ID   ORR24_ORYSI             Reviewed;         626 AA.
AC   A2X1N2;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Two-component response regulator ORR24 {ECO:0000305};
GN   Name=RR24 {ECO:0000305}; ORFNames=OsI_06112 {ECO:0000312|EMBL:EAY84742.1};
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; CM000127; EAY84742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2X1N2; -.
DR   SMR; A2X1N2; -.
DR   STRING; 39946.A2X1N2; -.
DR   PRIDE; A2X1N2; -.
DR   EnsemblPlants; BGIOSGA007015-TA; BGIOSGA007015-PA; BGIOSGA007015.
DR   Gramene; BGIOSGA007015-TA; BGIOSGA007015-PA; BGIOSGA007015.
DR   HOGENOM; CLU_024359_0_2_1; -.
DR   OMA; YIDGDWE; -.
DR   Proteomes; UP000007015; Chromosome 2.
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..626
FT                   /note="Two-component response regulator ORR24"
FT                   /id="PRO_0000433847"
FT   DOMAIN          30..145
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        210..269
FT                   /note="Myb-like GARP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         81
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   626 AA;  68344 MW;  2D893A3757FF9C5D CRC64;
     MTVEERQGRV GGHGVSGGGG GRDQFPVGMR VLAVDDDPTC LKILENLLLR CQYHVTTTGQ
     AATALKLLRE NKDQFDLVIS DVHMPDMDGF KLLELVGLEM DLPVIMLSAN GETQTVMKGI
     THGACDYLLK PVRLEQLRTI WQHVIRRKNC DAKNRGNDDD AGQKAQGMNN EGESIGANRN
     KRQSRKSRDE NGDDGDDSDE NSNENGDSST QKKPRVVWSV ELHRKFVAAV NQLGIEKAVP
     KKILDLMNVE NITRENVASH LQKYRLYLKR LSTDASRQAN LAAAFGGRNP AYINMNSFGN
     YNAYGRYRTV PTAGHTQANN ILTRMNSPSA FGVHGLLHSQ PIQLGHAQNN LSTSLNDLGG
     LNNGNMIRGA QMSTILTGPS GNSFPNISNG APLATANRSL QPLESSSQQH LSRVHSSSAD
     PFSTLVGESP QFPDLGRTTN TWQTAVPSNI QDRGHNDNMS QATLHMNGPK IEPVSSFTSS
     NQIPLLGNEM QGQVASLASN VPIAFNQDTS PFNYGSSTNS RDMLNNSHVF SNSSINTSLP
     NLSLDNPAVP KQTLDRGNTG IVSPMQDGRI HHQAVSNQLN YNDDLMRTTG LQRGLSGGLD
     DIVVDMFRPD REDDGVPYID GDWELV