ID U5YDB9_ATHFF Unreviewed; 171 AA. AC U5YDB9; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 29-MAY-2024, entry version 23. DE SubName: Full=Cryptochrome 2 {ECO:0000313|EMBL:AGZ88133.1}; DE Flags: Fragment; GN Name=CRY2 {ECO:0000313|EMBL:AGZ88133.1}; OS Athyrium filix-femina (Lady fern) (Polypodium filix-femina). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Polypodiopsida; Polypodiidae; Polypodiales; Aspleniineae; Athyriaceae; OC Athyrium; Athyrium sect. Athyrium. OX NCBI_TaxID=32110 {ECO:0000313|EMBL:AGZ88133.1}; RN [1] {ECO:0000313|EMBL:AGZ88133.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24116189; RA Rothfels C.J., Larsson A., Li F.-W., Sigel E.M., Huiet L., Burge D.O., RA Ruhsam M., Graham S.W., Stevenson D.W., Wong G.K., Korall P., Pryer K.M.; RT "Transcriptome-mining for single-copy nuclear markers in ferns."; RL PLoS ONE 8:E76957-E76957(2013). 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; KF553757; AGZ88133.1; -; Genomic_DNA. DR AlphaFoldDB; U5YDB9; -. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. DR GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:TreeGrafter. DR GO; GO:0003677; F:DNA binding; IEA:TreeGrafter. DR GO; GO:0071949; F:FAD binding; IEA:TreeGrafter. DR GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt. DR GO; GO:0032922; P:circadian regulation of gene expression; IEA:TreeGrafter. DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IEA:TreeGrafter. 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 InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf. DR InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd. DR InterPro; IPR002081; Cryptochrome/DNA_photolyase_1. DR InterPro; IPR018394; DNA_photolyase_1_CS_C. DR PANTHER; PTHR11455; CRYPTOCHROME; 1. DR PANTHER; PTHR11455:SF18; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE, MITOCHONDRIAL; 1. DR Pfam; PF03441; FAD_binding_7; 1. DR PRINTS; PR00147; DNAPHOTLYASE. DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1. DR PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1. PE 3: Inferred from homology; 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}. FT DOMAIN 83..171 FT /note="Cryptochrome/DNA photolyase FAD-binding" FT /evidence="ECO:0000259|Pfam:PF03441" FT BINDING 28 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1" FT BINDING 40..44 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1" FT BINDING 83 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AGZ88133.1" FT NON_TER 171 FT /evidence="ECO:0000313|EMBL:AGZ88133.1" SQ SEQUENCE 171 AA; 20086 MW; 4E9B3AB68F0243EF CRC64; LLARAWAPGW ANADRALESF INGSLMEYAV NRQKVDSATT SLLSPHLHYG ELSVRKIFHN IRMKQVLWVK EGKVEAEDSV NLFLRSIGFR EYSRYLSFNF PFTHERSLLS NLKFFPWRVD EGYFKAWRQG RTGYPLVDAG MRELWATGWL HNQIRVIVSS FCVKFLQLPW R //