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Database: UniProt
Entry: R1GHU0_BOTPV
LinkDB: R1GHU0_BOTPV
Original site: R1GHU0_BOTPV 
ID   R1GHU0_BOTPV            Unreviewed;       385 AA.
AC   R1GHU0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Casein kinase II subunit beta {ECO:0000256|RuleBase:RU361268};
DE            Short=CK II beta {ECO:0000256|RuleBase:RU361268};
GN   ORFNames=UCRNP2_7770 {ECO:0000313|EMBL:EOD45499.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD45499.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
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; KB916579; EOD45499.1; -; Genomic_DNA.
DR   RefSeq; XP_007587020.1; XM_007586958.1.
DR   AlphaFoldDB; R1GHU0; -.
DR   STRING; 1287680.R1GHU0; -.
DR   KEGG; npa:UCRNP2_7770; -.
DR   eggNOG; KOG3092; Eukaryota.
DR   HOGENOM; CLU_034027_1_1_1; -.
DR   OMA; QNGSPMA; -.
DR   OrthoDB; 5485421at2759; -.
DR   Proteomes; UP000013521; Unassembled WGS sequence.
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: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;
KW   Kinase {ECO:0000313|EMBL:EOD45499.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW   Transferase {ECO:0000313|EMBL:EOD45499.1}.
FT   REGION          60..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..81
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   385 AA;  42636 MW;  05C711856CA690C2 CRC64;
     MSSSSQVAES WITSFCNLLG HEYFAEVSED FIEDDFNLTG LQSQVPMYKE ALEMILDVEP
     EEDEDDEDEE DDDDDDDEIL GDEKPVGYRR SERRHLRMAS DLSVIESSAE LLYGLIHQRY
     ITSRPGIQQM AEKYELQHFG VCPRVHCNGA KVLPVGCSDT PGQETVKLFC PSCLDVYTPP
     NSRFQTVDGA FFGTTFGCLF FMTFPELEIG APRMDRQRDD HHLIADSSSQ TSNSKSRTAS
     SSSVAVGALP PQPTTINGVA PSNLAPGLGD GSIYEPRIYG FRVSERSRSG PRMKWLRMRP
     ADVNELDEAR IFHERRREMV EDIDEEDEEG EDSTMMDANA AAAEGVPVVP RKKAVARRRR
     TANGSVVTAG GRGSPMDTNG VGEGG
//
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