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Database: UniProt
Entry: I1LUJ1_SOYBN
LinkDB: I1LUJ1_SOYBN
Original site: I1LUJ1_SOYBN 
ID   I1LUJ1_SOYBN            Unreviewed;       995 AA.
AC   I1LUJ1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=100778128 {ECO:0000313|EnsemblPlants:KRH26990};
GN   ORFNames=GLYMA_12G206800 {ECO:0000313|EMBL:KRH26990.1};
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:KRH26990};
RN   [1] {ECO:0000313|EMBL:KRH26990.1, ECO:0000313|EnsemblPlants:KRH26990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH26990};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH26990.1};
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:KRH26990}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH26990};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH26990.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH26990.1};
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; KRH26990.1; -; Genomic_DNA.
DR   RefSeq; XP_006592855.1; XM_006592792.2.
DR   AlphaFoldDB; I1LUJ1; -.
DR   SMR; I1LUJ1; -.
DR   STRING; 3847.I1LUJ1; -.
DR   PaxDb; 3847-GLYMA12G33450-1; -.
DR   EnsemblPlants; KRH26990; KRH26990; GLYMA_12G206800.
DR   GeneID; 100778128; -.
DR   Gramene; KRH26990; KRH26990; GLYMA_12G206800.
DR   KEGG; gmx:100778128; -.
DR   eggNOG; ENOG502QQFB; Eukaryota.
DR   HOGENOM; CLU_000288_22_1_1; -.
DR   InParanoid; I1LUJ1; -.
DR   OMA; SFKEHIC; -.
DR   OrthoDB; 391466at2759; -.
DR   Proteomes; UP000008827; Chromosome 12.
DR   ExpressionAtlas; I1LUJ1; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0099402; P:plant organ development; IEA:UniProt.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR   PANTHER; PTHR48056:SF89; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 10.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF52047; RNI-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}; Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..995
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014578531"
FT   TRANSMEM        632..654
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          688..981
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         716
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   995 AA;  108961 MW;  FB450296FCA5BF1F CRC64;
     MVQQLLLFLI LFPFLSLPPT LSLNQDGLFL LEAKLQLSDP RNALSNWNHR DATPCNWTAV
     TCDAGGGVAT LDLSDLQLSG PVPAAALCRL PSLSSLNLSN NDINATLPAA AFTPCAALRH
     LDLSQNLLSG AIPATLPDSL ITLDLSSNNF SGKIPASFGQ LRRLQSLSLV SNLLTGTIPS
     SLSKISTLKT LRLAYNTFDP GPIPNDLGNL KNLEELWLAG CNLVGPIPPS LGKLSNLLNL
     DLSQNNLVGY IPEQLVSGLR NIVQIELYEN ALSGALPRAA FANLTNLERF DASTNELTGT
     IPEELCGLKK LESLILYANK FEGSLPETIV KSQNLYELKL FNNSLTGSLP SGLGNNSKLQ
     FFDVSFNRFS GEIPARLCGG GALEELILIY NSFSGRISES LGECKSLRRV RLRNNNFSGV
     VPEGLWGLPH LYLLEFVENS LSGSISNSIS GAWNLSILLI SGNKFSGSIP EGVGELGNLE
     AFVADHNSLT GRIPKSVVRL SQLDRLVLRD NQLFGEIPVG VGGWRKLNEL DLANNNRLNG
     SIPKELGDLP VLNYLDLSGN RFSGEIPIKL QNLKLNLLNL SNNQLSGVIP PLYDNENYRK
     SFLGNPGLCK PLSGLCPNLG GESEGKSRKY AWIFRFMFVL AGIVLIVGMA WFYFKFRDFK
     KMEKGFHFSK WRSFHKLGFS EFEIVKLLSE DNVIGSGASG KVYKVALSSE VVAVKKLWGA
     TKKGNGSVDS EKDGFEVEVE TLGKIRHKNI VKLWCCCNSK DSKLLVYEYM PKGSLADLLH
     SSKKSLMDWP TRYKIAIDAA EGLSYLHHDC VPSIVHRDVK SSNILLDDEF GAKVADFGVA
     KIFKGANQGA ESMSIIAGSY GYIAPEYAYT LRVNEKSDIY SFGVVILELV TGKPPLDAEY
     GEKDLVKWVH STLDQKGQDE VIDPTLDIQY REEICKVLSV GLHCTNSLPI TRPSMRSVVK
     MLKEVTELPK SFSGKLSSPY FQEETSDIDH QGSLV
//
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