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Database: UniProt
Entry: A0A1U7V7I6_NICSY
LinkDB: A0A1U7V7I6_NICSY
Original site: A0A1U7V7I6_NICSY 
ID   A0A1U7V7I6_NICSY        Unreviewed;       566 AA.
AC   A0A1U7V7I6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=(6-4)DNA photolyase isoform X1 {ECO:0000313|RefSeq:XP_009764097.1};
GN   Name=LOC104215867 {ECO:0000313|RefSeq:XP_009764097.1};
OS   Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009764097.1};
RN   [1] {ECO:0000313|Proteomes:UP000189701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA   Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA   Peitsch M.C., Ivanov N.V.;
RT   "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT   tomentosiformis.";
RL   Genome Biol. 14:R60.1-R60.17(2013).
RN   [2] {ECO:0000313|RefSeq:XP_009764097.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_009764097.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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 class-1 family.
CC       {ECO:0000256|ARBA:ARBA00005862}.
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DR   RefSeq; XP_009764097.1; XM_009765795.1.
DR   AlphaFoldDB; A0A1U7V7I6; -.
DR   STRING; 4096.A0A1U7V7I6; -.
DR   GeneID; 104215867; -.
DR   KEGG; nsy:104215867; -.
DR   eggNOG; KOG0133; Eukaryota.
DR   OrthoDB; 124765at2759; -.
DR   Proteomes; UP000189701; Unplaced.
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; 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   SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR   SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW   1}; Reference proteome {ECO:0000313|Proteomes:UP000189701}.
FT   DOMAIN          32..170
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         284..288
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         325..332
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         423..425
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            356
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            410
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            433
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   566 AA;  64304 MW;  C62A19350120BAFF CRC64;
     MLAISPTHST RLTLVNTPHC KSNFISTMAS GSNSLMWFRK GLRLHDNPAL EYAAKGSKFL
     YPVFVIDPHY MELDPTAFSP GSSKAGLNRI QFLLECLVDL DLSLSKLGSR LLVLKGDPGE
     VLTRCWKEWS IGKLCFEYDT EPYYQALDVK VKNHASVAGV EIFSPVSHTL YNPADIINKN
     GGSPPLTYQS FLKLAGQPSW ASTPLSTTIS SLPPIGNTGN FAVSGVPTVK ELGYEDLNED
     ERTPFKGGES EALKRLRESI ANKEWVANFE KPKGDPSAFM KPATTVLSPY LKFGCLSSRY
     FYQCIQDIQK SVKKHTSPPV SLLGQLLWRD FFYTVSFGTP NFDQMKGNRI CKQIPWKNDD
     ELLAAWRDSR TGFPWIDAIM AQLRKCGWMH HLARHSVACF LTRGDLFVHW EKGRDVFDRL
     LIDSDWAINN GNWLWLSCSS FFYQYHRIYS PTSFGKKYDP AGNYIRHFLP VLKDMPKEYI
     YEPWTAPLSV QRKARCIIGL DYPNPVVSHD SASKECRMRL GEAYELNKKL NGRVSEEDLN
     KLRRKNDNES AIVDSISRKK KQKLIC
//
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