ID A0A194S2U8_RHOGW Unreviewed; 579 AA.
AC A0A194S2U8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Myotubularin phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51339};
DE Flags: Fragment;
GN ORFNames=RHOBADRAFT_376 {ECO:0000313|EMBL:KPV74830.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV74830.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV74830.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV74830.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
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}.
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DR EMBL; KQ474079; KPV74830.1; -; Genomic_DNA.
DR RefSeq; XP_018270879.1; XM_018413448.1.
DR AlphaFoldDB; A0A194S2U8; -.
DR STRING; 578459.A0A194S2U8; -.
DR GeneID; 28973897; -.
DR OMA; RTMEGFM; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000053890; 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 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 Pfam; PF21098; PH-GRAM_MTMR6-like; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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:UP000053890}.
FT DOMAIN 132..570
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 528..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 363
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 275..278
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 300..301
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 363..369
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPV74830.1"
FT NON_TER 579
FT /evidence="ECO:0000313|EMBL:KPV74830.1"
SQ SEQUENCE 579 AA; 64740 MW; 598350D6CCBBC90F CRC64;
PDSSPLGHPT PGSLHLTAHH LVFKRDDVDA STDSGDEVWI PLTLLHSVTR TPPSLTGEPT
PLVLRTRDYL TYELSFASIA DADLAWDTLK AQCGTLSSGG LEARYAFAQP RRTAKGEGEG
DGAGKGKGRA DGWEVYDVEK EFARMGMGTR SKAWRFTNVN ADFQFCPSYP AKIVVPAKIS
DTTLSYAVKY RSKSRIPGLV YLHWANLGSI TRSSQPMVGI TQNARSIQDE KLIEAIFTSH
SQHSHALQPM HQIVYGATPS NIIIDARPTK NAYANSVKGA GTENMLYYRN CKKEYLGIDN
IHVMRSSLNG VFDALADAES TGTLDRAALR RTNWLSHLTN ILDGVLIVVR TVHLFNSHVL
VHCSDGWDRT SQLSALPQLC LDPYFRTARG FAVLIEKDWV SYGHRFADRS GHLCNDRVDF
VHKLGTDAST QQAFLASVTR QFAGSSHAFK ETCPVFQQFL DCVYQVQRQF PTRFEFNERL
LRHLVRETYG DAQGTFLFNS ERERAELDAR SRTASVWDTV FDPATGTLKP EFRNPAYDPA
LDDPHRKSPD ADQGVVLVDA HDVRWWHELF GRDDDEMNG
//
