ID A0A2S7PBA5_9HELO Unreviewed; 401 AA.
AC A0A2S7PBA5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Protein phosphatase {ECO:0000256|RuleBase:RU366020};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU366020};
GN ORFNames=CJF32_00004733 {ECO:0000313|EMBL:PQE11565.1};
OS Rutstroemia sp. NJR-2017a WRK4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070412 {ECO:0000313|EMBL:PQE11565.1, ECO:0000313|Proteomes:UP000238813};
RN [1] {ECO:0000313|EMBL:PQE11565.1, ECO:0000313|Proteomes:UP000238813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a WRK4 {ECO:0000313|EMBL:PQE11565.1,
RC ECO:0000313|Proteomes:UP000238813};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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}.
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:PQE11565.1}.
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DR EMBL; NJPR01000123; PQE11565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7PBA5; -.
DR STRING; 2070412.A0A2S7PBA5; -.
DR InParanoid; A0A2S7PBA5; -.
DR OrthoDB; 240602at2759; -.
DR Proteomes; UP000238813; 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; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR039123; PPTC7.
DR PANTHER; PTHR12320; PROTEIN PHOSPHATASE 2C; 1.
DR PANTHER; PTHR12320:SF1; PROTEIN PHOSPHATASE PTC7 HOMOLOG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS51746; PPM_2; 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:UP000238813}.
FT DOMAIN 97..396
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 401 AA; 42960 MW; 39E790F966F74C8A CRC64;
MAFSARGFAL AAHAPKSLIR SKRSICASAI IGSTRNRSSL SATTSLSKSA PWRRNPTCPT
PFRQFSTTKP FYSTPKFTYE YHYDPVKNVS QFNSYNAIAA PLKPPQLRPA SGQDSFFVAP
ISQTSDIALG IADGVGGWID SGVDPSDFSH GFCEYMAYTA YTSNTIDSAP ISARRLMQKG
YDLICESGKV RAGGSTACVG LLSSSGSMEV ANLGDSGFVQ LRLNAVHAAS EFQTHAFNTP
YQLSLVPETV LKQARKFGGE QLMDFPADAD VMGCELRHGD VVVFASDGVW DNLSSGDVLK
IVSRGMREHG AWVNGDEGEG IEVGDGLSGL VEKGEGEEDV INLQSALAVG IAGEAKAASM
SLRRDGPFAR EVQKRYPEED WRGGKADDIC VVVVVVVEEG K
//
