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Database: UniProt
Entry: S8BYI6_DACHA
LinkDB: S8BYI6_DACHA
Original site: S8BYI6_DACHA 
ID   S8BYI6_DACHA            Unreviewed;       891 AA.
AC   S8BYI6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=H072_5800 {ECO:0000313|EMBL:EPS40397.1};
OS   Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS   (Monacrosporium haptotylum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Dactylellina.
OX   NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS40397.1, ECO:0000313|Proteomes:UP000015100};
RN   [1] {ECO:0000313|EMBL:EPS40397.1, ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS40397.1,
RC   ECO:0000313|Proteomes:UP000015100};
RX   PubMed=24244185;
RA   Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   PLoS Genet. 9:E1003909-E1003909(2013).
RN   [2] {ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA   Ahren D.G.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001482,
CC         ECO:0000256|RuleBase:RU004273};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-6 (PP-V)
CC       subfamily. {ECO:0000256|ARBA:ARBA00038400}.
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:EPS40397.1}.
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DR   EMBL; AQGS01000405; EPS40397.1; -; Genomic_DNA.
DR   RefSeq; XP_011111614.1; XM_011113312.1.
DR   AlphaFoldDB; S8BYI6; -.
DR   STRING; 1284197.S8BYI6; -.
DR   eggNOG; KOG0373; Eukaryota.
DR   HOGENOM; CLU_014453_0_0_1; -.
DR   OMA; PDINYVF; -.
DR   OrthoDB; 19833at2759; -.
DR   Proteomes; UP000015100; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR047129; PPA2-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45619:SF10; SERINE/THREONINE-PROTEIN PHOSPHATASE 6 CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU004273};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        60..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        210..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        264..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        336..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        361..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        395..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..447
FT                   /note="Major facilitator superfamily (MFS) profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50850"
FT   REGION          448..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..580
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   891 AA;  96801 MW;  438ACFAA925160BE CRC64;
     MSTQTETITE VPAAVVAPLK RVELEPHEEI ELNTRKSASS GQVVAEDEAI KLTKDTMLKL
     MSAGFSFFFA GTSDGCLGAL IPYIIRTYGI STDLIAVIFA ASFGGWVMAA LTNSHLLKYL
     GVGSILTIGA FLQLLAHVLR VWTPPYPLFA VSFFFTSLGQ AFQDSHSNTY VSSIKGAHRW
     LGFIHAMYAL GLLVSPFVAT PIAVRVPDRW ALFYGFLIGL GVINIIAVMY SFRDSLNVHH
     RQEATEENED TSRSKSAVVE IKEVLSMPAL WFLSLYFFLF LGAGVTGGGW TVEFLVRIRG
     GDLSKMGYVP AGQNGGLFLG RLILAEPTKR WGERRMVLIW CILTLAFQLV FWLVPNIAVN
     IVAISFVGFF SGPFFATGIS VGSKLFPKRL QATSLGLVFA LAQAGGSLFP ALTGVIASKA
     GVQVLQPIMT ALLVATGITG LCETSTTLEA HPGQQPPNIS QQKAPTARRH SRSSSTNIFP
     AALLSELKAQ SESISAGQQV LVATGGPPAP LSSSSSSSSA ITADDDDSST SSAFAPSYVG
     FQNSIDSSVS TSSRTPGSAP YIPRRPSTDP STTGPMSVGE GGSSSGGGPD EWLEMAKKCR
     YLPESDMKRL CELVKECLME ESNIQPVKSP VTVCGDIHGQ FYDLMELFKV GGGFPPDINY
     VFLGDFVDRG YFSLETFTLL MCLKAKYPSH ITLVRGNHES RQITQVYGFY EECQTKYGNA
     SVWKSCCQVF DFLALAAIID GKVLCVHGGL SPEIRTLDQI RVVARAQEIP HEGAFCDLVW
     SDPEDVDTWA VSPRGAGWLF GDKVASEFNH VNNLTLIARA HQLVNEGYKY HFKNAVVTVW
     SAPNYCYRCG NVASIMQVEE DLQPEFKIFR AVPDDQRAVP PGRSGRGEYF L
//
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