ID A0A0V1LL81_9BILA Unreviewed; 722 AA.
AC A0A0V1LL81;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=phosphatidylinositol-3-phosphatase {ECO:0000256|ARBA:ARBA00013038};
DE EC=3.1.3.64 {ECO:0000256|ARBA:ARBA00013038};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000256|ARBA:ARBA00031219};
DE Flags: Fragment;
GN Name=Mtmr6 {ECO:0000313|EMBL:KRZ60264.1};
GN ORFNames=T02_676 {ECO:0000313|EMBL:KRZ60264.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ60264.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ60264.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ60264.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64;
CC Evidence={ECO:0000256|ARBA:ARBA00001291};
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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:KRZ60264.1}.
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DR EMBL; JYDW01000031; KRZ60264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1LL81; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14532; PTP-MTMR6-like; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF8; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR Pfam; PF21098; PH-GRAM_MTMR6-like; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054721}.
FT DOMAIN 147..522
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT ACT_SITE 359
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 296..297
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 359..365
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT NON_TER 722
FT /evidence="ECO:0000313|EMBL:KRZ60264.1"
SQ SEQUENCE 722 AA; 83179 MW; ABA95B6B2E8AB1F4 CRC64;
LRFQNMRPSD IIKIPKCVMG ADNSAFSDIA YIKVENVEWC DCQPNMSQRG TLYITNTHMI
FASEDGKELW ISHCQISSLQ RAQPVDSGWP LIISGKIFFA LTMIIPKERD CQDIYDSLLA
LSRPTCIDDL PAFCFVPEMK DLMQSEGWNE INMYDDYARL GLPNDNWTIS DLNKNFEYCD
GYPERIFVPK NVPTPVLIGS SKFRSRGRLP VLSYLHRTNQ ACICRCSQPL AGFSARCIED
ESLMRHIAKT NPHSKTLYIV DTRPKINAIV NKAAGKGFED ERNYSHVRYH FFAVENIHAV
RGSLQKMLEV VWNKKNVSVS NFLTGLVNSG WLKHIRSLLE TAVFVSETVI SGTSVVIHCS
DGWDRTPQIV SLSCILLDPF YRTIKGFETL IEKEWLQFGH KFSDRYGHIY TSDSKELAPV
FTQFLEAVWQ LTVQYPLEFE FNEFFLLTLH DHLHSCNFGT FLYNSTKDRI QSKVSSRTYS
LWGYMSRLEE SLRNPLYDPS DIKDILKPDL RPQQINYWRA MYNRYDFKCD SNEYLLDALI
SSRQQILSLK YHIQYLQDQL NQQREASFQQ CCLKFSNLLP KNSSSTDDNN CAVNGTLVAE
HCEIHKMSIS ANSDENDEEK NLETFSHPLS AAFSCENKAD NEMNVSLIDQ RCAIALDWAS
LRRSVRCSNR TCNAKFWPLE RRVVSLLELW TGILCEMLQL ENSTPGAWKL RSNGTSLCEM
HN
//
