ID A0A1V8U102_9PEZI Unreviewed; 571 AA.
AC A0A1V8U102;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=B0A51_15640 {ECO:0000313|EMBL:OQO17399.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO17399.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000256|PIRNR:PIRNR000909};
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|PIRNR:PIRNR000909,
CC ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936,
CC ECO:0000256|PIRNR:PIRNR000909};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000909}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-Z subfamily.
CC {ECO:0000256|ARBA:ARBA00029458, ECO:0000256|PIRNR:PIRNR000909}.
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:OQO17399.1}.
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DR EMBL; NAEU01001037; OQO17399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8U102; -.
DR STRING; 1974281.A0A1V8U102; -.
DR Proteomes; UP000192386; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07414; MPP_PP1_PPKL; 1.
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 PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR11668:SF484; SERINE_THREONINE-PROTEIN PHOSPHATASE PP-Z1-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PIRSF; PIRSF000909; PPPtase_PPZ; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR000909};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273};
KW Manganese {ECO:0000256|PIRNR:PIRNR000909};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000909};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|PIRNR:PIRNR000909};
KW Reference proteome {ECO:0000313|Proteomes:UP000192386}.
FT DOMAIN 360..365
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 571 AA; 61399 MW; F62FC44C45C8BA0A CRC64;
MGNESSKESK DNKSTGSQTP TGPSSSAGPS LDSYPSFSKS DTRESMRSFR QSLKTKIPGS
KSAESPRGSS SGLSLDTSGD GDKSDALSVR SATSGRSGSR PSRGVIEGAA GSRRGSLRGA
ALDEATQQQP PPSPTMSPSV SKGGHGDITE AQRSGEVDAV SDAPPAGGFA HGMHHTANRE
PGPSILVRRD PNAPKTASSP QAAPQGAAAV LALSDQLDKS TITPTSSTPT ASSSSNMDIG
ALTPSDLDDM IKRLVDAGYA GKVTKTVCLK NAEITAICTA AREVFLSQPA LIELSPPVKI
VGDVHGQYTD LIRMFEMCGF PPNSNFLFLG DYVDRGKQSL ETILLLLCYK LRYPENFFLL
RGNHECANVT RVYGFYDECK RRCNVKIWKT FVDTFNTLPI AAIVAGKIFC VHGGLSPSLG
HMDDIRNIAR PTDVPDYGLL NDLLWSDPAD MEADWEANER GVSYCFGKKV IMEFLAKHDF
DLVCRAHMVV EDGYEFFQER ILVTVFSAPN YCGEFDNWGA VMSVSGELLC SFELLKPLDS
SALKSHIKKG RSKRSAMMVN SPPASQFPQS Y
//
