ID C6TH15_SOYBN Unreviewed; 248 AA.
AC C6TH15;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Response regulatory domain-containing protein {ECO:0000259|PROSITE:PS50110};
GN Name=100788079 {ECO:0000313|EnsemblPlants:KRH66808};
GN ORFNames=GLYMA_03G130000 {ECO:0000313|EMBL:KRH66808.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:ACU21117.1};
RN [1] {ECO:0000313|EMBL:ACU21117.1}
RP NUCLEOTIDE SEQUENCE.
RA Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRH66808.1, ECO:0000313|EnsemblPlants:KRH66808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH66808};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH66808.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [3] {ECO:0000313|EnsemblPlants:KRH66808}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH66808};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KRH66808.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH66808.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a response regulator involved in His-to-Asp
CC phosphorelay signal transduction system. Phosphorylation of the Asp
CC residue in the receiver domain activates the ability of the protein to
CC promote the transcription of target genes. Type-A response regulators
CC seem to act as negative regulators of the cytokinin signaling.
CC {ECO:0000256|ARBA:ARBA00043855}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SIMILARITY: Belongs to the ARR family. Type-A subfamily.
CC {ECO:0000256|ARBA:ARBA00038244}.
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DR EMBL; BT096926; ACU21117.1; -; mRNA.
DR EMBL; CM000836; KRH66808.1; -; Genomic_DNA.
DR RefSeq; NP_001240226.1; NM_001253297.2.
DR AlphaFoldDB; C6TH15; -.
DR SMR; C6TH15; -.
DR STRING; 3847.C6TH15; -.
DR PaxDb; 3847-GLYMA03G28570-1; -.
DR EnsemblPlants; KRH66808; KRH66808; GLYMA_03G130000.
DR GeneID; 100788079; -.
DR Gramene; KRH66808; KRH66808; GLYMA_03G130000.
DR KEGG; gmx:100788079; -.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_000445_69_5_1; -.
DR InParanoid; C6TH15; -.
DR OMA; NDHREVE; -.
DR OrthoDB; 406014at2759; -.
DR Proteomes; UP000008827; Chromosome 3.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd17581; REC_typeA_ARR; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR InterPro; IPR045279; ARR-like.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43874; TWO-COMPONENT RESPONSE REGULATOR; 1.
DR PANTHER; PTHR43874:SF167; TWO-COMPONENT RESPONSE REGULATOR ARR9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 2: Evidence at transcript level;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT DOMAIN 11..149
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 192..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 248 AA; 28266 MW; F07E2431D08EA912 CRC64;
MGMAAAESQF HVLAVDDSII DRKLIERLLR TSSYQVTTVD SGSKALEFLG LRENDESNPS
IPSVCPNNHQ PQEVEVNLVI TDYCMPGMTG YDLLKKIKES SSLRNIPVVI MSSENVPSRI
NRCLEEGAEE FFLKPVRLSD LNKLKPHMKK TKFKDQKQET VERFEDSEVQ QQQSQQQIII
QNEHHQAPKL QVLQPESESE SHPQPTIEQQ QQILQQANNN NKRKTMEQGL SPETDRTRPR
YSGIATVV
//
