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ORR21_ORYSI
ID   ORR21_ORYSI             Reviewed;         691 AA.
AC   A2XE31;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Two-component response regulator ORR21 {ECO:0000305};
GN   Name=RR21 {ECO:0000305}; ORFNames=OsI_10579 {ECO:0000312|EMBL:EAY89091.1};
OS   Oryza sativa subsp. indica (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=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
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: Transcriptional activator that binds specific DNA sequence.
CC       Functions as a response regulator involved in His-to-Asp phosphorelay
CC       signal transduction system. Phosphorylation of the Asp residue in the
CC       receiver domain activates the ability of the protein to promote the
CC       transcription of target genes. May directly activate some type-A
CC       response regulators in response to cytokinins.
CC       {ECO:0000250|UniProtKB:Q940D0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC   -!- PTM: Two-component system major event consists of a His-to-Asp
CC       phosphorelay between a sensor histidine kinase (HK) and a response
CC       regulator (RR). In plants, the His-to-Asp phosphorelay involves an
CC       additional intermediate named Histidine-containing phosphotransfer
CC       protein (HPt). This multistep phosphorelay consists of a His-Asp-His-
CC       Asp sequential transfer of a phosphate group between first an His and
CC       an Asp of the HK protein, followed by the transfer to a conserved His
CC       of the HPt protein and finally the transfer to an Asp in the receiver
CC       domain of the RR protein. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ARR family. Type-B subfamily. {ECO:0000305}.
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DR   EMBL; CM000128; EAY89091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2XE31; -.
DR   SMR; A2XE31; -.
DR   STRING; 39946.A2XE31; -.
DR   EnsemblPlants; BGIOSGA012149-TA; BGIOSGA012149-PA; BGIOSGA012149.
DR   Gramene; BGIOSGA012149-TA; BGIOSGA012149-PA; BGIOSGA012149.
DR   HOGENOM; CLU_024359_1_1_1; -.
DR   OMA; CSQAKVA; -.
DR   Proteomes; UP000007015; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   InterPro; IPR045279; ARR-like.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR006447; Myb_dom_plants.
DR   InterPro; IPR017053; Response_reg_B-typ_pln.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43874; PTHR43874; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PIRSF; PIRSF036392; RR_ARR_type-B; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   TIGRFAMs; TIGR01557; myb_SHAQKYF; 1.
DR   PROSITE; PS51294; HTH_MYB; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Activator; Cytokinin signaling pathway; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..691
FT                   /note="Two-component response regulator ORR21"
FT                   /id="PRO_0000433841"
FT   DOMAIN          17..132
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        199..258
FT                   /note="Myb-like GARP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          139..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         68
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   691 AA;  73775 MW;  E3D60883B3A622D4 CRC64;
     MAPVEDGGGV EFPVGMKVLV VDDDPTCLAV LKRMLLECRY DATTCSQATR ALTMLRENRR
     GFDVIISDVH MPDMDGFRLL ELVGLEMDLP VIMMSADSRT DIVMKGIKHG ACDYLIKPVR
     MEELKNIWQH VIRKKFNENK EHEHSGSLDD TDRTRPTNND NEYASSANDG AEGSWKSQKK
     KRDKDDDDGE LESGDPSSTS KKPRVVWSVE LHQQFVNAVN HLGIDKAVPK KILELMNVPG
     LTRENVASHL QKFRLYLKRI AQHHAGIANP FCPPASSGKV GSLGGLDFQA LAASGQIPPQ
     ALAALQDELL GRPTNSLVLP GRDQSSLRLA AVKGNKPHGE REIAFGQPIY KCQNNAYGAF
     PQSSPAVGGM PSFSAWPNNK LGMADSTGTL GGMSNSQNSN IVLHELQQQP DAMLSGTLHS
     LDVKPSGIVM PSQSLNTFSA SEGLSPNQNT LMIPAQSSGF LAAMPPSMKH EPVLATSQPS
     SSLLGGIDLV NQASTSQPLI SAHGGGNLSG LVNRNPNVVP SQGISTFHTP NNPYLVSPNS
     MGVGSKQPPG VLKTENSDAL NHSYGYLGGS NPPMDSGLLS SQSKNTQFGL LGQDDITGSW
     SPLPNVDSYG NTVGLSHPGS SSSSFQSSNV ALGKLPDQGR GKNHGFVGKG TCIPSRFAVD
     EIESPTNNLS HSIGSSGDIM SPDIFGFSGQ M
 
 
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