ID J7R1W1_KAZNA Unreviewed; 710 AA.
AC J7R1W1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 / KCTC
OS 17520 / NBRC 10181 / NCYC 3082 / Yp74L-3) (Yeast) (Saccharomyces
OS naganishii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC 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., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT 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., Byrne K.P.,
RA 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, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={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|PIRNR:PIRNR000909,
CC 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; HE978315; CCK68800.1; -; Genomic_DNA.
DR AlphaFoldDB; J7R1W1; -.
DR STRING; 1071383.J7R1W1; -.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_3_0_1; -.
DR OrthoDB; 19833at2759; -.
DR Proteomes; UP000006310; Chromosome 2.
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 CDD; cd07414; MPP_PP1_PPKL; 1.
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:SF484; SERINE_THREONINE-PROTEIN PHOSPHATASE PP-Z1-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:UP000006310}.
FT DOMAIN 506..511
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..330
FT /note="Polar residues"
FT /evidence="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
//
