ID A0A1E4SDY6_9ASCO Unreviewed; 359 AA.
AC A0A1E4SDY6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Protein phosphatase {ECO:0000256|RuleBase:RU366020};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU366020};
GN ORFNames=CANTADRAFT_91161 {ECO:0000313|EMBL:ODV77693.1};
OS Suhomyces tanzawaensis NRRL Y-17324.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Suhomyces.
OX NCBI_TaxID=984487 {ECO:0000313|EMBL:ODV77693.1, ECO:0000313|Proteomes:UP000094285};
RN [1] {ECO:0000313|Proteomes:UP000094285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17324 {ECO:0000313|Proteomes:UP000094285};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-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}.
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DR EMBL; KV453914; ODV77693.1; -; Genomic_DNA.
DR RefSeq; XP_020062815.1; XM_020211782.1.
DR AlphaFoldDB; A0A1E4SDY6; -.
DR STRING; 984487.A0A1E4SDY6; -.
DR GeneID; 30985918; -.
DR OrthoDB; 240602at2759; -.
DR Proteomes; UP000094285; 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 CDD; cd00143; PP2Cc; 1.
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; PF07228; SpoIIE; 1.
DR SMART; SM00331; PP2C_SIG; 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:UP000094285};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..359
FT /note="Protein phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009162736"
FT DOMAIN 96..358
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 359 AA; 39129 MW; 6983464055FBFE2F CRC64;
MKVTRVIALV ILSMLLSFVS KRSVQAVRQG SSKRMFSWRG GSAGFGAGST GRSSSTIASA
AATAAALSTN YEDLTVLSQY TIAVAYQPKD REESNLFKKK HNQPLPALES PTGEDNAFVA
VHQDGSVAVG VADGVGGWAD AGYDSSAISR ELCATIKHQF SHDSQAQPKQ LLETSFQAIL
ESPKVEIGGT TACLGVISNR KLKVANLGDS WCGVFRNYQL VNETAFQTHK FNTPYQLAKI
PAHILRQAEL EGRRYIRDTP AQADVYEWDL QKDDVVLFAT DGVTDNVVPK DIEIFLRDQL
EDKKSDLGDV AKLFVKEVVK VSKDSNFPSA FAQELSTLTG QKYLGGKEDD ITVVMVRIN
//
