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
//