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Database: UniProt
Entry: A0A0D9V5E8_9ORYZ
LinkDB: A0A0D9V5E8_9ORYZ
Original site: A0A0D9V5E8_9ORYZ 
ID   A0A0D9V5E8_9ORYZ        Unreviewed;       649 AA.
AC   A0A0D9V5E8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
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:LPERR01G25880.1, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR01G25880.1, 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:LPERR01G25880.1, 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:LPERR01G25880.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
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DR   AlphaFoldDB; A0A0D9V5E8; -.
DR   STRING; 77586.A0A0D9V5E8; -.
DR   EnsemblPlants; LPERR01G25880.1; LPERR01G25880.1; LPERR01G25880.
DR   Gramene; LPERR01G25880.1; LPERR01G25880.1; LPERR01G25880.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_000288_106_3_1; -.
DR   Proteomes; UP000032180; Chromosome 1.
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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR047117; PERK1-13-like.
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; PTHR47982; PROLINE-RICH RECEPTOR-LIKE PROTEIN KINASE PERK4; 1.
DR   PANTHER; PTHR47982:SF32; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        215..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          320..596
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          28..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..180
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..261
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         349
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   649 AA;  70049 MW;  90CE8F9F7A78C2BA CRC64;
     MGMGAYTDPF LPPKMVSSAA FVAPMGAYGQ PQAAPRPPAC PYASSSSPPP VSASYHSWPP
     ATSASPVSSP PPVSSPPESS PPPALPPPPP DAAPPSLPPS PPPPPMSTDQ PRVQPRVYPS
     PPPPSLPPPP TSPTFSPPSP PPFHPPSSSP APAPAPAVVY PPPPPPRIAP PPPPRNHIKP
     HYAPRSPARS HSNSTRASSG AGKNIEISRE AATTIVALAG LAMLSFVGAT IWFVKKKRRR
     IEPPASLPTQ QPAPPPPPNY FASSGGSSLT SDAFFRSPGY PLRMFSAGSH GYPYSPADSG
     IGYSRMLFTP ENLAEFTNGF AEQNLLGEGG FGCVYKGILP DNRLVAVKKL KIGNGQGERE
     FRAEVDTISR VHHRHLVSLV GYCIADGQRM LVYDFVPNNT LYYHLHVSEA AVLDWRTRVK
     IAAGAARGIA YLHEDCHPRI IHRDIKSSNI LLDDNFEAQV SDFGLARLAA DSNTHVTTRV
     MGTFGYLAPE YALSGKLTAK SDVYSFGVVL LELITGRKPV DASQPLGDES LVEWARPLLM
     KAIEHREFGE LPDPRMENRF DENEIYHMIG AAAACIRHSA AMRPRMGQVV RALDSLADSN
     LNNGLQPGRS EVFLEPQSEE IRLFQLREFG SRDCSDEMSQ ASWRSRRDL
//
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