ID A0A1I7VZ23_LOALO Unreviewed; 1372 AA.
AC A0A1I7VZ23; A0A1S0U9H1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=LOAG_01159 {ECO:0000313|EMBL:EFO27314.2,
GN ECO:0000313|WBParaSite:EN70_7856};
OS Loa loa (Eye worm) (Filaria loa).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_7856};
RN [1] {ECO:0000313|EMBL:EFO27314.2, ECO:0000313|Proteomes:UP000095285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Henn M.R.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Loa loa.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:EN70_7856}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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DR EMBL; JH712108; EFO27314.2; -; Genomic_DNA.
DR STRING; 7209.A0A1I7VZ23; -.
DR EnsemblMetazoa; EFO27314.2; EFO27314.2; LOAG_01159.
DR WBParaSite; EN70_7856; EN70_7856; EN70_7856.
DR eggNOG; KOG4371; Eukaryota.
DR OMA; HRFMIKM; -.
DR OrthoDB; 2910505at2759; -.
DR Proteomes; UP000095285; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd17101; FERM_F1_PTPN13_like; 1.
DR CDD; cd00992; PDZ_signaling; 3.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011019; KIND_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46900:SF3; FERM AND PDZ DOMAIN-CONTAINING 2; 1.
DR PANTHER; PTHR46900; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 13; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00595; PDZ; 3.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00750; KIND; 1.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF50156; PDZ domain-like; 3.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS51377; KIND; 1.
DR PROSITE; PS50106; PDZ; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000095285};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 6..186
FT /note="KIND"
FT /evidence="ECO:0000259|PROSITE:PS51377"
FT DOMAIN 503..815
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 920..1003
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1195..1274
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1288..1370
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 192..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1372 AA; 152523 MW; 39DB168935F1D689 CRC64;
MGDVGVSLSE IVEVRGCGLN DDELLALIII GCEVLTKTTA GVFSPEHVIL HTDGELEIKS
VSRDKVSREY VPPEMQQGNT DVDPGAVHVY CLGEVIRFAG AAESGNADLF SLLNVMTVAH
IATRPSVTRL GQMAKNKLTI QNPKALLAEM YVLVMGDEAE DVDDLDISSG EYMPNSLGEN
GGLRSLKWNQ AGTSRSDTCD RSRKVTQADP FDGGEGTDVW ELSGGDPFSS VTIADEQVLQ
EAKDENSLLQ EEKQQKLSAG KIGVLLEQNE EEGKSVVGNN LHNLPTQSVS YDFDDDIVEY
SEENIPADEL NSISTVITAE HIEKVSEILD YNGHKLLSTN IIHEYNDSLS SLSPISEVDE
GQKMIASTIL SSDCQKIADK QGSLEESNCD SPSSNKNEDV PELVLSKEEN GKEPPSRVLE
ARVKGIVGTR KASGISVASE QQFMRRNSLL PNRISGRKSS SKHFKRRLKA EPEFVKNANA
SSICLKAPAQ RKKKVTLHRI EHTDVTVELL SGKHVEVSCR SDAVASEIAD VVMRHMNFSE
NSFFGLTVLR DGEHFFLDGH QRLEKFAPPG WKNARQYGSS KRLYMLFLRF RYYPASVAFI
RTEVVLHELY LQLRRDILDD RIQPKRGLLY DLAAFALQSE YSDQPNVTIL DYFDVQHYIP
KRCLDNCSEK TVIRDVMERH GRYRGMKHQD AEKRFILLCQ RLPDYGAHLH RVFASKPSIN
LGNTPLGDPE TGVAQWIAIM TRGIVLFEEE SGGRHAQIEH LWQNTQTLQF DKKRFVIASE
IHEPSTNVFY TDHYTKSAYF VRFAASQHRF MIKMRQWNHT LRRDSPFQFR RMPDVGADTN
FMEEVPSVHY MNTPDIPNMP EPVFTGSSNQ YTSGDSPSQN YTKAVHDSSF EPKASLINDR
VLEEISLEEF VENGDGYTLE ILLEKDPNSG LGLTLVDGNL NGIKGVYVKS VSEGGVGKKG
GVNVGDRLLS VNDVSLIGKD RHVTVDLVKK CGNYVHLKVF RLEAITSALA SGIIKDKTVT
DDQKGYKNHS FSVSKGLRSR TPPPPRKYSN ILKKRTRAVS DFGAVGDTLP DLNSEDLLSN
LRSESKLGYL RPETSLNDEI ECGMRYDVPV VSMYKFEDVD DELIDQSPKR SSTATYFPFK
TNENDWLKMG KSDVDQQKSP FNDWKSVQNY RKKPNLDWTD DLDDIAEPLP SDVSMVILER
NGSGSLGFQI ASSGGIVYVK QITAEPALSC PDIQVGDKII SVNHAKVQNL THQQLVDLLR
KGGDRVVIGL QNSGKEICTR DEGEQIVRVI LEKSHTGSLG LSLAKKTGFD GIYIRMISSG
SAADIDGTLH VGDKIWKVNG QSVSSCTPGA IVDLLKAASN PVEIVVKRTV VK
//
