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Database: UniProt
Entry: G0WAG6_NAUDC
LinkDB: G0WAG6_NAUDC
Original site: G0WAG6_NAUDC 
ID   G0WAG6_NAUDC            Unreviewed;       175 AA.
AC   G0WAG6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   22-FEB-2023, entry version 53.
DE   RecName: Full=Calcineurin subunit B {ECO:0000256|ARBA:ARBA00023832};
DE   AltName: Full=Calcineurin regulatory subunit {ECO:0000256|ARBA:ARBA00031295};
DE   AltName: Full=Protein phosphatase 2B regulatory subunit {ECO:0000256|ARBA:ARBA00032848};
GN   Name=NDAI0D04640 {ECO:0000313|EMBL:CCD24777.1};
GN   OrderedLocusNames=NDAI_0D04640 {ECO:0000313|EMBL:CCD24777.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS   0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD24777.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD24777.1, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent,
CC       calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
CC       {ECO:0000256|ARBA:ARBA00023754}.
CC   -!- SUBUNIT: Composed of a catalytic subunit (A) and a regulatory subunit
CC       (B). {ECO:0000256|ARBA:ARBA00023792}.
CC   -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC       {ECO:0000256|ARBA:ARBA00023774}.
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DR   EMBL; HE580270; CCD24777.1; -; Genomic_DNA.
DR   RefSeq; XP_003670020.1; XM_003669972.1.
DR   AlphaFoldDB; G0WAG6; -.
DR   STRING; 1071378.G0WAG6; -.
DR   GeneID; 11495180; -.
DR   KEGG; ndi:NDAI_0D04640; -.
DR   eggNOG; KOG0034; Eukaryota.
DR   HOGENOM; CLU_061288_10_1_1; -.
DR   OMA; DTNFDRD; -.
DR   OrthoDB; 339700at2759; -.
DR   Proteomes; UP000000689; Chromosome 4.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IEA:InterPro.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR015757; Calcineur_B.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR45942; PROTEIN PHOSPATASE 3 REGULATORY SUBUNIT B ALPHA ISOFORM TYPE 1; 1.
DR   PANTHER; PTHR45942:SF1; PROTEIN PHOSPATASE 3 REGULATORY SUBUNIT B ALPHA ISOFORM TYPE 1; 1.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00054; EFh; 4.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT   DOMAIN          21..56
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          60..88
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          90..125
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          131..166
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
SQ   SEQUENCE   175 AA;  19586 MW;  4E63EF88B35847C6 CRC64;
     MGAAPSKIVD NLLEDTNFDL DEIERLRKRF MKLDRDSSGS IDKNEFMSIP GVSSNPLAGR
     IMEVFDADNS GDVDFQEFIT GLSIFSGRGS KNEKLKFAFK IYDIDKDGFI SNGELFIVLK
     IMVGSNLNDE QLQQIVDRTI MENDLDGDGH LSFEEFKSAI ETTEVAKSLT LDIDI
//
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