ID   HD6_ORYSJ               Reviewed;         333 AA.
AC   B6F107;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Casein kinase II subunit alpha-2 {ECO:0000305};
DE            Short=OsCKA2 {ECO:0000303|PubMed:21229229};
DE            EC=2.7.11.1 {ECO:0000305};
DE   AltName: Full=Protein HEADING DATE 6 {ECO:0000305};
GN   Name=HD6 {ECO:0000305}; Synonyms=CKA2 {ECO:0000303|PubMed:21229229};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Khau Mac Kho;
RX   PubMed=21229229; DOI=10.1007/s00122-010-1524-1;
RA   Ebana K., Shibaya T., Wu J., Matsubara K., Kanamori H., Yamane H.,
RA   Yamanouchi U., Mizubayashi T., Kono I., Shomura A., Ito S., Ando T.,
RA   Hori K., Matsumoto T., Yano M.;
RT   "Uncovering of major genetic factors generating naturally occurring
RT   variation in heading date among Asian rice cultivars.";
RL   Theor. Appl. Genet. 122:1199-1210(2011).
CC   -!- FUNCTION: Casein kinases are operationally defined by their
CC       preferential utilization of acidic proteins such as caseins as
CC       substrates. It can phosphorylate a large number of proteins (By
CC       similarity). Involved in photoperiod sensitivity (PS). Increases days-
CC       to-heading under natural day (ND) and long day (LD) conditions, but not
CC       under short day (SD) conditions (By similarity).
CC       {ECO:0000250|UniProtKB:P48730, ECO:0000250|UniProtKB:Q9AR27}.
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:0000305};
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:0000305};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P48730}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48730}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P48730}.
CC   -!- MISCELLANEOUS: The Nipponbare allele of HD6 (AC Q9AQU1) contains a
CC       premature stop codon, resulting in a truncated non-functional product.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. CK2 subfamily. {ECO:0000305}.
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DR   EMBL; AB435662; BAG82854.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6F107; -.
DR   SMR; B6F107; -.
DR   STRING; 4530.OS07T0114400-01; -.
DR   eggNOG; KOG0668; Eukaryota.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0009908; P:flower development; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   CDD; cd14132; STKc_CK2_alpha; 1.
DR   InterPro; IPR045216; CK2_alpha.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24054; PTHR24054; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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; Cytoplasm; Flowering; Kinase; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..333
FT                   /note="Casein kinase II subunit alpha-2"
FT                   /id="PRO_0000437453"
FT   DOMAIN          34..319
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         40..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   333 AA;  39261 MW;  3F3037627FF2D123 CRC64;
     MSKARVYADV NVLRPKEYWD YEALTVQWGE QDDYEVVRKV GRGKYSEVFE GINVNNNEKC
     IIKILKPVKK KKIKREIKIL QNLCGGPNIV KLLDIVRDQH SKTPSLIFEY VNNTDFKVLY
     PTLTDYDIRY YIYELLKALD YCHSQGIMHR DVKPHNVMID HELRKLRLID WGLAEFYHPG
     KEYNVRVASR YFKGPELLVD LQDYDYSLDM WSLGCMFAGM IFRKEPFFYG HDNHDQLVKI
     AKVLGTEALN AYLNKYHIEL DPQLEALVGR HSRKPWSKFI NADNQHLVSP EAVDFLDKLL
     RYDHQDRLTA REAMAHPYFL QVRAAENSRA RPQ