ID A0A067NZ82_PLEOS Unreviewed; 204 AA.
AC A0A067NZ82;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=PLEOSDRAFT_1063653 {ECO:0000313|EMBL:KDQ28926.1};
OS Pleurotus ostreatus PC15.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ28926.1, ECO:0000313|Proteomes:UP000027073};
RN [1] {ECO:0000313|Proteomes:UP000027073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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|ARBA:ARBA00001512};
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|ARBA:ARBA00001482};
CC -!- SIMILARITY: Belongs to the dullard family.
CC {ECO:0000256|ARBA:ARBA00038346}.
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DR EMBL; KL198007; KDQ28926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067NZ82; -.
DR STRING; 1137138.A0A067NZ82; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1063653; -.
DR HOGENOM; CLU_020262_4_5_1; -.
DR InParanoid; A0A067NZ82; -.
DR OrthoDB; 5473812at2759; -.
DR Proteomes; UP000027073; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR PANTHER; PTHR12210:SF70; CTD NUCLEAR ENVELOPE PHOSPHATASE 1; 1.
DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000027073}.
FT DOMAIN 7..182
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
SQ SEQUENCE 204 AA; 22784 MW; 582919AB9ED71AD8 CRC64;
MLTRKPQRVP RKTLVLDLDE TLIHSTSRPM PMSGSSGFFG FGRRNNGPGH TVEVILGGKR
TVYHVYKRPF ADFFLRTVSS WYTLVIFTAS MQEYADPVID WLDAGRGILG RRLFRDSCTQ
LPSGTYTKDL AVVEQDLSNV CLIDNSPISY RINEANGIPI EGWTNDPADE ALLDLLPVLD
SLRFTNDVRR VLSLRTAGGV SFAS
//
