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Database: UniProt
Entry: A0A0M8MWJ1_9BASI
LinkDB: A0A0M8MWJ1_9BASI
Original site: A0A0M8MWJ1_9BASI 
ID   A0A0M8MWJ1_9BASI        Unreviewed;       313 AA.
AC   A0A0M8MWJ1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Casein kinase II subunit beta {ECO:0000256|RuleBase:RU361268};
DE            Short=CK II beta {ECO:0000256|RuleBase:RU361268};
GN   ORFNames=Malapachy_2171 {ECO:0000313|EMBL:KOS15734.1};
OS   Malassezia pachydermatis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS15734.1, ECO:0000313|Proteomes:UP000037751};
RN   [1] {ECO:0000313|EMBL:KOS15734.1, ECO:0000313|Proteomes:UP000037751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS15734.1,
RC   ECO:0000313|Proteomes:UP000037751};
RA   Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT   "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT   pachydermatis CBS1879.";
RL   Submitted (JUL-2015) 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:KOS15734.1}.
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DR   EMBL; LGAV01000002; KOS15734.1; -; Genomic_DNA.
DR   RefSeq; XP_017993366.1; XM_018136663.1.
DR   AlphaFoldDB; A0A0M8MWJ1; -.
DR   STRING; 77020.A0A0M8MWJ1; -.
DR   GeneID; 28728538; -.
DR   VEuPathDB; FungiDB:Malapachy_2171; -.
DR   OrthoDB; 5485421at2759; -.
DR   Proteomes; UP000037751; 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:SF0; 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:KOS15734.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037751};
KW   Transferase {ECO:0000313|EMBL:KOS15734.1}.
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   313 AA;  34951 MW;  3C72F07E1D98A2CF CRC64;
     MTTNASEAGA SAVEKGASAE KLDDMNKEET LSEVGEEELY ESETPSESGT EGLTWISWFC
     SLAGHQYFAE VAEDFIDDDF NLTGLNFLVP FYKEALEMIL DIEPQDSLKI PDISIVESSA
     ELLYGLIHQR YIITRQGMQQ MVEKFESGHF GMCPRVYCNS QFTLPCGRSD LPGLDTVKLF
     CPNCLDTYTP PSSRFHGIDG AFFGTTFPHL LLQCYRDLAP SILAPLPVLE HEEHGVEAPK
     GEIKKTVSPM DETSTAPSSP KPQTLTYSRL GRKVPHSGIY TPRIYGFKVS PFAVNGPRMQ
     WLRMRPTTLQ ELE
//
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