ID F9X977_ZYMTI Unreviewed; 342 AA.
AC F9X977;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Protein phosphatase {ECO:0000256|RuleBase:RU366020};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU366020};
DE Flags: Fragment;
GN ORFNames=MYCGRDRAFT_25073 {ECO:0000313|EMBL:EGP88137.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP88137.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP88137.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
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; CM001199; EGP88137.1; -; Genomic_DNA.
DR RefSeq; XP_003853161.1; XM_003853113.1.
DR AlphaFoldDB; F9X977; -.
DR STRING; 336722.F9X977; -.
DR EnsemblFungi; Mycgr3T25073; Mycgr3P25073; Mycgr3G25073.
DR GeneID; 13399738; -.
DR KEGG; ztr:MYCGRDRAFT_25073; -.
DR eggNOG; KOG1379; Eukaryota.
DR HOGENOM; CLU_029404_1_0_1; -.
DR InParanoid; F9X977; -.
DR OMA; FKTEGQW; -.
DR OrthoDB; 2101140at2759; -.
DR Proteomes; UP000008062; Chromosome 4.
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:SF24; PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR12320; PROTEIN PHOSPHATASE 2C; 1.
DR Pfam; PF13672; PP2C_2; 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:UP000008062}.
FT DOMAIN 64..340
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGP88137.1"
FT NON_TER 342
FT /evidence="ECO:0000313|EMBL:EGP88137.1"
SQ SEQUENCE 342 AA; 37376 MW; 6CF5C344D43453FE CRC64;
QHRSRDPQTG LKTPVPDGSA DKKSASPFYF AAGYAGWAKR PSRPFPPPFF SPPSGSFSDP
LSTTHRSMDR RPKVDGQMIR GVTNGDDAML VSETLIATND GVGAWATRER GCAPLWSRLI
AHFMALSAEK ALYAGGEDGE PEPVKWLEEA YEHTKAALSE PNEWHGTTTT SAALLHWKDD
KPLVYVTQLG DCKVLVVRPQ ESGEGEVLFS SVEQYHYFDC PRQLGTNSPD TPEGNAVLDK
VDVEEDDVVL ALSDGVTDNL WEEEISDYAA GALKTIKEKH GHDFDLQQAM KYVAQEIVLA
ARKIAEDPFA ASPFMEKAVE EGLAIEGGKP DDISVVAAIC KR
//
