YT91_CAEEL
ID YT91_CAEEL Reviewed; 364 AA.
AC P48458;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Putative serine/threonine-protein phosphatase C06A1.3;
DE EC=3.1.3.16;
GN ORFNames=C06A1.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z49886; CAA90052.1; -; Genomic_DNA.
DR PIR; T18972; T18972.
DR RefSeq; NP_496276.1; NM_063875.3.
DR AlphaFoldDB; P48458; -.
DR SMR; P48458; -.
DR BioGRID; 39942; 1.
DR STRING; 6239.C06A1.3; -.
DR EPD; P48458; -.
DR PaxDb; P48458; -.
DR PeptideAtlas; P48458; -.
DR EnsemblMetazoa; C06A1.3.1; C06A1.3.1; WBGene00007354.
DR GeneID; 174626; -.
DR KEGG; cel:CELE_C06A1.3; -.
DR UCSC; C06A1.3; c. elegans.
DR CTD; 174626; -.
DR WormBase; C06A1.3; CE02116; WBGene00007354; -.
DR eggNOG; KOG0374; Eukaryota.
DR GeneTree; ENSGT00970000196438; -.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; P48458; -.
DR OMA; NIFMEES; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; P48458; -.
DR PRO; PR:P48458; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00007354; Expressed in adult organism and 1 other tissue.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
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 Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..364
FT /note="Putative serine/threonine-protein phosphatase
FT C06A1.3"
FT /id="PRO_0000058915"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 364 AA; 41208 MW; 1384EAB0C9729913 CRC64;
MSTDGNNNKK GSKEGPKSSE ISKFDLAKEN PKLAEWMDDC IKRMNSLYKD TNINICNVMT
GHEIISIIRM VEAIFMEESN LCEAEAPIKV IGDIHAQYQD MNRLFDLIGR VPEEKLMFLG
DYVDRGPQGI EVLILLFCLK IRYRDRIYLL RGNHETPSVN KIYGFYVECQ YKYGIGLWWD
FQSCFNRMPM SGLISKRVLC MHGGLSPELI NLDTIRNIPR PCEPLDRGLL IDLLWSDPTN
KGEGWFHSIR GISYMFGKGV VEQACKSLEI DLIIRAHQVV QDGYEMMTGR RLITVFSVPN
YCAQFTNAAA VVCLNANLQI SFQQMIPPPL PEGTKAKAAP AIAIDPNIDA ARADKDAIKP
FVKE
