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UVR3_ORYSJ
ID   UVR3_ORYSJ              Reviewed;         551 AA.
AC   Q0E2Y1; A0A0P0VG67; B9F3X5; Q6Z6D9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=(6-4)DNA photolyase;
DE            EC=4.1.99.13;
GN   Name=UVR3; OrderedLocusNames=Os02g0204400, LOC_Os02g10990;
GN   ORFNames=OSJNBb0056C19.3, P0544H11.19;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Involved in repair of UV radiation-induced DNA damage.
CC       Catalyzes the photoreactivation of pyrimidine [6-4] pyrimidone
CC       photoproduct (6-4 products) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA).;
CC         EC=4.1.99.13;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD16007.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAD38427.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP005008; BAD16007.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP005915; BAD38427.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008208; BAF08157.2; -; Genomic_DNA.
DR   EMBL; AP014958; BAS77547.1; -; Genomic_DNA.
DR   EMBL; CM000139; EEE56527.1; -; Genomic_DNA.
DR   RefSeq; XP_015623929.1; XM_015768443.1.
DR   AlphaFoldDB; Q0E2Y1; -.
DR   SMR; Q0E2Y1; -.
DR   STRING; 4530.OS02T0204400-00; -.
DR   PaxDb; Q0E2Y1; -.
DR   PRIDE; Q0E2Y1; -.
DR   EnsemblPlants; Os02t0204400-00; Os02t0204400-00; Os02g0204400.
DR   GeneID; 4328669; -.
DR   Gramene; Os02t0204400-00; Os02t0204400-00; Os02g0204400.
DR   KEGG; osa:4328669; -.
DR   eggNOG; KOG0133; Eukaryota.
DR   HOGENOM; CLU_010348_3_4_1; -.
DR   InParanoid; Q0E2Y1; -.
DR   OMA; WQWSASS; -.
DR   OrthoDB; 378952at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q0E2Y1; OS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IBA:GO_Central.
DR   GO; GO:0003914; F:DNA (6-4) photolyase activity; IEA:UniProtKB-EC.
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:0006290; P:pyrimidine dimer repair; IEA:EnsemblPlants.
DR   GO; GO:0009411; P:response to UV; IEA:EnsemblPlants.
DR   Gene3D; 3.40.50.620; -; 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; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR11455; PTHR11455; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   SUPFAM; SSF48173; SSF48173; 1.
DR   SUPFAM; SSF52425; SSF52425; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA-binding; FAD; Flavoprotein; Lyase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..551
FT                   /note="(6-4)DNA photolyase"
FT                   /id="PRO_0000397887"
FT   DOMAIN          13..157
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT   REGION          374..379
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          508..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..526
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         254
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         268..272
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         309..313
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         372..375
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         378
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         407..409
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         413
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         419
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   SITE            340
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
FT   SITE            394
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
FT   SITE            417
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        40
FT                   /note="A -> V (in Ref. 4; EEE56527)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   551 AA;  62264 MW;  37C2FE84F92C34C8 CRC64;
     MDAAATAATA TAAAAMVWFR KGLRVHDNPA LDAARRGGAA ARLYPVFVLD PRYLRPDQAA
     PSPGSARAGV ARVRFLLESL SDLDARLRRL GSRLLLLRAR DDGDVAGTVC AALKDWNIGK
     LCFESDTEPY ALARDKKVMD FAAASGIDVF SPVSHTLFDP AEIIEKNGGR PPMTYQSFVA
     IAGEPPEPIM EEYSELPPVG DTGEYELLPV PRVEELGYGD ISQEDLSLFR GGETEALKRM
     RESLHDKEWV AKFEKPKGDP SAFLKPATTV LSPYLKFGCL SSRYFYHCIQ DIYRSTKKHT
     NPPVSLTGQL LWRDFFYTVA FGTPNFDQMK GNKICKQIPW TENEELFPAW RDGRTGYPWI
     DAIMIQLRKW GWMHHLARHS VACFLTRGDL FIHWEKGRDV FERLLIDSDW AINNGNWMWL
     SCSSFFYQYH RIYSPTSFGK KYDPNGNYIR HFIPVLKDMP KEYIYEPWTA PLSIQKKANC
     IIGKDYPKPV VDHAIASKEC KKMMGEAYAS NRLDDDKPDK GKSSNSSRRK LSAGSQVTPN
     SSKTKQLKRS S
 
 
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