(data stored in ACNUC27125 zone)

SWISSPROT: PP2B_EMENI

ID   PP2B_EMENI              Reviewed;         549 AA.
AC   P48457; C8V9L3; Q5ASB0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 3.
DT   11-DEC-2019, entry version 117.
DE   RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit;
DE            EC=3.1.3.16;
DE   AltName: Full=Calmodulin-dependent calcineurin A subunit;
GN   Name=cnaA; ORFNames=AN8820;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8013455; DOI=10.1002/j.1460-2075.1994.tb06544.x;
RA   Rasmussen C.D., Garen C., Brining S., Kincaid R.L., Means R.L., Means A.R.;
RT   "The calmodulin-dependent protein phosphatase catalytic subunit
RT   (calcineurin A) is an essential gene in Aspergillus nidulans.";
RL   EMBO J. 13:2545-2552(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase.
CC       This subunit may have a role in the calmodulin activation of
CC       calcineurin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Composed of two components (A and B), the A component is the
CC       catalytic subunit and the B component confers calcium sensitivity.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA57873.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=EAA60108.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
DR   EMBL; U13919; AAA57873.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AACD01000162; EAA60108.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BN001303; CBF77949.1; -; Genomic_DNA.
DR   PIR; S46322; S46322.
DR   RefSeq; XP_682089.1; XM_676997.1.
DR   SMR; P48457; -.
DR   STRING; 162425.CADANIAP00006237; -.
DR   PRIDE; P48457; -.
DR   EnsemblFungi; CBF77949; CBF77949; ANIA_08820.
DR   EnsemblFungi; EAA60108; EAA60108; AN8820.2.
DR   GeneID; 2868443; -.
DR   KEGG; ani:AN8820.2; -.
DR   HOGENOM; HOG000172699; -.
DR   InParanoid; P48457; -.
DR   KO; K04348; -.
DR   OMA; LWSLKIW; -.
DR   OrthoDB; 463522at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005955; C:calcineurin complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; ISA:AspGD.
DR   GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR   GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:AspGD.
DR   CDD; cd07416; MPP_PP2B; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041751; MPP_PP2B.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; P48457.
DR   SWISS-2DPAGE; P48457.
KW   Calmodulin-binding; Hydrolase; Iron; Metal-binding; Protein phosphatase;
KW   Reference proteome; Zinc.
FT   CHAIN           1..549
FT                   /note="Serine/threonine-protein phosphatase 2B catalytic
FT                   subunit"
FT                   /id="PRO_0000058834"
FT   ACT_SITE        173
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   METAL           112
FT                   /note="Iron"
FT                   /evidence="ECO:0000250"
FT   METAL           114
FT                   /note="Iron"
FT                   /evidence="ECO:0000250"
FT   METAL           140
FT                   /note="Iron"
FT                   /evidence="ECO:0000250"
FT   METAL           140
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           172
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           221
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           303
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        386..387
FT                   /note="ML -> IV (in Ref. 1; AAA57873)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        541
FT                   /note="M -> MVRRIR (in Ref. 1; AAA57873)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   549 AA;  63007 MW;  ECD795FCBBDF4991 CRC64;
     MDRNLARAVA DKQPVPEIDF TLHVMEDGTQ VSTLERVVKE VQAPALNKPS DDQFWDPEEP
     TKPNLQFLKQ HFYREGRLTE DQALWIIQAG TQILKSEPNL LEMDAPITVC GDVHGQYYDL
     MKLFEVGGDP AETRYLFLGD YVDRGYFSIE CVLYLWALKI WYPNTLWLLR GNHECRHLTD
     YFTFKLECKH KYSERIYEAC IESFCALPLA AVMNKQFLCI HGGLSPELHT LEDIKSIDRF
     REPPTHGLMC DILWADPLED FGQEKTGDYF IHNSVRGCSY FFSYPAACAF LEKNNLLSVI
     RAHEAQDAGY RMYRKTRTTG FPSVMTIFSA PNYLDVYNNK AAVLKYENNV MNIRQFNCTP
     HPYWLPNFMD VFTWSLPFVG EKITDMLIAI LNTCSKEELE DETPSTISPA EPSPPMPMDT
     VDTESTEFKR RAIKNKILAI GRLSRVFQVL REESERVTEL KTAAGGRLPA GTLMLGAEGI
     KQAITNFEDA RKVDLQNERL PPSHDEVVRR SEEERRIALD RAQHEADNDT GLATVARRIS
     MKIPSTTRR
//

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