OHK1_ORYSJ
ID OHK1_ORYSJ Reviewed; 968 AA.
AC A3BE68; Q0DAG5; Q67WC2;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Probable histidine kinase 1 {ECO:0000305};
DE Short=OsHK1 {ECO:0000303|PubMed:16891544};
DE EC=2.7.13.3 {ECO:0000305};
GN Name=HK1 {ECO:0000303|PubMed:17284581};
GN Synonyms=MHZ1 {ECO:0000312|EMBL:AIU40906.1};
GN OrderedLocusNames=Os06g0654300 {ECO:0000312|EMBL:BAF20158.1},
GN LOC_Os06g44410 {ECO:0000305};
GN ORFNames=OsJ_22203 {ECO:0000312|EMBL:EAZ37857.1};
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 [MRNA].
RC STRAIN=cv. Nipponbare;
RA Duan K., Ma B., Chen S., Zhang J.;
RT "MHZ1 positively regulates root ethylene response in rice.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
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).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=16891544; DOI=10.1104/pp.106.086371;
RA Pareek A., Singh A., Kumar M., Kushwaha H.R., Lynn A.M.,
RA Singla-Pareek S.L.;
RT "Whole-genome analysis of Oryza sativa reveals similar architecture of two-
RT component signaling machinery with Arabidopsis.";
RL Plant Physiol. 142:380-397(2006).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17284581; DOI=10.1104/pp.106.093666;
RA Schaller G.E., Doi K., Hwang I., Kieber J.J., Khurana J.P., Kurata N.,
RA Mizuno T., Pareek A., Shiu S.H., Wu P., Yip W.K.;
RT "Nomenclature for two-component signaling elements of rice.";
RL Plant Physiol. 143:555-557(2007).
CC -!- FUNCTION: Cytokinin receptor related to bacterial two-component
CC regulators. Functions as a histidine kinase and transmits the stress
CC signal to a downstream MAPK cascade. {ECO:0000250|UniProtKB:A1A698}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000305};
CC -!- DOMAIN: Histidine-containing phosphotransfer domain (HPt) contains an
CC active histidine that mediates the phosphotransfer. {ECO:0000305}.
CC -!- PTM: Activation probably requires a transfer of a phosphate group
CC between a His in the transmitter domain and an Asp of the receiver
CC domain. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Dwarf, chlorina and sterility phenotypes.
CC {ECO:0000269|PubMed:16891544}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD37425.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD37547.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF20158.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KF999959; AIU40906.1; -; mRNA.
DR EMBL; AP003565; BAD37425.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP003579; BAD37547.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008212; BAF20158.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000143; EAZ37857.1; -; Genomic_DNA.
DR RefSeq; XP_015641340.1; XM_015785854.1.
DR AlphaFoldDB; A3BE68; -.
DR SMR; A3BE68; -.
DR STRING; 4530.OS06T0654300-00; -.
DR PaxDb; A3BE68; -.
DR PRIDE; A3BE68; -.
DR GeneID; 4341709; -.
DR KEGG; osa:4341709; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_1974236_0_0_1; -.
DR OrthoDB; 27870at2759; -.
DR BRENDA; 2.7.13.3; 8948.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytokinin signaling pathway; Kinase; Phosphoprotein;
KW Reference proteome; Transferase; Two-component regulatory system.
FT CHAIN 1..968
FT /note="Probable histidine kinase 1"
FT /id="PRO_0000433803"
FT DOMAIN 372..655
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 818..965
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 737..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 89..120
FT /evidence="ECO:0000255"
FT COILED 169..204
FT /evidence="ECO:0000255"
FT MOD_RES 375
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 867
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 968 AA; 108791 MW; DDA1F0916417BBE5 CRC64;
MGDEYLAEPE DEVAISMWPE NIGDKHQKQF KMEKLGKDQD ALEDANFQQK PSSVDLNRLM
ELANSEKGVS QMQYFVKHWE YKRANTARLL KEQIGLLCQQ RKEIEQRKQQ ILEEQQFQDE
SYYAVKWQVP ILDEVYKDEW KRPSKKNDDL SHNQELKIDA EYDSISYWKE RAMQLEKTLE
ASLQRERSLE EKLEENIKNL QSHTPVEEFS GMLKRADYFL HLVLQSAPIV IAHQDADLRY
RFIFNHFPTL ADEDVIGKTD YEILSGEGIE EMNNVKKEVM ASGKATKREF VFNTPLFGAK
TFVTYIEPVF SKSGETIGVN YVAMDITDQV TRREKMADIR VREAVQKAKE TELSKSLHIT
EETMRAKQML ATMSHEIRSP LSGVLSMAEI LATTKLDKEQ YQLLEVMLSS GDLVLQLIND
ILDLSKVESG AMKLEATTFR PREVVKHVLQ TAAASLKKEL ILEGCIGDNV PLEVTGDVLR
IRQILTNLIS NAVKFTHEGK VGINLHVLDK QLPGCRIEGG QLHSKAHSAP AAAAEHFSAS
PRKCDNDTLG CSNHEDACQT GIPSNDNFGE HHEGDEVVWL RCDVYDTGIG IPEKSLPLLF
KRYMQASDDH ARKYGGTGLG LAICKQLVEL MGGTLTVVSK ENEGSTFSFV LPCKIPVKED
HSDDPDDMPS SGGDFTTSDI EGSFIFKPQA RPYLLTSGVS VMNNTKLIGG NQFYDPPNIL
EDRKPFSNGF VLAEDHSTNS ASTAHQSNGP SVSRTNKEQH DNAMVIELNR QAERVSSSRG
DTTSVSGLIH DERGPCRVHE EKSLHKKSKC SPSSNKAKIL LVEDNKVNIM VAKSMLEQLG
HGIDIVNNGL EAIRAIQKRQ YDIILMDVHM PEMDGLQATK FIRSFENTGC WDTSVKPEHD
QIIAGSDNLS DCAHMKKQGK RVPIIAMTAN SFSESAEECL AAGMDSYISK PVNFQNIKEC
LQQYLPPQ