ID A0A0S7DZ66_9EURO Unreviewed; 362 AA.
AC A0A0S7DZ66;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, 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=ALT_008073 {ECO:0000313|EMBL:GIM39591.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM39591.1};
RN [1] {ECO:0000313|EMBL:GIM39591.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM39591.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
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:GIM39591.1}.
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DR EMBL; BCLY01000009; GIM39591.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DZ66; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_5231; -.
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; 1.
DR PROSITE; PS01101; CK2_BETA; 1.
PE 3: Inferred from homology;
SQ SEQUENCE 362 AA; 40470 MW; 93DC76D6348A8FFD CRC64;
MSSSEGAPES WISSFCSLMG HEFFAEVSED FIEDDFNLTG LQSQVPMYKE ALEMILDVEP
EEDEDEEEEE EEEEEDDDEI LGDERPPGYR RAGDRRHARV ASDLSVIESS AELLYGLIHQ
RYITSRPGIQ QMLEKYEMQH FGVCPRAYCN GSKVLPVGCS DTPGQETVKL FCPSCQDLYT
PPNSRFHSVD GAFFGTTFGY LFFMTFPDLD IGPRLDPSML TAAPTNANNQ SRSSSLTSGV
NRATPDLPPP NQPTEINGVR TVNFCPGLGP GRIYESKIYG FRVSERSRVG PRMKWLRMKP
TDIRELDELA QYEAIHGSAN DAGDTEMNID AQNAAAIAAR KKAPMRRRRH NPDQMSINGA
EG
//
