ID   A0A0L6VEP7_9BASI        Unreviewed;       439 AA.
AC   A0A0L6VEP7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=VP01_1901g3 {ECO:0000313|EMBL:KNZ58580.1};
OS   Puccinia sorghi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ58580.1, ECO:0000313|Proteomes:UP000037035};
RN   [1] {ECO:0000313|EMBL:KNZ58580.1, ECO:0000313|Proteomes:UP000037035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ58580.1,
RC   ECO:0000313|Proteomes:UP000037035};
RA   Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA   Sacco F.;
RT   "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT   Schw, the Causal Agent of Maize Common Rust.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:RU004273};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-Z subfamily.
CC       {ECO:0000256|ARBA:ARBA00029458}.
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:KNZ58580.1}.
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DR   EMBL; LAVV01006728; KNZ58580.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6VEP7; -.
DR   STRING; 27349.A0A0L6VEP7; -.
DR   VEuPathDB; FungiDB:VP01_1901g3; -.
DR   OrthoDB; 19833at2759; -.
DR   Proteomes; UP000037035; Unassembled WGS sequence.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07414; MPP_PP1_PPKL; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR011159; PPPtase_PPZ/Ppq1.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF484; SERINE_THREONINE-PROTEIN PHOSPHATASE PP-Z1-RELATED; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PIRSF; PIRSF000909; PPPtase_PPZ; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU004273};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037035}.
FT   DOMAIN          240..245
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          1..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  49238 MW;  6810422CA12125FA CRC64;
     MGNNPSKKLR TRLREREPSI SAEESAEQNN NLNNHNHNQT DEQQPTPSSS SNYQQSIVQQ
     SSNSNESPNQ IQQPNSSNLK NNIEQPSDNT PTILSNPAAN PSNNLAKINH QQPQANGFSS
     TNPSFDIDEI INRLLDVGYS TKVTKSVCLK NSEITAISLA AREVLLSQPT LIELSPPVKI
     VGDVHGQYSD LIRLFEMCGF PPMANYLFLG DYVDRGKQSL ETILLLLCYK IKYPENFFLL
     RGNHECANVT RVYGFYDECK RRCNIKIWKT FIDVFNCLPI SAVVASKIFC VHGGLSPSLS
     AMDDIRRIQR PTDVPDFGLL NDLLWSDPSD TATDWEDNER GVSYCFGKSV IAEFLARYDF
     DLICRAHMVV EDGYEFWNER TLVTIFSAPN YCGEFDNFGA VMSVSEDLLC AFELLKPLDG
     AALKKEMQKK KRTSSVSGG
//