ID   CSK2B_CANAX             Reviewed;         294 AA.
AC   O59906;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Casein kinase II subunit beta;
DE            Short=CK II beta;
GN   Name=CKB1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12722181; DOI=10.1002/yea.977;
RA   Zelada A., De Souza F.S., Walz K., Giasson L., Passeron S.;
RT   "cDNA cloning, biochemical and phylogenetic characterization of beta- and
RT   beta'-subunits of Candida albicans protein kinase CK2.";
RL   Yeast 20:471-478(2003).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 64385 / 1001;
RX   PubMed=9143340; DOI=10.1006/abbi.1997.9923;
RA   Walz K., Pardo P.S., Passeron S.;
RT   "Purification and characterization of protein kinase CK2 from Candida
RT   albicans: evidence for the presence of two distinct regulatory subunits
RT   beta and beta'.";
RL   Arch. Biochem. Biophys. 340:347-354(1997).
CC   -!- FUNCTION: Regulatory subunit of casein kinase II/CK2 (By similarity).
CC       As part of the kinase complex regulates the basal catalytic activity of
CC       the alpha subunit a constitutively active serine/threonine-protein
CC       kinase that phosphorylates a large number of substrates containing
CC       acidic residues C-terminal to the phosphorylated serine or threonine
CC       (By similarity). {ECO:0000250|UniProtKB:P67870}.
CC   -!- SUBUNIT: Tetramer composed of two alpha chains, one beta chain and one
CC       beta' chain. {ECO:0000250|UniProtKB:P43639}.
CC   -!- PTM: Phosphorylated by alpha subunit. {ECO:0000250|UniProtKB:P67870}.
CC   -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; AF036546; AAC15240.1; -; Genomic_DNA.
DR   AlphaFoldDB; O59906; -.
DR   SMR; O59906; -.
DR   VEuPathDB; FungiDB:C2_00300C_A; -.
DR   VEuPathDB; FungiDB:CAWG_03810; -.
DR   GO; GO:0005956; C:protein kinase CK2 complex; IEA:InterPro.
DR   GO; GO:0019887; F:protein kinase regulator activity; IEA:InterPro.
DR   Gene3D; 1.10.1820.10; -; 1.
DR   InterPro; IPR016149; Casein_kin_II_reg-sub_N.
DR   InterPro; IPR035991; Casein_kinase_II_beta-like.
DR   InterPro; IPR000704; Casein_kinase_II_reg-sub.
DR   PANTHER; PTHR11740; PTHR11740; 2.
DR   Pfam; PF01214; CK_II_beta; 1.
DR   PRINTS; PR00472; CASNKINASEII.
DR   SMART; SM01085; CK_II_beta; 1.
DR   SUPFAM; SSF57798; SSF57798; 1.
DR   PROSITE; PS01101; CK2_BETA; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN           1..294
FT                   /note="Casein kinase II subunit beta"
FT                   /id="PRO_0000068252"
FT   REGION          66..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..294
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   294 AA;  33801 MW;  0592F8BC59FC33C9 CRC64;
     MPSDPEEDYI PWIQQLCELF GHDYFVQVSQ DFIEDDFNLT GLSSQVPYYR EALYTILDYQ
     VETAEDHNTD NTTTNTSNNN DSRNGTSKRN ASELPNKALL AHSAELLYGL IHARYIVSKQ
     GLTAMASKFE RNDFGSCPRY FCDGMHLIPV GSTDVPGQET VRLFCPCCND IYIPSSSRYL
     NIDGAFFGTT FPGLLVKMFP EIENQCRIRI TKFSQNDFGL KLFGFKINEL SATGPRMKWL
     RMHPETEGEK QELTHVNIMF QLATYMKTKR MEEDDEEEED EVEEEDDDRT MASE