ID A0A4Q1BS06_TREME Unreviewed; 684 AA.
AC A0A4Q1BS06;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Protein phosphatase {ECO:0000256|RuleBase:RU366020};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU366020};
GN ORFNames=M231_01962 {ECO:0000313|EMBL:RXK40710.1};
OS Tremella mesenterica (Jelly fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Tremellaceae; Tremella.
OX NCBI_TaxID=5217 {ECO:0000313|EMBL:RXK40710.1, ECO:0000313|Proteomes:UP000289152};
RN [1] {ECO:0000313|EMBL:RXK40710.1, ECO:0000313|Proteomes:UP000289152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28783 {ECO:0000313|EMBL:RXK40710.1,
RC ECO:0000313|Proteomes:UP000289152};
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|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:RXK40710.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SDIL01000015; RXK40710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q1BS06; -.
DR STRING; 5217.A0A4Q1BS06; -.
DR VEuPathDB; FungiDB:TREMEDRAFT_73064; -.
DR InParanoid; A0A4Q1BS06; -.
DR Proteomes; UP000289152; 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 Pfam; PF13672; PP2C_2; 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:UP000289152}.
FT DOMAIN 343..684
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 49..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 684 AA; 74566 MW; 4E8146471397836E CRC64;
MSKPKPGLGK GIVRTLAHHH PSSSITSSPL ILPLAPIVST YQHQNQPFIL PGPPPSFPLP
DEPGSSGSSR QPKPSSLQPL PFDITTTNTT GIINLNASNA GYAGPSRRNT FSPLISSNAY
LSLLPSWDLN TLSFSRLTKE ISSVGPIVSP YIIHKNRHKT LSKNALRRYT TPTSSNRAAV
EISPFTSNIF TPPLPSSLLT LEELNFPSNF SRNQDQFYSS PPPPPSPSSS PTPGQEQAQP
PQTVKTRPSS NHTVLSVTPL SDTSDSPSFQ LTNHPSFSSY HYDDLHLSQP STDTNSGTLG
LNSNSLIFHL GSAGIPKERT PPSSYGKPPP PLPRRIRSFP LPDISPPTSL RSIGVGEDAF
FTRLDGMCIA DGVGSWAKSN RGGADASRWS RLLTHFCEGE LDSWWASRED YMMKADEKKG
LEAVEVDDGP HAWARDGWKE GEASEKEKTG LKAERRRRRP LSPVEIMQKG FEKCLACSLQ
EGIHGSSTCL LALLYHSTLL IANVGDCALL LIRNGQVVFR TVEMQHSFNF PMQLGTHSRD
EPMKDAKRYD VGVDRGDVVI LASDGLTDNL FDDEILEVLS EFAPPLQNLP HSINLHTPPS
TPPTTSSSLP PFSPQQVSEA LAQRARNVSE QTTANTPFMH RAKEEGIDFV GGKRDGKSAF
LSVLLSCYPP HSPLFDIINI ISSS
//
