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Database: UniProt
Entry: A0A5J9VDM5_9POAL
LinkDB: A0A5J9VDM5_9POAL
Original site: A0A5J9VDM5_9POAL 
ID   A0A5J9VDM5_9POAL        Unreviewed;       481 AA.
AC   A0A5J9VDM5;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   ORFNames=EJB05_16070 {ECO:0000313|EMBL:TVU34239.1};
OS   Eragrostis curvula (weeping love grass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Chloridoideae; Eragrostideae; Eragrostidinae; Eragrostis.
OX   NCBI_TaxID=38414 {ECO:0000313|EMBL:TVU34239.1, ECO:0000313|Proteomes:UP000324897};
RN   [1] {ECO:0000313|EMBL:TVU34239.1, ECO:0000313|Proteomes:UP000324897}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Victoria {ECO:0000313|Proteomes:UP000324897};
RC   TISSUE=Leaf {ECO:0000313|EMBL:TVU34239.1};
RX   PubMed=31308395; DOI=.1038/s41598-019-46610-0;
RA   Carballo J., Santos B.A.C.M., Zappacosta D., Garbus I., Selva J.P.,
RA   Gallo C.A., Diaz A., Albertini E., Caccamo M., Echenique V.;
RT   "A high-quality genome of Eragrostis curvula grass provides insights into
RT   Poaceae evolution and supports new strategies to enhance forage quality.";
RL   Sci. Rep. 9:10250-10250(2019).
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|ARBA:ARBA00001512};
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|ARBA:ARBA00001482};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000256|ARBA:ARBA00006702,
CC       ECO:0000256|RuleBase:RU003465}.
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:TVU34239.1}.
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DR   EMBL; RWGY01000009; TVU34239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5J9VDM5; -.
DR   Proteomes; UP000324897; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR47992:SF160; PROTEIN PHOSPHATASE 2C 77; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW   ECO:0000256|RuleBase:RU003465};
KW   Reference proteome {ECO:0000313|Proteomes:UP000324897}.
FT   DOMAIN          149..471
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          62..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   481 AA;  50223 MW;  A270EB9C9F904C06 CRC64;
     MEDAVAVVVP PLAAPPVFSP AAAGLTLIAA AAADPIAAAV AEAMEGVPVP TVPPVRTASA
     VEDDALPPGA GAEAEGGEEA AAGSPCSVAS DCSSVASADF EGVGLGFFGA AAGGAMVFED
     SAALAATVEA EARVAAGGRS VFAVDCVPLW GYTSICGRRP EMEDAVATVP RFFDVPLWML
     TGNAVVDGLD PMTFRLPSHF FGVYDGHGGA QVADYCRERL HVALVEQLRR IEGTVSAANL
     GEVEFKKQWE KAFVDCFSRV DDEVGGKASR EGDGAGTSDA AAAVLDPVAP ETVGSTAVVS
     IICSSHIIVS NCGDSRAVLC RGKQPVPLSV DHKPNREDEY ARIEAEGGKV IQWNGYRVFG
     VLAMSRSIGD RYLKPWIIPV PEVRIVPRAK DDECLILASD GLWDVMSNEE VCDVARKRIL
     LWHKKNGTSS SSALRPGDAA DPAAQAAAEC LSKLALQKGS KDNITVVVVD LKAHRKFKIK
     T
//
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