ID B9SXC2_RICCO Unreviewed; 1517 AA.
AC B9SXC2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=RCOM_0782900 {ECO:0000313|EMBL:EEF31749.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; EQ974221; EEF31749.1; -; Genomic_DNA.
DR eggNOG; ENOG502QSMT; Eukaryota.
DR InParanoid; B9SXC2; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd00028; B_lectin; 1.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd01098; PAN_AP_plant; 2.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.90.10.30; -; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
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; 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; IPR021820; S-locus_recpt_kinase_C.
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:SF130; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 2.
DR Pfam; PF11883; DUF3403; 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; 1.
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; PS50026; EGF_3; 2.
DR PROSITE; PS50948; PAN; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
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|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEF31749.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEF31749.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 335..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1121..1141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..51
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 180..218
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 240..323
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 319..634
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 708..829
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 958..996
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1018..1101
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 1200..1485
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 1228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1517 AA; 171398 MW; B6EE52E2DE18D021 CRC64;
MGNLVLYGED SDPVWSTNAS VETTGNLAQL LDSGNLVLVQ RNKDKSILWQ SFDHPTDTLL
PGMKIGVNRK TGQNWMLKSW RSENDPGIGN YSQRVNTNGS PQIFQYNGTA HYWRSSPWPW
RVFPEVYYCN FVSNRDEIYY ECSFHNTSVI SRRVLDHSGI LKWLIWQEND GQWKEFLSLS
RDRCYNYGRC GAYGKCDSNT VTRYECTCLP GYEPKSPRNW NLWDGKDGCV RKRKGTSSVC
GHGEGFIKVE NLKLPDASAA VWVDMTMSHT DCEQECKRNC ACSAYSTIFI AGNGSGCLAW
YGELIDTMTY SPAGGYDLYV RVDALELGNF LEMKGILIVS VASVWFVIII FIYCWLKTKK
EKRKMKRRLF DPINGSNYYR GTMAAADELE GGSRSHQDLL QHRNLVKLLG CCVERNEQML
IYEYLANKSL DTFLFDERKR SLISWETRFN IIVGIARGIL YLHQDSRLTI IHRDLKSSNI
LLDADMNPKI SDFGMARLFK SDELQDQTNR IVGTYGYMSP EYAVFGKYSV KSDIFSFGII
LLEIISGKKT NGFTQKDASL NLIGQVWELW KEERALEIVD SSLTGSCNSD EVLRCIQVGL
LCVQEDAMDR PAMLEVVLML KSDSSLPSPK QPAFIFRASS SNTNSAGGNG GSCSINGVTI
TAVSTRNDFV SINKNCFFKA SGLIVMETKT WFSFLLILVR SIVRTASNDT ISINQILKDG
DLLISKEENF AFGFFGPGSS SYRYLGIWFH KIPGQTVVWV ANRNNPINGS SGFLSINQQG
NLVLFGENSD PVWSTNVSVE ITGNTAQLLD SGNLVLVQRN KDKSILWQSF DHPTDTLLPG
MKIGVNRKTG QNWMLKSWRS ENDPGIGNFF YRLNPNGSPQ IFLYNDTTRY WRSNPWPWRI
NLEVYYCSFI NNQDEICYNC SLRNTSVISR QQLDHLGIMR WLVWQENDDQ WKEFLSLPRD
RCDDYGRCGG YGKCDSNTVT RYECACLPGY EPKSPRNWNL WDGRDGCVRK RKESSSVCGH
GEGFIKVESV KLPDASAAVW VDMSTSHIDC EQQCKRNCAC SAYSTIFIAG NGSGCLAWYG
ELIDTKTYPP DVGYDLYVRV DALELADSAR RSSSSIETKR ILIVSVASVW FIIILIIYCW
LKKKKKKRNW NTIVLDHPIN GSNYYRGTMA AADELEGGSR SHQDLVLFKL STILVATDNF
SPVNKIGQGG FGTVYKGQLS NGKEIAIKRM SKTSMQGIEE LKNEVMLIAK LQHRNLVKLL
GCCVERNEQM LIYEYLANKS LDTFLFDERK RSLISWETRF NIIVGIARGI LYLHQDSRLT
IIHRDLKSSN ILLDADMNPK ISDFGMARLF KSDELQDQTN RIVGTYGYMS PEYAVFGKYS
VKSDIFSFGI ILLEIISGKK TNGFNQKDAS LNLIGQVWEL WKEERALEIV DSSLTGSCNS
DEVLRCIQVG LLCVQEDAVD RPIMSEVVLM LKSDSSLPSP KQPAFIFRAS SSNTISPGGN
EGSCSINDVT ITAVLTR
//
