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Database: UniProt
Entry: A0A1E5V139_9POAL
LinkDB: A0A1E5V139_9POAL
Original site: A0A1E5V139_9POAL 
ID   A0A1E5V139_9POAL        Unreviewed;       810 AA.
AC   A0A1E5V139;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
GN   ORFNames=BAE44_0020108 {ECO:0000313|EMBL:OEL18876.1};
OS   Dichanthelium oligosanthes.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Dichantheliinae; Dichanthelium.
OX   NCBI_TaxID=888268 {ECO:0000313|EMBL:OEL18876.1, ECO:0000313|Proteomes:UP000095767};
RN   [1] {ECO:0000313|EMBL:OEL18876.1, ECO:0000313|Proteomes:UP000095767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Kellogg 1175 {ECO:0000313|Proteomes:UP000095767};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OEL18876.1};
RA   Studer A.J., Schnable J.C., Brutnell T.P.;
RT   "The draft genome of Dichanthelium oligosanthes: A C3 panicoid grass
RT   species.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|PIRNR:PIRNR000641};
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         ECO:0000256|PIRNR:PIRNR000641};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OEL18876.1}.
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DR   EMBL; LWDX02055344; OEL18876.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E5V139; -.
DR   STRING; 888268.A0A1E5V139; -.
DR   OrthoDB; 339054at2759; -.
DR   Proteomes; UP000095767; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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; 1.
DR   CDD; cd00053; EGF; 1.
DR   CDD; cd01098; PAN_AP_plant; 1.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
DR   Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   PANTHER; PTHR47974; OS07G0415500 PROTEIN; 1.
DR   PANTHER; PTHR47974:SF4; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF00024; PAN_1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00954; S_locus_glycop; 1.
DR   PIRSF; PIRSF000641; SRK; 1.
DR   SMART; SM00108; B_lectin; 1.
DR   SMART; SM00473; PAN_AP; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50948; PAN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000641};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000641}; Receptor {ECO:0000313|EMBL:OEL18876.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095767};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR000641};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..810
FT                   /note="Receptor-like serine/threonine-protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009187622"
FT   DOMAIN          17..146
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          280..316
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          330..414
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          524..802
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         552
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   810 AA;  90520 MW;  FCBF0C85BC121A17 CRC64;
     MAPFFSFLPI LSLLPLLSSA ASPDILPRRS SLSIDKYQTD VLRSPNGTFT CGFYSIYDNA
     FTFSIWYPNS VDKTVVWTAN RDRPVHASGA AVTLRKGGAL VLTDYDGEVV WQTEGNLEGV
     QYAQLLDTGN LVMKNSSGMV VWQSFDSPTD TLLPTQHISA STKLVSTTGL HVPGHYIFHF
     TDSSILSLIY DDANVHEIYW PDPDNGEYQN NRNRYNSTRL AGLDERGNFF SSDFANQQAI
     VASDEGHGIK RRLTLDPDGN LRLYSLNNSD GRWSVSWIAV SQPCNIHGLC GPNGICHYLP
     TPTCSCPPGY VMSNPGNWSQ GCRAVVDIAC TVEQAQPVKF LRLPGTDFWG SDQQHVEHIS
     LQACRNICRS DCTCKGFQYQ QGSGTCYPKA FLYNGKAYTS PTKSTRMMYL KLPVGVNISG
     TPIPQTNVLI SRKQHPDCGQ MSVSTMEPFP DVHKTNQGES KWFYFYGFAG AIFVLEVFFI
     ASAWCFVLRW ELGASEIQAV EKGYKMMTSN FRRYSYKELV KATRKFKDEL GRGGSGIVYK
     GILDDSRAVA VKMLENVRQC EEEFQAELSI IGRINHMNLV RIWGFCSESS HRMLVTEYIE
     SGSLANILFK DNILLEWRQR FNIALGVAKG LAYLHHECLE WVIHCDVKPE NILLDRNLEP
     KIADFGLAKL LNRGGSNQNV SRVRGTIGYI APEWISSLQI TARVDVYSYG VVLLELVLGQ
     RVLDLAIGAD EVHKVLRKLV GMLALMLDKQ ESSSIAEVVD CRLNGQFNCM QVRTLIKLAV
     SCLDEDGSKR PTMESIVQTL LLADESCSMR
//
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