ID   A0A090LEA5_STRRB        Unreviewed;      1133 AA.
AC   A0A090LEA5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=BcDNA.GH04637 {ECO:0000313|EMBL:CEF66478.1, ECO:0000313|WBParaSite:SRAE_2000114600.1};
GN   ORFNames=SRAE_2000114600 {ECO:0000313|EMBL:CEF66478.1,
GN   ECO:0000313|WBParaSite:SRAE_2000114600.1,
GN   ECO:0000313|WormBase:SRAE_2000114600};
OS   Strongyloides ratti (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF66478.1};
RN   [1] {ECO:0000313|EMBL:CEF66478.1, ECO:0000313|Proteomes:UP000035682}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC   ECO:0000313|WBParaSite:SRAE_2000114600.1}, and ED321 Heterogonic
RC   {ECO:0000313|EMBL:CEF66478.1};
RA   Martin A.A.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SRAE_2000114600.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (DEC-2020) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC         [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC         COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; EC=3.5.1.98;
CC         Evidence={ECO:0000256|ARBA:ARBA00001028};
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; LN609529; CEF66478.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090LEA5; -.
DR   STRING; 34506.A0A090LEA5; -.
DR   EnsemblMetazoa; SRAE_2000114600.1; SRAE_2000114600.1; WBGene00261348.
DR   WBParaSite; SRAE_2000114600.1; SRAE_2000114600.1; WBGene00261348.
DR   WormBase; SRAE_2000114600; SRP11755; WBGene00261348; -.
DR   eggNOG; KOG1089; Eukaryota.
DR   OrthoDB; 5474662at2759; -.
DR   Proteomes; UP000035682; Chromosome X.
DR   CDD; cd00065; FYVE_like_SF; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
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; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR   PANTHER; PTHR10807:SF8; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   Pfam; PF21098; PH-GRAM_MTMR6-like; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000035682}.
FT   DOMAIN          132..520
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   ACT_SITE        355
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT   BINDING         294..295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT   BINDING         355..361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ   SEQUENCE   1133 AA;  131364 MW;  552065139E4D1B06 CRC64;
     MLFTDIGIVK FHKICLQQSR FSSKTEILGS VHVTSSHVIF TSESRRKEMW VSTGLISTID
     KEGETGSRYK ITIKTKHFLT MVFFANKEKE CQELYDALVR ASIITNISEV FAFRNKKPEI
     NEKVNNIDNI INWKRLDWKQ EFRRQKVSSQ WKRSNFNHDF EKCDTYPCDL WFPSKVSMQI
     LIGSSKYRAR SRLPILTYFN SENNASICIC AKFVQDYSAS CIEDDDLIKA ICETNIIKKQ
     LYIIDIQNYI VNNINNNIDK NEDEIIIEMD DNFKEIIIKK EEPEIKTHYF DISNIHCIRN
     SYIKLIQATQ CNGSQSEYLS LLDESEWHKH IKSVLDCSIF IFESIKNGIS CLVQCTDGWD
     RAIQTTSLAE LMLDPYYRTL KGFQILVEKD WLGFGHKFSD RCGHVTSVNQ EMKMEVSPIF
     TLFLDCVHQI MKQNPRAFEF NERWLIEINE YVYSCEFGTF IGNCEKDRSD LKVVETTPSV
     WNYFDEHIDD YKNPFYDNSI SVITNLSTHP SDLDVWSFLY NRYDSGILPR ESIEELVSSF
     NNHINAAKLL IKPSKYQSIF NVISCSEPSC FQEFNCVLDK RNNCNYCGLI YCKKCLKTKN
     SINICLSCSR KFSQIHQLQI DIEKLDPNFS KHYNTWDKNH IEVPERLSSI LNSLNNSRVT
     NHLTILEPVD GKLEDIYLNH PKEYVDEFKD VCSKSDGEMI KYCENHEDIY VNKDSYTCAL
     RSVGCCVKLM ETLLLNRGST GFAGVRPPGH HAYKDYPNGF CFFNNAAICA KKALKLGIKK
     VLIIDWDVHA GQGTQFSIEG IDGISLISIH RYENGCFWPN LEESGLGSLK SSKNTINIPL
     NQIGLGDFEY LTVFNKIILP YICDYKPELI IVSCGFDAAI GDPEGKMKIS PYGYGLLTRL
     LASTGINLCM ILEGGYFIES VKESCLKVIE SLVEKKVFSY ISKESLEKND KNFMYYLYGI
     MKNISFNNNI ITDILLLLEK YHNINGTKIT FDIKTNDYKG IRNVPKPYAT TNLYDPYDYE
     TEQKFLNELK NSLIIGEFKC IGDEIFVDFK INCICFTDKL KIEHVININS KQEAAFIIYC
     LILVNIWRWN IPCNMIDFTY WIQSFPEKRE ICDNDSFLKS LHTFSLKYNL EIF
//