UniProt: K3WGW7

Database: UniProt
Entry: K3WGW7_GLOUD

LinkDB:  K3WGW7_GLOUD 
Original site:  K3WGW7_GLOUD

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (3)   
   Pfam (1)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (12)   

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ID   K3WGW7_GLOUD            Unreviewed;       325 AA.
AC   K3WGW7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Protein phosphatase {ECO:0000256|RuleBase:RU366020};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU366020};
OS   Globisporangium ultimum (strain ATCC 200006 / CBS 805.95 / DAOM BR144)
OS   (Pythium ultimum).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Pythiales; Pythiaceae;
OC   Globisporangium.
OX   NCBI_TaxID=431595 {ECO:0000313|EnsemblProtists:PYU1_T004208, ECO:0000313|Proteomes:UP000019132};
RN   [1] {ECO:0000313|Proteomes:UP000019132}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DAOM:BR144 {ECO:0000313|Proteomes:UP000019132};
RX   PubMed=20626842; DOI=10.1186/gb-2010-11-7-r73;
RA   Levesque C.A., Brouwer H., Cano L., Hamilton J.P., Holt C., Huitema E.,
RA   Raffaele S., Robideau G.P., Thines M., Win J., Zerillo M.M., Beakes G.W.,
RA   Boore J.L., Busam D., Dumas B., Ferriera S., Fuerstenberg S.I.,
RA   Gachon C.M., Gaulin E., Govers F., Grenville-Briggs L., Horner N.,
RA   Hostetler J., Jiang R.H., Johnson J., Krajaejun T., Lin H., Meijer H.J.,
RA   Moore B., Morris P., Phuntmart V., Puiu D., Shetty J., Stajich J.E.,
RA   Tripathy S., Wawra S., van West P., Whitty B.R., Coutinho P.M.,
RA   Henrissat B., Martin F., Thomas P.D., Tyler B.M., De Vries R.P., Kamoun S.,
RA   Yandell M., Tisserat N., Buell C.R.;
RT   "Genome sequence of the necrotrophic plant pathogen Pythium ultimum reveals
RT   original pathogenicity mechanisms and effector repertoire.";
RL   Genome Biol. 11:R73-R73(2010).
RN   [2] {ECO:0000313|Proteomes:UP000019132}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM:BR144 {ECO:0000313|Proteomes:UP000019132};
RA   Buell R., Hamilton J., Hostetler J.;
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblProtists:PYU1_T004208}
RP   IDENTIFICATION.
RC   STRAIN=DAOM BR144 {ECO:0000313|EnsemblProtists:PYU1_T004208};
RG   EnsemblProtists;
RL   Submitted (FEB-2015) to UniProtKB.
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; GL376567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; K3WGW7; -.
DR   STRING; 431595.K3WGW7; -.
DR   EnsemblFungi; PYU1_T004208; PYU1_T004208-p1; PYU1_G004198.
DR   EnsemblProtists; PYU1_T004208; PYU1_T004208; PYU1_G004198.
DR   VEuPathDB; FungiDB:PYU1_G004198; -.
DR   eggNOG; ENOG502R82Q; Eukaryota.
DR   HOGENOM; CLU_049556_0_0_1; -.
DR   InParanoid; K3WGW7; -.
DR   OMA; GFGPSYM; -.
DR   Proteomes; UP000019132; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000019132}.
FT   DOMAIN          21..324
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   325 AA;  35487 MW;  3A979B0808E8263E CRC64;
     MRSCKHDDSV SSGSHNGHGA SSCFASVASA AHSYHGDDAV GYGPGYMVIA DGVSGTMKAS
     GVLARLLVSE TLAALAKLKK RTREEPIKSA EFSLAVQDAT KAARRATKRK GRLDSTLSVV
     YFDDVGHQMF VYTIGDCKCV LLRNNKIVFE SDSIIYDFNV PAVVSNNKTI NYNGDVNIQT
     CAYEAGDVCM IFSDGVHDNL YVDQVVACVE PCPENAEEIA KKTVQMAKLT FTECDTYIPF
     AVSAAGFCRD AMEELKTSNS VNPEEFETFR QKCENIPAFE ITRPMFAKEN RVRQLAFYSA
     SNLLAFAHKR QGKRDDVSVC AAVLA
//

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