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CRYD_ORYSJ
ID   CRYD_ORYSJ              Reviewed;         582 AA.
AC   Q651U1;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Cryptochrome DASH, chloroplastic/mitochondrial;
DE   Flags: Precursor;
GN   Name=CRYD; OrderedLocusNames=Os06g0661800, LOC_Os06g45100;
GN   ORFNames=OSJNBa0051O02.40, OSJNBb0065C04.7;
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=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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-582.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: May have a photoreceptor function. Binds ss- and ds-DNA in a
CC       sequence non-specific manner, lacks photolyase activity (By
CC       similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC         Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000250};
CC       Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
CC       {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}. Mitochondrion
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000305}.
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DR   EMBL; AP004744; BAD45850.1; -; Genomic_DNA.
DR   EMBL; AP005769; BAD46426.1; -; Genomic_DNA.
DR   EMBL; AP014962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK072287; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK102315; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015644118.1; XM_015788632.1.
DR   AlphaFoldDB; Q651U1; -.
DR   SMR; Q651U1; -.
DR   STRING; 4530.OS06T0661800-01; -.
DR   PaxDb; Q651U1; -.
DR   GeneID; 4341749; -.
DR   KEGG; osa:4341749; -.
DR   eggNOG; KOG0133; Eukaryota.
DR   InParanoid; Q651U1; -.
DR   OrthoDB; 378952at2759; -.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   Genevisible; Q651U1; OS.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0003913; F:DNA photolyase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR   GO; GO:0000719; P:photoreactive repair; IBA:GO_Central.
DR   Gene3D; 3.40.50.620; -; 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   PANTHER; PTHR11455; PTHR11455; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   PRINTS; PR00147; DNAPHOTLYASE.
DR   SUPFAM; SSF48173; SSF48173; 1.
DR   SUPFAM; SSF52425; SSF52425; 1.
DR   TIGRFAMs; TIGR02765; crypto_DASH; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Chromophore; DNA-binding; FAD; Flavoprotein; Mitochondrion;
KW   Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..49
FT                   /note="Chloroplast and mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..582
FT                   /note="Cryptochrome DASH, chloroplastic/mitochondrial"
FT                   /id="PRO_0000235320"
FT   DOMAIN          84..234
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT   REGION          560..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        304
FT                   /note="A -> S (in Ref. 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   582 AA;  65342 MW;  0E05B16E516D7AD6 CRC64;
     MLHFLSSSSP LNPQFLLLPR QSARLRVLLS IPVSAMSSSS SSSSRGALAA AAVPSLSADE
     AGAAADEAFL RYTSPSMRRS GGGGVAIVWF RNDLRVLDNE AVVRAWAASD AVLPVYCVDP
     RISAGSTHYF GFPKTGALRA QFLIECLEDL KRNLTKQGLD LLIRHGKPED ILPSIAKAVT
     AHTVYAHKET CSEELLVEHL VRKGLEQVVI PQGGASNQKK PRNPKLQLIW GATLYHVDDL
     PFSVNNLPDV YTQFRKAVES KSSVRNCSKL PPSLGPPPGS GLDEIGGWGT VPTLESLGLS
     MTKAEKGMHF VGGESAALGR VHEYFWKKDQ LKVYKETRNG MLGPDYSTKF SPWLASGSLS
     PRYICEEVKR YEKQRIANDS TYWVLFELIW RDYFRFISAK YGNSIFHLGG PRNVESKWSQ
     DQALFESWRD GRTGYPLIDA NMKELLATGF MSNRGRQIVC SFLVRDMGID WRMGAEWFET
     CLLDYDPASN YGNWTYGAGV GNDPREDRYF SIPKQAKTYD PDGEYVAYWL PELRSIAKER
     RNFPGASYIK QVVPLKFDGG HQKRDQQFNR QRRPGHMYRR QK
 
 
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