(data stored in SCRATCH zone)

SWISSPROT: Q75C30_ASHGO

ID   Q75C30_ASHGO            Unreviewed;       257 AA.
AC   Q75C30;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 92.
DE   RecName: Full=Casein kinase II subunit beta {ECO:0000256|RuleBase:RU361268};
DE            Short=CK II beta {ECO:0000256|RuleBase:RU361268};
GN   ORFNames=AGOS_ACR087C {ECO:0000313|EMBL:AAS51313.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51313.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51313.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Plays a complex role in regulating the basal catalytic
CC       activity of the alpha subunit. {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|RuleBase:RU361268}.
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DR   EMBL; AE016816; AAS51313.1; -; Genomic_DNA.
DR   RefSeq; NP_983489.1; NM_208842.1.
DR   STRING; 33169.AAS51313; -.
DR   EnsemblFungi; AAS51313; AAS51313; AGOS_ACR087C.
DR   GeneID; 4619616; -.
DR   KEGG; ago:AGOS_ACR087C; -.
DR   HOGENOM; HOG000039270; -.
DR   InParanoid; Q75C30; -.
DR   KO; K03115; -.
DR   OMA; CPRVLCQ; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0032545; C:CURI complex; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005956; C:protein kinase CK2 complex; IBA:GO_Central.
DR   GO; GO:0034456; C:UTP-C complex; IBA:GO_Central.
DR   GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR   GO; GO:0035690; P:cellular response to drug; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:EnsemblFungi.
DR   GO; GO:0006356; P:regulation of transcription by RNA polymerase I; IBA:GO_Central.
DR   GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IEA:EnsemblFungi.
DR   Gene3D; 1.10.1820.10; -; 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; PTHR11740; 1.
DR   Pfam; PF01214; CK_II_beta; 1.
DR   PRINTS; PR00472; CASNKINASEII.
DR   SMART; SM01085; CK_II_beta; 1.
DR   SUPFAM; SSF57798; SSF57798; 1.
DR   PROSITE; PS01101; CK2_BETA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75C30.
DR   SWISS-2DPAGE; Q75C30.
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   257 AA;  29599 MW;  7A6BE054B7EB445E CRC64;
     MSERRLEEHG TAETADVEMA DAVETNSTGS SDYVELWIDL FLGKKGHEYF CDVDTEYITD
     RFNLINLQKT VSKFTQVIQY MVDELDDTTL EAMSRTKLTQ LEADARKLYG LIHARYIITI
     KGLQKMLQKY RDADFCRCPR VHCNFQPLLP VGLHDVPGID CVKLYCPSCE DLYIPKSSRH
     SSIDGAYFGT SFPGMFLQAF PEVVPKHPTK RYVPKVFGFD LHKQAQLARW QELQRLKLER
     ELIKKGVDLT KNGGYKK
//

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