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Database: UniProt
Entry: E3LE44_CAERE
LinkDB: E3LE44_CAERE
Original site: E3LE44_CAERE 
ID   E3LE44_CAERE            Unreviewed;      1774 AA.
AC   E3LE44;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=CRE-MTM-5 protein {ECO:0000313|EMBL:EFO82341.1};
GN   Name=Cre-mtm-5 {ECO:0000313|EMBL:EFO82341.1};
GN   ORFNames=CRE_00256 {ECO:0000313|EMBL:EFO82341.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; DS268407; EFO82341.1; -; Genomic_DNA.
DR   RefSeq; XP_003117743.1; XM_003117695.1.
DR   STRING; 31234.E3LE44; -.
DR   EnsemblMetazoa; CRE00256.1; CRE00256.1; WBGene00051714.
DR   eggNOG; KOG1090; Eukaryota.
DR   HOGENOM; CLU_002298_1_1_1; -.
DR   InParanoid; E3LE44; -.
DR   OMA; KITESLW; -.
DR   OrthoDB; 3195274at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.450.200; -; 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; 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; 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   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; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          14..412
FT                   /note="UDENN"
FT                   /evidence="ECO:0000259|PROSITE:PS50211"
FT   DOMAIN          998..1479
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   DOMAIN          1570..1620
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1673..1773
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
SQ   SEQUENCE   1774 AA;  203093 MW;  CBF072B9F66F64FC CRC64;
     MRDPDKVKSG PICDTVAVIV LEESEDENAL PDVLHEVQSP HTSDTIPTSS IKKFVRPRGW
     YNQSETSPSE FFYQILTTEK GARRIAYVLS TWEEDETTKN FKAVSIVLIS QNFHPKAFKE
     ILLEISNDLR TPEFSSSSEL IRFLTDELVE EGSTIEIRTK TLHVELGFEL SPVSPVTGKD
     VAMLFKMLGF RNVVKVIHAL LSDCRIVLAS SSLMRLSRCQ NAILSLLYPF VYVHSCVTIL
     PDSLAEVLES PTPFLIGVLT EFVTSFGDEN IVVYLDNGEV HIPDHTEIFK ADDYYYESLH
     QRLRDVLFTT TSQEDLAVPS EERLDVDEFI LDKKLRACFI LYFAELLYGY QYYILYTRIK
     GNFEKKLTTS LTFHVGAFRG FRKLTDMMSS SLLKSVYFQT FILSRALPRR KHDLFDEISC
     LKELDQLIYK QKSNSYESRK IIEQISCELI QKERYMEKCS VRKQEVFTKI YWTTGKELAP
     NNNSIIHTVK PKMRSNVILQ AMLPVVNTHV EYHANQFEAY AHRIEALRNC LGDIFESKVS
     FASKSLDAVK SSMRFAPLRI ELCRLLNQKS SALAVLSDKQ FDDIALLMNA ALQAECEEDK
     DGVVRSLMYL SSVYSRKLTQ GVQQYMYTAL QEHKVWKNQR FWTSCFYYEV HEMLFSEMLK
     QDRKITESLW CHTLRPCAME MIDTDDTDQE ELVRQENEMI QAQAKHFANL IICLLIPLTD
     EFFDNEENHT AVQTEKSKWI AYTLDSILGV TGRINGLPLS RIQNYVEAHV ESLRDVYLEL
     SHGDHLKKDN FDPILVCPSE FLLSDPIDCY LLTNTEESTM SLNRLENLLP ASGSLFLTNY
     RVIFKGKSVD INVTNGTIVQ TLPLYSVESF KKLTSKKMIP SQLIEKGVKI EHIIAIRSSC
     AATIIVAFDE DEINNLAIEK FLEVIESSSR NSFAFYNIRK DKTITDTSSH KFSTLNSAIR
     GFTKKKTDPR RIRSHSSHRG SVHIQFDKIE DFDHLKKNAY IRYAVIDYPR LGLNSKNVKL
     RMSAANLDYN ICPSYPGNFI VPSETNESEI AKVAKVFYSI MFNIVKILFK GFVDHRLPVV
     VWMHGNGSLL IRASAFTSTD MVKKLKKVVN YRRNAPKLTG TMTGSQQTLH SKASSNEESC
     SNVVAGAEIK SAEVQLNYFA KLANSSQKVV SFALPTQYAE KNSVFNDGCT LTHHNGYSSR
     TANTETVTIT ANGFPVSRFH RKALYVLLEK GHAVKIPTDS NAEAIMVRSV KESELRRSLQ
     KARQIYSKEF PKDAKISNLE AWNLSNWPQS VSRMIELSNA IVALMSLYNS SVAICLEAGR
     SITTILSSLA QLLSDPYYRT FAGFRVLIEK EWLSFGHYFH KDAEMCSPSF LCFLDCVHQV
     MQQYPSAFEF SDFYLNFMAF HSAAGYFRTF VDDCEEKRLQ SDANEFYLPD DLTTISIWEY
     IKLRIRVSTS FLNEMYEPFG DVLVPSSSLS QIRMWSFLTE THLRFGSPYD IESSYHERKL
     VDAECEEEDW SNLDTTEDLD KSVSFTKPPE TDSTKMNAIK ALQKSFLVEL FDASEKKTTS
     NGEANGKETV HELAPFAVGA RPVQCCYCAN ILTRWSKAVH CKKCRIHIHE GCVNRNITIG
     NIVHTWEAKP LENIKMPSAA IQISTPTAEK VAYSPSNTLT RESMSPPISN NIPPLCTGYL
     SKRGAKLKLW VPRFFVLYRD TPKVYYYEDL DNWKNSEKPS GLIDLVEYKN CHLEQNGRRA
     FMELHMKNRT YRLLSENMNE AVRWKECIEQ VIRD
//
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