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Database: UniProt
Entry: A0A0A1V8L7_9HYPO
LinkDB: A0A0A1V8L7_9HYPO
Original site: A0A0A1V8L7_9HYPO 
ID   A0A0A1V8L7_9HYPO        Unreviewed;       343 AA.
AC   A0A0A1V8L7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Casein kinase II subunit beta {ECO:0000256|RuleBase:RU361268};
DE            Short=CK II beta {ECO:0000256|RuleBase:RU361268};
GN   ORFNames=X797_000648 {ECO:0000313|EMBL:EXV05931.1};
OS   Metarhizium robertsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=568076 {ECO:0000313|EMBL:EXV05931.1, ECO:0000313|Proteomes:UP000030151};
RN   [1] {ECO:0000313|EMBL:EXV05931.1, ECO:0000313|Proteomes:UP000030151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXV05931.1,
RC   ECO:0000313|Proteomes:UP000030151};
RA   Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA   Gibson D.M.;
RT   "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT   ARSEF 2575.";
RL   Submitted (FEB-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXV05931.1}.
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DR   EMBL; JELW01000001; EXV05931.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1V8L7; -.
DR   eggNOG; KOG3092; Eukaryota.
DR   HOGENOM; CLU_034027_1_1_1; -.
DR   OrthoDB; 5485421at2759; -.
DR   Proteomes; UP000030151; 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:EXV05931.1};
KW   Transferase {ECO:0000313|EMBL:EXV05931.1}.
FT   REGION          60..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..79
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   343 AA;  38428 MW;  8CC998BC28848418 CRC64;
     MSTDSGAPES WISSFCALLG HEYFAEVSEE FIEDDFNLTG LQTQVAMYKE ALEMILDVEP
     EDDEDEEEEE EEEDDNESGL GDGQERMGGR PGERRHHSRM ASDLSVIESS AEMLYGLIHQ
     RFICSRAGIQ QMSEKYELGH FGCCPRTNCD QARTLPVGLS DIPGEDTVKL FCPACLDVYV
     PPNSRFQTVD GAFFGRTFGA LFLLTFPEYD LTKRGVEVLS SATSRIAADE ELVNGMYTRN
     IAPGLGPGRI YEPKIYGFRV SERARSGPRM QWLRARPIDV NDLDESRIYA EQCAESEDDD
     ESMNLNGRAM VRRRPPGNAR LRQRQNQNGS PMALSTNGAE SEL
//
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