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Database: UniProt
Entry: A0A0D9X5C0_9ORYZ
LinkDB: A0A0D9X5C0_9ORYZ
Original site: A0A0D9X5C0_9ORYZ 
ID   A0A0D9X5C0_9ORYZ        Unreviewed;       949 AA.
AC   A0A0D9X5C0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
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:LPERR08G05480.2, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR08G05480.2, 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:LPERR08G05480.2, 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:LPERR08G05480.2}
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; A0A0D9X5C0; -.
DR   EnsemblPlants; LPERR08G05480.2; LPERR08G05480.2; LPERR08G05480.
DR   Gramene; LPERR08G05480.2; LPERR08G05480.2; LPERR08G05480.
DR   Proteomes; UP000032180; Chromosome 8.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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; 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:SF34; OS08G0203400 PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 3.
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   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..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..949
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002349468"
FT   TRANSMEM        545..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          603..875
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          905..949
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..941
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   949 AA;  104451 MW;  1A413B5819614260 CRC64;
     MKKRCSSSGG GGHGSQLLWV VIAWSWIAAD RAQAQQAPRT DPVEVAALNA ILGRWGTKPP
     TAWNTTGDPC SGTAVDDTDI DNDPVINPGI KCDCSYSNRT VCHITRLNLQ QNYLTGPVPS
     FIGKLTSMQY LSLAINALSG PIPREIGKLT DLRSLALSMN KFVGPLPEEI QTLTKLEQLW
     ASDNEFTGLI PDYFGIFSDL EILKLQGNNF DGPIPASLSN LSKISSLRIG DLTSGTSSMD
     FVSNMTSLNV LILRNCRIYG NLTAMNFSQL LTLTYLDLSF NSITGEIPPA LLNLSLLDSL
     FLGSNNLSGN LPDNIGPSLS VMNLVWNNFV VDSSNGRAST RGSDKNSYEP DDANLLGASY
     YVTSSTRWGV SNTGRFMESP NATNLIYTPF QFNNTLDTKL FQTARMSPSS LRYYGIGLKN
     GFYDVKLQFA EIFFPDNQTW KSVGRRIFDI YIQGELREKD FDIKKDTNGK SYTVVQRQYN
     VEVTKNFMEI HLFWAGKGTC CIPFLQGHYG PSISALSVSS YGEEDPGQKK NNTGGGNASN
     RKISLIVGIV VGVVVLVSLA LTGAFVWRQK GKRSELGMEE LLSIVGRPDI FSYGEIKSAT
     NNFSPQNILG KGGYGPVYKG KLFDGSMVAV KQLSATSHQG KREFMTEIAT ISAVQHRNLV
     KLHGCCIENN TPLLVYEYLE NGSLDQAIFG KTNLNLDWST RFDICVGIAR GLAYLHEESS
     TRIVHRDIKA SNVLLDADLN PKISDFGLAR HYKDNMTHLS TGVAGTLGYL APEYAMMGHL
     TEKADVFAYG IVAMEIIAGR PNFDESLEDD KKYLLGSVWR LHESMETLKI LDPNLSEFNE
     EEVVRVINII LVCTMGQPQQ RPSMSKVVSM LTEDIEMTEV DTNMRPSYVP HLQLKSGSDS
     FFASYSSGSS TQQTSGSQVS SGNNTKSQRE TFPLVLSTHS SSEFDEGRR
//
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