ID B6QKF9_TALMQ Unreviewed; 308 AA.
AC B6QKF9;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 03-JUL-2019, entry version 57.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=PMAA_053880 {ECO:0000313|EMBL:EEA21586.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA21586.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomeA.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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}.
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DR EMBL; DS995903; EEA21586.1; -; Genomic_DNA.
DR RefSeq; XP_002150195.1; XM_002150159.1.
DR EnsemblFungi; EEA21586; EEA21586; PMAA_053880.
DR GeneID; 7027715; -.
DR EuPathDB; FungiDB:PMAA_053880; -.
DR eggNOG; ENOG410IN85; Eukaryota.
DR eggNOG; ENOG410XPVF; LUCA.
DR OrthoDB; 766640at2759; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:InterPro.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR037979; PPP1CA.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668:SF377; PTHR11668:SF377; 1.
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 Complete proteome {ECO:0000313|Proteomes:UP000001294};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294}.
FT DOMAIN 120 125 SER_THR_PHOSPHATASE.
FT {ECO:0000259|PROSITE:PS00125}.
SQ SEQUENCE 308 AA; 35548 MW; D237428A67161817 CRC64;
MADQDVDLDS IIDRLLEVRG SRPGKQVQLL ESEIRHLCTK AREIFISQPI LLELEAPIKI
CGDIHGQYYD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFIL
RGNHECASIN RIYGFYDECK RRYNIKLWKT FTDCFNCLPI AAIIDEKIFT MHGGLSPDLN
SMEQIRRVMR PTDIPDCGLL CDLLWSDPDK DITGWSENDR GVSFTFGPDV VSRFLQKHDM
DLICRAHQVV EDGYEFFSKR QLVTLFSAPN YCGEFDNAGA MMSVDESLLC SFQILKPAEK
KQNRFGRK
//