ID A7E4J2_SCLS1 Unreviewed; 174 AA.
AC A7E4J2;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=SS1G_00214 {ECO:0000313|EMBL:EDN90814.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN90814.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(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; CH476621; EDN90814.1; -; Genomic_DNA.
DR RefSeq; XP_001598128.1; XM_001598078.1.
DR AlphaFoldDB; A7E4J2; -.
DR SMR; A7E4J2; -.
DR STRING; 665079.A7E4J2; -.
DR EnsemblFungi; EDN90814; EDN90814; SS1G_00214.
DR GeneID; 5494742; -.
DR KEGG; ssl:SS1G_00214; -.
DR VEuPathDB; FungiDB:sscle_03g028850; -.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_10_1_1; -.
DR InParanoid; A7E4J2; -.
DR OMA; DTNFDRD; -.
DR OrthoDB; 339700at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005955; C:calcineurin complex; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:EnsemblFungi.
DR GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0019902; F:phosphatase binding; IBA:GO_Central.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR GO; GO:0071444; P:cellular response to pheromone; IEA:EnsemblFungi.
DR GO; GO:0031505; P:fungal-type cell wall organization; IEA:EnsemblFungi.
DR GO; GO:0006873; P:intracellular monoatomic ion homeostasis; IEA:EnsemblFungi.
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:UP000001312}.
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; 19753 MW; 473D1D99EF03A32F CRC64;
MGNTSSAVLE NIVQGSNFDR DEVDRLRKRF MKLDKDNSGT IEREEFLSLP QISSNPLATR
MIAIFDEDGG GDVDFQEFVS GLSAFSSKGN KEQKLRFAFK VYDIDRDGYI SNGELFIVLK
MMVGSNLKDQ QLQQIVDKTI MEADLDRDGK ISFEEFTKMV ENTDVSMSMT LDQF
//
