PP2B_ASPFU
ID PP2B_ASPFU Reviewed; 534 AA.
AC Q4WUR1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 105.
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=AFUA_5G09360;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL91665.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAHF01000003; EAL91665.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_753703.1; XM_748610.1.
DR PDB; 6TZ7; X-ray; 2.50 A; A=2-370.
DR PDBsum; 6TZ7; -.
DR AlphaFoldDB; Q4WUR1; -.
DR SMR; Q4WUR1; -.
DR STRING; 746128.CADAFUBP00005572; -.
DR PRIDE; Q4WUR1; -.
DR GeneID; 3511045; -.
DR KEGG; afm:AFUA_5G09360; -.
DR eggNOG; KOG0375; Eukaryota.
DR HOGENOM; CLU_004962_6_3_1; -.
DR InParanoid; Q4WUR1; -.
DR OrthoDB; 463522at2759; -.
DR PHI-base; PHI:3849; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0005955; C:calcineurin complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
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; PTHR45673; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 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; Reference proteome; Zinc.
FT CHAIN 1..534
FT /note="Serine/threonine-protein phosphatase 2B catalytic
FT subunit"
FT /id="PRO_0000286158"
FT REGION 375..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:6TZ7"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:6TZ7"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:6TZ7"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:6TZ7"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:6TZ7"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6TZ7"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:6TZ7"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:6TZ7"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:6TZ7"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:6TZ7"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:6TZ7"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:6TZ7"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:6TZ7"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:6TZ7"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:6TZ7"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 296..304
FT /evidence="ECO:0007829|PDB:6TZ7"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:6TZ7"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:6TZ7"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:6TZ7"
FT HELIX 347..364
FT /evidence="ECO:0007829|PDB:6TZ7"
SQ SEQUENCE 534 AA; 61107 MW; 94B717B7011B1C1B CRC64;
MEDGTQVSTL ERVIKEVQAP ALSTPTDEMF WSPEDPSKPN LQFLKQHFYR EGRLTEEQAL
WIIHAGTQIL RSEPNLLEMD APITVCGDVH GQYYDLMKLF EVGGDPSETR YLFLGDYVDR
GYFSIECVLY LWALKIWYPN SLWLLRGNHE CRHLTDYFTF KLECKHKYSE RIYEACIESF
CALPLAAVMN KQFLCIHGGL SPELHTLEDI KSIDRFREPP THGLMCDILW ADPLEEFGQE
KTGDYFVHNS VRGCSYFFSY PAACAFLEKN NLLSIIRAHE AQDAGYRMYR KTRTTGFPSV
MTIFSAPNYL DVYNNKAAVL KYENNVMNIR QFNCTPHPYW LPNFMDVFTW SLPFVGEKIT
DMLIAILNTC SKEELEDETP TSVSPSAPSP PLPMDVESSE FKRRAIKNKI LAIGRLSRVF
QVLREESERV TELKTAAGGR LPAGTLMLGA EGIKQAITNF EDARKVDLQN ERLPPSHEEV
IKRSEEERRA ALERAQQEAD NDTGLATVAR RISMSAGSGR SRRQRDAARE TREA
