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Database: UniProt
Entry: S9VSH6_9TRYP
LinkDB: S9VSH6_9TRYP
Original site: S9VSH6_9TRYP 
ID   S9VSH6_9TRYP            Unreviewed;       345 AA.
AC   S9VSH6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   31-JUL-2019, entry version 28.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=AGDE_00077 {ECO:0000313|EMBL:EPY43844.1}, AGDE_01620
GN   {ECO:0000313|EMBL:EPY42303.1}, AGDE_02436
GN   {ECO:0000313|EMBL:EPY41488.1}, AGDE_03473
GN   {ECO:0000313|EMBL:EPY40455.1};
OS   Angomonas deanei.
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae;
OC   Strigomonadinae; Angomonas.
OX   NCBI_TaxID=59799 {ECO:0000313|EMBL:EPY43844.1};
RN   [1] {ECO:0000313|EMBL:EPY43844.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23560078;
RA   Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA   Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P.,
RA   Brocchi M., Colabardini A.C., de Araujo Lima B., Machado C.R.,
RA   de Almeida Soares C.M., Probst C.M., de Menezes C.B., Thompson C.E.,
RA   Bartholomeu D.C., Gradia D.F., Pavoni D.P., Grisard E.C.,
RA   Fantinatti-Garboggini F., Marchini F.K., Rodrigues-Luiz G.F.,
RA   Wagner G., Goldman G.H., Fietto J.L., Elias M.C., Goldman M.H.,
RA   Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA   Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA   de Souza W., Schenkman S., de Vasconcelos A.T.;
RT   "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and
RT   Their Respective Endosymbionts Reveals New Aspects of the
RT   Trypanosomatidae Family.";
RL   PLoS ONE 8:E60209-E60209(2013).
RN   [2] {ECO:0000313|EMBL:EPY43844.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Motta M.C.M., Martins A.C.A., Preta C.M.C.C., Silva R., de Souza S.S.,
RA   Klein C.C., de Almeida L.G.P., Cunha O.L., Colabardini A.C.,
RA   Lima B.A., Machado C.R., Soares C.M.A., de Menezes C.B.A.,
RA   Bartolomeu D.C., Grisard E.C., Fantinatti-Garboggini F.,
RA   Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L.R.,
RA   Ciapina L.P., Brocchi M., Elias M.C., Goldman M.H.S., Sagot M.-F.,
RA   Pereira M., Stoco P.H., Teixeira S.M.R., de Mendonca-Neto R.P.,
RA   Maciel T.E.F., Mendes T.A.O., Urmenyi T.P., Teixeira M.M.G.,
RA   de Camargo E.F.P., de Sousa W., Schenkman S., de Vasconcelos A.T.R.;
RL   Submitted (MAR-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EPY43844.1}.
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DR   EMBL; ATMG01003471; EPY40455.1; -; Genomic_DNA.
DR   EMBL; ATMG01002435; EPY41488.1; -; Genomic_DNA.
DR   EMBL; ATMG01001619; EPY42303.1; -; Genomic_DNA.
DR   EMBL; ATMG01000077; EPY43844.1; -; Genomic_DNA.
DR   EnsemblProtists; EPY40455; EPY40455; AGDE_03473.
DR   EnsemblProtists; EPY41488; EPY41488; AGDE_02436.
DR   EnsemblProtists; EPY42303; EPY42303; AGDE_01620.
DR   EnsemblProtists; EPY43844; EPY43844; AGDE_00077.
DR   OrthoDB; 766640at2759; -.
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,
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}.
FT   DOMAIN      159    164       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION       39     60       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     39     59       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   345 AA;  39204 MW;  EEC836CE6624ED82 CRC64;
     MSVNLDAVVS KLLLSPTHNR AAPYSEEEQV PTFTRQSRLD AHEMTSGVPS RTVKTRGARS
     TSCKAEELSE EEVVHLVMES RKLFMSQPML IEIEAPVKMC GDVHGQYHDL LRLFDLGGYP
     PESNYIFLGD YVDRGEQSLE TICLLLAYKL KFPDNFFLLR GNHETSSINR IYGFFDECKR
     RYSVKLWKLF TDTFNCMPVA GLVDDRILCM HGGLSPELRN LDQIRRILRP TDVPDTGLVC
     DLLWSDPGED GLVGWGENDR GVSWTFGEDV VNHITKVCDL DLICRAHQVV DEGYQFFAKR
     KLVTVFSAPN YCGEFNNAGA FLCVDENLKC SIVQIRPTYN VDVFY
//
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