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Database: UniProt
Entry: A0A0E0INB5_ORYNI
LinkDB: A0A0E0INB5_ORYNI
Original site: A0A0E0INB5_ORYNI 
ID   A0A0E0INB5_ORYNI        Unreviewed;      1370 AA.
AC   A0A0E0INB5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
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:ONIVA09G19970.2};
RN   [1] {ECO:0000313|EnsemblPlants:ONIVA09G19970.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA09G19970.2};
RA   Wing R.A., Hsing Y.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ONIVA09G19970.2}
RP   IDENTIFICATION.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA09G19970.2};
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   -!- 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   EnsemblPlants; ONIVA09G19970.2; ONIVA09G19970.2; ONIVA09G19970.
DR   Gramene; ONIVA09G19970.2; ONIVA09G19970.2; ONIVA09G19970.
DR   HOGENOM; CLU_000288_116_4_1; -.
DR   Proteomes; UP000006591; 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: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; 2.
DR   CDD; cd01098; PAN_AP_plant; 2.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
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; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR32444:SF229; OS05G0163500 PROTEIN; 1.
DR   Pfam; PF01453; B_lectin; 2.
DR   Pfam; PF08276; PAN_2; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00954; S_locus_glycop; 2.
DR   SMART; SM00108; B_lectin; 2.
DR   SMART; SM00473; PAN_AP; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50927; BULB_LECTIN; 2.
DR   PROSITE; PS50948; PAN; 2.
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   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006591};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          84..216
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          410..495
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          520..656
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          845..931
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          1031..1325
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         1059
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1370 AA;  148873 MW;  DE321B6BCA924FEB CRC64;
     MASGKADVGV GGGEAMRRFN NSGRRLPVFF LGFNPTELPV PGTMSGGSWR APSSGERRPE
     MNWIAFNYLT TAIFLLLLPA CVADDQLVPG KPLSIGSTVV SNGGAFALGF FSPTNSTSSN
     LYLGIWYNDI SPLTLVWVAN RGTPVKDGGH GSSSSAPSLT LSNSSGLVLA DGDGRVLWTT
     DITIIAANSP AVAVLMNTGN LVVRSPNGAT LWQSFDHPTD TYLPGMKIGI NYRTRVGERL
     LSWNDGPGDP SPGSFSFGGD PDTFLQLFIW NQSRPYWRSP VWTGNPIPSQ LMVNGTTVIY
     LSVVDADDEI YLSFGISDRA PRTRYVLTNS GKLQVLSWDG GDGASEWSKL GELPKYECEH
     YGYCGPYGYC YYSEVAPTCE CLDGFEPRSK EEWSNGRFSR GCRRTEELPC GGDGGDAVFL
     EMQGMQLPDK FVRVRNKTFH ECAAECAGDC SCTAYAYANL GGSGSARKDA TRCLVWLGEL
     IDTQKVGPDW VPWGIMDWSS SAFTCIAAFL LLSPALCAAD DRIVSGKPLS PGAAVISDGG
     DFALGFFAPS NSTPAKLHLG IWYNNIPRRT VVWVANRATP IIVNGSSNSS LPSLAMTNTS
     DLVLSDASGQ IVWTTNLTAV ASSSSLSPSL STAVLMNTGN LVVRSQNGTV LWQSFSQPTD
     TLLPGMKVRL SYRTLAGDRL VSWKSPEDPS PGSFSYGGDS DTFVQFFIWN GSRPAWRAGV
     WTGYMVTSSQ FQANARTAVY LALVDTDNDL SIVFTVADGA PPTHFLLSDS GKLQLLGWNK
     EASEWMMLAT WPAMDCFTYE HCGPGGSCDA TGAVPTCKCL DGFEPVSAED GLFSRGCRRK
     EALRCSGDGH FVALPGMKVP DRFVHVGNRS LDECAAECGG DCNCVAYAYA TLNSSAKSRG
     DVTRCLVWAG DGELVDTGRL GPGQVWGTVG AGGDSRETLY LRVAGMPNSG KRKQRNAVKI
     AVPVLVIVTC ISLSWFCIFR GKKRSVKEHK KSQVQGVLTA TALELEEAST THDHEFPFVK
     FDDIVAATNN FSKSFMVGQG GFGKVYKGML QGCQEVAVKR LSRDSDQGIV EFRNEVTLIA
     KLQHRNLVRL LGCCVEGHEK LLIYEYLPNK SLDVAIFKSE RGVTLDWPAR FRIIKGVARG
     LVYLHHDSRL TIIHRDLKTS NVLLDSEMRP KIADFGMARI FGDNQQNANT RRVVGTYGYM
     APEYAMEGMF SVKTDVYSFG VLLLEVISGV KISNIDRIMD FPNLIVYGVL MQSEDAWSLW
     MEGRAKELVD LNITESCTLD EALLCIHVGL LCVQENPDDR PLMSSVVSIL ENGSTTLPTP
     NHPAYFAPRK NGADQRRDNV FNSGNEMTLT LELSSFISQL VAKLILIITG
//
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