ID C5MHE5_CANTT Unreviewed; 550 AA.
AC C5MHE5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=CTRG_05499 {ECO:0000313|EMBL:EER31047.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER31047.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER31047.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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 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|ARBA:ARBA00001482,
CC ECO:0000256|PIRNR:PIRNR000909, 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}.
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DR EMBL; GG692402; EER31047.1; -; Genomic_DNA.
DR RefSeq; XP_002551201.1; XM_002551155.1.
DR AlphaFoldDB; C5MHE5; -.
DR STRING; 294747.C5MHE5; -.
DR EnsemblFungi; CTRG_05499-t43_1; CTRG_05499-t43_1-p1; CTRG_05499.
DR GeneID; 8300557; -.
DR KEGG; ctp:CTRG_05499; -.
DR VEuPathDB; FungiDB:CTRG_05499; -.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_4_0_1; -.
DR OrthoDB; 19833at2759; -.
DR Proteomes; UP000002037; 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 GO; GO:0090029; P:negative regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion; IEA:EnsemblFungi.
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:SF300; SERINE_THREONINE-PROTEIN PHOSPHATASE-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PIRSF; PIRSF000909; PPPtase_PPZ; 1.
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:UP000002037}.
FT DOMAIN 366..371
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 61278 MW; F4276C3750FA1ED3 CRC64;
MGNSPSKNDP LPKSSSSNKS SNGTASSSTT ASGTDLDPDE MAPALSQLII NSHLTTNSTV
DTDSSNNNNN RQTRNTNNGL KQETSMLSTS MITTTATAPQ RIPSTKRKSY ASQESYDFDL
EIGMSMAKLL KNQESTSSGS SKASPVFTTI SNDEDSSFSS TNSSPRDPKS NKQYIDNVAP
LNKLDVIAEI HSLESSPTPK TTTSKLSKKN LKKHDKSVAK QLTKKNPSST SSLLDSPPLV
GTTHKLDIDI DAVIERLLAT KKKSTSRKSK SHLPVETSEI KYILSKSRSI FLEQPTLLKL
SPPVKIVGDI HGQFHDLIRI FNCCGYPPHS NYLFLGDYVD RGEKSLETIL LLLCYKIKYP
ENFFMLRGNH ESANITKIYG FYDECKRRLG NNKLWRSFID VFNTLPIAAV INEKIFCVHG
GLSPQLENFR QIEDIKRPTD VPDKGLLADL LWSDPDASVK NFSLTNWPKN DRGVSYCFGK
KHVDYFCSKF KLDLIVRGHM VVEDGYEFFN KRKLVTVFSA PNYCGEFNNF GAIMSVDKTL
YCSFELIKPN
//
