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Database: UniProt
Entry: A0A0D9Y1G2_9ORYZ
LinkDB: A0A0D9Y1G2_9ORYZ
Original site: A0A0D9Y1G2_9ORYZ 
ID   A0A0D9Y1G2_9ORYZ        Unreviewed;       758 AA.
AC   A0A0D9Y1G2;
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=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
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:LPERR12G15840.1, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR12G15840.1, 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:LPERR12G15840.1, 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:LPERR12G15840.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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DR   AlphaFoldDB; A0A0D9Y1G2; -.
DR   STRING; 77586.A0A0D9Y1G2; -.
DR   EnsemblPlants; LPERR12G15840.1; LPERR12G15840.1; LPERR12G15840.
DR   Gramene; LPERR12G15840.1; LPERR12G15840.1; LPERR12G15840.
DR   eggNOG; ENOG502QQPF; Eukaryota.
DR   HOGENOM; CLU_000288_43_5_1; -.
DR   Proteomes; UP000032180; Chromosome 12.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045274; WAK-like.
DR   InterPro; IPR025287; WAK_GUB.
DR   PANTHER; PTHR27005:SF165; OS03G0642600 PROTEIN; 1.
DR   PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR   Pfam; PF13947; GUB_WAK_bind; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS01187; EGF_CA; 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}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; 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   Signal {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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..758
FT                   /note="Protein kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002350683"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          435..715
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         464
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   758 AA;  84516 MW;  D9CC9682FC79AEDC CRC64;
     MAQLHTSFLL MLIVFHTMAT STTASEPTIS LPGCPDKCGN ISIPYPFGIG AGCAATSLSS
     YFTITCNDTF QPPRPMVRDK LETREVISIS LEHGEVRIYG PVSYTCFTSN TTMPDNSTTG
     FTLEGTPFVP STTRNRFMVI GCNALGIIGG YMHNNPDLYV GGCYSYCQGI KSTSNGALCT
     GMGCCETTII PDLTDFAAIL VMNQSTVWDF NPCFYAMLVE VGWYRFRQQD LVGHLSFVNE
     RANRGVPVIH DWAIRNGSCP EGKKVPKDYA CVSSNSNCVQ ASNSQGYLCK CSEGYEGNPY
     LPNGCQDIDE CKLCMEDPKY KELYPCRHGI CQNIPGGYMC KCGIGKRSDG TNYGCQPALG
     HVERVVAGLS VSAVVVMALV CLLVMKLQRR KHRKEKDEYF KQNGGLRLFD EMRSKQVDTI
     RILTEKEIKK STENYSDDRV LGCGGHGMVY KGTLDDGKEV AIKKSKVIGD YCREEFVNEI
     IILSQINHRN IVKLLGCCLE VDVPMLVYEF VSNGTLSEFL HGNDRQTPIP LDLRLNIATQ
     SAEALAYIHS STSRTILHGD VKSLNILLDD EYNAKVADFG ASALKPMDKN DFIMFVQGTL
     GYLDPETFVS HHLTDKSDTY SFGVVLLEIM TRKKAFYNDN LNEKKALSHI FPLMFHQQRL
     CDMLDYEIIE DKVMVVLQKL AELAMHCLNP RGADRPTMKE VAERLQILRR LHMQLVSKSG
     PVRVHYCFKG SSMSVPLDPM KYQSMETAKL VLDADIAR
//
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