ID A0A0D9WV70_9ORYZ Unreviewed; 1792 AA.
AC A0A0D9WV70;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR07G01930.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR07G01930.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR07G01930.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR07G01930.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Ser/Thr protein kinase family.
CC {ECO:0000256|ARBA:ARBA00010217}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the leguminous lectin
CC family. {ECO:0000256|ARBA:ARBA00008536}.
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DR STRING; 77586.A0A0D9WV70; -.
DR EnsemblPlants; LPERR07G01930.1; LPERR07G01930.1; LPERR07G01930.
DR Gramene; LPERR07G01930.1; LPERR07G01930.1; LPERR07G01930.
DR eggNOG; ENOG502QSJ4; Eukaryota.
DR HOGENOM; CLU_238322_0_0_1; -.
DR Proteomes; UP000032180; Chromosome 7.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 3.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27007; -; 1.
DR PANTHER; PTHR27007:SF41; LECTIN-LIKE RECEPTOR PROTEIN KINASE FAMILY PROTEIN-RELATED; 1.
DR Pfam; PF00139; Lectin_legB; 3.
DR Pfam; PF00069; Pkinase; 3.
DR SMART; SM00220; S_TKc; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 3.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 3.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {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:UP000032180};
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, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 201..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 772..794
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1415..1436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 255..547
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 827..1110
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1470..1751
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 856
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1792 AA; 199437 MW; 6AB7C04F0EA28A4C CRC64;
MGSEVHRNDN AILNIFKPTK TESGCSDAAD QFVYSGFTGS NLTLDGGARI TPSGLLELTN
GMVRLKGHAF HPTPLYQRKS PNGTVESFSV SFVFAILCDY PDSCGHGLAF FIAPSKNFSS
AFWTQYLGLV NNKNNGDPNN HIFATELDTV QNDDLQDIRT VSGKHYVLGW SFGMNSPAPS
IDIAKLPRLD QKTRSKVLQT ILPIAAVVFL LSAGTAIFFC VWRNLRYAEL REDWEVEYGP
QRFCYKDLFH ATEGFKNKNL LGTGGFGSVY RGILPISRLD IAVKRVSHDS TQGMKEFIAE
IVSIGCLQHR NLVKLLGYCR RKGELLLVYD YMPNGSLDKY LYGNRGKPTL DWAQRFQIIK
GVASGLLYLH EESKKVIIHR DIKASNVLLD NDINAWIGDF GLARLYDHGT DPETTRVVGT
IGYLAPELAR GGKATPLTDV FAFGMFILEV ICGKSLSSKT QKTTSWCLLI GCFNIGIKAH
SLIQWTSNFK LLFLGLNLAS FTIAEEQFIY SGFIQANLSL DGTATITPEG LLQLTNGTFN
LKGHAFHPTP MQFRRHPTGN MQSFSLTFIF SILSTIPDKG ADGMAFFIST NKSFSSALSA
QYLGILNDQN NGNTSNHIFV VELDTIQNSE FQDISDNHVG ININSLHSVQ SRNAGFCDDK
NGDFKNLTLI SRELMQVWVE YDAGSAQVDV TLAPIKMAKP ARPLVLAIYN LSTVLTDTAY
VGFSSATGVI NSRYYVLGWS FSMGGNASGI DIMKLPKLPH VGPRPRSKVL KIMMPVTLAA
SIFVAGILVI ILVWRKLAHT ELKEDWEAEF GPNRFSYKDL LLATEGFKNK NLLGTGGFGT
VYKGILPTSK LEVAVKRLSH ESKQGTKEFI TESVSIGRLR HCNLVQPLGY CRQKGELLLV
YDYMPNGSLD RHLYSEDKLP LDWTKRFHII KGVASCLLYL HEECERVVIH RDIKASNVLL
DREMNGCLGD FGLAKSYDHG TDPQTTRVVG TMGYLAPELN AQGDRFILVD WVLEHWQKGS
MVEAIDKRLQ GNCNIDEACL VLKPGLLCSQ PFASTRPSMN HVMLYLNGDM QLPEFRPTDM
SLNMPALMEN RVFDPLENEP MIQMKNLIFF LLLILNAGEL NLTAGDDNNN DGDQFVYSGF
TGSNLTLDGA AVITQTGLLE LTNGTLRQKS HAIHPIPFRL RRPSSSSPAT AIRSFSSSFV
FAIICPDADA CGHGIVLFVA PANHSFAGAF PSQYIGLFNG SSDGDAANRL VGVELDTDQN
NEFRDIDGNH VGVDINSLTS INSTSTGYYD DEENSGENSH GLFHNLTLSS HDKAMRVWVD
YDATAKKIDV AIAPLKMAKP SRPLLSTTYD LSMVFVDDEP YMIGFSSATG SFNSKHYVLG
WSFAMDGRPA PAIDIDRLPR LPRFAPKRKP KMVEIIPPLA TAMFIIAMGI VSFVLVRRRM
RYTELREDWE VEFGPHRFSY KDLFRATDGF KSMNLVGVGG FGRVYKGVLP SSKLEIAVKR
VSHDSKQGMK EFIAEVVSIG RLQHRNLVQL LGYCRREGEL LLVYEYMSNG SLDKHLYSDS
GDKHVLNWDK RFQIIKGIAS GLLYLHEEWE KVIVHRDIKT SNVLLDNEMN SRLGDFGLAR
LYDRGADPKT THVVGTIGYL APELGRSSKA TPLTDIFAFG IFILEVTCGQ RPIMQVPEGE
QHVLVDWVLE NWHKGSIIET VDTKLQGNYN VDEVYLVLKL GLLCSHPLSN ERPNIRQVMK
YLNEDMAMPE LVPTHHNFHT LALMQNQGFD SYVMSYPSLA SISTVSNLSE QR
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