ID A0A1E3I7L1_9TREE Unreviewed; 514 AA.
AC A0A1E3I7L1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=L202_00586 {ECO:0000313|EMBL:ODN84693.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN84693.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN84693.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN84693.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) 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:ODN84693.1}.
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DR EMBL; AWGJ01000001; ODN84693.1; -; Genomic_DNA.
DR RefSeq; XP_018998496.1; XM_019133791.1.
DR AlphaFoldDB; A0A1E3I7L1; -.
DR STRING; 1295533.A0A1E3I7L1; -.
DR GeneID; 30151895; -.
DR OrthoDB; 19833at2759; -.
DR Proteomes; UP000094065; 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:UP000094065}.
FT DOMAIN 304..309
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 514 AA; 55487 MW; 6C38B229D87DD284 CRC64;
MGQANSSSKK LGRTSSKQLS PNDLADSLSR TAIADTDTRN IPKRSKAPGH EPRQSSSSSY
GSTRPALNTQ GSYDNAPSIR STTSAGPSSP SSPSNIPTTK TIVAAPEKAG RKSSLIPGGG
SPPPPSAMSI SPSSGRSASP PPLGSSPATP GNSHISRDSA NSLLAPNGAA LTQSISRSSV
GPGGGVQVLD VDNMIQRLLE AGYSGKVTKS PPLKNAEIMS VCAAAREVFL SQPTLIELSP
PVKIVGDVHG QYADLLRMFE MCGFPPAANY LFLGDYVDRG KQSLETILLL LCYKIKYPEN
FFLLRGNHEC ANVTRVYGFY DECKRRTNIK IWKTFIDVFN TLPIASIVAS KIFCVHGGLS
PSLKSMDDIR RIQRPTDVPD YGLLNDLVWS DPSDTALDWE DNERGVSFCY GKSVINAFLA
THDMDLICRA HMVVEDGYEF YNDRTLVTVF SAPNYCGEFD NFGAVMSVSE DLLCSFELLK
PLDGAALKKE MTRSKRKSLQ NHQSPPNNPM AQSF
//
