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Database: UniProt
Entry: A0A0U5FYD8_9EURO
LinkDB: A0A0U5FYD8_9EURO
Original site: A0A0U5FYD8_9EURO 
ID   A0A0U5FYD8_9EURO        Unreviewed;       399 AA.
AC   A0A0U5FYD8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   31-JUL-2019, entry version 12.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=ASPCAL03315 {ECO:0000313|EMBL:CEL02143.1};
OS   Aspergillus calidoustus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=454130 {ECO:0000313|EMBL:CEL02143.1, ECO:0000313|Proteomes:UP000054771};
RN   [1] {ECO:0000313|EMBL:CEL02143.1, ECO:0000313|Proteomes:UP000054771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jaenicke S.;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|SAAS:SAAS01116782};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
CC         [protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
CC         COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
CC         EC=3.1.3.16; Evidence={ECO:0000256|RuleBase:RU004273,
CC         ECO:0000256|SAAS:SAAS01116780};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01017257}.
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DR   EMBL; CDMC01000003; CEL02143.1; -; Genomic_DNA.
DR   EnsemblFungi; CEL02143; CEL02143; ASPCAL03315.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000054771; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000054771};
KW   Hydrolase {ECO:0000256|RuleBase:RU004273,
KW   ECO:0000256|SAAS:SAAS01017252};
KW   Manganese {ECO:0000256|SAAS:SAAS01017251};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01017255};
KW   Protein phosphatase {ECO:0000256|SAAS:SAAS01017274};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054771}.
FT   DOMAIN      167    172       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION      369    399       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    369    388       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   399 AA;  43979 MW;  3EEE9134C7D1EFC0 CRC64;
     MSTPPVTTLD TGGEFILNSR ESYPVLVSPS IPLAKDPGSP IAAEGSATSP ELDVDATISK
     LLQVGRSRRI PRLFCLEPAE ISAICLAASD VLLADPSLLE ISAPVKIVGD IHGQFTDLIR
     IFDLCGFPED TQYLFLGNYV SKGRNSLETI LLLLCYKLKY PKTFFLLRGN HECASIARLS
     SFYSECKYRC RLNVWKTFRS VFDSLPIAAI VSEKLFCVHG GLSPSLTNLD GIRAISRPTD
     VSDAGLLTDL LWSDPADVEV DWTENDRGVS YYFNKSVTRN FLQRSGLDMI CRGHMVVDEG
     YKFHHDMSVV TIFSAPNVGL TKPLDVGFYA YDHLVQHLDD LDNSGAIMAV AADLSYGFEV
     LKPVDPYGRG RKVPRGNRPG EPEGETEESF HGLPLAQDF
//
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