ID F7W9C0_SORMK Unreviewed; 531 AA.
AC F7W9C0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273};
GN ORFNames=SMAC_08068 {ECO:0000313|EMBL:CCC05200.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC05200.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC05200.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC05200.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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|PIRNR:PIRNR000909};
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|PIRNR:PIRNR000909,
CC ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936,
CC ECO:0000256|PIRNR:PIRNR000909};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000909}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-Z subfamily.
CC {ECO:0000256|ARBA:ARBA00029458, ECO:0000256|PIRNR:PIRNR000909}.
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:CCC05200.1}.
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DR EMBL; CABT02000050; CCC05200.1; -; Genomic_DNA.
DR RefSeq; XP_003347500.1; XM_003347452.1.
DR AlphaFoldDB; F7W9C0; -.
DR STRING; 771870.F7W9C0; -.
DR GeneID; 10804910; -.
DR KEGG; smp:SMAC_08068; -.
DR VEuPathDB; FungiDB:SMAC_08068; -.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_3_2_1; -.
DR InParanoid; F7W9C0; -.
DR OMA; AEIMAIC; -.
DR OrthoDB; 19833at2759; -.
DR Proteomes; UP000001881; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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; 2.
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 Cytoplasm {ECO:0000256|PIRNR:PIRNR000909};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273};
KW Manganese {ECO:0000256|PIRNR:PIRNR000909};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000909};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|PIRNR:PIRNR000909};
KW Reference proteome {ECO:0000313|Proteomes:UP000001881}.
FT DOMAIN 321..326
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 58253 MW; 65B9622C3B183316 CRC64;
MGNSSSKDAG ASSKNRGDDD LKSYPSFSKS DTKDSSRSFR GLRSKIPGGG KTDSPRNSTI
LSSEEIAEKT NALNGKNGKP SVNTRPSRRD MSPSPVSPSP SSPSSPSLDA ATLASPTGEP
QPPPSPVHGA TTGRHDVRAA QESGEVDHIS DQPPSGGGGA NPNQQPGQSI LVKRENTINP
VYDTPTQDPQ NEQSVSGVAM SDIKDIDLDD FIKRLLDAAY AGKVTKSVCL KNAEIVAICH
RARELFLSQP ALLELDAPVK IVGDVHGQYT DLIRMFEMCG FPPHSNYLFL GDYVDRGKQS
LETILLLMCY KLKYPENFFL LRGNHECANV TRVYGFYDEC KRRCNVKIWK TFVDTFNCLP
IAAIVAGKIF CVHGGLSPAL GHMDDIRNIA RPTDVPDYGL LNDLLWSDPA DMDQDWEANE
RGVSYCFGKK VISDFLATHD FDLVCRAHMV VEDGYEFYTD RVLVTIFSAP NYCGEFDNWG
AVMAVSTELL CSFELLKPLD SAALKTHIKK GRHRRNNMLN SPPAHFNPQS V
//
