ID B9RXX5_RICCO Unreviewed; 1480 AA.
AC B9RXX5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
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_0906850 {ECO:0000313|EMBL:EEF43981.1};
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; EQ973828; EEF43981.1; -; Genomic_DNA.
DR eggNOG; ENOG502QUDG; Eukaryota.
DR InParanoid; B9RXX5; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
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; 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:SF63; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 2.
DR Pfam; PF11883; DUF3403; 1.
DR Pfam; PF08276; PAN_2; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF00954; S_locus_glycop; 1.
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); 2.
DR PROSITE; PS50927; BULB_LECTIN; 2.
DR PROSITE; PS50026; EGF_3; 1.
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}; 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, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEF43981.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1480
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002888737"
FT TRANSMEM 366..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 503..519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1085..1106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..154
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 270..349
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 421..692
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 665..791
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 928..966
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 986..1065
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 1163..1440
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 1191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1480 AA; 166308 MW; 18368EC384DA0D10 CRC64;
MAAAKKWFLL YRLPFLQFPI CNSADVITMN QSFKEGDQLI SKENKFAFGF FSPDSSSHRY
LGIWFHEISD SSAAWVANKN NPITASSAAL SINQYGSLVL YNDLNQQVVV WSTNVTAKVT
DACRSKRIVW QSFDYPTNTQ LPGMRLGLNH KTGLVWELTS WRSADYPGTG DYSVKQKLKG
LTEVILYKGS VPHWRAHLWP TRKFSTVYNY TLVNSEDEIY SFYSINDASI IIKTTHVGLK
NPDKFECSCL PGCEPKSPRD WYLRDAAGGC IRKRLESSST CGHGEGFVKG TNMSSMECEQ
ECLRNCSCSA YANVENGEKE RGCLIWYWEL INMVDIVDGE ADVYVRVDAV ELAENMRSNG
FHEMKWMLTI LVVSVLSTWF FIIIFAYLWL RRRKKRNTLT ANELQASRFF NTSTILTAAN
NSPANRIGQG GFGLSKNSRQ GIQEFKNEVR LIAKLQHRNL VKLLGCCIQD EERILIYEYL
RNGSLDLFLF DETKKSMLNW RKRFEIIVGI APGILYLHQD SRLRIIHRDL KSSNILLDAE
LNPKISDFGL AKLLDGDQVQ YRTHKVVGTY FGVILLEIIT GKRSTSSHEE VASLSLIGRV
WELWKQEKAL EMVDPLVLNE SHVALPPPKQ PAFIFRDSSE RDGECSVDEM TITATVASFH
SCICIDTITS RNSIKDGDIL VSSGQGFALG FFSPAGNPAR RYVGIWYNKV TEKTVVWVAN
RDNPINDTSG VLAINSKGNL VLYGHNQTIP VWSANVSLSS LNKNNSIVQL LETGNLLLLQ
QDSNTVLWQS FDHPTDTMLP YMKLGLDRKT GKNWFLSSWK SKDDPGTGNI FYRIDPTGYP
QLFLYKGSLR WWRGGPWTGQ RWSGVPEMTR NYIFNASFVN TEDEVFITYG LTTNATIFSR
MMVNESGTVQ RATWNDRDGR WIGFWSAPKE PCDNYGECGA NSNCDPYDSD NFICKCLPGF
YPKSPGSWYL RDGSDGCNRK AGVSTCRDGE GFVRLALVKV PDTATARVNM SLSLKACEQE
CLRNCSCTAY TSAYESGIGC LTWYGDLVDI RTYSSVGQDI YVRVDAVELA KYGKSKSRLT
KGVQAILIAS VSVASFLAVF VVYCLVKKRR KARDRRRSKS LFSFTQSPTD LGDSHGGKGN
DEDGIPDLPF FDLSAIATAT SNFSDDNKLG EGGFGSVYKG LLHGGKEIAV KRLSRYSGQG
TEEFKNEVAL IAKLQHRNLV RMIGYCVQEP EKMLIYEYLP NKSLDSFIFD EAKRSLLDWS
IRHSIICGIA RGILYLHQDS RLRIIHRDLK ASNVLLDASM NPKISDFGMA RIVGVDQIEA
NTNRVVGTYG YMSPEYAMQG LFSVKSDVYS FGVLLIEIIT GRKNSSFYEE STSSNLVGYV
WDLWREGRAL EIVDISLGDA YPEHEVLRCI QIGLLCVQES AVDRPAMTTV VFMLSNHTIL
PSPNQPAFIM KRSYNSGEPV SASDGGNSVN EVTMTVLEAR
//
