ID J7L971_NOCAA Unreviewed; 437 AA.
AC J7L971;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=FAD binding domain of DNA photolyase family protein {ECO:0000313|EMBL:AFR10203.1};
GN OrderedLocusNames=B005_1517 {ECO:0000313|EMBL:AFR10203.1};
OS Nocardiopsis alba (strain ATCC BAA-2165 / BE74).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1205910 {ECO:0000313|EMBL:AFR10203.1, ECO:0000313|Proteomes:UP000003779};
RN [1] {ECO:0000313|EMBL:AFR10203.1, ECO:0000313|Proteomes:UP000003779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RX PubMed=23105086; DOI=10.1128/JB.01522-12;
RA Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT "Whole-Genome Sequence of Nocardiopsis alba Strain ATCC BAA-2165,
RT Associated with Honeybees.";
RL J. Bacteriol. 194:6358-6359(2012).
RN [2] {ECO:0000313|Proteomes:UP000003779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RA Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT "Whole-genome sequence of Nocardiopsis alba strain ATCC BAA-2165 associated
RT with honeybees.";
RL Submitted (AUG-2012) 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; CP003788; AFR10203.1; -; Genomic_DNA.
DR RefSeq; WP_014912657.1; NC_018524.1.
DR AlphaFoldDB; J7L971; -.
DR STRING; 1205910.B005_1517; -.
DR KEGG; nal:B005_1517; -.
DR PATRIC; fig|1205910.3.peg.1433; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_2_2_11; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000003779; 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; 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:AFR10203.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003779}.
FT DOMAIN 3..126
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 408..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 228..232
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 258
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 356..358
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 290
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 343
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 366
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 437 AA; 48790 MW; DB7B854C6E3A59D1 CRC64;
MGTPVLVLFT QDLRLHDHPA LTAALEESET VVPLFVLEPG LLRRAARNRR AYLTEALADL
RSGLRDLGGD LVLRRGDTTT EVRVLARETG ARAVHLGGGV SRFAARREAA LRATDLEVRV
HPGPTIVPPG AITPAKGDHY KVFTPYWRAW EAEERRKIRT APARVRPPEG IDPGPLPDLD
AEPGGIGALA PERTRGGPTR ARERLRRWID RGLADYPDRH DDLPGAATSH LSADLRFGCL
SPLEVEAAAR DLPGGPEYVR QLAWRDFHHQ VTAAFPEIAT RDYRPRDREW RHDPEALEAW
KEGRTGVPIV DAGMRQLLAE GFMHNRTRMI TAAFLTRTLR VHWREGAAHF DAHLTDGDVA
DEYGNWQWVA GTGNDTRPNR AFNPLRQARR FDPEGEYVRR HLPELAGLPG RRAHTPWEEA
EGEGTAGYPR PIADPGR
//
