ID   O82779_ADICA            Unreviewed;       718 AA.
AC   O82779;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Blue-light photoreceptor {ECO:0000313|EMBL:BAA32809.1};
GN   Name=CRY3 {ECO:0000313|EMBL:BAA32809.1};
OS   Adiantum capillus-veneris (Maidenhair fern).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC   Vittarioideae; Adiantum.
OX   NCBI_TaxID=13818 {ECO:0000313|EMBL:BAA32809.1};
RN   [1] {ECO:0000313|EMBL:BAA32809.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Protonemata {ECO:0000313|EMBL:BAA32809.1};
RX   PubMed=9790588; DOI=10.1007/s004380050821;
RA   Kanegae T., Wada M.;
RT   "Isolation and characterization of homologues of plant blue-light
RT   photoreceptor (cryptochrome) genes from the fern Adiantum capillus-
RT   veneris.";
RL   Mol. Gen. Genet. 259:345-353(1998).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB012628; BAA32809.1; -; mRNA.
DR   EMBL; AB012631; BAA32812.1; -; Genomic_DNA.
DR   AlphaFoldDB; O82779; -.
DR   GO; GO:0009882; F:blue light photoreceptor activity; IEA:InterPro.
DR   GO; GO:0097159; F:organic cyclic compound binding; 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; IPR014134; Cryptochrome_pln.
DR   InterPro; IPR018394; DNA_photolyase_1_CS_C.
DR   InterPro; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR02766; crypt_chrom_pln; 1.
DR   PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR   PANTHER; PTHR11455:SF18; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE, MITOCHONDRIAL; 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   2: Evidence at transcript level;
KW   Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW   1}; Receptor {ECO:0000313|EMBL:BAA32809.1}.
FT   DOMAIN          4..133
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          616..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..646
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         230
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         242..246
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         285
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         385..387
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            319
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            372
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            395
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   718 AA;  80290 MW;  B89CAFE321EE42BC CRC64;
     MAKSCTVVWF RRDLRLEDNP ALAAAARAGA VVPVFIWSPD EEGQFRPGRV SRWWLKQSLI
     QLDISLRSLG VSLVMINAND TVSALLELVK TTGASQVVYN HLYDPVSLVR DHRVKQSLVQ
     NGIQVQSFNG DLLYEPWEVL DDHGKPFTYF ESYWAKCLTM PFEPESPLLP PRRLTAAPAG
     IVHSLTPDEL GLEDEADKSS NALLARAWAP GWSNADKALE AFLAGPFLNY SRNRHEIDGP
     TTSLLSPHLH FGEVSVRKVF HSVRRLQVLW AKDGSMLGEE SINYFMRSIG FREYSRYLCF
     NFPFTHERSL LSNLKSFPWR VDEGLFKAWR QGRTGYPLVD AGMRELWATG WLHNRVRVIV
     SSFCVKFLQL PWRWGMKYFW DTLLDADLES DILGWQYISG SLPDGHELDR MDNPQTEGYK
     HDPLGEYVRR WLPELVRLPT EWIHHPWDAP PGVLRAAGVE LGSNYPRPVV EVAAARERLR
     DAVTHMWEQE AALKAAGDKG IEEASVGDSI AKVNCQPEVA AQPCKIPKAS VSQATNGDME
     VSSAGSSRRD QMVPTFAKEL KTQADALCGD YGSIALPLPS QQNLPCPSTN FSAIRGVSKL
     SPGNRGDMVD TTEALRNTHS EPLPPVSDTN PMTESSSSSS PREQISSIKD DPPMIWVPAI
     AHQRPSSDFG CVPYAGDAEQ LRKHLLILQN ARTDDKVEDG VQLNGSQWAR GSKRKAKS
//