ID A0A0P1BJJ4_9BASI Unreviewed; 452 AA.
AC A0A0P1BJJ4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Casein kinase II subunit beta {ECO:0000256|RuleBase:RU361268};
DE Short=CK II beta {ECO:0000256|RuleBase:RU361268};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH16529.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH16529.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CCYA01000318; CEH16529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1BJJ4; -.
DR STRING; 401625.A0A0P1BJJ4; -.
DR OrthoDB; 5485421at2759; -.
DR Proteomes; UP000054845; Unassembled WGS sequence.
DR GO; GO:0005956; C:protein kinase CK2 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0019887; F:protein kinase regulator activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Kinase {ECO:0000313|EMBL:CEH16529.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW Transferase {ECO:0000313|EMBL:CEH16529.1}.
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 49150 MW; EF39757CFD9B924B CRC64;
MEEDLVEESV GAEGADGASQ DNHRSRERHD QGEWAENGAR SGTGAGAGRG GLAQEEDQVS
NEVALGADGL PEEEEEEMNE EERILAEEEA RLGLDEELYE SESITSSATD SLTWISWFCS
LPGHEYFAEV AEEFIEDDFN LTGLNALVPF YKEALEMILD VEPQEDSLKI PDVSIVESSA
ELLYGLIHQR FILTRQGLSQ MAEKYEAGHF GYCPRVFCHS HPVLPCGRSD LPGLDTVKLF
CPNCIDNYSP PSSRFHGVDG AFFGTTFPHL LFQSFREMAP SPIAPKGSNQ LSLNTQSSPP
EYILSLNTQS SPPEYIVGGS VSPEAEEERA REAADAPLGG TLDPKLLGTK TPASRLYTPR
IYGFRVSELA KSGPRMRWMR MRPESFQELE TGRLGSGSVA ARGPSGVGAG VTAAGGASAF
DEASIALTKC ETGRKDHRAE HYSALLASFQ AQ
//
