(data stored in ACNUC27125 zone)

HOGENOM: NEUCR_13_PE208

ID   NEUCR_13_PE208                       STANDARD;      PRT;   575 AA.
AC   NEUCR_13_PE208; Q05681; Q1K7G7; Q9HEE2;
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   (NEUCR_13.PE208).
GN   Name=cna-1; ORFNames=99H12.070, NCU03804;
OS   NEUROSPORA CRASSA.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=5141;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS NEUCR_13.PE208.
CC       Neurospora crassa supercontig 7.11 EF1 full sequence 1..902551 annotate
CC       Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:PP2B_NEUCR
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.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B
CC       subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA33565.1; Type=Erroneous initiation;
CC       Sequence=CAC18243.1; Type=Erroneous gene model prediction;
CC       Sequence=EAA31957.2; Type=Erroneous gene model prediction;
CC   -!- GENE_FAMILY: HOG000172699 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Neurospora_crassa;EFNCRG00000003474;EFNCRT00000003478;EFNCRP00000003478.
DR   UniProtKB/Swiss-Prot; Q05681; Q1K7G7; Q9HEE2; -.
DR   EMBL; M73032; AAA33565.1; ALT_INIT; mRNA.
DR   EMBL; AL451018; CAC18243.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AABX02000011; EAA31957.2; ALT_SEQ; Genomic_DNA.
DR   PIR; A40942; A40942.
DR   RefSeq; XP_961193.2; XM_956100.2.
DR   UniGene; Ncr.7826; -.
DR   ProteinModelPortal; Q05681; -.
DR   SMR; Q05681; 46-410.
DR   EnsemblFungi; EFNCRT00000003478; EFNCRP00000003478; EFNCRG00000003474.
DR   GeneID; 3877353; -.
DR   eggNOG; fuNOG05461; -.
DR   GeneTree; EFGT00050000001947; -.
DR   OrthoDB; EOG45XC4G; -.
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; NEUCR_13.PE208; -.
KW   EFNCRG00000003474g.scaffold_90100000011;
KW   Q05681;
KW   Calmodulin-binding; Complete proteome; Hydrolase; Iron; Metal-binding;
KW   Protein phosphatase; Reference proteome; Zinc.
SQ   SEQUENCE   575 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MESNNGTGAP GAFHTQQVDN AIRAIQHKRP LPEIDFTIHT MEDGSQVSTM ERVCKDVQAP
     AMFKPSDEQF FEDETHTKPD IQFLKQHFYR EGRLTEEQAL WIIREGTKLL RAEPNLLEMD
     APITVCGDVH GQYYDLMKLF EVGGDPAETR YLFLGDYVDR GYFSIECVLY LWALKIHYPK
     TLWLLRGNHE CRHLTDYFTF KLECKHKYSE AIYEACMESF CCLPLAAVMN KQFLCIHGGL
     SPELHTLDDI RNIDRFREPP TQGLMCDILW ADPLEDFGQE KTTDFFVHNH VRGCSYFFSY
     SAACHFLEKN NLLSIIRAHE AQDAGYRMYR KTRTTGFPSV MTIFSAPNYL DVYNNKAAVL
     KYENNVMNIR QFNCTPHPYW LPNFMDVFTW SLPFVGEKIT DMLIAILSTC SEEELREDSA
     TTSPGSASPA LPSAANQDPD SIEFKRRAIK NKILAIGRLS RVFQVLREES ERVTELKTVS
     GGRLPAGTLM LGAEGIKNAI SSFEDARKVD LQNERLPPSH DEVVKMQDEE RAQALERATR
     EADNDKKLQT LSRRLSTIRN YVRESSEGFM GVLWE
//

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