GenomeNet

Database: UniProt
Entry: K3XVT1_SETIT
LinkDB: K3XVT1_SETIT
Original site: K3XVT1_SETIT 
ID   K3XVT1_SETIT            Unreviewed;       642 AA.
AC   K3XVT1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Photolyase/cryptochrome alpha/beta domain-containing protein {ECO:0000259|PROSITE:PS51645};
GN   Name=101782687 {ECO:0000313|EnsemblPlants:KQL10631};
OS   Setaria italica (Foxtail millet) (Panicum italicum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX   NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQL10631, ECO:0000313|Proteomes:UP000004995};
RN   [1] {ECO:0000313|EnsemblPlants:KQL10631, ECO:0000313|Proteomes:UP000004995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL10631,
RC   ECO:0000313|Proteomes:UP000004995};
RX   PubMed=22580951; DOI=10.1038/nbt.2196;
RA   Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA   Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA   Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA   Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA   Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA   Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT   "Reference genome sequence of the model plant Setaria.";
RL   Nat. Biotechnol. 30:555-561(2012).
RN   [2] {ECO:0000313|EnsemblPlants:KQL10631}
RP   IDENTIFICATION.
RC   STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL10631};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) 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}.
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; AGNK02002452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004965414.1; XM_004965357.3.
DR   AlphaFoldDB; K3XVT1; -.
DR   SMR; K3XVT1; -.
DR   STRING; 4555.K3XVT1; -.
DR   EnsemblPlants; KQL10631; KQL10631; SETIT_006039mg.
DR   GeneID; 101782687; -.
DR   Gramene; KQL10631; KQL10631; SETIT_006039mg.
DR   KEGG; sita:101782687; -.
DR   eggNOG; KOG0133; Eukaryota.
DR   InParanoid; K3XVT1; -.
DR   OMA; ETLIDWD; -.
DR   OrthoDB; 124765at2759; -.
DR   Proteomes; UP000004995; Chromosome IV.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0009882; F:blue light photoreceptor activity; IEA:InterPro.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IBA:GO_Central.
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   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}; Reference proteome {ECO:0000313|Proteomes:UP000004995}.
FT   DOMAIN          5..135
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          533..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         233
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         245..249
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         288
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         388..390
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            322
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            375
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            398
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   642 AA;  72808 MW;  F17623AE551D58D6 CRC64;
     MSRSEKTVVW FRRDLRIDDN PALATAAKEG SVLPLFIWCP ADYKQYYPGR CSRWWLKQSL
     GHLRKSLESL GCPLILIHAE DSTLAALLES VHSTGATRVV YNRLYDPISL VHDDKIKNEL
     SALGISVQSF NGDLLYEPWE VYDENGQAFT TFNMYWEKCM NLPLDISQPL APVRLVPVPG
     IDNVRGCSID DLGLESSKDE ESSNALLSRA WSPGWCNAEN TLQEFVSYGL LEYSKHGMKV
     GGTTTSLLSP YLHFGELSVR KVYQLVKMHQ VKCENEGKSE AEESVQLFLR SIGFREYSRY
     LCFNFPFTHE RSLLGNLKHY PWRSDEDRFK SWRQGMTGYP LVDAGMRELW ATGWTHNRIR
     VIVSSFAVKF LQIPWIWGMK YFWDVLLDAD LESDILGWQY ISGSLPDGHE LSRLDNPEVQ
     GQKYDPDGEY IRTWIPELAR MPTEWIHCPW DAPSSILEVA GVELSFNYPK PIVELHMARE
     CLDDAISTMW QLDTAAKLAE LDGEVVEDNM NNIRSFDIPK VVLKKELSPS TSSIYQRMPS
     SSGQKKKLQP MEVTNASNME DTGSTAKSQV SRKRSSGDSA FNVPSCSSSL IMHSRIPDPD
     SCFVLYSDYL QQKAERNGAG KVEDNDSEDS GTSISRPSKR AA
//
DBGET integrated database retrieval system