(data stored in ACNUC27125 zone)

HOGENOM: ASFUM1_5_PE807

ID   ASFUM1_5_PE807                       STANDARD;      PRT;   558 AA.
AC   ASFUM1_5_PE807; Q4WUR1;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit;
DE   EC=3.1.3 16;AltName: Full=Calmodulin-dependent calcineurin A subunit;
DE   (ASFUM1_5.PE807).
GN   Name=cnaA; ORFNames=AFUA_5G09360;
OS   ASPERGILLUS FUMIGATUS AF293.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Neosartorya.
OX   NCBI_TaxID=330879;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ASFUM1_5.PE807.
CC       Aspergillus fumigatus (strain FGSC A1100 / CBS 101355 / Af293) chromoso
CC       5, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:PP2B_ASPFU
CC   -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein
CC       phosphatase. This subunit may have a role in the calmodulin
CC       activation of calcineurin.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- COFACTOR: Binds 1 Fe(3+) ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Composed of two components (A and B), the A component is
CC       the catalytic subunit and the B component confers calcium
CC       sensitivity (By similarity).
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B
CC       subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL91665.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000172699 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q4WUR1; -.
DR   EMBL; AAHF01000003; EAL91665.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_753703.1; XM_748610.1.
DR   HSSP; Q08209; 1MF8.
DR   ProteinModelPortal; Q4WUR1; -.
DR   SMR; Q4WUR1; 6-370.
DR   STRING; Q4WUR1; -.
DR   EnsemblFungi; CADAFUAT00005983; CADAFUAP00005983; CADAFUAG00005983.
DR   GeneID; 3511045; -.
DR   GenomeReviews; CM000173_GR; cnaA.
DR   KEGG; afm:AFUA_5G09360; -.
DR   eggNOG; fuNOG05461; -.
DR   GeneTree; EFGT00050000001947; -.
DR   OrthoDB; EOG45XC4G; -.
DR   PhylomeDB; Q4WUR1; -.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004843; Metallo_PEstase_dom.
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.
DR   HOGENOMDNA; ASFUM1_5.PE807; -.
KW   EAL91665.1g.C_scaffold_1320000031;
KW   Calmodulin-binding; Complete proteome; Hydrolase; Iron; Metal-binding;
KW   Protein phosphatase; Reference proteome; Zinc.
SQ   SEQUENCE   558 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDQALARAVR DKKPVPEIDF TLHTMEDGTQ VSTLERVIKE VQAPALSTPT DEMFWSPEDP
     SKPNLQFLKQ HFYREGRLTE EQALWIIHAG TQILRSEPNL LEMDAPITVC GDVHGQYYDL
     MKLFEVGGDP SETRYLFLGD YVDRGYFSIE CVLYLWALKI WYPNSLWLLR GNHECRHLTD
     YFTFKLECKH KYSERIYEAC IESFCALPLA AVMNKQFLCI HGGLSPELHT LEDIKSIDRF
     REPPTHGLMC DILWADPLEE FGQEKTGDYF VHNSVRGCSY FFSYPAACAF LEKNNLLSII
     RAHEAQDAGY RMYRKTRTTG FPSVMTIFSA PNYLDVYNNK AAVLKYENNV MNIRQFNCTP
     HPYWLPNFMD VFTWSLPFVG EKITDMLIAI LNTCSKEELE DETPTSVSPS APSPPLPMDV
     ESSEFKRRAI KNKILAIGRL SRVFQVLREE SERVTELKTA AGGRLPAGTL MLGAEGIKQA
     ITNFEDARKV DLQNERLPPS HEEVIKRSEE ERRAALERAQ QEADNDTGLA TVARRISMSA
     GSGRSRRQRD AARETREA
//

If you have problems or comments...

PBIL Back to PBIL home page