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Database: UniProt
Entry: S6E5Q8_ZYGB2
LinkDB: S6E5Q8_ZYGB2
Original site: S6E5Q8_ZYGB2 
ID   S6E5Q8_ZYGB2            Unreviewed;       473 AA.
AC   S6E5Q8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   11-DEC-2019, entry version 31.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=BN860_07690g {ECO:0000313|EMBL:CDF89036.1};
OS   Zygosaccharomyces bailii (strain CLIB 213 / ATCC 58445 / CBS 680 / CCRC
OS   21525 / NBRC 1098 / NCYC 1416 / NRRL Y-2227).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=1333698 {ECO:0000313|EMBL:CDF89036.1, ECO:0000313|Proteomes:UP000019375};
RN   [1] {ECO:0000313|Proteomes:UP000019375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 213 / ATCC 58445 / CBS 680 / CCRC 21525 / NBRC 1098 / NCYC
RC   1416 / NRRL Y-2227 {ECO:0000313|Proteomes:UP000019375};
RX   PubMed=23969048; DOI=10.1128/genomeA.00606-13;
RA   Galeote V., Bigey F., Devillers H., Neuveglise C., Dequin S.;
RT   "Genome sequence of the food spoilage yeast Zygosaccharomyces bailii CLIB
RT   213(T).";
RL   Genome Announc. 1:E0060613-E0060613(2013).
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; HG316456; CDF89036.1; -; Genomic_DNA.
DR   EnsemblFungi; BN860_07690g_2-1; CDF89036; BN860_07690g_2.
DR   PhylomeDB; S6E5Q8; -.
DR   Proteomes; UP000019375; Unassembled WGS sequence.
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:UP000019375}.
FT   DOMAIN          277..282
FT                   /note="SER_THR_PHOSPHATASE"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..77
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..142
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   473 AA;  52882 MW;  D9BCA541A7C274E0 CRC64;
     MGNSPSRCNT NFAVPSASNG LLQTSDDNNN EPNEPDDSGP TMSIDIGNSN YNLNCGNRDR
     SRSYSTDSGT TVVGSDRRGS VDKNFLLDVD ISTARAFGTG SYGSSGGSSG SDNTLISSRP
     HKSQYNTPGS SGPSSIPNYR DKSQRVILQR YPHDASNNEG LDVDDAIEKL LKIGETRYYK
     SRDFPFRSWE IQLICCHARE VLLSQPSLLQ LQAPIKVVGD VHGQFTDLLR ILKLSGVPPE
     TNYLFLGDYV DRGKQSLETI LLLLCYKIKY KDNFFMLRGN HESANVTKIY GFYDECKRRT
     SSRVWKMFVD VFNTLPFAAI IQDRIFCVHG GISPHLHSMQ QIAQIARPTD IPEDGLVTDL
     LWSDPDSQVS NWSENNRGVS YTFGKKNVLD FCSQFKFDLV IRGHMVVEDG YEFFAKKKFV
     TVFSAPNYCG EFNNWGAVMS VTTGLMCSFE XXXXXXXXXX XXXXXXXXXX IYI
//
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