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Database: UniProt
Entry: A0A078IZQ8_BRANA
LinkDB: A0A078IZQ8_BRANA
Original site: A0A078IZQ8_BRANA 
ID   A0A078IZQ8_BRANA        Unreviewed;       713 AA.
AC   A0A078IZQ8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=(rape) hypothetical protein {ECO:0000313|EMBL:CAF2043360.1};
DE   SubName: Full=BnaAnng13370D protein {ECO:0000313|EMBL:CDY54706.1};
GN   Name=BnaAnng13370D {ECO:0000313|EMBL:CDY54706.1};
GN   ORFNames=DARMORV10_A09P29920.1 {ECO:0000313|EMBL:CAF2043360.1},
GN   GSBRNA2T00014520001 {ECO:0000313|EMBL:CDY54706.1};
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY54706.1, ECO:0000313|Proteomes:UP000028999};
RN   [1] {ECO:0000313|EMBL:CDY54706.1, ECO:0000313|Proteomes:UP000028999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX   PubMed=25146293; DOI=10.1126/science.1253435;
RA   Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA   Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA   Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA   Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA   Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA   Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA   Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA   Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA   Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA   Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA   Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA   Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA   Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT   "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT   Brassica napus oilseed genome.";
RL   Science 345:950-953(2014).
RN   [2] {ECO:0000313|EMBL:CDY54706.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CAF2043360.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope - CEA;
RA   William W.;
RL   Submitted (JAN-2021) 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; HG994363; CAF2043360.1; -; Genomic_DNA.
DR   EMBL; LK033344; CDY54706.1; -; Genomic_DNA.
DR   STRING; 3708.A0A078IZQ8; -.
DR   PaxDb; 3708-A0A078IZQ8; -.
DR   EnsemblPlants; CDY54706; CDY54706; GSBRNA2T00014520001.
DR   Gramene; CDY54706; CDY54706; GSBRNA2T00014520001.
DR   OMA; KYFPWVV; -.
DR   Proteomes; UP000028999; Unassembled WGS sequence.
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; 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:UP000028999}.
FT   DOMAIN          10..139
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          550..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..571
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         234
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         246..250
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         289
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         389..391
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            323
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            376
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            399
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   713 AA;  80285 MW;  E17E2F0A214361D1 CRC64;
     MSNSCSGGGG CSIVWFRRDL RVEDNPALAA AVRAGPVIAV FVWAPEEEGH YQPGRVSRWW
     LKNSLAQLDS SLRSLGTCLI TKRSTDSVAS LLEVVKSTGA SQIFFNHLYD PLSLVRDHRA
     KDALTAEGIA VKSFNADLLY EPWEVTDELG RPFSMFAAFW ERCLSMPYDP ESPLLPPKKI
     ISAGDVSKCV ADTLIFEDES EKGSNALLAR AWSPGWSNAD KALTTFINGP LIEYSKNRRK
     ADSATTSFLS PHLHFGEVSV RKVFHLLRIK QVAWANEGNQ AGEESVNLFL KSIGLREYSR
     YISFNHPYSH ERPLLGHLKF FPWAVDENYF KAWRQGRTGY PLVDAGMREL WATGWLHDRI
     RVVVSSFFVK VLQLPWRWGM KYFWDTLLDA DLESDALGWQ YITGTLPDSR EFDRIDNPQF
     EGYKFDPNGE YVRRWLPELS RLPTEWIHHP WNAPESVLQA AGIELGSNYP RPIVGLDEAK
     ARLHEALSQM WQLEAASRAA IENGSEEGLG DSTEFVEAPI EFPRDITMEE TEPTRLNPVR
     RYEDQMVPSI TTSLIRPEED QESSLSLRNS GGDSRAEVPR NMVNTNQARQ QEARADPVSN
     QVTAMIPEFN IRIVAENTEE STAESSSSGR RERDGGIVPE WSGYSEQFAS EENGIGGGST
     TSSYLQNHHE IVNWRRLSQT GVDFNVQKTF CGLSDFTGNE AQGEELHKDC NSG
//
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