ID A0A2T4AQM8_TRIHA Unreviewed; 392 AA.
AC A0A2T4AQM8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Protein phosphatase {ECO:0000256|RuleBase:RU366020};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU366020};
GN ORFNames=M431DRAFT_74757 {ECO:0000313|EMBL:PTB59367.1};
OS Trichoderma harzianum CBS 226.95.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB59367.1, ECO:0000313|Proteomes:UP000241690};
RN [1] {ECO:0000313|EMBL:PTB59367.1, ECO:0000313|Proteomes:UP000241690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB59367.1,
RC ECO:0000313|Proteomes:UP000241690};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-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|RuleBase:RU366020};
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|RuleBase:RU366020};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU366020};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU366020};
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU366020}.
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DR EMBL; KZ679676; PTB59367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4AQM8; -.
DR STRING; 983964.A0A2T4AQM8; -.
DR OrthoDB; 2101140at2759; -.
DR Proteomes; UP000241690; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR039123; PPTC7.
DR PANTHER; PTHR12320:SF24; PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR12320; PROTEIN PHOSPHATASE 2C; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366020};
KW Magnesium {ECO:0000256|RuleBase:RU366020};
KW Manganese {ECO:0000256|RuleBase:RU366020};
KW Metal-binding {ECO:0000256|RuleBase:RU366020};
KW Protein phosphatase {ECO:0000256|RuleBase:RU366020};
KW Reference proteome {ECO:0000313|Proteomes:UP000241690}.
SQ SEQUENCE 392 AA; 42846 MW; 2419836ADB19E9F0 CRC64;
MVGMRTSPSP TLATFLTSTS PSRLKLFADP LWRGRCQRSL VSVASQQSQS PSQYGKPPFR
FETGIGLFAK RSPRPFPPPF LSPPSVSFSD PLSTHHQSRD RRARAFVNGE LIKGLTNGDD
AVYASDYFIC ANDGVGAWAA RPRGHAGLWS RLILHFWATA IEEESAQNLF QQKAYQPDPI
ASLQTAFEQT QEATGAHNWQ GTTTACGAQL HYKMVMDAGR QVAAPVLYVT NLGDCQVLVL
RPRDQGVVFK TTEQWHWFDC PRQLGTNSPD TPRENAVVDV VDLEEGDVVL AMSDGVIDNL
WGHEIATRVF QSIKEWEAKK GADGDADRTG GRNGGMSVVA QDLVAAAKVI ALDPYAESPF
MEHAIEEGLA SEGGKLDDIS VVAALCVRDT ER
//
