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Database: UniProt
Entry: K7LVT4_SOYBN
LinkDB: K7LVT4_SOYBN
Original site: K7LVT4_SOYBN 
ID   K7LVT4_SOYBN            Unreviewed;       967 AA.
AC   K7LVT4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   Name=100785090 {ECO:0000313|EnsemblPlants:KRH26676};
GN   ORFNames=GLYMA_12G188100 {ECO:0000313|EMBL:KRH26676.1};
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:KRH26676.1};
RN   [1] {ECO:0000313|EMBL:KRH26676.1, ECO:0000313|EnsemblPlants:KRH26676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH26676};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH26676.1};
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:KRH26676}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH26676};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH26676.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH26676.1};
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR   EMBL; CM000845; KRH26676.1; -; Genomic_DNA.
DR   RefSeq; XP_006592774.1; XM_006592711.2.
DR   AlphaFoldDB; K7LVT4; -.
DR   SMR; K7LVT4; -.
DR   PaxDb; 3847-GLYMA12G31360-2; -.
DR   EnsemblPlants; KRH26676; KRH26676; GLYMA_12G188100.
DR   GeneID; 100785090; -.
DR   Gramene; KRH26676; KRH26676; GLYMA_12G188100.
DR   KEGG; gmx:100785090; -.
DR   eggNOG; ENOG502QPQ4; Eukaryota.
DR   HOGENOM; CLU_000288_114_6_1; -.
DR   InParanoid; K7LVT4; -.
DR   OrthoDB; 1210136at2759; -.
DR   Proteomes; UP000008827; Chromosome 12.
DR   ExpressionAtlas; K7LVT4; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR47986; OSJNBA0070M12.3 PROTEIN; 1.
DR   PANTHER; PTHR47986:SF29; PROTEIN KINASE; 1.
DR   Pfam; PF00560; LRR_1; 3.
DR   Pfam; PF08263; LRRNT_2; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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        513..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          620..899
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          445..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..492
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         648
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   967 AA;  105874 MW;  A93DD85766B7CE61 CRC64;
     MRVSWQTMEG VQLEKVVFLL CFGLIITMSY GATNPNDVKV LNDFRKGLEN PELLKWPEEG
     DDPCGPPLWP FVYCSGDRVT QIQAKDLGLR GTLPHNFNQL SELFNLGLQR NNLSGMLPTF
     SGLSKLKYAF LDYNAFDAIP ADFFDGLSSL MVLTLEKNPL NVSSGWSFPM DLEKSVQLTN
     LSLAFCNLVG PLPDFLGRLP SLTQLSLSGN KLTGAIPATF AQSSIQDLWL NNQEGGGLSG
     PIDVIASMIL LRHVLLHGNQ FTGPIPQNIG NLTSLQELNL NSNQLVGLIP ESLAHMELEI
     LVLNNNMLMG PIPEFKAANV SYDNNLFCQP EPGLECSPQV AALLDFLDKL NYPSFLISDW
     VGDEPCTRST GSWFGLSCNS NSEVSVINLP RHKLNGTLSP SLAKLDSLLE IRLAGNNITG
     SVPGNFTDLK SLRLLDLSDN NLEPPLPKFH NDPKVVTVGN PLLPNQTGGS PSPMPINNPP
     SPQNPSHPPS SHESPVPDQS SRSNQSKPND LKIFKAVGIV AGVAVFAVVA LLVVYPFLCC
     RKNKKASLDA PSSIMVHPRD PSDSDNMVKI TVSNATGSLS TKTGTSSQSN ISGETQNSHI
     IEDGNLVISI QVLRKVTNDF ASENELGRGG FGTVYKGELE DGTKIAVKRM EHGVISSKAL
     EEFQAEIAVL SKVRHRHLVS LLGYSIDGNE RLLVYEYMSL GALSQHLFHW KSLKLEPLSW
     SQRLAIALDV ARGMEYLHSL ARQTFIHRDL KSSNILLGDD FRAKISDFGL VKHAPDSEKS
     VATKLAGTFG YLAPEYAVMG KITTKVDVFS YGVVLMELLT GLVALDESRP EESRYLAEWF
     WRIKSSKEKL MAAIDPVLEA SEETFESITI VAELAGHCTA REAHHRPDMG HAVNVLAALV
     EKWKPVDDEL DCYSGIDYTR PLPQMLKIWK EAESGEFSYA SCLENSRSSI AARPSGFADS
     FTSADAR
//
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