SEY12_TRIVA
ID SEY12_TRIVA Reviewed; 792 AA.
AC A2EK80;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Protein SEY1 homolog 2 {ECO:0000255|HAMAP-Rule:MF_03109};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN ORFNames=TVAG_100140;
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; DS113411; EAY06973.1; -; Genomic_DNA.
DR RefSeq; XP_001319196.1; XM_001319161.1.
DR AlphaFoldDB; A2EK80; -.
DR SMR; A2EK80; -.
DR STRING; 5722.XP_001319196.1; -.
DR GeneID; 4764857; -.
DR KEGG; tva:TVAG_100140; -.
DR VEuPathDB; TrichDB:TVAG_100140; -.
DR eggNOG; KOG2203; Eukaryota.
DR InParanoid; A2EK80; -.
DR OMA; DERPDNI; -.
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 Coiled coil; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..792
FT /note="Protein SEY1 homolog 2"
FT /id="PRO_0000384961"
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..792
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 703..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 691..718
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 723..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..777
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 792 AA; 91331 MW; 49A874B764EA8710 CRC64;
MEQIITGDGA LVSNLDEKIT SSGIADAGVD YHTVAIIGPQ SSGKSTILNL LFGTKFATMN
EQRGRQQTTQ GIHAAKSVND PILLFDVEGC DSRERGDSDA LFERKSALFA LALSEVLVIN
MWESDIGRYQ ASNIPMLKTV FEVNIQLFLA QNTTKSKILF VIRDSTAVNF EAIKFQLNRD
ITNIWDEINL PDSFKGKQME DFFEFLYFPI HHMVIQRDQF DADVNTLRKW FNEPPLKDYL
FAEKSTKVVP GEGLSQYIRN LWEVINENKE LNIPSQRTML ARFKCDENAA EALSKFNKFV
EENLQRDPDQ PITIIQDFKP LCDKSVENAL KYYHDNSWRY SEAVVKEREA QLKQEISDVL
LPYFNSQCKL FCDNTLKRFN EFISSIDQEL HVGGTWESDV QGKIDSLNMD LKKNIKDTTV
EPFSWNYPDY EVMKVMFNAT ESMKGKLVKQ LEQTIITEQM RSFDEQANDI LAKVDNLMWD
NLRNLIRKVS TETTQNTNQV LKTNVSGVHA RNDIKRDFQT HTISLVRESA NYIVLKMKNT
FDRTFKYEKN GRPRVWTRRD NINQIYENSR DAGLKVLRHF TYCRLAESDD EVKPNDPLTQ
VLIPHERASE IEDKFERIII HAYEEARANI KAQANREQIP GWAWLATFLC SSNYIMKLLA
NPIFFALAVI IGGIYSILRM LGLQDVAKKT LLDKFNSLLK NLTKDENEQE KEGEENEEPE
EDQPLPNNNR KRMKLMEKSV SQEFSQKSIY KSSEYKGSGD SLMIPQTSPL GNNDSPEKPR
DSLTRTQSLE FM
