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Database: UniProt
Entry: M5BWZ4_THACB
LinkDB: M5BWZ4_THACB
Original site: M5BWZ4_THACB 
ID   M5BWZ4_THACB            Unreviewed;       300 AA.
AC   M5BWZ4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   RecName: Full=Casein kinase II subunit beta {ECO:0000256|RuleBase:RU361268};
DE            Short=CK II beta {ECO:0000256|RuleBase:RU361268};
GN   ORFNames=BN14_05724 {ECO:0000313|EMBL:CCO31676.1};
OS   Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS   rot fungus) (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO31676.1, ECO:0000313|Proteomes:UP000012065};
RN   [1] {ECO:0000313|EMBL:CCO31676.1, ECO:0000313|Proteomes:UP000012065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065};
RX   PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA   Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA   Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA   Schlueter A.S.;
RT   "Establishment and interpretation of the genome sequence of the
RT   phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL   J. Biotechnol. 0:0-0(2013).
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:CCO31676.1}.
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DR   EMBL; CAOJ01008594; CCO31676.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5BWZ4; -.
DR   HOGENOM; CLU_034027_8_1_1; -.
DR   Proteomes; UP000012065; 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; 2.
DR   PRINTS; PR00472; CASNKINASEII.
DR   SMART; SM01085; CK_II_beta; 1.
DR   SUPFAM; SSF57798; Casein kinase II beta subunit; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:CCO31676.1};
KW   Transferase {ECO:0000313|EMBL:CCO31676.1}.
FT   REGION          248..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..290
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   300 AA;  33728 MW;  069AB17088C1C4AF CRC64;
     MSRLPGVIPG QTPQELGQEG NAVEDDAMND DQAEQEGYGE DFIEDDFNLT GLNGLVPFWR
     EAMEMVLDVE PEDALKIPDV SIVESSAELL YGLVHQRYIL TRPGLQAMVE KYEAGHFGLE
     TVKLYCPNCN DIYSPPSSRF QGVDGAFFGT TFPHLLFQTY RELAPAPFSP TAPPVDSVST
     RRQPAITDPF INPNPHGGQK QPADRVYTAK IYGFRVSERA RSGPRMRWLR LRPQALDELN
     AVDWRGRWIG SDDDAGFEDS DREGGPLERF DDDEGSQEDE EEEEEEEEER QQPPLTGSPM
//
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