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Database: UniProt
Entry: G0RNP0_HYPJQ
LinkDB: G0RNP0_HYPJQ
Original site: G0RNP0_HYPJQ 
ID   G0RNP0_HYPJQ            Unreviewed;       518 AA.
AC   G0RNP0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   31-JUL-2019, entry version 42.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273};
GN   ORFNames=TRIREDRAFT_79535 {ECO:0000313|EMBL:EGR47186.1};
OS   Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   Trichoderma.
OX   NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN   [1] {ECO:0000313|EMBL:EGR47186.1, ECO:0000313|Proteomes:UP000008984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QM6a {ECO:0000313|EMBL:EGR47186.1,
RC   ECO:0000313|Proteomes:UP000008984};
RX   PubMed=18454138; DOI=10.1038/nbt1403;
RA   Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M.,
RA   Baker S.E., Chapman J., Chertkov O., Coutinho P.M., Cullen D.,
RA   Danchin E.G., Grigoriev I.V., Harris P., Jackson M., Kubicek C.P.,
RA   Han C.S., Ho I., Larrondo L.F., de Leon A.L., Magnuson J.K.,
RA   Merino S., Misra M., Nelson B., Putnam N., Robbertse B., Salamov A.A.,
RA   Schmoll M., Terry A., Thayer N., Westerholm-Parvinen A., Schoch C.L.,
RA   Yao J., Barabote R., Nelson M.A., Detter C., Bruce D., Kuske C.R.,
RA   Xie G., Richardson P., Rokhsar D.S., Lucas S.M., Rubin E.M.,
RA   Dunn-Coleman N., Ward M., Brettin T.S.;
RT   "Genome sequencing and analysis of the biomass-degrading fungus
RT   Trichoderma reesei (syn. Hypocrea jecorina).";
RL   Nat. Biotechnol. 26:553-560(2008).
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|PIRNR:PIRNR000909,
CC         ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01116780};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000909};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-Z subfamily.
CC       {ECO:0000256|PIRNR:PIRNR000909}.
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DR   EMBL; GL985069; EGR47186.1; -; Genomic_DNA.
DR   RefSeq; XP_006966772.1; XM_006966710.1.
DR   STRING; 51453.EGR47186; -.
DR   EnsemblFungi; EGR47186; EGR47186; TRIREDRAFT_79535.
DR   GeneID; 18489041; -.
DR   KEGG; tre:TRIREDRAFT_79535; -.
DR   EuPathDB; FungiDB:TRIREDRAFT_79535; -.
DR   KO; K06269; -.
DR   Proteomes; UP000008984; Unassembled WGS sequence.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0048037; F:cofactor binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004724; F:magnesium-dependent protein serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR011159; PPPtase_PPZ/Ppq1.
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   PIRSF; PIRSF000909; PPPtase_PPZ; 2.
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:UP000008984};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000909,
KW   ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01017252};
KW   Manganese {ECO:0000256|PIRNR:PIRNR000909,
KW   ECO:0000256|SAAS:SAAS01017251};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000909,
KW   ECO:0000256|SAAS:SAAS01017255};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR000909,
KW   ECO:0000256|SAAS:SAAS01017274};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008984}.
FT   DOMAIN      308    313       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION        1    152       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      499    518       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS      1     34       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     52     66       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     74    106       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    118    132       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    502    518       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   518 AA;  56686 MW;  5DB275D08AE13939 CRC64;
     MGNQTSKEGG SSSKNGAGSG DALQSYPSFS KSDTKDSTRS FRGLRSKIPG SGKTDSPRNS
     IVANGDTGDA ASVRSGKSGR SSISRSGRSS DTIPLRGNSV DLTAESPSLD DQIPPPSPVS
     ESVKSGTHDV SAAQASGEVD HVSDQPPSAN ASLNTHLLPP GQSILVKRED APVKKPPKKP
     KNDTMGMDEI KEMDLDDYIK RLLDAGYAGK VTKSVCLKNA EIMAICARVR EVFLAQPALL
     ELDAPVKIVG DVHGQYTDLI RMFEMCGFPP TSNYLFLGDY VDRGKQSLET ILLLLCYKLK
     FPENFFLLRG NHECANVTRV YGFYDECKRR CNIKIWKTFI DCFNTLPIAA IVAGKIFCVH
     GGLSPALSHM DDIRNIARPT DVPDYGLLND LLWADPADME QDWEANERGV SYCFGKRVIT
     DFLAQHDFDL VCRAHMVVED GYEFFNDRVL VTVFSAPNYC GEFDNWGAVM SVSSELLCSF
     ELLKPLDSSA LKSHIKKGRS KRQQMLNSPP ASVMPQSV
//
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