ID W2ZZX5_PHYPR Unreviewed; 302 AA.
AC W2ZZX5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE RecName: Full=Casein kinase II subunit beta {ECO:0000256|RuleBase:RU361268};
DE Short=CK II beta {ECO:0000256|RuleBase:RU361268};
GN ORFNames=F442_02516 {ECO:0000313|EMBL:ETP52496.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP52496.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP52496.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP52496.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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:ETP52496.1}.
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DR EMBL; ANIY01000542; ETP52496.1; -; Genomic_DNA.
DR AlphaFoldDB; W2ZZX5; -.
DR EnsemblProtists; ETP52496; ETP52496; F442_02516.
DR Proteomes; UP000018948; 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:SF38; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000018948}.
FT REGION 31..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..72
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 34155 MW; 5915D5E094FD40D0 CRC64;
MSQPVNGGQA ADEAELERLF GHMEDLRVSE AALASVSASE DEEDEEEDSS ALDDSDDDDG
DEDNDVEGSD EEETSWIAWF CSLRENSFLC EVDEDYIEDD FNLTGLSSIV PYYDYALDII
LDIETPNDST LTQIQQEMIE SAAEMLYGLI HARYILTTKG MAAMLDKYQN VDFGRCHRVY
CQGQPVLPVG QSDVPRHTTV NVFCPKCRDI FFPKSQRAGQ IDGAYFGATF PHVFLMTHPH
LVVPPPTQTY VPRVFGYKIH SSSEYYTGKK KSSSGREREK NRKMKTLIDR LKGRPNDEQQ
AR
//
