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Database: UniProt
Entry: K1VNG2_TRIAC
LinkDB: K1VNG2_TRIAC
Original site: K1VNG2_TRIAC 
ID   K1VNG2_TRIAC            Unreviewed;       312 AA.
AC   K1VNG2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   26-FEB-2020, entry version 40.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=A1Q2_03508 {ECO:0000313|EMBL:EKD02146.1};
OS   Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD02146.1, ECO:0000313|Proteomes:UP000006757};
RN   [1] {ECO:0000313|EMBL:EKD02146.1, ECO:0000313|Proteomes:UP000006757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD02146.1,
RC   ECO:0000313|Proteomes:UP000006757};
RX   PubMed=23193141; DOI=10.1128/EC.00264-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Genome sequence of the Trichosporon asahii environmental strain CBS
RT   8904.";
RL   Eukaryot. Cell 11:1586-1587(2012).
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         Evidence={ECO:0000256|SAAS:SAAS01116782};
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         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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKD02146.1}.
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DR   EMBL; AMBO01000296; EKD02146.1; -; Genomic_DNA.
DR   STRING; 82508.K1VNG2; -.
DR   EnsemblFungi; EKD02146; EKD02146; A1Q2_03508.
DR   HOGENOM; CLU_004962_0_0_1; -.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000006757; 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   Hydrolase {ECO:0000256|RuleBase:RU004273, 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:UP000006757}.
FT   DOMAIN          122..127
FT                   /note="SER_THR_PHOSPHATASE"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
SQ   SEQUENCE   312 AA;  35743 MW;  7AD088893F0E7F25 CRC64;
     MADAANDIDL DSVIDRLLEV RGNRPGKAVQ LQEYEIKHLC TKAREIFISQ PILLELEAPI
     KICGDIHGQY YDLLRLFEYG GFPPEANYLF LGDYVDRGKQ SLETICLLLA YKIKYPENFF
     ILRGNHECAS INRIYGFYDE CKRRYNIKLW KTFTDCFNCL PIAAIIDEKI FCMHGGLSPD
     LQSMEQIRRV MRPTDVPDTG LLCDLLWSDP DKDITGWSEN DRGVSFTFGP DVVSRFLQKH
     DMDLICRAHQ VVEDGYEFFA KRQLVTLFSA PNYCGEFDNA GAMMSVDDTL LCSFQPAEKK
     APKYGYGGGR RQ
//
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