ID A0A0E0GP70_ORYNI Unreviewed; 836 AA.
AC A0A0E0GP70;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA03G23480.3};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA03G23480.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA03G23480.3};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA03G23480.3}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA03G23480.3};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433,
CC ECO:0000256|PIRNR:PIRNR000641};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775,
CC ECO:0000256|PIRNR:PIRNR000641};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A0E0GP70; -.
DR STRING; 4536.A0A0E0GP70; -.
DR EnsemblPlants; ONIVA03G23480.3; ONIVA03G23480.3; ONIVA03G23480.
DR Gramene; ONIVA03G23480.3; ONIVA03G23480.3; ONIVA03G23480.
DR eggNOG; ENOG502QRH4; Eukaryota.
DR OMA; DCRLSGQ; -.
DR Proteomes; UP000006591; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR CDD; cd00028; B_lectin; 1.
DR CDD; cd00053; EGF; 1.
DR CDD; cd01098; PAN_AP_plant; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR47974:SF31; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR47974; OS07G0415500 PROTEIN; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00954; S_locus_glycop; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000641};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000641}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000006591};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000641}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 461..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..148
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 280..315
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 330..413
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 523..802
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 551
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 836 AA; 93475 MW; CBA72347F3E66C77 CRC64;
MCSTTGEVTA AASAPRGLLA GAAGARRLSV PAATSPLSPD NDVLQSADGT FSCGFLTIYS
NAFAFSIWYT NSKNKTVVWT ANRGRPVHAR RSVVTLQKDG AMVLKDYDGT VVWQSDSNSI
DVQYAQLLDT GNLVMKNSSG KVVWQSFDSP TDTLLPTQKI TAATKLVSTT GLYVPGHYTF
HFTDSSILSL MYDDADVHEI YWPDPDRGEY GNKRNRYNNT RMGFLDDNGD FVSSDFADQQ
PFSASDKGSG IKRRLTLDHD GNLRLYSLSN GEWLVSWVAI SQPCNIHGLC GPNGICHYSP
TPTCSCPPGY EMNSHGNWSQ GCKAIVDISC SVAKVQFKFV HLPDTDFWGS DQQLVNHVSW
QACMNICRSD CNCKGFQYLK GEGTCFPKSF LFNGRAYPSH FVSPRSMYLK IPISMNISGM
PVSQSNVLDS RKHSLNCDQM DEKTRELFPD VHKTSQGETR WFYLCGFAGA IFILEVFFIG
FAWFFVSRWD LDALEIQAVE QGYKVMASNF RRYNYKELAK ATRKFKCELG RGGSGIVYKG
TLDDGRVVAV KMLENVRQCE EEFQAELRII GKINHMNLVR IWGFCSENSH RMLVTEYIEN
GSLANILFNE NILLEWRQRF NIAVGVAKGL AYLHHECLEW VIHCDVKPEN ILLDGNFEPK
IADFGLAKLL NRGGSNQNVS RVRGTIGYIA PEWISSLQIT AKVDVYSYGV VLLELVSGKR
VLDLATNANE EVHVVLRRLV NMFVNNLSGN EPSWIAEFVD CRLSGQFNYT QVRTMITLAV
ACLDEERSKR PTMESIVQLL LLVDESCSSN VLCPEMPTRW TTGHAKANAS FCIHSL
//