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Database: UniProt
Entry: A0A445LRN9_GLYSO
LinkDB: A0A445LRN9_GLYSO
Original site: A0A445LRN9_GLYSO 
ID   A0A445LRN9_GLYSO        Unreviewed;       997 AA.
AC   A0A445LRN9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=D0Y65_004578 {ECO:0000313|EMBL:RZC25953.1};
OS   Glycine soja (Wild soybean).
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=3848 {ECO:0000313|EMBL:RZC25953.1, ECO:0000313|Proteomes:UP000289340};
RN   [1] {ECO:0000313|EMBL:RZC25953.1, ECO:0000313|Proteomes:UP000289340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC   TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZC25953.1};
RA   Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT   "A high-quality reference genome of wild soybean provides a powerful tool
RT   to mine soybean genomes.";
RL   Submitted (SEP-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RZC25953.1}.
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DR   EMBL; QZWG01000002; RZC25953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445LRN9; -.
DR   Proteomes; UP000289340; Chromosome 2.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; PTHR27008; OS04G0122200 PROTEIN; 1.
DR   PANTHER; PTHR27008:SF281; OS06G0186100 PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 9.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
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; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS51450; LRR; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RZC25953.1};
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}; Receptor {ECO:0000313|EMBL:RZC25953.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289340};
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        622..644
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          694..989
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         722
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   997 AA;  110500 MW;  6941B96923F0BCD2 CRC64;
     MSELSSENSN KKSENALSDE ESCIKQTSII FRSIVLLFFF LGTVQSRVLH GKENAGIVNG
     KNSLISFMSG IVSDPQNALK SWKSPGVHVC DWSGVRCNNA SDMIIELDLS GGSLGGTISP
     ALANISSLQI LDLSGNYFVG HIPKELGYLV QLGQLSLSGN FLQGHIPSEF GSLHNLYYLN
     LGSNHLEGEI PPSLFCNGTS LSYVDLSNNS LGGEIPLNKE CILKDLRFLL LWSNKLVGQV
     PLALAYSTKL KWLDLELNML SGELPFKIVS NWPQLQFLYL SYNNFTSHDG NTNLEPFFAS
     LVNLSHFQEL ELAGNNLGGK LPHNIGDLPT SLQQLHLEKN LIYGSIPPQI GNLVNLTFLK
     LSSNLLNGSI PPSLGHMNRL ERIYLSNNSL SGDIPSILGD IKHLGLLDLS RNKLSGPIPD
     SFANLSQLRR LLLYDNQLSG TIPLSLGKCV NLEILDLSHN KITGLIPAEV AALDSLKLYL
     NLSNNNLHGS LPLELSKMDM VLAIDVSMNN LSGSVPPQLE SCTALEYLNL SGNSFEGPLP
     YSLGKLLYIR ALDVSSNQLT GKIPESMQLS SSLKELNFSF NKFSGRVSHK GAFSNLTIDS
     FLGNDGLCGR FKGMQHCHKK RGYHLVFLLI PVLLFGTPLL CMLFRYSMVT IKSKVRNRIA
     VVRRGDLEDV EEGTEDHKYP RISYKQLREA TGGFSASSLI GSGRFGQVYE GMLQDNTRVA
     VKVLDTTHGE ISRSFRREYQ ILKKIRHRNL IRIITICCRP EFNALVFPLM PNGSLEKYLY
     PSQRLDVVQL VRICSDVAEG MSYLHHYSPV KVVHCDLKPS NILLDEDMTA LVTDFGISRL
     VQSDENTSIN ESASFSSTHG LLCGSVGYIA PEYGMGKHAS TEGDVYSFGV LVLEMVSGRR
     PTDVLSHEGS SLCEWIKKQY THQHQLENFV EQALQRFSPC GVPNHRNKIW KDVILELIEL
     GLVCTQYNPS TRPSMHDIAQ EMERLKDYLT KSNLPPH
//
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