GenomeNet

Database: UniProt
Entry: A0A367YNE1_9ASCO
LinkDB: A0A367YNE1_9ASCO
Original site: A0A367YNE1_9ASCO 
ID   A0A367YNE1_9ASCO        Unreviewed;       527 AA.
AC   A0A367YNE1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   Name=PPT1_0 {ECO:0000313|EMBL:RCK67354.1};
GN   ORFNames=Cantr_02297 {ECO:0000313|EMBL:RCK67354.1};
OS   Candida viswanathii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK67354.1, ECO:0000313|Proteomes:UP000253472};
RN   [1] {ECO:0000313|EMBL:RCK67354.1, ECO:0000313|Proteomes:UP000253472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK67354.1,
RC   ECO:0000313|Proteomes:UP000253472};
RA   Ahn J.;
RT   "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT   Korea University).";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-5 (PP-T)
CC       subfamily. {ECO:0000256|ARBA:ARBA00008786}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RCK67354.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QLNQ01000001; RCK67354.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367YNE1; -.
DR   STRING; 5486.A0A367YNE1; -.
DR   Proteomes; UP000253472; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR013235; PPP_dom.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR   PANTHER; PTHR45668:SF5; SERINE_THREONINE-PROTEIN PHOSPHATASE 5; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF08321; PPP5; 1.
DR   Pfam; PF13432; TPR_16; 1.
DR   PIRSF; PIRSF033096; PPPtase_5; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253472};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   REPEAT          6..39
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          305..310
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
SQ   SEQUENCE   527 AA;  59787 MW;  A7A11F28E7FADD50 CRC64;
     MTKEEAIKLK DQGNAYLKDH KYDQAIESYT QAIALDPQNA IFYSNRAQVH IKLENYGLAI
     QDCDAAIAID PGFLKAYYRK GVSLMAILQY KQAQLNFKLI LNKLPGDKLT VENYKQCTNY
     LKRQAFEKAI AGTDHTLVIN SVDYQSIQIE KSWEGPELKI TPRKSKDGEI TVEIDGLDEG
     YLKYMIKLFK DGGKLPKKHV FAIITKVYEL LKKEKTMTEI TLEHSQISDK LNDDEIIGGK
     KLTVVGDTHG QFYDLLNLFT KFGHVSKDHV FLFNGDFVDR GSWSCEVALY LYVLKILYPT
     SIFINRGNHE TSDMNKTYGF TDECEYKYSK KIFEAFTESF GALPLASLIN REYLCMHGGL
     FSNDKVTLAD IKSINRFPTN GSTQPPKEGL AMELLWTDPQ EVNGRSPSKR GIGMQFGPDV
     TERFCLNNKI RKILRSHEVR MGGVEEEQKG RLITVFSAPN YCDSTGNLGG IVNFEENKNY
     DKEKDNGEGY RDVNDSNTPW ALTTETFEAV PHPDMKPMAY SKGGFGF
//
DBGET integrated database retrieval system