ID A0A1D6DXH9_MAIZE Unreviewed; 655 AA.
AC A0A1D6DXH9;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 2.
DT 27-MAR-2024, entry version 39.
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=ZEAMMB73_Zm00001d002174 {ECO:0000313|EMBL:ONM13342.1};
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:ONM13342.1};
RN [1] {ECO:0000313|EMBL:ONM13342.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM13342.1};
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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM007648; ONM13342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6DXH9; -.
DR SMR; A0A1D6DXH9; -.
DR STRING; 4577.A0A1D6DXH9; -.
DR PaxDb; 4577-GRMZM2G010962_P01; -.
DR eggNOG; ENOG502QSMT; Eukaryota.
DR InParanoid; A0A1D6DXH9; -.
DR OMA; GCRRTED; -.
DR ExpressionAtlas; A0A1D6DXH9; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
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 Gene3D; 2.90.10.10; Bulb-type lectin domain; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR32444:SF142; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF08276; PAN_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00954; S_locus_glycop; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00219; TyrKc; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000313|EMBL:ONM13342.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:ONM13342.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:ONM13342.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT BINDING 501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 655 AA; 72431 MW; 7E4E5E513F4FCEAA CRC64;
MATSKKGLMA MVYIRSAFIL IFLSSPCQSN DQLTQTKPLL LEDTLISEGG DFALGFFSPT
NSSKKLYIGI WYHRVTERTV VWVANRDNPI TTPSAMLAIT DNLELVLSDS QGHTLWMATG
NTSGDAGGAA SAVLLNSGNF VLRLPNGTEV WHSFDHPTDT ILPTMRILLS FKTQPATRLI
AWKGPDNPST GDISSGMDST NLQMFIWKGA LPYYRFPVVN DMAVAGAMYQ QSNGNAAIMY
ETRVNAGDAL YYTYTVSSGS PYTRFSLDYT GKGRLLSWNS TTSSWTVIIE HPHSCDLYAS
CGPFSYCDQM GPLPTTCQCP DGFELLNSLN FSRGCRRKEE LKCGVGNYFM AMSSMKLPDK
FLHIKNRTFD QCADECTRNC SCMAYAYANL SSIGAVGDTS RCLVWSGDLI DMEKNSFSEV
LYIRLGGSGK RQKKRVQKRR MLEYLSSTDD AGDKNINFPF ISFENIVTAT DNFSESNLLG
KGGFGKVYKG MLEGTKEVAV KRLSTGSGQG KEEFKNEVVL IAKLQHKNLV KLLGCCIHED
EKLFCKKINA SVANKAWNMW KDGKPEDFLD SSVTESCSLD EVSRCIHIGL LCAQDNPSCR
PLMSTVVSML ENKATPLPTP KQPKDFALRD YNPGNEGVHR ELSVNDTSLT MVEGR
//