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Database: UniProt
Entry: G0V1Y8_TRYCI
LinkDB: G0V1Y8_TRYCI
Original site: G0V1Y8_TRYCI 
ID   G0V1Y8_TRYCI            Unreviewed;       292 AA.
AC   G0V1Y8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   RecName: Full=Casein kinase II subunit beta {ECO:0000256|RuleBase:RU361268};
DE            Short=CK II beta {ECO:0000256|RuleBase:RU361268};
GN   ORFNames=TCIL3000_11_11480 {ECO:0000313|EMBL:CCC95659.1};
OS   Trypanosoma congolense (strain IL3000).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX   NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC95659.1};
RN   [1] {ECO:0000313|EMBL:CCC95659.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IL3000 {ECO:0000313|EMBL:CCC95659.1};
RX   PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA   Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA   Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA   Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA   Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA   Hertz-Fowler C., Berriman M.;
RT   "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT   African trypanosome species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
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; HE575324; CCC95659.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0V1Y8; -.
DR   VEuPathDB; TriTrypDB:TcIL3000.11.11480; -.
DR   OrthoDB; 5485421at2759; -.
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:SF0; 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;
FT   REGION          224..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..292
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   292 AA;  33303 MW;  CA6E258EFE906CD6 CRC64;
     MSYPMFTGEY SDDRPGFDEE VDEEVIPWIV WFCEMKSHEF FCVVDRDFID DDFNLTGLST
     MVSFYHYALD LILDLETQSN SRLTDEQQRL VESSAETLYG LIHARFITTP RGLKLMEEKF
     AEAEFGRCPR VFCGGQAVLP VGQSDVVRES SVKLFCPKCQ DIYYPRSSRH RMLDGAFWGT
     TFPHLFLMHL RESGKLIPRP KQQYVPRIYG FRLHNREKCV HEDSVDQTGG AGGAAAGAGE
     CDDDDERQED EQQQTCAVDA GLGDTLMNTP NSRKGRGSAR DSKDDMEDTL RR
//
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