ID A0A1J9QQJ5_9PEZI Unreviewed; 174 AA.
AC A0A1J9QQJ5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 15.
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=BKCO1_5600020 {ECO:0000313|EMBL:OJD30728.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD30728.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD30728.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD30728.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OJD30728.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNUE01000056; OJD30728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9QQJ5; -.
DR STRING; 236234.A0A1J9QQJ5; -.
DR OrthoDB; 339700at2759; -.
DR Proteomes; UP000183809; 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 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:UP000183809}.
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 174 AA; 19752 MW; B90F3D5EFD3C465C CRC64;
MGNANSQMLD NIVSGSNFDR EEVDRLRKRF MKLDKDNSGT IERDEFLSLP QVSSNPLATR
MIAIFDEDGG GDVDFQEFVS GLSAFSSKGN KEEKLRFAFK VYDIDRDGYI SNGELFIVLK
MMVGSNLKDQ QLQQIVDKTI MEADLDHDGK ISFEEFTKMV ENTDVSMSMT LDQF
//
