ID A0A0C2AXN4_9ACTN Unreviewed; 451 AA.
AC A0A0C2AXN4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KIF73670.1};
GN ORFNames=QR77_06100 {ECO:0000313|EMBL:KIF73670.1};
OS Streptomyces sp. 150FB.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF73670.1, ECO:0000313|Proteomes:UP000031584};
RN [1] {ECO:0000313|EMBL:KIF73670.1, ECO:0000313|Proteomes:UP000031584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=150FB {ECO:0000313|EMBL:KIF73670.1,
RC ECO:0000313|Proteomes:UP000031584};
RA Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT 150.";
RL Submitted (NOV-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}.
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:KIF73670.1}.
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DR EMBL; JTHL01000001; KIF73670.1; -; Genomic_DNA.
DR RefSeq; WP_040020142.1; NZ_JTHL01000001.1.
DR AlphaFoldDB; A0A0C2AXN4; -.
DR STRING; 1576605.QR77_06100; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000031584; 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:KIF73670.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031584}.
FT DOMAIN 2..131
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 176..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 217
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 229..233
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 261
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 359..361
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 293
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 346
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 369
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 451 AA; 50069 MW; 77A01714144AD220 CRC64;
MSVAVLLFTS DLRVHDQPAL RAALRDAREV VPLFVLDEGV RAAGFDAPNR RAFLADCLAS
LDAGLRDRGG RLVVRSGDVV ERVREVVEET GARRVHVAAG VSGYAARREE RLRTELEGSG
RGLDVHDAVI TAVPPGQVTP AGNDHFAVFT PYFRRWRESG QRQVTAAPRT VRVPAIDSDP
LPVRDDIAGT SPGLARGGED VGRELLSGWM GDGIASYEDR HDDLPGDATS RLSPYIHFGA
LSPVELTHRA RRVGGAGADA FVRQLAWRDF HHQVLAARPE AAWSDYRARG DRWRTDEDEA
AAWRAGRTGY PVVDAAMRQL LHEGWMHNRA RLLVASFLTK TLYLDWRVGA RHFLDLLVDA
DLANNQLNWQ WAAGTGTDTR PNRVLNPLTQ ARRFDPRGDY VRRWVPELAE VAGAAVHQPW
TLKGPDRARL DYPDPIVDLA EGRDRFLRAR G
//
