYVRR FVPELRSISG SAVHHPPVPR PGGYPPPLR
//
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