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Database: UniProt
Entry: A0A0B2P8F8_GLYSO
LinkDB: A0A0B2P8F8_GLYSO
Original site: A0A0B2P8F8_GLYSO 
ID   A0A0B2P8F8_GLYSO        Unreviewed;       682 AA.
AC   A0A0B2P8F8;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Cryptochrome-1 {ECO:0000313|EMBL:KHN03902.1, ECO:0000313|EMBL:RZC06782.1};
DE   SubName: Full=Cryptochrome-1 isoform B {ECO:0000313|EMBL:RZC06783.1};
DE   SubName: Full=Cryptochrome-1 isoform C {ECO:0000313|EMBL:RZC06784.1};
DE   SubName: Full=Cryptochrome-1 isoform D {ECO:0000313|EMBL:RZC06785.1};
GN   ORFNames=D0Y65_014293 {ECO:0000313|EMBL:RZC06782.1}, glysoja_045678
GN   {ECO:0000313|EMBL:KHN03902.1};
OS   Glycine soja (Wild soybean).
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=3848 {ECO:0000313|EMBL:KHN03902.1};
RN   [1] {ECO:0000313|EMBL:KHN03902.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Root {ECO:0000313|EMBL:KHN03902.1};
RA   Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT   "Identification of a novel salt tolerance gene in wild soybean by whole-
RT   genome sequencing.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RZC06782.1, ECO:0000313|Proteomes:UP000289340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC   TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZC06782.1};
RA   Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT   "A high-quality reference genome of wild soybean provides a powerful tool
RT   to mine soybean genomes.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KN669632; KHN03902.1; -; Genomic_DNA.
DR   EMBL; QZWG01000006; RZC06782.1; -; Genomic_DNA.
DR   EMBL; QZWG01000006; RZC06783.1; -; Genomic_DNA.
DR   EMBL; QZWG01000006; RZC06784.1; -; Genomic_DNA.
DR   EMBL; QZWG01000006; RZC06785.1; -; Genomic_DNA.
DR   SMR; A0A0B2P8F8; -.
DR   OrthoDB; 124765at2759; -.
DR   Proteomes; UP000053555; Unassembled WGS sequence.
DR   Proteomes; UP000289340; Chromosome 6.
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; IPR020978; Cryptochrome_C.
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:SF50; CRYPTOCHROME-1; 1.
DR   Pfam; PF12546; Cryptochrome_C; 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; PS00691; DNA_PHOTOLYASES_1_2; 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:UP000289340}.
FT   DOMAIN          6..135
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          492..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..569
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         229
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         241..245
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         284
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         384..386
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            318
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            371
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            394
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   682 AA;  77041 MW;  054A4084165D65C8 CRC64;
     MSGGGCSSIV WFRRDLRIED NPALTAGVRA GAVVAVFIWA PEEEGQYYPG RVSRWWLKNS
     LAHLDSSLRN LGTPLITKRS TDTLSSLFEV VKSTGATQLF FNHLYDPLSL VRDHRAKEVL
     TAQGITVRSF NADLLYEPWD VNDAHGRPFT TFAAFWERCL SMPYDPESPL LPPKRIIPGD
     ASRCPSDTLL FEDELEKASN ALLARAWSPG WSNANKALTT FINGPLIEYS KNRRKADSAT
     TSLLSPHLHF GELSVKKVFH LVRIKQVLWA NEGNKAGEES VNLFLKSIGL REYSRYISFN
     HPYSHERPLL GHLKFFPWVV NEGYFKAWRQ GRTGYPLVDA GMRELWATGW LHDRIRVVVS
     SFFVKVLQLP WRWGMKYFWD TLLDADLESD ALGWQYISGS LPDGREIDRI DNPQFEGYKF
     DPNGEYVRRW LPELSRLPTE WIHHPWNAPE SVLQAAGIEL GSNYPLPIVG IDAAKNRLLE
     ALSKMWQQEA ASRAAMENGT EEGLGDSSES VPAAFPQDTR MEETHEPVRN NPLPIARRYQ
     DQMVPSITSS LLRVEEEETS SDLRNSAEES SRAEVPVTAN AQQNAGVALN ERMLQTTNRN
     TQTQYNTTMD LRNVADDSAV ESSSGTRRER DGGLVPVWSP PASSYSEQFV GDENGITSSS
     SYLQRHPQSH QMLNWKQLPQ TG
//
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