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Database: UniProt
Entry: J7R1W1_KAZNA
LinkDB: J7R1W1_KAZNA
Original site: J7R1W1_KAZNA 
ID   J7R1W1_KAZNA            Unreviewed;       710 AA.
AC   J7R1W1;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   31-JUL-2019, entry version 38.
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   Name=KNAG0B03580 {ECO:0000313|EMBL:CCK68800.1};
GN   OrderedLocusNames=KNAG_0B03580 {ECO:0000313|EMBL:CCK68800.1};
OS   Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 /
OS   CCRC 22969 / KCTC 17520 / NBRC 10181 / NCYC 3082) (Yeast)
OS   (Saccharomyces naganishii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1071383 {ECO:0000313|EMBL:CCK68800.1, ECO:0000313|Proteomes:UP000006310};
RN   [1] {ECO:0000313|EMBL:CCK68800.1, ECO:0000313|Proteomes:UP000006310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC   / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S.,
RA   Byrne K.P., Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type
RT   switching accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN   [2] {ECO:0000313|Proteomes:UP000006310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC   / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S.,
RA   Byrne K.P., Wolfe K.H.;
RT   "Genome sequence of Kazachstania naganishii.";
RL   Submitted (AUG-2012) 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,
CC         ChEBI:CHEBI:43474, 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-
CC         [protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
CC         COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
CC         EC=3.1.3.16; Evidence={ECO:0000256|PIRNR:PIRNR000909,
CC         ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01116780};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000909};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-Z subfamily.
CC       {ECO:0000256|PIRNR:PIRNR000909}.
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DR   EMBL; HE978315; CCK68800.1; -; Genomic_DNA.
DR   STRING; 588726.J7R1W1; -.
DR   EnsemblFungi; CCK68800; CCK68800; KNAG_0B03580.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000006310; Chromosome 2.
DR   GO; GO:0048037; F:cofactor binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004724; F:magnesium-dependent protein serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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   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   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006310};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000909,
KW   ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01017252};
KW   Manganese {ECO:0000256|PIRNR:PIRNR000909,
KW   ECO:0000256|SAAS:SAAS01017251};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000909,
KW   ECO:0000256|SAAS:SAAS01017255};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR000909,
KW   ECO:0000256|SAAS:SAAS01017274};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006310}.
FT   DOMAIN      506    511       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION        1    125       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      168    215       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      244    274       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      312    336       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     30     53       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     67     82       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     91    111       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    172    189       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    312    330       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   710 AA;  77851 MW;  8B715375E1A215EF CRC64;
     MGNSSSKGVS GKHNSHSAPK LKRPVPHRQP SKKSSSTLRS DPEPNSTAVV SEQEPSMVPH
     APATTPAPAA TVSSPFTNIP SHRRAHSQHD LTTSHNTLPV INVTPSGADN PKSVDDSGHH
     NHNHNHIGQA GMGRVAMNRR SSFNTTVDLP PSMIQMAPKQ PILKKQYSFG LPGKTSRGSL
     HSNAEDANGA GQNDAHHHHH HHHSHTGSAG SSGNHLHRLD RRQVKSSDNL TSDLSQDSGL
     IARPSLSNFR SNSHNSSLYS RKSSLTSNST TAFTTPVNTP GAHYSGGKSL GAAFEENGDY
     FGPIHHSAFN SSAGGTPTIT STSMPTTKAH TDSGEGHRLA DLNKDHYPMQ IPGEVETVID
     TIVPPMEEPI NIQGTTSDAQ LSKVKKPMKP IDIDATIQKL LDAGYAAKRT KSVCLKNSEI
     LQICQMTREI FLSQPSLLEL SPPVKIAGDI HGQYGDLLRL FTKCGFPPSS NYLFLGDYVD
     RGKQSLETIL LLFCYKIKYP ENFFLLRGNH ECANVTRVYG FYDECKRRCN IKIWKAFIDT
     FNTMALAAIV AGKIFCVHGG LSPVLNSMDE IRHVSRPTDV PDFGLINDLL WSDPTDSPNE
     WEDNERGVSY CYNKVAINKF LNKFGFDLVC RAHMVVEDGY EFFNDRSLVT VFSAPNYCGE
     FDNWGAVMTV SDGLLCSFEL LDPLDSAALK QVMKKGRKER KLASEQQLLN
//
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