ID   A0A0D9VWT3_9ORYZ        Unreviewed;      1900 AA.
AC   A0A0D9VWT3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
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:LPERR03G22640.3, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR03G22640.3, 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:LPERR03G22640.3, 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:LPERR03G22640.3}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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DR   EnsemblPlants; LPERR03G22640.3; LPERR03G22640.3; LPERR03G22640.
DR   Gramene; LPERR03G22640.3; LPERR03G22640.3; LPERR03G22640.
DR   Proteomes; UP000032180; Chromosome 3.
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; 2.
DR   CDD; cd16279; metallo-hydrolase-like_MBL-fold; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
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; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
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:SF165; OS03G0642600 PROTEIN; 1.
DR   PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF13947; GUB_WAK_bind; 2.
DR   Pfam; PF12706; Lactamase_B_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS01187; EGF_CA; 1.
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   Kinase {ECO:0000256|ARBA:ARBA00022777};
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}.
FT   DOMAIN          751..1042
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1546..1840
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1848..1882
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1851..1865
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         779
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1575
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1900 AA;  206886 MW;  E154C85368104DB9 CRC64;
     MEPPVAAAAS SSSLIFLGTG CSGALPDARC LIHPSTPPCP VCSQSLSLQP ERNPNYRCNT
     SLLIDYCQDD GTHKYILIDV GKTFREQVLR WFIYHKIPYV DSMTLLTRFR TMQIILTHEH
     ADAVLGLADV WLVQPSNEFG QVPIFLTQFT MDSVAARFPY LMKNKLEEDD EASQVPQFNW
     KIIEGDIDKP FVSSGLEFVP LPVRATVVMH GEDYVCLGFL FGRKERIAYL SDVSRILPRT
     EHAISKSGGQ LDLLILETNM LHGEGDAGSC HLTLSQTLNA VKRISPRKAL LIGMNHEFEH
     QKENQTLAEW SSRTPATTMQ EAQSPRFFLL VVFLATATTS SSSSVSPAAA GRALSLPGCP
     DKCGNVSIPY PFGIGDRCAA VGLNPYFNLT CDGSRSPPVP KVGDPGMQAV ILDIELDRGE
     LRLNGYVNYV CYSSNTTTSL TAPPGGLGVR DTELRLSPSR NQLTVIGCNA LGLAGGTHMD
     RLGIVDDYAT GCYTHCAGVN STDPDGAPCA GAGCCQLPIS PDLASVVTGF PPNWTNTAWE
     FNPCLYAVIA EVGWYSFRRR HLAGVLGFFN ETRRTRIPIV LDWAVRDGSY CPVTPEEKVR
     RMYACKSANS YCVNSTNGIG YSYVDECALR RQGRQYEDMH PCKHGICINT PGSYHCKCKA
     GTKLDGTNFG CQQVLPVAAK VIIGLSACSI VVMALSCLLV IQLQRRKHIT EKQEYFRRNG
     GLRLYDEMMS RQVDTVRVLT LDEIKKATDN FSDDRVLGRG GHGTVYHGTL DDLRQVAIKR
     SKAAAIDDGD DDGGCIKEEF VNEIIVLSQI NHRHVVRLLG CCLEVHVPML VYEFVPNGTL
     FDLLHGRNGA GVRRPVSLGL RLKIAAQSAE ALAYLHSSAS RAILHGDVKS LNILLDDVLD
     AKVADFGASA LRSMDEGEFV EFVQGTLGYL DPESFVNREL TDKSDVYSFG VVLVELIARK
     KAVYDDGVSG EKRSLSSTFL AVVSARGELW RVVDREIMDG ISDDAATASV VRELAELAAR
     CMGPSGEERP AMKEVAERLE VLRRLEMQVD VRRKSNGGEE VDAGFYGGGG VGQHGHLDMT
     TSSYYQSMET DKLQLDDLDL QTVTMQEAWF GFLLLLLIST ATSSTSAVSP TAGRVVTLPG
     CPDKCGNVTI PYPFGVGDRC AAVGLNPYFN LTCNGSRSPP VPMWGDPGLQ VEVIDISLDR
     GELRLYALPS YVCYASANNL STNQTFFLSL EGSPFRVSSS RNRLTVIGCS TLGMAAGTGG
     AARGDDDVYA TGCYTYCGSL NVTGGDGAPC AGTGCCQVAI SADVPYLGAV VQVDNWTNTA
     WRFNPCFYAM VAEDGWYSFR RRDLEGVLRY YNETVEAGGV PVVIDWAVRD GWCPATEEKY
     ACVSANSHCV NSTNGIGYTC HCSQGYQGNP YLNDGCQDIN ECALREQDPK YEEMYPCRHG
     MCVNTPGSYR CKCKAGRKKD GTNFGCQPVL PMAAKVVVGL SACAILAMTV SSFLVIRLER
     RKHKQEKLQY FKQNGGLKLF EEMVSRQVDT VRVLTEDELK KATNNFKDDQ VIGCGGHGTV
     YRGTLDDHRQ VAIKKSKAAA IDVDGDDGSG CKDEFINEII VLSQINHRHI VRLLGCCLEV
     HVPMLVYEFV PNGTLFNLLH GGNGAGVRRP VSLGLRLKIA AQSAEALSYL HSSASTAILH
     GDVKSLNILL DGELDAKVAD FGASALKSMD EGEFIEYVQG TLGYLDPESF VNRHLTDKSD
     VYSFGVVLAE LATRKKAVYD DGNGVKRSLS TVFPAALRHG ELWSVLDRDL LVGAAAADED
     DKATAAGVVR ELAELAARCM GPSGEERPSM KEVAERLQVL RRAEMQATVA GAGRGSSSDG
     QVDQWNMYGG ESGGRGHLDT TASYQSTEVD RLTLSVDLAR
//