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Database: UniProt
Entry: A0A1J9Q7W9_9EURO
LinkDB: A0A1J9Q7W9_9EURO
Original site: A0A1J9Q7W9_9EURO 
ID   A0A1J9Q7W9_9EURO        Unreviewed;       478 AA.
AC   A0A1J9Q7W9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=ACJ73_04083 {ECO:0000313|EMBL:OJD24552.1};
OS   Blastomyces percursus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=1658174 {ECO:0000313|EMBL:OJD24552.1, ECO:0000313|Proteomes:UP000242791};
RN   [1] {ECO:0000313|EMBL:OJD24552.1, ECO:0000313|Proteomes:UP000242791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EI222 {ECO:0000313|EMBL:OJD24552.1,
RC   ECO:0000313|Proteomes:UP000242791};
RA   Cuomo C.A., Schwartz I.S., Kenyon C., De Hoog G.S., Govender N.P.,
RA   Botha A., Moreno L., De Vries M., Munoz J.F., Stielow J.B.;
RT   "Emmonsia species relationships and genome sequence.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:RU004273};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-5 (PP-T)
CC       subfamily. {ECO:0000256|ARBA:ARBA00008786}.
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:OJD24552.1}.
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DR   EMBL; LGTZ01000539; OJD24552.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9Q7W9; -.
DR   STRING; 1658174.A0A1J9Q7W9; -.
DR   VEuPathDB; FungiDB:ACJ73_04083; -.
DR   OrthoDB; 1107740at2759; -.
DR   Proteomes; UP000242791; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07417; MPP_PP5_C; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041753; PP5_C.
DR   InterPro; IPR013235; PPP_dom.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR   PANTHER; PTHR45668:SF5; SERINE_THREONINE-PROTEIN PHOSPHATASE 5; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF08321; PPP5; 1.
DR   PIRSF; PIRSF033096; PPPtase_5; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242791};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803}.
FT   DOMAIN          279..284
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
SQ   SEQUENCE   478 AA;  54488 MW;  80F8FE1F97E47F9F CRC64;
     MASTNKEAAT ALKLQGNKAF ASHDWIQALD FYSKAIEKYD QDPSFFCNRA QVHIKREAYG
     YAVADATKAI ELDPNYVKAY WRRAIANTAI LNSRAALKDF KTVVRKAPND RDAKLKLAEC
     EKLVRRIEFE KAIEVADPPS AFEGLDIDGM IVEESYDGVR LSESMTQEFI DDMIERFKTG
     KKIHKKYAFQ IVRATKDIVY NEPTMVEVRV KEGTRLTVCG DTHGQFFDLL EIFRLNGYPS
     DTHAYLFNGD FVDRGSWSTE VALLLYAYKW LRPHKFFLNR GNHETDDMNR AYGFEGECKA
     KYNERLFKTF SESFSALPLA TLIGDKFLTL HGGLFSDDKV SLDDIRKLNR HNQRQPGQSG
     LMMEMLWTDP QTAPGRGPSK RGVGMQFGPD VTKRFCENNG LEAVIRSHEV RMEGYEVEHD
     GRCITVFSAP RYCDSTENKG AYINIGPELK LEFHKFEAVP HPDIKPMAYA ANSIMSLM
//
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