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Entry: G8BZG8_TETPH
LinkDB: G8BZG8_TETPH
Original site: G8BZG8_TETPH 
ID   G8BZG8_TETPH            Unreviewed;       279 AA.
AC   G8BZG8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Casein kinase II subunit beta {ECO:0000256|RuleBase:RU361268};
DE            Short=CK II beta {ECO:0000256|RuleBase:RU361268};
GN   Name=TPHA0K01630 {ECO:0000313|EMBL:CCE65296.1};
GN   OrderedLocusNames=TPHA_0K01630 {ECO:0000313|EMBL:CCE65296.1};
OS   Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS   Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE65296.1, ECO:0000313|Proteomes:UP000005666};
RN   [1] {ECO:0000313|EMBL:CCE65296.1, ECO:0000313|Proteomes:UP000005666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC   {ECO:0000313|Proteomes:UP000005666};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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       {ECO:0000256|ARBA:ARBA00029397}.
CC   -!- FUNCTION: Regulatory subunit of casein kinase II/CK2. As part of the
CC       kinase complex regulates the basal catalytic activity of the alpha
CC       subunit a constitutively active serine/threonine-protein kinase that
CC       phosphorylates a large number of substrates containing acidic residues
CC       C-terminal to the phosphorylated serine or threonine.
CC       {ECO:0000256|RuleBase:RU361268}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|RuleBase:RU361268}.
CC   -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC       {ECO:0000256|ARBA:ARBA00006941, ECO:0000256|RuleBase:RU361268}.
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DR   EMBL; HE612866; CCE65296.1; -; Genomic_DNA.
DR   RefSeq; XP_003687730.1; XM_003687682.1.
DR   AlphaFoldDB; G8BZG8; -.
DR   STRING; 1071381.G8BZG8; -.
DR   GeneID; 11533302; -.
DR   KEGG; tpf:TPHA_0K01630; -.
DR   eggNOG; KOG3092; Eukaryota.
DR   HOGENOM; CLU_034027_3_0_1; -.
DR   OMA; QNGSPMA; -.
DR   OrthoDB; 5485421at2759; -.
DR   Proteomes; UP000005666; Chromosome 11.
DR   GO; GO:0005956; C:protein kinase CK2 complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0019887; F:protein kinase regulator activity; IEA:InterPro.
DR   Gene3D; 2.20.25.20; -; 1.
DR   Gene3D; 1.10.1820.10; protein kinase ck2 holoenzyme, chain C, domain 1; 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; CASEIN KINASE II SUBUNIT BETA; 1.
DR   PANTHER; PTHR11740:SF44; CASEIN KINASE II SUBUNIT BETA; 1.
DR   Pfam; PF01214; CK_II_beta; 1.
DR   PRINTS; PR00472; CASNKINASEII.
DR   SMART; SM01085; CK_II_beta; 1.
DR   SUPFAM; SSF57798; Casein kinase II beta subunit; 1.
DR   PROSITE; PS01101; CK2_BETA; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005666}.
FT   REGION          79..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   279 AA;  32382 MW;  066D0517C1571012 CRC64;
     MSKEYVADNS HLDSSEEESG TYDEWIPSFC SRFGHEYFCQ VPTDFIEDDF NMTSLAQEIP
     HYRKALDLIL DLEPVSDDDS FENNTKHNDN SNNKSNNNDS NDKDINNSSA NIVNKSILEH
     SAEQLYGLIH ARFILTKHGL QAMAEKFDHK EFGTCPRYYC GGMQLLPCGL SDTIGKHTVR
     LYCPSCQDIY LPQSSRHLSL EGAYWGTSFP GIFLKHFKEL EDYVEKKNKE TYELKVFGFK
     ISAYSISGPR MKWLRQYPST EEEWKEFEKC EFEIPEDLY
//
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