ID A0A183EUC6_9BILA Unreviewed; 183 AA.
AC A0A183EUC6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=GPUH_LOCUS24565 {ECO:0000313|EMBL:VDN43009.1};
OS Gongylonema pulchrum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Spiruroidea; Gongylonematidae; Gongylonema.
OX NCBI_TaxID=637853 {ECO:0000313|Proteomes:UP000050760, ECO:0000313|WBParaSite:GPUH_0002459701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:GPUH_0002459701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN43009.1, ECO:0000313|Proteomes:UP000271098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-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|ARBA:ARBA00001482};
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DR EMBL; UYRT01101587; VDN43009.1; -; Genomic_DNA.
DR WBParaSite; GPUH_0002459701-mRNA-1; GPUH_0002459701-mRNA-1; GPUH_0002459701.
DR Proteomes; UP000050760; Unplaced.
DR Proteomes; UP000271098; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR043587; Phosphatase_SSH-like.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR PANTHER; PTHR45864:SF2; PROTEIN PHOSPHATASE SLINGSHOT; 1.
DR PANTHER; PTHR45864; SLINGSHOT PROTEIN PHOSPHATASE HOMOLOG; 1.
DR Pfam; PF08766; DEK_C; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR PROSITE; PS51998; DEK_C; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000271098}.
FT DOMAIN 1..42
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 144..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 183 AA; 21073 MW; 7AC47A221B833051 CRC64;
MQTVDLDEVT SRDIRLKVEE SLGMNLDEYK DFISRQVMVI MGQMDTASQI FPYLYLGTEW
NACDWQWLEN NNLVLGYFLN ISIAICSVKY IVNVTNEEYG WALSEAMEHV KNKRDCITPN
LGFVEQLRTF EGMLHAFKKR DQFDVSPSTS STESSDSLRS RNKDEKSTAC ADDAVLLRNP
FKI
//
