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Database: UniProt
Entry: A0A0E0INB4_ORYNI
LinkDB: A0A0E0INB4_ORYNI
Original site: A0A0E0INB4_ORYNI 
ID   A0A0E0INB4_ORYNI        Unreviewed;      1699 AA.
AC   A0A0E0INB4;
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:ONIVA09G19970.1};
RN   [1] {ECO:0000313|EnsemblPlants:ONIVA09G19970.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA09G19970.1};
RA   Wing R.A., Hsing Y.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ONIVA09G19970.1}
RP   IDENTIFICATION.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA09G19970.1};
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   STRING; 4536.A0A0E0INB4; -.
DR   EnsemblPlants; ONIVA09G19970.1; ONIVA09G19970.1; ONIVA09G19970.
DR   Gramene; ONIVA09G19970.1; ONIVA09G19970.1; ONIVA09G19970.
DR   eggNOG; ENOG502QSWF; Eukaryota.
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; 2.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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:SF106; OS09G0111950 PROTEIN; 1.
DR   Pfam; PF01453; B_lectin; 2.
DR   Pfam; PF08276; PAN_2; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR   Pfam; PF00954; S_locus_glycop; 2.
DR   SMART; SM00108; B_lectin; 2.
DR   SMART; SM00473; PAN_AP; 2.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS50927; BULB_LECTIN; 2.
DR   PROSITE; PS50948; PAN; 2.
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   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, ECO:0000256|SAM:Phobius};
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, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1699
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002363132"
FT   TRANSMEM        1306..1325
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..155
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          354..439
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          526..812
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          885..1026
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          1219..1289
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          1380..1657
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1677..1699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         553
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1407
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1699 AA;  184902 MW;  F032D1D8724AF49D CRC64;
     MEYAGCTCTQ AATAIFLFLL SLPLAASDDR LAVGKTLSPG ATLVSDGGAF AMGFFSPSNS
     SGLYLGIWYN NVPKLTVVWV ADQLAPITDH PSSSKLAMAD DSSNLVLSDA AGRVLWRTNV
     TAGGVNSSGA VAVLVNSGNL VLRLPDDTAL WQTFEHPSDV FMAGMKLGID YRSHSGMRIV
     SWKGAGDPSP GSFSFGVDPE RPLQAKIWNG SRVHWRSSMW TGYMVDSNYQ KGGSSAIYTA
     VVYTDDEIYA SFTLSAGAPP MHYLMSYSGD LHLQSWSNVS SAWVTNARFP RRDCSLFGYC
     GAFGYCGNST GGGAGAGGGV STCHCLEGFE PASGADWSRG DFSLGCRRKE AARCGDGFAE
     FPDMKLPDGY ALVGNMNAGE CAAACRRNCS CVAYAYADLS SSTRRDPTRC LMWGGELLDM
     EKVNESWGDL GETLYLRMAG AGRGSKRSAV KFALPIVLAS ILIPTCILIC VPKFKEMIVK
     HDGKNNKKRA LRVLSVSDEF GKEIPAQDLD FPFVEYNEIA TATENFSDAA MIGKGGFGKV
     YKGVIGGREV AIKRLSRCSE QGVVEFRNEV LLIAKLQHRN LVRLVGCSIE GDEKLLIYEF
     MANKSLDASL FNSERKSSLN WSTRFKIIKG VARGLLYLHQ DSRLTVIHRD LKASNILLDA
     EMNPKISDFG MARIFGDNQQ NGITRRVVGT YGYMAPEYAM GGIFSMKSDV YSFGVLLLEI
     VSGSRISSTD FIEDFPNLSI YAWNLWNEGK AKNMIDPSIV ASCLLDEVML CIHVGLLCVQ
     ENLNDRPLMS SVMLILENGS NSLPAPNRPA YFAQRDIEME QPRDDTQNSN NTVTLTLHLH
     KFRHNCKVQG QVSSSSMDWP ASASTCIAIL LFVFLISWPS LCASDDRLAI GKTLSPGATL
     VSDGGAFAMG FFSPSSNSTN ATSSGLYLVI WYNNIPKLTV VWVADQAAPI ADHPSSPAST
     LAVASDGNLV LSDGATGRVL WRTNVTAGVN SSASSGGGVG AVAVLANSGN LVLRLPDGTA
     LWETFENPGN AFLPGMKIGV TYRTRGGVRL VSWKGATDPS PGNFSFGGDP DRPLQVVIWK
     GSRVYWRSNP WKGYMVVDSN YQKGGRSAIY TAVVSTDEEI YAAFTLSDGA PPMQYTLGYA
     GDLRLQSWST ETSSWATLAE YPTRACSAFG SCGPFGYCGD VTATASTCYC LPGFEPASAA
     GWSRGDFALG CRRREAVRCG DGFVAVANLK LPDWYLHVGN RSYEECAAEC RRNCSCVAYA
     YANLTGSSTR DATRCLVWGG DLVDMEKVVG TWGDFGRKPR TSALRFALPI VLASVLIPIC
     ILICAPKIKE IIKKKYGENN KRRALRVLSI SDELGQEIPA KDLEFPFVEY DKILVATDNF
     SEASLIGKGG FGKVYKGVLD GREVAVKRLS SWSEQGIVEF RNEVVLIAKL QHRNLVRLVG
     CSIEGDEKLL IYEYMPNKSL DASLFKGKRK SVLDWSTRFK IVKGVARGLL YLHQDSRLTI
     IHRDLKASNI LLDAEMNPKI SDFGMARIFG NNQQKEVTKR VVGTYGYMAP EYAMGGIFSM
     KSDVYSFGVL LLEIVSGSKI SSIDLIEDSP NLPVYAWNLW NEGKADIMID STITANCLLD
     EVILCIHVAL LCVQENLNDR PLMSDVVLIL EKGSKSLPAP HRPAYFAQRN NNEVEQVRNG
     SQGAQNSNNN MTLTDLEGR
//
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