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Database: UniProt
Entry: A0A0V1CAJ9_TRIBR
LinkDB: A0A0V1CAJ9_TRIBR
Original site: A0A0V1CAJ9_TRIBR 
ID   A0A0V1CAJ9_TRIBR        Unreviewed;      1038 AA.
AC   A0A0V1CAJ9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 26.
DE   SubName: Full=Protein diaphanous-like protein 3 {ECO:0000313|EMBL:KRY46272.1};
GN   Name=Diaph3 {ECO:0000313|EMBL:KRY46272.1};
GN   ORFNames=T03_281 {ECO:0000313|EMBL:KRY46272.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY46272.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY46272.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY46272.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC       subfamily. {ECO:0000256|ARBA:ARBA00008214}.
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:KRY46272.1}.
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DR   EMBL; JYDI01000298; KRY46272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1CAJ9; -.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   Gene3D; 1.20.58.630; -; 1.
DR   Gene3D; 6.10.30.30; -; 1.
DR   Gene3D; 1.10.20.40; Formin, diaphanous GTPase-binding domain; 1.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014767; DAD_dom.
DR   InterPro; IPR044933; DIA_GBD_sf.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR010472; FH3_dom.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   InterPro; IPR010473; GTPase-bd.
DR   PANTHER; PTHR45691; PROTEIN DIAPHANOUS; 1.
DR   PANTHER; PTHR45691:SF6; PROTEIN DIAPHANOUS; 1.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 1.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM01139; Drf_FH3; 1.
DR   SMART; SM01140; Drf_GBD; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT   DOMAIN          70..439
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          504..898
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          920..955
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          993..1020
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          486..513
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          881..912
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1005..1020
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1038 AA;  118793 MW;  D3355A64C2D60EF5 CRC64;
     MNQRREKNWS ILGKVGNSFR HTSKHGKDSS KCDGNGDDSW TVTDSQRPAY EHNTLHGLPN
     TSTAVSEYDI DSLSSKELDL IFEDMLNDMN LSEAKKAPLR TASIEQKRVM ILQKIRTDQT
     LRGAKVKCDD PGDYIRILSA SEDNSPKLVR ILQSLRVSLS NNPVSWIEKF GTRGLNLLLN
     ILQWVSENPL VEASSMRIQH ECIKCLRAFM NNNYGLRQIM EHNQSCEILV QSLNVVNQSS
     TIDAVKLLAA ICVMPSPNST VQSGHEKVLN ALSSYAEHSE IRRFVPIVQG LGVAANPALQ
     NAFMQLVNAI ITIADDLDYR MHLRNEFMRT GMTDVLEIME CSENEDLKLQ VKIFTENRDA
     DLDELFQRHE NLRIEMDSPR KCYEALEHSL RNSPTSYYFL SILQHLLFIR DDDVELRTSY
     YKLLDDVISS VVLHKSGYEV DVHNQKRLAL NIEDLLEKVT EHQKHDLDSI GSSSDRLASE
     DMKVKFEAVV TENQELEAKL TQLASKIEEY KNETFNLRQH VDPSQMIESS FWAKTEEERF
     KSKTFFHHLE EHFSTASTAN GNLTSFQKKT IKKVKEAKVL PPNAVKTLEI IHGSTKMSAA
     EFRDALLELD ESKLTENILE RFWKIFSEPE LVSNLKSIQG EFNDLAGVEQ FAITLTSIRA
     LSVRLQCMCF KKKFSELIAD IKPSIVAVTA ACDEIKTSKG FGLFLEYVLL AGNYMNSCGK
     NTLAYGFLFS ILSKLREVKS IRQDVTLMHV LYEIFSKSFP EYAKFTDDFI HLNKAAEVKT
     EIVQQGINQM KNNITVLENS LKNYNRQAEN DNYVEVMSSF LTVAREQFQL LETMHKKMQD
     VCRSLLKYFS FDSKTYPVDQ CLADLRDFKV AYEKTAKEIA FAKEKENRIR LAEEARALKE
     KEMQERKQQK MKLIEMTRGD QEGVMDSLLE ALSSGKAFPQ RAKTPAREKS RMRRRNSQFN
     HVTIVNVSGD TVSADRERTP KMNSNDAPKM RIRRKGKKTV DPLSDGQKFN ASNGHNSEVH
     YQDASDLEDL LRRLKCDF
//
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