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Database: UniProt
Entry: A0A0D9WZW0_9ORYZ
LinkDB: A0A0D9WZW0_9ORYZ
Original site: A0A0D9WZW0_9ORYZ 
ID   A0A0D9WZW0_9ORYZ        Unreviewed;       642 AA.
AC   A0A0D9WZW0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
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:LPERR07G14870.1, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR07G14870.1, 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:LPERR07G14870.1, 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:LPERR07G14870.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR   AlphaFoldDB; A0A0D9WZW0; -.
DR   STRING; 77586.A0A0D9WZW0; -.
DR   EnsemblPlants; LPERR07G14870.1; LPERR07G14870.1; LPERR07G14870.
DR   Gramene; LPERR07G14870.1; LPERR07G14870.1; LPERR07G14870.
DR   eggNOG; ENOG502QWDY; Eukaryota.
DR   HOGENOM; CLU_000288_35_7_1; -.
DR   Proteomes; UP000032180; Chromosome 7.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002902; GNK2.
DR   InterPro; IPR038408; GNK2_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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; PTHR27006:SF554; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE ISOFORM 1; 1.
DR   PANTHER; PTHR27006; PROMASTIGOTE SURFACE ANTIGEN PROTEIN PSA; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01657; Stress-antifung; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51473; GNK2; 2.
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   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..642
FT                   /note="Protein kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002349768"
FT   TRANSMEM        289..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..127
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          142..254
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          350..631
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         379
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   642 AA;  70505 MW;  C9007C84B0ABF086 CRC64;
     MLAGYGILAV VVAVLMLPSG TPAEMFECEM GVTSTYQSNR TFEANLNLLA ANVSSAPAGY
     AVATVGAAPD QVYGLALCRG DVVVANASAC RACVAAAYAD GKRNCSGVSG VTMYEDACVV
     RFSRQRFMDS LNADQWNVEA MIWRQEVSPS SVKVPEVGWF NAAVTKILAA LINNAVAATG
     NSSTMKYFVT GEVKDFDPKI YGFAQCVPEL TSKQCNECLT TLLFYEKQAY LGKSLLWVRT
     NSVWCRLTYD LQPFYGGRAM LQVSAPPSPP AVETPVLIPG PGAGKRKSVA GIVAGVASSV
     VVLLILSIFA YVFFRRRTKV TQTEHSLKKI TRGQCMIFDL SVLQQATENF SQNNKLGEGG
     FGAVYKGVLS DGHEVAVKKL VGTTEHGLDQ LHNEIQLLAE LQHKNLVRLQ GFCLHQGQTL
     LVYEYVKNRS LDNFIFDTSR ENALKWDQQY NIILGIAKGI LYLHEDSSLR IIHRDLKSNN
     ILLGDDMEPK IADFGLARLL AEGHTHTMTS RIVGTYGYMA PEYALDGNVS TKIDIFSFGV
     LVLEILTRIR NRHSDHHDLA SEVWNCWTKG TVTKMVDQSL DGFSEKQALR CIHIGLLCVQ
     SDPDDRPHIS SVIFMLTREN TELQPPAQPA FFFETESASS SP
//
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