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Database: UniProt
Entry: D7LGP6_ARALL
LinkDB: D7LGP6_ARALL
Original site: D7LGP6_ARALL 
ID   D7LGP6_ARALL            Unreviewed;       448 AA.
AC   D7LGP6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Photolyase/blue-light receptor 2 {ECO:0000313|EMBL:EFH56573.1};
GN   Name=PHR2 {ECO:0000313|EMBL:EFH56573.1};
GN   ORFNames=ARALYDRAFT_483939 {ECO:0000313|EMBL:EFH56573.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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   EMBL; GL348716; EFH56573.1; -; Genomic_DNA.
DR   RefSeq; XP_002880314.1; XM_002880268.1.
DR   AlphaFoldDB; D7LGP6; -.
DR   STRING; 81972.D7LGP6; -.
DR   EnsemblPlants; fgenesh2_kg.4__2999__AT2G47590.1; fgenesh2_kg.4__2999__AT2G47590.1; fgenesh2_kg.4__2999__AT2G47590.1.
DR   Gramene; fgenesh2_kg.4__2999__AT2G47590.1; fgenesh2_kg.4__2999__AT2G47590.1; fgenesh2_kg.4__2999__AT2G47590.1.
DR   eggNOG; KOG0133; Eukaryota.
DR   HOGENOM; CLU_010348_0_0_1; -.
DR   OrthoDB; 124765at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR   InterPro; IPR036155; Crypto/Photolyase_N_sf.
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:SF2; BLUE-LIGHT PHOTORECEPTOR PHR2; 1.
DR   PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR   Pfam; PF00875; DNA_photolyase; 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|PIRSR:PIRSR602081-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR602081-1};
KW   Lyase {ECO:0000313|EMBL:EFH56573.1};
KW   Receptor {ECO:0000313|EMBL:EFH56573.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT   DOMAIN          116..250
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         365..369
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         414..421
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ   SEQUENCE   448 AA;  49014 MW;  E5710086B322C831 CRC64;
     MDSNLEEKNL NPETKSAEEE NPLAIIHSSL PIASLSLTLF PTSTQFLKLF SHHPNKVKIP
     TQASSLTHLS LSSSPVSPLP SRISFKSTIA ANPLHSPLSI VPRRPVDPSS AAALRRAAVV
     WFRNDLRVHD NECLNSANDE CVSVLPVYCF DPRDYGKSSS GFDKTGPFRA QFLIESVSEL
     RKNLQARGSN LVVRVGKPEA VLVELAKEIG ADAVYAHREV SHDEVKAEGK IESAMKEEGV
     EVKYFWGSTL YHLDDLPFKI EDLPSNYGAF KDKVHKLEIR KTIAALDQLK SLPSRGDVEL
     GDIPSLLDLG ISPTARTSQE GKPTMVGGET EALTRLKSFA ADCQARLSKG NQKGGNNSVF
     GANFSCKISP WLAMGSISPR SMFDELKKTI SASTTTTTPR NGPGDTGLNW LMYELLWRDF
     FRFITKKYSS AKTQVEAGPA TACTGAFV
//
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