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
//