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OHK1_ORYSI
ID   OHK1_ORYSI              Reviewed;         968 AA.
AC   A2YFR6;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Probable histidine kinase 1 {ECO:0000305};
DE            Short=OsHK1 {ECO:0000305};
DE            EC=2.7.13.3 {ECO:0000305};
GN   Name=HK1 {ECO:0000305}; ORFNames=OsI_23953 {ECO:0000312|EMBL:EAZ01927.1};
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: 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}.
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DR   EMBL; CM000131; EAZ01927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2YFR6; -.
DR   SMR; A2YFR6; -.
DR   STRING; 39946.A2YFR6; -.
DR   EnsemblPlants; BGIOSGA023392-TA; BGIOSGA023392-PA; BGIOSGA023392.
DR   Gramene; BGIOSGA023392-TA; BGIOSGA023392-PA; BGIOSGA023392.
DR   HOGENOM; CLU_000445_104_17_1; -.
DR   OMA; HEDACQT; -.
DR   Proteomes; UP000007015; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblPlants.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblPlants.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:EnsemblPlants.
DR   GO; GO:0071219; P:cellular response to molecule of bacterial origin; IEA:EnsemblPlants.
DR   GO; GO:0071732; P:cellular response to nitric oxide; IEA:EnsemblPlants.
DR   GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IEA:EnsemblPlants.
DR   GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; IEA:EnsemblPlants.
DR   GO; GO:0090333; P:regulation of stomatal closure; IEA:EnsemblPlants.
DR   GO; GO:0048364; P:root development; IEA:EnsemblPlants.
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   3: Inferred from homology;
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_0000433804"
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;  108775 MW;  7482099665EFC047 CRC64;
     MGDEYLAEPE DEVAISMWPE NIGDKHQKQF KMEKLGKDQD ALEDANFQQK PSSVDLNRLM
     ELANSEKGVS QMQYFVKHWE YKRANTARLL KEQIGLLCQQ RKEIEQRKQQ ILEEQQFQDE
     SYYAVKRQVP 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 EERGPCRVHE EKSLHKKSKC SPSSNKAKIL LVEDNKVNIM VAKSMLEQLG
     HGIDIVNNGL EAIRAIQKRQ YDIILMDVHM PEMDGLQATK FIRSFENTGC WDTSVKPEHD
     QIIAGSDNLS DCAHMKKQGK RVPIIAMTAN SFSESAEECL AAGMDSYISK PVNFQNIKEC
     LQQYLPPQ
 
 
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