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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//