ID A0A0V0XL14_TRIPS Unreviewed; 921 AA.
AC A0A0V0XL14;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=FYVE, RhoGEF and PH domain-containing protein 1 {ECO:0000313|EMBL:KRX88636.1};
GN Name=FGD1 {ECO:0000313|EMBL:KRX88636.1};
GN ORFNames=T4E_10450 {ECO:0000313|EMBL:KRX88636.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX88636.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX88636.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX88636.1};
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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:KRX88636.1}.
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DR EMBL; JYDU01000228; KRX88636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XL14; -.
DR STRING; 6337.A0A0V0XL14; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00065; FYVE_like_SF; 1.
DR CDD; cd13388; PH1_FGD1-4_like; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF241; PROTEIN CBG10230; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 390..578
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 591..686
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 708..769
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 797..898
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 51..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..362
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 921 AA; 103585 MW; A0D3E5257519C16F CRC64;
MTGFGKISAC GVGGGGACGC AEAKTCCPFI KQCIGLFLSF MDGHAFQKEH WSEESRAERS
TTRTVDDDKS ERRQLGAAMN DSDEHKRAES FSWKKSSTAT VGIDRPLLAP LLQDAAVASL
LDLKNIGCAL AFLQPDGCGS GDAVYSTSTM SSSTRTVNTD TSTCTTAQGQ NPTQTVSSKK
TYNVTSRVTS TRHSSREVTL NTGGKDLASL DLADLAKELE KHQPRESNGD LTMPFLDAAQ
LAGVDSPAAI IFQQLLNVEK ERFANLFPQL RCVRSSSVPL ETTVRIIRNA DGTVTRIQTV
QSRSVIRCRQ VTKQKGDETK STVRAVVQYE GPGGKVRLKL EDDGSVDSEE SDDDDDDDDD
NAQQLLQSPA KLGLPSPNSD QPLAEGASEK AFYAAQELVD TERRYVGKLI LLVETFKKRI
EQENSNGRLI PVQKSRALFA NLDSIYAFHK QHFLPQLQNR LRDWPKEQKI SDVVCQQAPF
LKMYSEYINN YKRATKVFEE LYKKGGKFAQ IVDEVERMPE CDNLSLVSHI IGPVQRVMRY
HLLMQEALEL VKSAASHANE IMRKLDKYKD LVELQEQLGC QVIELVSPSR ELIKQGRLLK
LSSKSDEQQT RHLNDMLLVC SERKVPIHKY KLRSLLEISG MTVLDGDYLD IENTFYVRTK
RKVIAFCAGT FKEKADWMES LWSTIRELAA QRQSFRISGR KFSKLDDRMP RKTCSLCSSA
FSIFRREYTC QACRKAVCKR CCCSTNKMSP AHEVGKEKRM CSACFEALRP NDSATQRQDR
DAQSNSSAGM LLVPANDNML HGYLEMRSLK RPWTKSFFRL KNDFLLYRYA DEKDKTPVAS
MPLPGIKVSL LDSRQESNSA LSEWNQFIVE HKNRSYFFRC STQEEMAKWM AVLDLASKAE
IPSSESPVCR NLDQVLYNTD Q
//
