ID A0A1R2B394_9CILI Unreviewed; 624 AA.
AC A0A1R2B394;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=phosphatidylinositol-3-phosphatase {ECO:0000256|ARBA:ARBA00013038};
DE EC=3.1.3.64 {ECO:0000256|ARBA:ARBA00013038};
GN ORFNames=SteCoe_30635 {ECO:0000313|EMBL:OMJ71217.1};
OS Stentor coeruleus.
OC Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ71217.1, ECO:0000313|Proteomes:UP000187209};
RN [1] {ECO:0000313|EMBL:OMJ71217.1, ECO:0000313|Proteomes:UP000187209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM001 {ECO:0000313|EMBL:OMJ71217.1};
RA Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA Sood P.;
RT "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT introns.";
RL Submitted (NOV-2016) 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:OMJ71217.1}.
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DR EMBL; MPUH01001012; OMJ71217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R2B394; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000187209; 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; cd14507; PTP-MTM-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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000187209}.
FT DOMAIN 183..559
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT COILED 591..618
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 396
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 336..337
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 396..402
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 624 AA; 71705 MW; 58CDD82C9625FC60 CRC64;
MRGNANDSKF VDSDPLRVKI FQPDPVPNEL IPEPPCEVEV KFTRNFTLLE GEKILLHKGS
KRADSIPCSV VLPNLPVLSG QFSLTNYRVV IEPNDSQWTY QNKVRPQFFD IPLLLMQRVE
KTIDKNNIIL DISTKDGRYL RAVISNSLQS EFNVFPTLYS GAFPQNPTNR FAFSHTFCGQ
IDGWKIYNPQ NDYARLGVNP TKPDCRWRFL DNSTGEYCET YPDIIVVPND LPLMTIKTCA
SFRSKNRLPV LVWCNTRRGA TLWRCSQPKT GIRTSRCVED EEYLRRLAQS SQRDPVLHIF
DARPFVNAHA QRALGGGVEN VNHYENTELH FLNIENIHCI RESWVGMMVG LNNTNPSKYL
SAVEKSGWLE HVSLLLQGAC GIVESLQNGV SCLIHCSDGW DRTSQLCSLV QICMDSHYRS
LRGFAQVIEK DWVSFGHQFE VRLAHANPNL QDDKRSPIFL QFLDCVYQIT LQFPTHFEFN
TLLLHDLALY AYSGRFGTFM GNCARDRINL NLTAKTVSVW SYVFENLDNY TNPYYQAGQD
DPIEPIYSIR KLVIWHDLFS QWLGDFYYIV PQLLGPNDHK EALMRSAGEG MQLYKALIMQ
KDQEIKDCKR EIAELKEKLA KLRG
//
