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Database: UniProt
Entry: A0A1D6EB48_MAIZE
LinkDB: A0A1D6EB48_MAIZE
Original site: A0A1D6EB48_MAIZE 
ID   A0A1D6EB48_MAIZE        Unreviewed;       811 AA.
AC   A0A1D6EB48;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=ZEAMMB73_Zm00001d003723 {ECO:0000313|EMBL:ONM17574.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM17574.1};
RN   [1] {ECO:0000313|EMBL:ONM17574.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM17574.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) 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}.
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DR   EMBL; CM007648; ONM17574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6EB48; -.
DR   SMR; A0A1D6EB48; -.
DR   PaxDb; 4577-GRMZM2G134432_P01; -.
DR   eggNOG; ENOG502QUMK; Eukaryota.
DR   InParanoid; A0A1D6EB48; -.
DR   OMA; IIWSTQS; -.
DR   OrthoDB; 379573at2759; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 1.
DR   CDD; cd01098; PAN_AP_plant; 1.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 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; 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:SF19; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF08276; PAN_2; 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; 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};
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:ONM17574.1};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR000641}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   BINDING         528
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   811 AA;  87664 MW;  BAFEB78AEE97AAC0 CRC64;
     MHVVRAFVLS VLLVILHAPS PYAATDTLRH GHALAGSDKL VSGNGKFALG FLQLQPGSSY
     YLGIWFDKVP VLTPVWAANR DNPVSANSTW RELVISDDGN MVFQAQGATV WSTRANTTTN
     DTVAVLLGNG NLVLRSASNS SLTFWESFDY PTDTQLPGVK VGWNKVTGLN RRLVSRKNAV
     DLSSGIYSST LGRDGVARML WNSSSVYWSS TWNGRFFSAV PEMSAGSPLA NFTFVNNDQE
     VYFTYNIFDE STIVRTTLHV SGQNQVRVWT GQDWMTGNNQ PAHQCDVYAV CGPFAVCEPN
     GDTLCSCMKG FSVRSPSDWE VEDRTGGCVR DTPLLSCGAG DGNSGTGMAA DKFYSMPGIR
     LPQNGKAMPA DASSAKQCAQ VCLSSCSCTA YSYGKDGCSI WHGELLNVAT EGDSDDTIYL
     RLAAKEFRSG KGSSRSGVVI GAAVGASVAA AAALVFVLLV LIWRRNGRRW SRPVVHNDKG
     SVVGIVAFKY ADLQDATKKF SEKLGEGGFG SVFKGCLGDS TTTVVAVKRL DGARQGEKQF
     RAEVNSIGIV QHINLVRLIG FCCEGDRRLL VYEHMPNGSL DSHLFRSHGG AGVGAGAALD
     WNVRYKIAVG VARGLAYLHH GCRDCIIHCD IKPQNILLDA SFLPKIADFG MAKFLGRDFS
     RVVTTMRGTV GYLAPEWISG TPITSKIDVY SYGMVLLEIV SGKRNSITQQ SSSHTIEGQQ
     GDYLPVQVAG KLLRGDVLSV VDADLRGDVN VEEVERVCRI ACWCIQDREF DRPTMVEVVQ
     FLEGICEPEI PPMPRLLHAI AGGGSNQTAG V
//
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