ID A0A0D2DV36_9EURO Unreviewed; 436 AA.
AC A0A0D2DV36;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Casein kinase II subunit beta {ECO:0000256|RuleBase:RU361268};
DE Short=CK II beta {ECO:0000256|RuleBase:RU361268};
GN ORFNames=PV06_02577 {ECO:0000313|EMBL:KIW46958.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW46958.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW46958.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW46958.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-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}.
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DR EMBL; KN847333; KIW46958.1; -; Genomic_DNA.
DR RefSeq; XP_016267174.1; XM_016403277.1.
DR AlphaFoldDB; A0A0D2DV36; -.
DR STRING; 215243.A0A0D2DV36; -.
DR GeneID; 27354651; -.
DR VEuPathDB; FungiDB:PV06_02577; -.
DR HOGENOM; CLU_034027_1_1_1; -.
DR OrthoDB; 5485421at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
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; 2.
DR PROSITE; PS01101; CK2_BETA; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053342}.
FT REGION 61..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..88
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..395
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 436 AA; 47207 MW; 23F04A75B923B673 CRC64;
MSQSSSQSPD SWIGQFCSLV GHEYFAEVSE DFIEDDFNLT GLQAQVPMYK DALEMILDVE
PSDTNSSALS DEEEEEEEEE DDGLLGDELD DPAANGGARR QSGMSAGGRK HGRSSSDTSV
IESSAELLYG LIHARYITSR PGIQQMMEKY ELAHFGYCPR VYCAGAKVLP IGLTDTPGQQ
TVKLFCPSCQ DAYTPPNSRF QAVDGAFFGT TFPYLFLMSY PDLDIAPPKR PRARDSSHQG
NDDVESTLSP SEANVSRAGM TASRSSSLTL PQPPTIPGIT TAKDAQQASG NAPPTLPPQP
ASINGIATGN LAPGLGRGKI YEPKIYGFRV SERAKSGPRM RWLRSKPADI NELDEARLWH
ERYGGTVDGD PEEEAEQTAG EQEDEDAEDD VADADGDAIM ASQSQANIKD KQGSGKSKQK
SAGQKQGQQQ ETSTWI
//
