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SEY11_TRIVA
ID   SEY11_TRIVA             Reviewed;         804 AA.
AC   A2EI35;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Protein SEY1 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03109};
DE            EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN   ORFNames=TVAG_273580;
OS   Trichomonas vaginalis.
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=5722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC PRA-98 / G3;
RX   PubMed=17218520; DOI=10.1126/science.1132894;
RA   Carlton J.M., Hirt R.P., Silva J.C., Delcher A.L., Schatz M., Zhao Q.,
RA   Wortman J.R., Bidwell S.L., Alsmark U.C.M., Besteiro S.,
RA   Sicheritz-Ponten T., Noel C.J., Dacks J.B., Foster P.G., Simillion C.,
RA   Van de Peer Y., Miranda-Saavedra D., Barton G.J., Westrop G.D., Mueller S.,
RA   Dessi D., Fiori P.L., Ren Q., Paulsen I., Zhang H., Bastida-Corcuera F.D.,
RA   Simoes-Barbosa A., Brown M.T., Hayes R.D., Mukherjee M., Okumura C.Y.,
RA   Schneider R., Smith A.J., Vanacova S., Villalvazo M., Haas B.J., Pertea M.,
RA   Feldblyum T.V., Utterback T.R., Shu C.L., Osoegawa K., de Jong P.J.,
RA   Hrdy I., Horvathova L., Zubacova Z., Dolezal P., Malik S.B.,
RA   Logsdon J.M. Jr., Henze K., Gupta A., Wang C.C., Dunne R.L., Upcroft J.A.,
RA   Upcroft P., White O., Salzberg S.L., Tang P., Chiu C.-H., Lee Y.-S.,
RA   Embley T.M., Coombs G.H., Mottram J.C., Tachezy J., Fraser-Liggett C.M.,
RA   Johnson P.J.;
RT   "Draft genome sequence of the sexually transmitted pathogen Trichomonas
RT   vaginalis.";
RL   Science 315:207-212(2007).
CC   -!- FUNCTION: Probable GTP-binding protein that may be involved in cell
CC       development. {ECO:0000255|HAMAP-Rule:MF_03109}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03109}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03109}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU01052}.
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DR   EMBL; DS113394; EAY07674.1; -; Genomic_DNA.
DR   RefSeq; XP_001319897.1; XM_001319862.1.
DR   AlphaFoldDB; A2EI35; -.
DR   SMR; A2EI35; -.
DR   STRING; 5722.XP_001319897.1; -.
DR   PRIDE; A2EI35; -.
DR   GeneID; 4765569; -.
DR   KEGG; tva:TVAG_273580; -.
DR   VEuPathDB; TrichDB:TVAG_273580; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   InParanoid; A2EI35; -.
DR   OMA; TNFDVMD; -.
DR   Proteomes; UP000001542; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_03109; Sey1; 1.
DR   InterPro; IPR030386; G_GB1_RHD3_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008803; RHD3/Sey1.
DR   PANTHER; PTHR45923; PTHR45923; 1.
DR   Pfam; PF05879; RHD3; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51715; G_GB1_RHD3; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..804
FT                   /note="Protein SEY1 homolog 1"
FT                   /id="PRO_0000384960"
FT   TOPO_DOM        1..638
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        639..659
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        660..662
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        663..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        684..804
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          28..245
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          706..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..731
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..791
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38..45
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   804 AA;  92417 MW;  CF1459A3107DBF6E CRC64;
     MEQIITGEGQ IVPDLDEHIT RSGIDQAGTD YHMVSIIGCQ SSGKSTLLNL LFGTKFETMN
     EQKGRQQTTK GIHAARAVNG PILLFDVEGS DSRERGDSDA LFERKSSLFA LALSELLVIN
     MWESDIGRYN AANIPMLKTV MEVNVQLFLA QSTSKSKILF VIRDSTIPNF DVIKFQINRD
     MENIWAEITL PDSLKDKTIH DFFDFDFYAI HHMVIQRDIF DKDISALRQR FIDEKEENYL
     FKEKSTKVVP GGGLSTYIRN LWEVINENKE LNIPSQKLML SRFKCEENAK AAYDQFKEKV
     TKTILEPMAD ESVNLGDKFK SNAEEAIKAA NKFYHDNSWR YQQAAVEEFQ QKLSTDIGDL
     LISYYIKHCN YYARQVMQEF TKFISGLPDS FEKGGKWAIE VQAKIDELSL RLDSTCRDSL
     IEGYKWQFPS FKTIKAMDDA RKSYEEIMTK KLYKNIFAEE KIAFDDKASE LLMIADQNMW
     ENLRKLIEAS AKVTDDRFME IIKTNVLNPK PQEGTLKRFQ RHALNIVKES ANYIMMKMKT
     AFDRSFRYEK NGRPRVWTRR HNLNQIYEES RASGRKVLIL FTYCRLASPD DQTPNNPLNQ
     VLIPVEKSQE IEEKFEKLII HAYEEARASV LASQNNEHIP PWAWFLFLFS CSDYILWWLS
     NPLLFSLTVL FGGTYLVLNQ LGLWDTAVQK LLDIIKKKIV ELGATPDENN ETETNQTIPV
     EESQITPPPP TETTTDDGPV MKRRVHRSKA QGLTKTESNV TFANVSNAND EQSLTKNNTE
     DSLNTGSSSS GQRHRKRVRV GTLV
 
 
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