ID   PK01_HELAN              Reviewed;         242 AA.
AC   P85193;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Putative serine/threonine-protein kinase {ECO:0000250|UniProtKB:Q9FE20, ECO:0000303|Ref.2};
DE            EC=2.7.11.1;
DE   Flags: Fragment;
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. ANN1312 {ECO:0000269|Ref.1};
RA   Michelmore R.W., Knapp S., Rieseberg L., Bradford K., Kesseli R., Boore J.,
RA   Kozik A., Matvienko M., Lavelle D., Lai Z.;
RT   "Sunflower (Helianthus annuus) ESTs (set 2) from the compositae genome
RT   project http://compgenomics.ucdavis.edu/.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RA   Garcia J.S., Souza G.H.M.F., Eberlin M.N., Arruda M.A.Z.;
RT   "Evaluation of metal-ion stress in sunflower (Heliantus annus L.) leaves
RT   through proteomic changes.";
RL   Metallomics 1:107-113(2009).
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:0000250|UniProtKB:Q9FE20};
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:0000250|UniProtKB:Q9FE20};
CC   -!- INDUCTION: Neither up- or down-regulated in response to zinc ion
CC       contamination and in response or to mixed metal ion contamination
CC       (cadmium, copper, lead and zinc). {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; DY919178; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P85193; -.
DR   SMR; P85193; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..>242
FT                   /note="Putative serine/threonine-protein kinase"
FT                   /id="PRO_0000397227"
FT   DOMAIN          49..>242
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         55..63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         77
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NON_TER         242
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   242 AA;  27010 MW;  9B1F8ECAED4DF562 CRC64;
     MKMCFPCLQC FCSTSDDKVV VSKNDKGGES GKKFRLFSYH ELKVACDGFS SKNKVGEGGC
     GAVYKGRLTD GTMVAIKVLS VELESMRGER EFISEIAALS DAQHENLVNL HGCCVEEATR
     CLVYDYMENN SLAYQFLGRE QNRNSFDWTK RKNVLLGVAK ALAYLHEEIN PHIVHRDIKA
     SNVLLDHNFN PKVADFGLAR LFQEGTSHIS TRVAGTLGYL SPEYAVSERL TRKSDVYSFG
     VL