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Database: UniProt
Entry: I1KS30_SOYBN
LinkDB: I1KS30_SOYBN
Original site: I1KS30_SOYBN 
ID   I1KS30_SOYBN            Unreviewed;      1030 AA.
AC   I1KS30;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=100776798 {ECO:0000313|EnsemblPlants:KRH42681};
GN   ORFNames=GLYMA_08G105000 {ECO:0000313|EMBL:KRH42680.1};
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|EnsemblPlants:KRH42681};
RN   [1] {ECO:0000313|EMBL:KRH42680.1, ECO:0000313|EnsemblPlants:KRH42681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH42681};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH42680.1};
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   [2] {ECO:0000313|EnsemblPlants:KRH42681}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH42681};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH42680.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH42680.1};
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   -!- 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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR   EMBL; CM000841; KRH42680.1; -; Genomic_DNA.
DR   EMBL; CM000841; KRH42681.1; -; Genomic_DNA.
DR   EMBL; CM000841; KRH42682.1; -; Genomic_DNA.
DR   EMBL; CM000841; KRH42683.1; -; Genomic_DNA.
DR   EMBL; CM000841; KRH42684.1; -; Genomic_DNA.
DR   EMBL; CM000841; KRH42685.1; -; Genomic_DNA.
DR   EMBL; CM000841; KRH42686.1; -; Genomic_DNA.
DR   EMBL; CM000841; KRH42687.1; -; Genomic_DNA.
DR   RefSeq; XP_003531201.1; XM_003531153.3.
DR   RefSeq; XP_006585121.1; XM_006585058.2.
DR   RefSeq; XP_006585123.1; XM_006585060.2.
DR   RefSeq; XP_006585124.1; XM_006585061.2.
DR   RefSeq; XP_014634343.1; XM_014778857.1.
DR   AlphaFoldDB; I1KS30; -.
DR   SMR; I1KS30; -.
DR   STRING; 3847.I1KS30; -.
DR   PaxDb; 3847-GLYMA08G11060-4; -.
DR   EnsemblPlants; KRH42680; KRH42680; GLYMA_08G105000.
DR   EnsemblPlants; KRH42681; KRH42681; GLYMA_08G105000.
DR   EnsemblPlants; KRH42682; KRH42682; GLYMA_08G105000.
DR   EnsemblPlants; KRH42683; KRH42683; GLYMA_08G105000.
DR   EnsemblPlants; KRH42684; KRH42684; GLYMA_08G105000.
DR   EnsemblPlants; KRH42685; KRH42685; GLYMA_08G105000.
DR   EnsemblPlants; KRH42686; KRH42686; GLYMA_08G105000.
DR   EnsemblPlants; KRH42687; KRH42687; GLYMA_08G105000.
DR   GeneID; 100776798; -.
DR   Gramene; KRH42680; KRH42680; GLYMA_08G105000.
DR   Gramene; KRH42681; KRH42681; GLYMA_08G105000.
DR   Gramene; KRH42682; KRH42682; GLYMA_08G105000.
DR   Gramene; KRH42683; KRH42683; GLYMA_08G105000.
DR   Gramene; KRH42684; KRH42684; GLYMA_08G105000.
DR   Gramene; KRH42685; KRH42685; GLYMA_08G105000.
DR   Gramene; KRH42686; KRH42686; GLYMA_08G105000.
DR   Gramene; KRH42687; KRH42687; GLYMA_08G105000.
DR   KEGG; gmx:100776798; -.
DR   eggNOG; KOG0519; Eukaryota.
DR   HOGENOM; CLU_000445_16_2_1; -.
DR   InParanoid; I1KS30; -.
DR   OMA; ATHEKCL; -.
DR   OrthoDB; 5476858at2759; -.
DR   Proteomes; UP000008827; Chromosome 8.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.250.1190; -; 1.
DR   Gene3D; 3.30.450.350; CHASE domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR006189; CHASE_dom.
DR   InterPro; IPR042240; CHASE_sf.
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; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43719:SF73; HISTIDINE KINASE 3; 1.
DR   PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF03924; CHASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM01079; CHASE; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50839; CHASE; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        13..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        91..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        394..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          159..385
FT                   /note="CHASE"
FT                   /evidence="ECO:0000259|PROSITE:PS50839"
FT   DOMAIN          453..721
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          749..870
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          895..1027
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         945
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1030 AA;  115071 MW;  A8C6E4B49C7BCC2D CRC64;
     MSLLHVVGFG LKVGHLLLVL CCWVVSVVYL NWFLSSGIIM DTKMGGGGGG GSKMWHKKWW
     EKISGQGCKI HQQYYQYIGS KKVKRALWRK LLLTWVVGWF IVSLRIFCYM SSQGTEKRKE
     TLASMCDERA RMLQDQFNVS MNHIQAMSIL ISTFHHAKSP SAIDQKTFAK YTERTAFERP
     LTSGVAYAVR VLHSEREQFE KQQGWTIKRM DTLEQNPVHK DDYAPEALEP SPVQEEYAPV
     IFAQDTIAHV ISVNVLSGKE DRENVLRARE SGKGVLTAPF RLLKTNRLGV ILTFAVYKRD
     LPSNTTPNER IQATDGYLGG VFDVESLVEK LLQQLASKQT VIVHVYDTTN RTHPIAMYGS
     NESGDFFYHV STLNFGDPFR KHEMHCRFKQ KPPWPWVAIT TSIGILVIAL LVGYIFHATV
     NRIAKVEDDY REMMELKKRA EAADVAKSQF LATVSHEIRT PMNGVLGMLH MLMDTDLDVT
     QQEYVRTAQE SGKALVSLIN EVLDQAKIEF GKLELEAVLF DIRAILDDVL SLFSEKSQGK
     RVELAVYVSD HVPELLIGDP GRFRQIITNL MGNSIKFTDK GHIFVTIHLV EEVVRSIEVD
     KESNSENTLS GSPVADSRRS WEGFKAFSQE GPLGSFSSPS NDLVNLIVSV EDTGEGIPLE
     SQPLIFTPFM QVGSSISRKH GGTGIGLSIS KCLVGLMNGE IGFVSIPKIG STFTFTAVFT
     NGHRSSSECK IQQINNQPQS ASSEFEGMTA LIIDPRSVRA EVSGYHIQRL GIHVEMVSDL
     KQGLSTISNG NVVVNMVLIE QEVWDRDLGL SSHFVNNTRR IDHGVPPKLF ILVNSSSSFK
     ASVNLGVHNP TVITKPLRAS MLAASLQRAM GVQNKGAPHR ELQSLSLRHL LRGRKILIVD
     DNGVNRAVAA GALKKYGADV VCVSSGKDAI SSLKPPHQFD ACFMDIQMPE MDGFEATKRI
     REMEDSVNRE VSMDDFENIT NWHVPILAMT ADVIQATHEE CLRCGMDGYV SKPFEAEQLY
     REVSRFFQSS
//
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