ID   A0A158Q909_9BILA        Unreviewed;       690 AA.
AC   A0A158Q909;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   SubName: Full=FH2 domain-containing protein {ECO:0000313|WBParaSite:EEL_0000930301-mRNA-1};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000930301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0000930301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the formin homology family.
CC       {ECO:0000256|ARBA:ARBA00023449}.
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DR   AlphaFoldDB; A0A158Q909; -.
DR   STRING; 1147741.A0A158Q909; -.
DR   WBParaSite; EEL_0000930301-mRNA-1; EEL_0000930301-mRNA-1; EEL_0000930301.
DR   Proteomes; UP000050640; Unplaced.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; IEA:InterPro.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR043592; FMNL_animal.
DR   PANTHER; PTHR45857:SF8; FORMIN-HOMOLOGY AND ZINC FINGER DOMAINS PROTEIN 1; 1.
DR   PANTHER; PTHR45857; FORMIN-LIKE PROTEIN; 1.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   PROSITE; PS51444; FH2; 1.
PE   3: Inferred from homology;
FT   DOMAIN          321..690
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..326
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   690 AA;  77358 MW;  03EDDA5BC850940D CRC64;
     MPANDGTERK PLSSSPLQQQ AQMSLHQQLD LSVDASSGTV TTTPTTTPSA LNAEFFHCLT
     QNLLATTAAG TSGQPQATDA ATGASVAAAF GLPIPDVSMM YGNEEPISHM EEYADEVEQL
     MKRCFPTVRG RGRPVHSNIR PSTASSSSTV NTESNNNSSR NSANSIASVN KISARYTHSY
     RRRGIKHPVQ EMTHEIYSSV SNKRVKNEND YENESEIAIN QAPIDASGQS SPSEEDSSST
     SNVPHNGIKE TYSKNISYSH GTNSYYDRNG TNDYNDEVNK YRSSTGYQNG TDQSETVAND
     SSPSSSEHVN NEAELETESN DSSVHDFDEE EQPLGYIDHI RPRYLPQNVN WWILANDQLK
     GTIFESFQLS EVLHRFPRQP YKLDSKFFVT QEQLKRVQEV RQQLTLDLTK LRDALCNLDL
     SVLPTEQVDL IANIAPTSMD VFYLLDCESA DPTALTGGNE QFLLELAKID RIEEKLHAMS
     FMGHINSRVT EILKSFEDLT NIVKVLKKNR GFRALLRVVL VLMNFIIGDF TARTIRGFRA
     SDLAKICATE VCNSPKTTLL NIVASSTISE FPEVCIFRDT LPALERASRV RRLERDYLRF
     DREASRLDDK GQMAGYREVI RNKVMEVKDS YRECKIGLCK TMRFFGELVD EDIGPEIPET
     FFASIATFYR QLQRAWIDVH LHGIPVTKAV
//