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Database: UniProt
Entry: I1JUL6_SOYBN
LinkDB: I1JUL6_SOYBN
Original site: I1JUL6_SOYBN 
ID   I1JUL6_SOYBN            Unreviewed;       584 AA.
AC   I1JUL6;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Cryptochrome DASH {ECO:0000256|RuleBase:RU367151};
GN   Name=100783312 {ECO:0000313|EnsemblPlants:KRH61917};
GN   ORFNames=GLYMA_04G074500 {ECO:0000313|EMBL:KRH61917.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH61917.1};
RN   [1] {ECO:0000313|EMBL:KRH61917.1, ECO:0000313|EnsemblPlants:KRH61917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH61917};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH61917.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH61917}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH61917};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH61917.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH61917.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May have a photoreceptor function.
CC       {ECO:0000256|RuleBase:RU367151}.
CC   -!- COFACTOR:
CC       Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC         Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|RuleBase:RU367151};
CC       Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
CC       {ECO:0000256|RuleBase:RU367151};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602081-1,
CC         ECO:0000256|RuleBase:RU367151};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR602081-1,
CC       ECO:0000256|RuleBase:RU367151};
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000256|ARBA:ARBA00005862, ECO:0000256|RuleBase:RU367151}.
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DR   EMBL; CM000837; KRH61917.1; -; Genomic_DNA.
DR   RefSeq; XP_003522656.2; XM_003522608.3.
DR   AlphaFoldDB; I1JUL6; -.
DR   SMR; I1JUL6; -.
DR   STRING; 3847.I1JUL6; -.
DR   PaxDb; 3847-GLYMA04G07870-1; -.
DR   EnsemblPlants; KRH61917; KRH61917; GLYMA_04G074500.
DR   GeneID; 100783312; -.
DR   Gramene; KRH61917; KRH61917; GLYMA_04G074500.
DR   KEGG; gmx:100783312; -.
DR   eggNOG; KOG0133; Eukaryota.
DR   InParanoid; I1JUL6; -.
DR   OMA; LIFELLW; -.
DR   OrthoDB; 124765at2759; -.
DR   Proteomes; UP000008827; Chromosome 4.
DR   ExpressionAtlas; I1JUL6; baseline and differential.
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:0000719; P:photoreactive repair; IBA:GO_Central.
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; IPR014133; Cry_DASH.
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; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR02765; crypto_DASH; 1.
DR   PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR   PANTHER; PTHR11455:SF22; CRYPTOCHROME DASH; 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; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   Chromophore {ECO:0000256|RuleBase:RU367151};
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:UP000008827}.
FT   DOMAIN          90..225
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         335
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         348..352
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         388..395
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         485..487
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            419
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            472
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            495
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   584 AA;  66584 MW;  4CFBC09C4D1895E9 CRC64;
     MAILHCTSLP FLSLRTTISS SKSTLTSTRI PLFLAMNSFA KSEPVSSSAS SSSSTYQQVP
     EQDANNDLDR VADNTFRRYT SNVTKGSGKG TAIVWFRNDL RVLDNEALYK AWLSSETVLP
     VYCVDPRLFA TTYHFGFPKT GALRAQFLLE CLADLRKNLM KRGLNLLVQH GKPEEILPSL
     AKSFQAHTVY AQKETCSEEL NVERLVMRGL KQVVTSPEES SGITVSNNIP KLQLVWGTTM
     YHLDDLPFDA TSLPDVYTQF RKLVETKCTI RSCIKLPASL GPPPTVQDWG CLPSLEQLGL
     SSQSVNKGMK FVGGETAALS RVYEYFWKKD LLRVYKETRN GMLGPDYSTK FSPWLASGSL
     SPRFIYEEVK RYENDRLANS STYWVLFELI WRDYFRFLSV KYGNSLFHLG GPRKVQRNWS
     QDKNLFESWR DGCTGYPLID ANMKELSTTG FMSNRGRQIV CSFLVRDMGI DWRMGAEWFE
     TCLLDYDPCS NYGNWTYGSG VGNDPREDRY FSIPKQAQTY DPEGEYVAYW LPQLRKIPKE
     KRNFPGNLIY IPQIVPLKFG TTSGHNKDKF FGARRTNDRG SKRR
//
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