ID A0A0D9VB90_9ORYZ Unreviewed; 733 AA.
AC A0A0D9VB90;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:LPERR02G00730.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR02G00730.1, 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:LPERR02G00730.1, 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:LPERR02G00730.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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DR AlphaFoldDB; A0A0D9VB90; -.
DR STRING; 77586.A0A0D9VB90; -.
DR EnsemblPlants; LPERR02G00730.1; LPERR02G00730.1; LPERR02G00730.
DR Gramene; LPERR02G00730.1; LPERR02G00730.1; LPERR02G00730.
DR eggNOG; ENOG502QQPF; Eukaryota.
DR HOGENOM; CLU_000288_43_5_1; -.
DR Proteomes; UP000032180; Chromosome 2.
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 CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
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:SF482; OS01G0580150 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; SSF57196; EGF/Laminin; 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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..733
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002347639"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 415..687
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 733 AA; 81299 MW; 5CBA9B0B1656E1A1 CRC64;
MARLLILASI LLLGVIKITM ASRMAKPGCR ETCGNLTITY PFGIGDGCFY SPGFDVSCED
SRTYMHNSSS QMEIYNISLL TGQVRVSSLI ASECYSTTGR IERGWASVNT ATLFTISSKA
NKLTAIGCNT LAFLNGYNEQ EVGAGCFSMC LENQTVDSGR QCSGMGCCQT SIAPNLTSFN
VTFDSRFNNS QVLNFNPCSY AFVVEQDWFR FEAAYLEGNK LTEKYNDGVP AVLDWVAGYE
SCDEAQKNRS SYACVSANSR CISSPDATGY LCVCKNGFAG NPYLEEGCQD IDECKFPDQY
PCNGICSNAI GDYRCNCQPG THSIDPKKET CSPNTTSERA RLTKMFIGIS VCAILLLVCI
FALVIECQKR KLTKEKERFF QQNGGLLLYE QIRSKQVDTV RIFTKQELES ATDNFDSSRE
LGRGGHGTVY KGILKDNRVV AIKRSKIMNM VQKDEFVQEM IILSQINHRN VVKLLGCCLE
VEVPMLVYEF IPNGTLFELI HGKYRTSSIS MDARLRIAQE SAEALAYLHS SASPPIVHGD
VKSPNILLGD NYIAKVTDFG ASRMLPKDEI QFMTMVQGTI GYLDPEYLQE RQLTEKSDVY
SFGVVLLELI TGKTAIYSDS VEEKKSLASS FLLALKENRL QTILDGDILV VGTELLQDVA
QLAKRCLSMK GEERPFMTEV AEGLKAIRST WREQLIESAN EETVCLLQNT LQYDPSITGQ
HGSLMTLDLE TGR
//
