ID A0A1C5EY24_9ACTN Unreviewed; 257 AA.
AC A0A1C5EY24;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:SCG00189.1};
DE Flags: Fragment;
GN ORFNames=GA0115259_1068610 {ECO:0000313|EMBL:SCG00189.1};
OS Streptomyces sp. MnatMP-M17.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839780 {ECO:0000313|EMBL:SCG00189.1, ECO:0000313|Proteomes:UP000198886};
RN [1] {ECO:0000313|EMBL:SCG00189.1, ECO:0000313|Proteomes:UP000198886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MnatMP-M17 {ECO:0000313|EMBL:SCG00189.1,
RC ECO:0000313|Proteomes:UP000198886};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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}.
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DR EMBL; FMDK01000652; SCG00189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5EY24; -.
DR Proteomes; UP000198886; 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 InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR InterPro; IPR018394; DNA_photolyase_1_CS_C.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF9; CRYPTOCHROME-1; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 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:SCG00189.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198886}.
FT DOMAIN 64..252
FT /note="Cryptochrome/DNA photolyase FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03441"
FT BINDING 20
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 32..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 64
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 163..165
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:SCG00189.1"
SQ SEQUENCE 257 AA; 29456 MW; E438898576524890 CRC64;
GESEGRRRLR SWLAGPLARY ADLHDDLAAD ATSRLSPYLH FGCLSPVELL DRVRALGGPG
AHAFVRQLAW RDFHHQVLAA RPDAARHDYR PRRHNRRRRN AEEIRAWQEG RTGYPVVDAA
MRQLRYEGWM PGRARLLTAS FLTKTLCADW RVGAGYFLEL LVDGDVANNQ LNWQWMAGTG
TDTRPNRVLN PLVQARRFDP GGEYVRHWLP ELRDLDAASV HRLARPGETL RTATDYPPPI
VDLTEATDRF ARHRRTD
//
