ID A0A0M9WL46_9EURO Unreviewed; 1012 AA.
AC A0A0M9WL46;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Myotubularin phosphatase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACN38_g112 {ECO:0000313|EMBL:KOS49005.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS49005.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS49005.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS49005.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-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 -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC {ECO:0000256|ARBA:ARBA00010761, ECO:0000256|RuleBase:RU003624}.
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:KOS49005.1}.
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DR EMBL; LHQQ01000001; KOS49005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9WL46; -.
DR STRING; 229535.A0A0M9WL46; -.
DR OrthoDB; 5474662at2759; -.
DR Proteomes; UP000037696; Unassembled WGS sequence.
DR GO; GO:0022626; C:cytosolic ribosome; IEA:UniProt.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd02413; KH-II_40S_S3; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.1140.32; Ribosomal protein S3, C-terminal domain; 1.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
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; IPR036419; Ribosomal_S3_C_sf.
DR InterPro; IPR001351; Ribosomal_uS3_C.
DR InterPro; IPR018280; Ribosomal_uS3_CS.
DR InterPro; IPR005703; Ribosomal_uS3_euk/arc.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR NCBIfam; TIGR01008; uS3_euk_arch; 1.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF8; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR Pfam; PF21098; PH-GRAM_MTMR6-like; 1.
DR Pfam; PF00189; Ribosomal_S3_C; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR SUPFAM; SSF54821; Ribosomal protein S3 C-terminal domain; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00548; RIBOSOMAL_S3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000037696};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU003624};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|RuleBase:RU003624};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00118}.
FT DOMAIN 137..657
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 772..843
FT /note="KH type-2"
FT /evidence="ECO:0000259|PROSITE:PS50823"
FT REGION 512..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 409
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 345..346
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 409..415
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1012 AA; 113577 MW; 3414E37928494FD7 CRC64;
MEKTRIAKVD NVTLARRGEQ VDGTLHLTPH HLIFSHTPPI SPEDHTKGVI TRPRELWITY
PIIAFCTLRP APAASRQLSS IRLRCRDFTF VCFYFINEHK AREVFESIKQ WTCKSSRIDK
LYAFTYQPPP PEKELNGWEL YNPRKEWARQ GCLDEGKAWR LSEINVNYEF SPTYPALIPV
PFSISDNTLN YAGRYRSRAR IPALTYFHPV NNCTITRSSQ PLVGVRQNRS IQDEKLLSTI
FLTSRSERPL ASFSATEKET DSSSPEASQV MVPELNNAEE LEDDLLAAAR GDPEDDRSIY
GAQQSNLIVD ARPTVNAFAM QAVGLGSENM DNYKFATKAY LGIDNIHVMR DSLNKVIDAL
KESDVTPLGP SRDQLARSGW LKHIGGILDG ARLITRQVGL THSHVLIHCS DGWDRTSQLS
ALSQICLDPY FRTLEGFMVL VEKDWLSFGH MFRHRAGHLN SEKWFQIENE RIGGDPNRAF
GDGGGAGKAI ENAFLSAKGF FGRDNNSRDS LADSDGELQN YDSDTPVKKP PAPRSGVSEK
EITKPKETSP VFHQFLDATY QLLHQHPTRF EFNERFLRRL LYHLYSCQFG TFLFNNEKER
VDCKANERTR SVWDYFLARR EQFTNPRYDP VIDDNQRGKE RLIFPRVSET RWWNEVFGRT
DAEMNGPRSS PAPSDIPEST VLTGIETAGT NSAGKMTDVS GITAAVTSGV SKLAFPAERT
DKPTEIEVSR PRSPPSTTPD STTTRNVKMA AVQGAISKRR KFVADGVFYA ELNEFFQREL
AEEGYSGVEV RVTPTVTDII VRATHTQEVL GEQGRRIREL TSLIQKRFKF PENSVSLYAA
KVQNRGLSAV AQCESLRYKL LNGLAVRRAC YGVLRFIMES GAKGCEVVVS GKLRAARAKS
MKFTDGFMIH SGQPAKEFID SATRHVLLRQ GVLGIKVKIM RGSDPEGKAG PQKTLPDSVT
IIEPKEEQPV LQPMSQDYGA KAIAAQQAAE QQRLAEQQAA EAEGGAETFA QE
//
