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Database: UniProt
Entry: A0A0E0AX80_9ORYZ
LinkDB: A0A0E0AX80_9ORYZ
Original site: A0A0E0AX80_9ORYZ 
ID   A0A0E0AX80_9ORYZ        Unreviewed;      1499 AA.
AC   A0A0E0AX80;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM08G20630.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM08G20630.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM08G20630.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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DR   STRING; 40148.A0A0E0AX80; -.
DR   EnsemblPlants; OGLUM08G20630.1; OGLUM08G20630.1; OGLUM08G20630.
DR   Gramene; OGLUM08G20630.1; OGLUM08G20630.1; OGLUM08G20630.
DR   eggNOG; ENOG502QQPF; Eukaryota.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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; 3.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_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   InterPro; IPR045274; WAK-like.
DR   InterPro; IPR025287; WAK_GUB.
DR   PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR   PANTHER; PTHR27005:SF174; WALL-ASSOCIATED RECEPTOR PROTEIN KINASE FAMILY PROTEIN-RELATED; 1.
DR   Pfam; PF07645; EGF_CA; 3.
DR   Pfam; PF13947; GUB_WAK_bind; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
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:UP000026961};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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        321..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1116..1139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          397..668
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1172..1442
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         432
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1499 AA;  164987 MW;  00BC3A8798A4B41C CRC64;
     MRKYNHTLPV RCIGNDRCFR EGFKLVCDPD YDPPKLFMNG PGYEVHKIKL ARRVLHLDTG
     ITQMLGGDSY NQKWILDLDD KLFRVSADMN VFITLGCGFH FFIVLLQQQE TMLLAAANCV
     SNCRPGYPIL ATDGTCYGIG CCNASVVEDH NSYTIKLLSL SSPRAVPFNA SMVVVKGEWW
     RRADNAMLLQ QEVLSRLGAT AAGALDAARN VGVRTVVNWM LGNSSCVEAK KLSDFGCLSD
     NSECFDGPAG RGYACKCRSG YDGNPYMPNG CQDINECMLP NPPLCFGKCI NTVGSYECIC
     PGGTSGNAHI QNGCVSSKLK FSGLIIGIGL GGSLIIVVLI LAGIVVRRKF KSRRAKKLKE
     FFFKQNRGLL LHQLVDKDIA ERMIFSLEEL EKATNNFDES RKLGGGGHGT VYKGILSDQR
     VVAIKKSRYA IKREIDGFIN EVAILSQVNH RNVVKLFGCC LETEVPLLVY EFILNGTLHE
     HLHVNSAQSV PWKERLRIAL EIARSLSYLH SAASVSIIHR DIKTTNILLD DRFIAKVSDF
     GASRGIPIDQ NIVTTTIQGT FGYLDPEYYR KSRPTEKSDV YSFGVILAEL ITRRRPTSYI
     SPEGFNLTEQ FILLVSEDRL LEIVDSQITE EQGEEEAREV AEIAVMCLNL KGEDRPTMRQ
     VEVKLEGLQG AVNTIRGDQK AQRRAVQLNS PLTEESDSNI VAVGDAGYHN SSRRLSMEEE
     FCFSWNICNC KELPSCISRI LHNSFEAHCE ESKMEKHAVA LAAFTFLAAP LLQPPLFVAG
     NGSSCTTSCG NVSFEYPFGV EAGCYHPGFD LTCNHSYSPP RLFLGQESST MHQVLEISIP
     NGTVRINSSR MVFASAVLEN STTMRWEVGK SYFLSDLNII ALVGCNAQVS LRDWGDTLVN
     SCITSCPLSL ESGNGSCSGI GCCQASIAMH IPVYSISANQ VVDPGAGPDP NEPNFFVYIV
     DQASFHFDTN MVTKGISNTP EALPAMLNWL ILSNSSACSA STNASAPSSS PECRSANSFC
     KGYNDIDECK SPHIYPCYGD CKNTRGGYDC QCHHGYKGNA SILNGCQDIN ECAEPEKYSC
     YGGLCINTPG AFVCRCHDGS YGDPFTKGGC RSSKGLTIGL IVSGGSVLLL LGLAAPFIVR
     KVKLQRLISR NTDFAERMII TLQELEMATN NFDKSREVGT GGHGVVYKGI IDLHVVAIKK
     SKIIVQREID EFINEVAILS QVNHRNVVKL LGCCLETEVP LLVYEFISNG TLYHHLHVEG
     SISLPWDDRL RIALEVARAL SYLHSSASMP IFHRDIKSSN ILLDDNLTAK VSDFGASRYI
     SINETGITTA VQGTIGYLDP MYYYTGRLTS KSDVFSFGVL LMELLTRKKP IGGTFDNGDG
     LVSHFISLLS KGNLYNIIDS QVKEEEDGEV LEVATLATTC TKFKGEERPM MREVEMALES
     IVSKKGSFCN KNSQSSSRPD ENRISALYMS IEGVTKDKTI TITESSTEEE IPLSSRFSR
//
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