ID A0A0V0WU37_9BILA Unreviewed; 1119 AA.
AC A0A0V0WU37;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=PH and SEC7 domain-containing protein 3 {ECO:0000313|EMBL:KRX79292.1};
DE Flags: Fragment;
GN Name=PSD3 {ECO:0000313|EMBL:KRX79292.1};
GN ORFNames=T06_1402 {ECO:0000313|EMBL:KRX79292.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX79292.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX79292.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX79292.1};
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 -!- 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:KRX79292.1}.
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DR EMBL; JYDK01000055; KRX79292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WU37; -.
DR STRING; 92179.A0A0V0WU37; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd13295; PH_EFA6; 1.
DR Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041681; PH_9.
DR InterPro; IPR001605; PH_dom-spectrin-type.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR10663:SF376; PH AND SEC7 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF01369; Sec7; 1.
DR PRINTS; PR00683; SPECTRINPH.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48425; Sec7 domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1119
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006872055"
FT TRANSMEM 813..836
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 848..866
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 886..909
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 930..955
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 980..1004
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1025..1044
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1064..1083
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 317..475
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT DOMAIN 513..625
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 199..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX79292.1"
FT NON_TER 1119
FT /evidence="ECO:0000313|EMBL:KRX79292.1"
SQ SEQUENCE 1119 AA; 126009 MW; 14E6F8F05539E29E CRC64;
LNVATVFPLG WKISILGFCA ASMMHVASQS PLIHYTSAEG KESVGRKVEE KKDGSEAFSS
IVNKQKGAET VTMAEQTACR RTPRFESFVM TGEKILCLTP KISESYAKLK RLELPEHMEI
ATSGMATMPQ SFQLVEPSTS GSSAEPDSLN ESGQKISSMV VAGNALHQEE ENFTPTCGNN
KQIVDGHVAT TAIGDKEKYD NFNSISDSDT DSDGDGDDDD DDHKCKVQGN FGVENVEQVE
QEEEGEEEKV PIIKASDTKD VDELIIAEAS SIANVEQSPP CSSRYDGMKN GSTTLDKLTQ
LTRLHDSDDA CSLNSTVLRA GGLETARRLA RRLYQLDGFK PSDVYAHISK SDDFSMLVSQ
EYMKMFNFSG FRIDAALRCF LTYVLLSPDQ MVLSDCVPLA LFSQRYHKCN PCLFNSEDEI
LSLVCSLLAL DLKLHAGSSK SCRITCHDFI ESTSQAGYVY SRDLLKKLYS SLKRNPLRDF
AYIQVENGER CSGYGNSILR PNPRMMPDSD SQVEYKKGWV MRKCVVDKGG KKVPFGRRTW
RMFYAILKGT ILYLQKDEGN AKSGAYITYR NAIGLHHSFA ERAVDYTKKQ HVFKLQTYTY
AEYLFQTSDP NEVASWIHVI NFIAACFSAP KPIVVDESIS NWSLFGRPTM STTMSTKLSM
TDQLKAHGDR VMEIERLLEA HRDHPPCRNC KPNLLLEFAE KEVNLLYELK RYKKYVEMLQ
DKVDEYASEE ENMCESAYVY SVPTIASPGG RSGQSDRLSY CAAIDNCMSA DIAYSAKNIK
DEERNFAFYS MNQTVLISSS PSSVTQSKHI SEIILIVQAN AAFLAFFLDW FIFSIFHKHT
YRKLDVCAIT NFAIGNMLCA VGTFLSTCHR FYVIKHFFNV EIWKCIFLFI YFPVIQFGRD
SAALSLLFCA FERLAFFTHP KLHRRMVEQL ASNSILLLGT TAVAVLDLVA ISIVASPRFD
QPIAAFCLRS EVISQQYMKI YSIIRIALGV FEALQYGISF FALIHNSRVL SATCLNVMRR
QRDRYTLRCL MMVFACSFAT QIIPWTVSLN LTQNSWHVSA FFKLLAKLET CILPLPPLLF
LLVHPDLRHD ARRVLAKKSC FNCKSKIEKQ HAVYIGSVL
//
