ID F1KQD1_ASCSU Unreviewed; 1975 AA.
AC F1KQD1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 08-NOV-2023, entry version 64.
DE SubName: Full=Myotubularin-related protein 5 {ECO:0000313|EMBL:ADY40085.1};
DE Flags: Fragment;
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY40085.1};
RN [1] {ECO:0000313|EMBL:ADY40085.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
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; JI164171; ADY40085.1; -; mRNA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00029; C1; 1.
DR CDD; cd13208; PH-GRAM_MTMR5_MTMR13; 1.
DR Gene3D; 3.30.450.200; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 3.40.50.11500; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR022096; SBF1/SBF2.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF109; SET DOMAIN BINDING FACTOR, ISOFORM A; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF12335; SBF2; 1.
DR Pfam; PF03456; uDENN; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00568; GRAM; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00800; uDENN; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 12..423
FT /note="UDENN"
FT /evidence="ECO:0000259|PROSITE:PS50211"
FT DOMAIN 1112..1625
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 1779..1830
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1876..1974
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1837..1863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1845..1863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1975
FT /evidence="ECO:0000313|EMBL:ADY40085.1"
SQ SEQUENCE 1975 AA; 222489 MW; DD79E857556596C0 CRC64;
MDDNGGAIRL ADYIVVIAFD ESQIRHGNSV GNIVQRLPQH DWPDISLSPN LEVFSQPQGW
SLSAEVKPAT FFVNTLTDIL GSRQYAYCLQ VQEPCGSIIE DVDDVTLSGA TLYKPKVIVI
LSRFPFFELF RNCLNRFHVA LLDSECNAEA MTATLLSSTK LAIGAPPVSF NFASERLCVR
APLSRTVPVT SDKVALFMQQ LGTIQNVLSL LSAILTDRKV LFRSSSMTRL ADSCYAICAL
LYPFEYPHTF VPVLPEQLIE YLESPTPYIM GLLHSVRNLN VELDTTIVVD LDIGAVYIPP
TVTLPLIPEP FAQRFICSLQ MVLNPSLSNA DDAWKMGQPP HPSCEVQDKR IRACFIRFFA
DILGGYRCCL EVVRLHTPPL IVFHKSAFLG LRGFSSCPLI RTFLDSLLFQ SFICERGLPY
RICDLFDDLV SHSNDHINGD QSKTSIMDSI ANIAEKLRDN EHQDSSFSMT PLLTNKRFLM
SNVPTKLPLF DEKLVARFIE ENRKYRCNTP HCTLRPRKVP TGNWFCMKEE RLGAVSRRLQ
VLSSCLHYIF DLKLSDARKM LCAVELSMRS VNARVALCQL LWLNLNPVNR ATLLPQQFEL
VIRLINCALN QESKEDEHGI AYAMLYLSNI YCRRLTAGVH QFAYTCIQEH PVWENEQFWE
AAFFHDVHRQ LRRLYMPIKE DLDCPFSVQE NATDTWNLME EPSGMDLVSE RLANVSRYDE
GELRMRAAEE HSIIFGQAKH YINLMVYLRI PLDVSKLRRV NVRELERRSD RNGRRREVFD
DETVVSESES DVESGFIESD DGDLGNATVK WIRRLIDRIC SAAGLEHAQI ERLCDEIPGF
VALHIDNLEQ VYTESKRLSP MHKPKLLQPA LLLPSEHVLL GGMRVFLLND GRSLGNVCGD
SPQSLLPAEG AIFLTNYRLV FKGQPCDPFL CEQVVIRTVT IMSITKEKQI ADQSIQNSSQ
LEGIPTRVAH QLHDAFQIRS ANAQLMKVAF DEEVSSEKAE EFLQTLASLR WPPTLPHTLF
AYSAASSILS STFARTSTKH KYGTIRELKK TLIRNPLKDK KRARTPLKAL AYPNGHETMP
VALSAGASPT TSRSSHASDY LDLSDVTDLA TSQLHHHYMV DYERLGLTHR TFRLSNVNSK
YELSKSYPSV VVVPSSVADE SFAKIGKGFK HGRFPVVTWK SEDDALLIRG AGLASQTVVA
RIKKQANLLG NVDTQGSGFV GSRVSLNSRD FNAPNSVEMQ ERYMSTFVAL SPHATSVDGR
SLLSESMESL LSLDSMVTFD GISLASATPD IYRKTQTSDF TRHATNFVRS SGGKTTMRPM
NNGRSVIYGD YVMNQARRAA TFLPPSQASR PLLSLTRNSL YVFGDRNQAK VLKLDKGCEF
IPVSYPSAHN VKIAFKKFLR AVCPSWAPSE EHSISFYKQL DDSNWLQMIS SLLHLSNAVA
DLIDLQHSSV CICIEDGWDA TSQIMALSQL LLDPYYRTID GFRVLIEKEW LAFGHRFSHR
ANHSIVSQNS GIAPMFLMFL DAVHQICEQC PSAFEFNDFF LRFLAYHSSS ACFRTFVLDS
ECERIAFDTL CVSACDPRSA SIWTYINEKR HGSPIFNNFS YTPDLHGVLR PQASIASLTL
WSLFSEDHLA HGSPYDIEVA DVEEQEREDE QFESLSEMRP TGALTRRVLD ANYREPHLLL
LDGFSISLDN YTRIRTLLPG EDDKANEPWT SVMAVIDARS APSVSFTLDD KESSLLNGWR
RHVQRAVHKK ETVKLLLRGM THQSSNPRMR ESIAGSSTGH HFVSQHVTAG DMCAVCHQNV
PGVVVRMVHR CTGCGMICHE KCSPLVSSTC PASIEEKRRS LTPMPEPSVT ASKRASADTT
ADSKTLTMSV SRPYTNATHC GFLMKKGATF KMWKPRWFVL DASRHQLRYY ESETDVNCRG
VIELADIKGV DISSSHALRK PLIEIRTVRR VYSLLAETKN DADMWMEKIL AALRD
//
