ID E3LW52_CAERE Unreviewed; 404 AA.
AC E3LW52;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=CRE_03017 {ECO:0000313|EMBL:EFO83465.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) 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 -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
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DR EMBL; DS268417; EFO83465.1; -; Genomic_DNA.
DR RefSeq; XP_003111604.1; XM_003111556.1.
DR AlphaFoldDB; E3LW52; -.
DR STRING; 31234.E3LW52; -.
DR EnsemblMetazoa; CRE03017.1; CRE03017.1; WBGene00078032.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; E3LW52; -.
DR OMA; LSKNNKC; -.
DR OrthoDB; 2881726at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd00144; MPP_PPP_family; 1.
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 PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR11668:SF491; SERINE_THREONINE-PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00149; Metallophos; 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 Hydrolase {ECO:0000256|RuleBase:RU004273};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT DOMAIN 165..170
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 361..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 404 AA; 45565 MW; 9EB8444E072FA155 CRC64;
MVKEQRTDTA KFIHRHMNVK KWLNYREVRE KVTANNFNNH FQQSYTKQEL INLALDARDV
FKQNREDKKD INSKVLALAT ISPPVLVVGD IHGQYADLMR ILNTCPNKPA EKKDERPAPN
NKRAGFFNNR FVFLGDYVDR GSHSVECISL MFALKVHYPS QYVLLRGNHE TRAINFAYGF
REELQIKLGE ADGQEVWEAF NETFAWMPLA CLIGRKILCM HGGISQGMTL DLIRKIPLPL
EDVGTNVLAQ DLLWADPTPD QTIASALQTP QWGKNLVRGL SCTFNPAAVT ETVGRLDLKL
IIRAHQMIPD GFKFAANHQL LTIFSAPRYM NETDNRGAIV RIQENGDFGI IVLKNTKGAG
GKNPLNDELT RADDVPNESA KKKSDSAVNV MKLSSSKTKN SPKF
//
