ID   CRY1_SINAL              Reviewed;         501 AA.
AC   P40115;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Cryptochrome-1;
DE   AltName: Full=Blue light photoreceptor;
GN   Name=PHR1;
OS   Sinapis alba (White mustard) (Brassica hirta).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Sinapis.
OX   NCBI_TaxID=3728;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8252071; DOI=10.1046/j.1365-313x.1993.04040705.x;
RA   Batschauer A.;
RT   "A plant gene for photolyase: an enzyme catalyzing the repair of UV-light-
RT   induced DNA damage.";
RL   Plant J. 4:705-709(1993).
RN   [2]
RP   FUNCTION.
RX   PubMed=7756321; DOI=10.1021/bi00020a037;
RA   Malhotra K., Kim S.-T., Batschauer A., Dawut L., Sancar A.;
RT   "Putative blue-light photoreceptors from Arabidopsis thaliana and Sinapis
RT   alba with a high degree of sequence homology to DNA photolyase contain the
RT   two photolyase cofactors but lack DNA repair activity.";
RL   Biochemistry 34:6892-6899(1995).
CC   -!- FUNCTION: Mediates blue light-induced gene expression in addition to
CC       its role in blue light-dependent inhibition of stem growth.
CC       {ECO:0000250, ECO:0000269|PubMed:7756321}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC       Note=Binds 1 FAD per subunit.;
CC   -!- COFACTOR:
CC       Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC         Xref=ChEBI:CHEBI:15636;
CC       Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INDUCTION: By visible light.
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be a DNA photolyase.
CC       {ECO:0000305|PubMed:8252071}.
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DR   EMBL; X72019; CAA50898.1; -; mRNA.
DR   PIR; S48120; S48120.
DR   AlphaFoldDB; P40115; -.
DR   SMR; P40115; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009882; F:blue light photoreceptor activity; IEA:InterPro.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
DR   Gene3D; 3.40.50.620; -; 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   PANTHER; PTHR11455; PTHR11455; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   PRINTS; PR00147; DNAPHOTLYASE.
DR   SUPFAM; SSF48173; SSF48173; 1.
DR   SUPFAM; SSF52425; SSF52425; 1.
DR   TIGRFAMs; TIGR02766; crypt_chrom_pln; 1.
DR   PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR   PROSITE; PS00691; DNA_PHOTOLYASES_1_2; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chromophore; FAD; Flavoprotein; Nucleotide-binding;
KW   Photoreceptor protein; Receptor; Sensory transduction.
FT   CHAIN           1..501
FT                   /note="Cryptochrome-1"
FT                   /id="PRO_0000085123"
FT   DOMAIN          5..134
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT   BINDING         231
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         243..247
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         356
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         386
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         388
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         405
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   501 AA;  57022 MW;  C6B25CE0A33890DB CRC64;
     MSTNKKTIVW FRRDLRIEDN PALAAAAHEG SVFPVFIWCP EEEGQFYPGR ASRWWMKQSL
     AHLRQSLKAL GSELTLIKTH STVSAILDCV RATGATKVVF NHLYDPVSLV RDHTVKEKLV
     ERGISVQSYN GDLCMSPGRY TVKRANLLLV LILTGKKCLD MSVESVVLPP PWRLMPLSAA
     ETVWACSVEE LGLENEAEKP SNALLTRAWS PGWSNADKIL NEFIEKQLID YAKNSKKVVG
     NSTSLLSPYL HFGEISVRRV FQCARMKQII WARDKNGEGE ESADLFLRGI GLRDYSRIIC
     FNFPFTHEQS LLSHLRFFPW DADVDKFKAW RQGRTGYPLV DAGMRELWAT GWMHNRIRVI
     VSSFAVKFLL LPWKWGMKYF WDTLLDADLE CDIIGWQYIS GSLPDGHELD RLDNPAIQGA
     KYDPEGEYIR QWLPELARLP TEWIHHPWDA PLTVLKASGV ELGTNYAKPI VVIDTARELL
     TKAISRTREA QIMIGACGDE M