GenomeNet

Database: UniProt
Entry: A0A0E0GP70_ORYNI
LinkDB: A0A0E0GP70_ORYNI
Original site: A0A0E0GP70_ORYNI 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system