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Database: UniProt
Entry: A0A0D9WEG7_9ORYZ
LinkDB: A0A0D9WEG7_9ORYZ
Original site: A0A0D9WEG7_9ORYZ 
ID   A0A0D9WEG7_9ORYZ        Unreviewed;       936 AA.
AC   A0A0D9WEG7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Leersia perrieri.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX   NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR05G07590.6, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR05G07590.6, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:LPERR05G07590.6, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA   Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA   Zhang J., Wing R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:LPERR05G07590.6}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; A0A0D9WEG7; -.
DR   EnsemblPlants; LPERR05G07590.6; LPERR05G07590.6; LPERR05G07590.
DR   Gramene; LPERR05G07590.6; LPERR05G07590.6; LPERR05G07590.
DR   Proteomes; UP000032180; Chromosome 5.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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; IPR032675; LRR_dom_sf.
DR   InterPro; IPR021720; Malectin_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48006; LEUCINE-RICH REPEAT-CONTAINING PROTEIN DDB_G0281931-RELATED; 1.
DR   PANTHER; PTHR48006:SF53; NON-SPECIFIC SERINE/THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF11721; Malectin; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..936
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002348932"
FT   TRANSMEM        530..555
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          590..882
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          905..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..930
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   936 AA;  103413 MW;  AB2E8D5DA279F461 CRC64;
     MRRYCSSWIS GFACHLVWLV LVCSWSWTWR IAAAQAQQSP KTDPLEMTAL NTILGRWGKT
     ASSEWNISGE PCSGLAADKN DWDYYPNINP FIKCDCSFSN NTVCHIIKLR VVNFSVVGQI
     PSELQNFTYM QDLNLGYNYL TGALPSFFGK ALPFNALSGP LPKELGNLTN LLSLGISFNN
     YSGQLPEELG NMTNLQQMRA SDNEFTGKIP DYLGSMPNLE DIRIGDIVNG SSSLSFISNF
     TSLSNLILRN CKISGNLGPV DFSKFAALIL LFLGNNSLTG SLPDAISPSL NTIDFSYNQL
     TGSLPSWATQ NNLQLNLVAN NFVLGSTDHS NRSTRGFDGT IYEADAPNLG TASYYVTSET
     RWGVSNVGNY FLATDGTNII NSLQKFQNAV DSKLFETARM SASSVRYYGL GLENGNYTVL
     LQFAEFGYPD SQTWVSLGRR VFDIYIQGDL KEKNFDIRKT AGGKSFTAVN RTYTVTVSKN
     FLEIHLFWAG KGTCCVPIQG YYGPMVSALS VTPNFTPTVR NGVPKRRSKA GVIAGISIGA
     LILGLVALFG IFMIVKKRRT IAQQKEELYN LVGQPDVFSN TELKLATDNF SSHNIIGEAF
     CNLSVQNIHV TSGKFFLRQG KLPDGRVVAV KQLSETSHQG KGEFVTEVAT ISAVQHRNLV
     KLHGCCIDSK TPLLVYEYLE NGSLDRAIFG KSSLNLDWAM RFEIILGIAR GLTYLHEESS
     VRIVHRDIKA SNVLLDSDFT PKISDFGLAK LYDEKKTHVS TRIAGTLGYL APEYAMRGHL
     SEKADIFAFG VVMLETVAGR SNTNNSLEES KIYLLEWAWG MYEMGQTLQV VDPSLEEFDE
     DEAFRVIRIA LLCTQGSPHQ RPSMSKVVAM LSGDVDVADV FTKPSYVTEW QLKDGWTSSY
     TSSSYAGSSN TDFSRQKETN PLTLSPTITK ANLEAR
//
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