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Database: UniProt
Entry: A0A1X0Q9A0_9MICR
LinkDB: A0A1X0Q9A0_9MICR
Original site: A0A1X0Q9A0_9MICR 
ID   A0A1X0Q9A0_9MICR        Unreviewed;       308 AA.
AC   A0A1X0Q9A0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   10-APR-2019, entry version 8.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   Name=GLC7B {ECO:0000313|EMBL:ORD96264.1};
GN   ORFNames=HERIO_1791 {ECO:0000313|EMBL:ORD96264.1};
OS   Hepatospora eriocheir.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia;
OC   Enterocytozoonidae; Hepatospora.
OX   NCBI_TaxID=1081669 {ECO:0000313|EMBL:ORD96264.1};
RN   [1] {ECO:0000313|EMBL:ORD96264.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB1 {ECO:0000313|EMBL:ORD96264.1};
RX   PubMed=28345194; DOI=10.1111/1462-2920.13734;
RA   Wiredu Boakye D., Jaroenlak P., Prachumwat A., Williams T.A.,
RA   Bateman K.S., Itsathitphaisarn O., Sritunyalucksana K.,
RA   Paszkiewicz K.H., Moore K.A., Stentiford G.D., Williams B.A.;
RT   "Decay of the glycolytic pathway and adaptation to intranuclear
RT   parasitism within Enterocytozoonidae microsporidia.";
RL   Environ. Microbiol. 19:2077-2089(2017).
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:ORD96264.1}.
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DR   EMBL; LVKB01000108; ORD96264.1; -; Genomic_DNA.
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      118    123       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
SQ   SEQUENCE   308 AA;  35435 MW;  E9F308EA46125A2E CRC64;
     MATEFDIDKI ISKLISVRTK NNKIVNLTEE ELEGLIQRVQ NIFESQPILL EIKTPINICG
     DIHGQYSDLL SLFEFGYYPP KSNYLFLGDY VDRGKQSLEC IALLFAYKIK YPENFFLLRG
     NHESEEINRI YGFYDECKRR YNIRLWKKFC EAFNWMPVCA LVGERIFCMH GGISPDFASM
     DHIRNISRPT GITDQGLLCD LLWSDPDKQI TGWGTNDRGV SVTFGADKVK EFLEKFNLDI
     IVRAHQVVED GYEFFGEKDL VTVFSAPNYC GEFTNSGAIL TVEEGLHCSF KVLKPTNSSE
     YSLDKIKR
//
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