ID A0A0V1L4W4_9BILA Unreviewed; 914 AA.
AC A0A0V1L4W4;
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 6 {ECO:0000313|EMBL:KRZ54595.1};
GN ORFNames=T02_2973 {ECO:0000313|EMBL:KRZ54595.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ54595.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ54595.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ54595.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ54595.1}.
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DR EMBL; JYDW01000134; KRZ54595.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1L4W4; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd13389; PH1_FGD5_FGD6; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
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:SF159; RAC GUANINE NUCLEOTIDE EXCHANGE FACTOR JJ; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF02466; Tim17; 1.
DR SMART; SM00064; FYVE; 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; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT TRANSMEM 58..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 468..511
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 540..637
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 679..737
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 783..887
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 643..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 104452 MW; 82D63595A4AF22A6 CRC64;
MEKNDNEKVT SRSIIERIFL SPRRKGEMQN DAVVPLTFPS PPPLLPEEVF IQRVMESCIF
KTILASVVGC GAGALFGIFT ASVDPVHTIA DPAKVTIKDI IRETRQRAVL YAKNFGVLGL
MFAGFECTVE TYRGKTDMKN GILSGAITGG LIGLRAGIKP AVLGAVSFAA FSAIIEHYLL
FSMVSGVGYV DSSEFLLMRS AVPPPVPPKP LHLVEKYRHL RNSPLRAVRP APAPPIFGDR
KSNVQCDDKR RVTLPVLVKS QSFHRWHSEN ALHQSSSCNS LRHSFSFGDL SLSRRSSKWR
KSLLKKLNEN RRYNYLPGHD SYFSERSSGV YSASESSEEE EIIYQEPQQK DKLYRVAEEM
CRTEWAYVNT LKALSVDFPK FIESQSLINQ RLLVQPDVSN EIARHLHALR KLHLEIAERL
QSRLDKELAT QLIQNCRQYP DFAAAVHNFE KKHFGGLLLV HQLDCVHQRI CRYPLLLSTY
LKYCSPNLEE YKSALEAKRL LESVALEIEH GLVEGDNLRK MFHLQRRLYS DYEIIQPGRK
LLKEGEVMKH SRKEIHPRFL VLFNDILLYC APVVHGSSML RVRNVLPLET LDMPVLPKND
ATSKEFHLRS QRRSIIILAK SLSERDEWIK AVKEAMQMSK SRFSDSNLTL EQSENSSVHG
DKQSPTEEIG RKAPPWVPDD RVTMCQHCIT PFTTLRRRHH CRACGKVICR RCIGKAPLEY
ADFSVEIVCP LCYDILLNRS FGADASSKIF SPEFLKCNMF FPPRCRVEQK KSSNGNLITL
DDDCVMKGYV WHQRKRDAWK RYWCILRKDS VMEFYAASED KVCKWKVVLI SYEALKIRGV
EGLPDMLEIS HKNQVMTTQS QSLKMVLKGD TNEVTHNWYN AVKSVLIDFE DAFCCNESSV
TDLSVTEFNR SKFS
//
