ID A0A100IN63_ASPNG Unreviewed; 753 AA.
AC A0A100IN63;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Myotubularin phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51339};
GN ORFNames=ABL_06939 {ECO:0000313|EMBL:GAQ44278.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ44278.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ44278.1}.
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DR EMBL; BCMY01000012; GAQ44278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100IN63; -.
DR PaxDb; 5061-CADANGAP00013710; -.
DR VEuPathDB; FungiDB:An18g03320; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1154892; -.
DR VEuPathDB; FungiDB:ATCC64974_109180; -.
DR VEuPathDB; FungiDB:M747DRAFT_292452; -.
DR OMA; RTMEGFM; -.
DR Proteomes; UP000068243; 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; cd17666; PTP-MTM-like_fungal; 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 PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF8; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR Pfam; PF06602; Myotub-related; 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;
FT DOMAIN 136..661
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 247..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 412
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 348..349
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 412..418
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 753 AA; 84269 MW; 76B584ACB1049309 CRC64;
MLQVEDVTLA RRGEQVVGTL HLTPHHIIFS HTPPPPSSST DASQAPGPSG RPKELWITYP
IISLCTCRPT PAASRQPSSI RLRCRDFTFV CFYFTTESKA RDVYETIKCW TCKVGRIDKL
YAFSYRPPPP EQKFNGWELY NPSKEWARQG VDQAGSGWRI SQLNTDYGFS ATYPALLPVP
SAISDNTLNH AGKYRSRARV PVLTYLHPVN NCSITRSSQP LVGVRQNRSI QDEALLAAIF
STSRSERPLA SFTPPGFDSD SSNSTPGNAS RSHMLADLTV PDDLEDELLS PVRENPEGKA
QVYGAQQHNL IVDARPTVNA FAMQAVGLGS ENMDNYKFAT KAYLGIDNIH VMRDSLSKVI
DALKDSDVTP LGPNKDQLAR SGWLKHISGI LDGARLIARQ VGLQHSHVLI HCSDGWDRTS
QLSALSQICL DPYYRTMEGF MVLVEKDWLS FGHMFRHRSG HLNSEKWFQI ENERIGGDSN
RGFGEGGGAG RALENAFLSA KGFFNRDNNS RDAIGESDGE MQSYDAENLK KPNNAIPRTA
AADKEVTKVK ETSPVFHQFL DATYQLLYQY PTRFEFNERF LRRLLYHLYS CQFGTFLFNS
EKERADWNAK ERTRSVWDYF LARREQFTNP QYEPQIDDHK RGQERLIFPR INEVRWWSES
FGRTDAEMNG VRSSGSRPPI GRDATSTQPS PVLTGIETAN HSLGAGSSGK DTLSAASTGM
AAVTAGISNL AFPKSKEDGQ DPKSLNRMEV EMQ
//
