ID A0A445KXM8_GLYSO Unreviewed; 1011 AA.
AC A0A445KXM8;
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_009169 {ECO:0000313|EMBL:RZC15707.1};
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:RZC15707.1, ECO:0000313|Proteomes:UP000289340};
RN [1] {ECO:0000313|EMBL:RZC15707.1, 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:RZC15707.1};
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:RZC15707.1}.
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DR EMBL; QZWG01000004; RZC15707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445KXM8; -.
DR OrthoDB; 940962at2759; -.
DR Proteomes; UP000289340; Chromosome 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 CDD; cd14066; STKc_IRAK; 1.
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:SF29; SERINE-THREONINE PROTEIN KINASE, PLANT-TYPE; 1.
DR Pfam; PF00560; LRR_1; 5.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
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; 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:RZC15707.1};
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:RZC15707.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000289340};
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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1011
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019334334"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 701..985
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 731
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1011 AA; 112221 MW; F961F4EB8D381429 CRC64;
MSKIHLFMLK FPFHLLLLLS VIVPFQVISQ SENTEQTILL TLKHELGDPP SLRSWIPSPS
APCDWAEIRC AGGSVTRLLL SGKNITTTTK NLSSTICNLK HLFKLDFSGN FISDEFPTTL
YNCTNLRHLD LSDNNLAGPI PADVDRLETL AYLNLGSNYF SGEIPPAIGN LPELQTLLLY
KNNFNGTIPR EIGNLSNLEI LGLAYNPKLK RAKIPLEFSR LRKLRIMWMT QCNLMGEIPD
YFGNILTNLE RLDLSRNNLT GSIPRSLFSL RKLKFLYLYY NRLSGVIPSP TMQGLNLTEL
DFGNNILTGS IPREIGNLKS LVTLHLYSNH LYGEIPTSLS LLPSLEYFRV FNNSLSGTLP
PELGLHSRLV VIEVSENHLS GELPQHLCVG GALIGVVAFS NNFSGLLPQW IGNCPSLATV
QVFNNNFSGE VPLGLWTSRN LSSLVLSNNS FSGPLPSKVF LNTTRIEIAN NKFSGPVSVG
ITSATNLVYF DARNNMLSGE IPRELTCLSR LSTLMLDGNQ LSGALPSEII SWKSLSTITL
SGNKLSGKIP IAMTALPSLA YLDLSQNDIS GEIPPQFDRM RFVFLNLSSN QLSGKIPDEF
NNLAFENSFL NNPHLCAYNP NVNLPNCLTK TMPHFSNSSS KSLALILAAI VVVLLAIASL
VFYTLKTQWG KRHCGHNKVA TWKVTSFQRL NLTEINFLSS LTDNNLIGSG GFGKVYRIAT
NRLGEYVAVK KIWNRKDVDD KLEKEFLAEV EILGNIRHSN IVKLLCCYAS EDSKLLVYEY
MENQSLDKWL HGKKKTSPSG LSWPTRLNIA IGVAQGLYYM HHECSPPVIH RDVKSSNILL
DSEFKAKIAD FGLAKMLANL GEPHTMSALA GSFGYIPPEY AYSTKINEKV DVYSFGVVLL
ELVTGRKPNK GGEHACSLVE WAWDHFSEGK SLTDAFDEDI KDECYAVQMT SVFKLALLCT
SSLPSTRPSA KDILLVLRQC CHSGSTCRRA GNEFDIAPLL GDTRYIYSYK E
//
