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 27-MAR-2024, entry version 133.
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;
OC Aspergillus subgen. Nidulantes.
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};
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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 AlphaFoldDB; P48457; -.
DR SMR; P48457; -.
DR STRING; 227321.P48457; -.
DR EnsemblFungi; CBF77949; CBF77949; ANIA_08820.
DR GeneID; 2868443; -.
DR KEGG; ani:AN8820.2; -.
DR VEuPathDB; FungiDB:AN8820; -.
DR eggNOG; KOG0375; Eukaryota.
DR HOGENOM; CLU_004962_6_0_1; -.
DR InParanoid; P48457; -.
DR OMA; YPAACNF; -.
DR OrthoDB; 1488111at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR GO; GO:0005955; C:calcineurin complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IEA:EnsemblFungi.
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:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:EnsemblFungi.
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 GO; GO:1905949; P:negative regulation of calcium ion import across plasma membrane; IEA:EnsemblFungi.
DR GO; GO:1903473; P:positive regulation of mitotic actomyosin contractile ring contraction; IEA:EnsemblFungi.
DR GO; GO:0140281; P:positive regulation of mitotic division septum assembly; IEA:EnsemblFungi.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:EnsemblFungi.
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; IPR043360; PP2B.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45673; SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR PANTHER; PTHR45673:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
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 REGION 399..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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
//
