ID A0A165I7J7_9BASI Unreviewed; 175 AA.
AC A0A165I7J7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 18.
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 ORFNames=CALCODRAFT_492813 {ECO:0000313|EMBL:KZT60226.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT60226.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT60226.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT60226.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV423933; KZT60226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165I7J7; -.
DR STRING; 1353952.A0A165I7J7; -.
DR InParanoid; A0A165I7J7; -.
DR OrthoDB; 339700at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
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; PR01697; PARVALBUMIN.
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:UP000076842}.
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; 19628 MW; A70791C1D5F0A556 CRC64;
MGQTSSQFMD EMGKKSNFTP AELERLKRRF MKLDSDNSGS IDREEFLSIP AIATNPLASR
MIAIFDEDGG GTVDFQEFIS GLSAFSGRGG REEKLKFAFN VYDMDRDGYI SNGELFLVLK
MMVGNNLKDQ QLQQIVDKTI MEADKDGDGK LNFGEFANMV SNTDVIKQMS LENLF
//
