ID   PP2B1_CRYNH             Reviewed;         639 AA.
AC   O42773; J9W089;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit A1;
DE            EC=3.1.3.16;
DE   AltName: Full=Calcineurin A1;
GN   Name=CNA1; ORFNames=CNAG_04796;
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX   PubMed=9184205; DOI=10.1093/emboj/16.10.2576;
RA   Odom A., Muir S., Lim E., Toffaletti D.L., Perfect J.R., Heitman J.;
RT   "Calcineurin is required for virulence of Cryptococcus neoformans.";
RL   EMBO J. 16:2576-2589(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA   Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA   Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA   Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA   Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA   Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA   Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
CC   -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase.
CC       This subunit may have a role in the calmodulin activation of
CC       calcineurin (By similarity). {ECO:0000250}.
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}.
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DR   EMBL; AF042082; AAB97372.1; -; Genomic_DNA.
DR   EMBL; CP003829; AFR97420.1; -; Genomic_DNA.
DR   RefSeq; XP_012052213.1; XM_012196823.1.
DR   PDB; 6TZ8; X-ray; 3.30 A; A/D=34-402.
DR   PDBsum; 6TZ8; -.
DR   AlphaFoldDB; O42773; -.
DR   SMR; O42773; -.
DR   GeneID; 23888175; -.
DR   KEGG; cng:CNAG_04796; -.
DR   VEuPathDB; FungiDB:CNAG_04796; -.
DR   HOGENOM; CLU_004962_6_1_1; -.
DR   OrthoDB; 1488111at2759; -.
DR   PHI-base; PHI:89; -.
DR   Proteomes; UP000010091; Chromosome 10.
DR   GO; GO:0005955; C:calcineurin complex; IPI:UniProtKB.
DR   GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IEA:EnsemblFungi.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0008199; F:ferric iron binding; IDA:UniProtKB.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0097720; P:calcineurin-mediated signaling; IEA:EnsemblFungi.
DR   GO; GO:0071277; P:cellular response to calcium ion; IEA:EnsemblFungi.
DR   GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IEA:EnsemblFungi.
DR   GO; GO:0035556; P:intracellular signal transduction; IMP:UniProtKB.
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:1900182; P:positive regulation of protein localization to nucleus; IMP:UniProtKB.
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   1: Evidence at protein level;
KW   3D-structure; Calmodulin-binding; Hydrolase; Iron; Metal-binding;
KW   Protein phosphatase; Zinc.
FT   CHAIN           1..639
FT                   /note="Serine/threonine-protein phosphatase 2B catalytic
FT                   subunit A1"
FT                   /id="PRO_0000058832"
FT   REGION          494..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..512
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        181
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   HELIX           59..62
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           73..81
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           88..104
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          107..111
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          113..118
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           125..135
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   TURN            138..140
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          150..153
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           156..169
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   TURN            171..173
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           184..189
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           192..199
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           202..212
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          218..221
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   TURN            222..224
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          225..227
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           239..243
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          253..255
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           256..262
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   TURN            267..270
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          277..280
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   TURN            282..284
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          285..290
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           292..302
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          305..309
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          317..320
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   TURN            325..327
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          329..335
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           341..343
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          349..354
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          359..364
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           374..376
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           379..398
FT                   /evidence="ECO:0007829|PDB:6TZ8"
SQ   SEQUENCE   639 AA;  71500 MW;  4B92EBE361C80579 CRC64;
     MASPATQTAN AIAAINNRSN LVIPEIDFTQ HQLENGEIVS TTERVIKDVQ APAMYVPTDD
     QFWSKVDKTK PDIAFLKNHF YREGRLTEEQ ALYILEKGGE LLRSEPNLLE VDAPITVCGD
     IHGQYYDLMK LFEVGGNPAD TRYLFLGDYV DRGYFSIECV LYLWSLKMWY PDTLFLLRGN
     HECRHLTDYF TFKLECKHKY SETVYNACME SFCNLPLAAV MNKQFLCIHG GLSPELHTLD
     DLRSINRFRE PPTQGLMCDI LWADPLEDFG SEKTNENFLH NHVRGCSYFF TYNAACQFLE
     RNNLLSIIRA HEAQDAGYRM YRKTKTTGFP SVMTIFSAPN YLDVYSNKAA VLKYESNVMN
     IRQFNCTPHP YWLPNFMDVF TWSLPFVGEK ITDMLIAILN CCTKEELEEE DEEFPLNAPE
     PTDAESAAER RQIIKNKILA VGRMSRVFSL LREESERVSE LKSISGSNAL PAGMLASGAE
     GIKEAIQGFE DARKSDIENE RLPPDIIDPD EDKPASPSAS PIMPATPEEI PSEIPYDSPI
     TGTPRTPISS AIASGSPGSP GTPTSPSIGG PPLTAWRPGH GRRTSLGTTK TSPSTRRRSL
     ENTMHLIRDV VGGKDAQGDG QLERLAEVIS SPTKGGQGE
//