ID W6QEM1_PENRF Unreviewed; 367 AA.
AC W6QEM1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, 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 Name=ckb-1 {ECO:0000313|EMBL:CDM28032.1};
GN ORFNames=PROQFM164_S01g001843 {ECO:0000313|EMBL:CDM28032.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM28032.1};
RN [1] {ECO:0000313|EMBL:CDM28032.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM28032.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG792015; CDM28032.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QEM1; -.
DR STRING; 1365484.W6QEM1; -.
DR OMA; QNGSPMA; -.
DR OrthoDB; 5485421at2759; -.
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:CDM28032.1};
KW Transferase {ECO:0000313|EMBL:CDM28032.1}.
FT REGION 60..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..367
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 218..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 41046 MW; A74EE48A3F968B76 CRC64;
MSSSEGAPES WISSFCSLMG HEFFAEVSED FIEDDFNLTG LQSQVPMYKE ALEMILDVEP
EDDEEEEEEE EEEDEDDALG GEPAYRRAGD RRHARVASDL SVIESSAELL YGLIHQRYIT
SRPGIQQMLE KYEMQHFGTC PRVNCNGCKV LPVGRSDTPG HETVKLFCPG CMDIYTPPNS
RFHSVDGAFF GTTFGCLFFM TFPDLDIGPR LDAALSSISP RNAATQSRTG SLTRTPAGRQ
ARSPTPENQP LEINGVRTPN LCPGLGKGKI YDPKIYGFKV SEVSRVGPRM KWLRMKPKNV
VELDEAWNHE HGMSPQEARD DKEGDTEMNP EQSQDAAIAN RKKAPMRRRR PNLGALVPTD
PMDVHGR
//
