ID A0A1V8SBW9_9PEZI Unreviewed; 263 AA.
AC A0A1V8SBW9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-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};
DE Flags: Fragment;
GN ORFNames=B0A51_18804 {ECO:0000313|EMBL:OQN96698.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQN96698.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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:OQN96698.1}.
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DR EMBL; NAEU01002039; OQN96698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8SBW9; -.
DR STRING; 1974281.A0A1V8SBW9; -.
DR Proteomes; UP000192386; 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:UP000192386}.
FT DOMAIN 1..36
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 40..68
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 70..105
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 111..146
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OQN96698.1"
SQ SEQUENCE 263 AA; 29722 MW; 44B7AAE2BBD5F5E2 CRC64;
DELDRLRKRF MKLDKDGSGT IEREEFLQLP QVSSNPLATR MIAIFDEDGG GDVDFQEFVS
GLSAFSSKGN KEEKLKFAFK VYDIDRDGFI SNGELFIVLK MMVGSNLKDQ QLQQIVDKTI
MEADLDRDGK ISFEEFTKMV ENTDVSMSMT LGRFLSSAKR MYSAQRADVH KLGCPDRVRA
TVSSVEIVTG TEIRWMYSFH VIPMVRPSTA FIAMPSVRAQ PFAKALYEAP MAWVPEDCTW
LEFLPEQLAL AAHVNQDSTT TLT
//