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Database: UniProt
Entry: A0A1L0DH32_9ASCO
LinkDB: A0A1L0DH32_9ASCO
Original site: A0A1L0DH32_9ASCO 
ID   A0A1L0DH32_9ASCO        Unreviewed;       572 AA.
AC   A0A1L0DH32;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   11-DEC-2019, entry version 13.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=SAMEA4029010_CIC11G00000000352 {ECO:0000313|EMBL:SGZ55248.1};
OS   [Candida] intermedia.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Clavispora; Clavispora/Candida clade.
OX   NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ55248.1, ECO:0000313|Proteomes:UP000182334};
RN   [1] {ECO:0000313|EMBL:SGZ55248.1, ECO:0000313|Proteomes:UP000182334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ55248.1,
RC   ECO:0000313|Proteomes:UP000182334};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|SAAS:SAAS01116782};
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         ECO:0000256|SAAS:SAAS01116780};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01017257}.
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DR   EMBL; LT635760; SGZ55248.1; -; Genomic_DNA.
DR   EnsemblFungi; SGZ55248; SGZ55248; SAMEA4029010_CIC11G00000000352.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000182334; Chromosome v.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01017252};
KW   Manganese {ECO:0000256|SAAS:SAAS01017251};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01017255};
KW   Protein phosphatase {ECO:0000256|SAAS:SAAS01017274};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182334}.
FT   DOMAIN          384..389
FT                   /note="SER_THR_PHOSPHATASE"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..79
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..222
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..246
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   572 AA;  63263 MW;  9924AA385353E0DB CRC64;
     MGNNPSKNDP LPNISSAVSL SSSGVAVADL DSDDASPALS RPTGNGSDIL LEKMSNFKLN
     DPSPYSKASP QSIPSRKPQR TSVPARDYQL DIDIDTSMAA LLSTNSHSPH SPSSPAKLPR
     SASNYVLTSD YVVAEYASSV DSLRSGHLSV SPVFTTSGEH KDESLVLSVS SLANSPIYVK
     SGSGHGNPFQ TPLESSLDPI VEGSVESTPE PKHSRRSSHS KSADLGRTVL SKQSSKSSAR
     SSASISPPLL PVNRKVDFDL DLIIDKLLEI GMKKVSSPYS PLKSRRGKDK LPLTTQELKQ
     ILAKSRSIFM EQPTLLKLSP PVKIVGDIHG QFHDLIRIFN SCGYPPHTNY LFLGDYVDRG
     YKSLETILLL LCYKIKYPEN FFMLRGNHES ANITKIYGFY DECKRRLPLI SGSHKLWKNF
     IDVFNTLPIA ATINDKIFCI HGGLSPELHS LKQIEQIQRP TDIPDKGLLA DLLWSDPDPL
     VRTFSHTNWP KNDRGVSYCF GKKHVDHFLS NFNMDLIVRG HMVVEDGYEF FNKRKLVTVF
     SAPNYCGEFN NYGAIMSVDK KLCCSFELLK PQ
//
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