HD6_ORYSI
ID HD6_ORYSI Reviewed; 333 AA.
AC Q9AR27;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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:0000303|PubMed:11416158};
GN Name=HD6 {ECO:0000303|PubMed:11416158};
GN Synonyms=CKA2 {ECO:0000303|PubMed:21229229};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC STRAIN=cv. Kasalath;
RX PubMed=11416158; DOI=10.1073/pnas.111136798;
RA Takahashi Y., Shomura A., Sasaki T., Yano M.;
RT "Hd6, a rice quantitative trait locus involved in photoperiod sensitivity,
RT encodes the alpha subunit of protein kinase CK2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7922-7927(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Kasalath, and cv. Shuusoushu;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. KDML 105, and cv. Suphan Buri 1;
RA Roongsattham P., Peyachoknagul S.;
RT "Detection of DNA methylation in Hd1, Hd3a, and Hd6 genes in rice KDML 105
RT (Oryza sativa L.).";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 (PubMed:11416158).
CC {ECO:0000250|UniProtKB:P48730, ECO:0000269|PubMed:11416158}.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CK2 subfamily. {ECO:0000305}.
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DR EMBL; AB036786; BAB21589.1; -; Genomic_DNA.
DR EMBL; AB036788; BAB21591.1; -; mRNA.
DR EMBL; AB435660; BAG82852.1; -; Genomic_DNA.
DR EMBL; AB435661; BAG82853.1; -; Genomic_DNA.
DR EMBL; DQ157463; ABB17668.1; -; Genomic_DNA.
DR EMBL; DQ157464; ABB17669.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AR27; -.
DR SMR; Q9AR27; -.
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:0010229; P:inflorescence development; IMP:Gramene.
DR GO; GO:0009648; P:photoperiodism; IMP:Gramene.
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 2: Evidence at transcript level;
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_0000437452"
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