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Database: UniProt
Entry: F2Q0J3_TRIEC
LinkDB: F2Q0J3_TRIEC
Original site: F2Q0J3_TRIEC 
ID   F2Q0J3_TRIEC            Unreviewed;       399 AA.
AC   F2Q0J3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=TEQG_06645 {ECO:0000313|EMBL:EGE07661.1};
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN   [1] {ECO:0000313|Proteomes:UP000009169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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         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-6 (PP-V)
CC       subfamily. {ECO:0000256|ARBA:ARBA00038400}.
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DR   EMBL; DS995763; EGE07661.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2Q0J3; -.
DR   VEuPathDB; FungiDB:TEQG_06645; -.
DR   eggNOG; KOG0373; Eukaryota.
DR   HOGENOM; CLU_004962_8_3_1; -.
DR   Proteomes; UP000009169; 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   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR047129; PPA2-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45619:SF10; SERINE/THREONINE-PROTEIN PHOSPHATASE 6 CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF033096; PPPtase_5; 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   Hydrolase {ECO:0000256|RuleBase:RU004273}.
FT   DOMAIN          199..204
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   399 AA;  44519 MW;  FDA443BBD709AF1F CRC64;
     MVDPSVPQPG PARLKPNAGP DEWLEAAKNC KYLSEHHMKQ LCELVKEYMM EESNIQPVST
     PVTICGDIHG QFYDLLELFR VAGGMPGDTR PAAPSTQAPI ITSEDIEPPS TITDPKLKRR
     LRKSSPPNSV IEDDGDEETG EQATESNADN EVGEEDKSAS PIGNFIFLGD YVDRGYFSLE
     TLTLLLCLKA RYPNKITLVR GNHESRQITQ VYGFYDECVQ KYGNASVWKA CCQVFDFMTL
     GVIVDGKVLC LHGGLSPEIR TLDQVRIVAR AQEIPHEGAF CDLVWSDPDE TEDLTWAVSP
     RGAGWLFGSR VADEFCAVND LNLIARAHQL VNEGYKYHFD SQAMVTVWSA PNYCYRCANM
     ASVCEVREDL KPVFKLFAAV PAEMRHVPAS RPQKAEYFL
//
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