SEY13_TRIVA
ID SEY13_TRIVA Reviewed; 827 AA.
AC A2FJ32;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Protein SEY1 homolog 3 {ECO:0000255|HAMAP-Rule:MF_03109};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN ORFNames=TVAG_204380;
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; DS113824; EAX95096.1; -; Genomic_DNA.
DR RefSeq; XP_001308026.1; XM_001308025.1.
DR AlphaFoldDB; A2FJ32; -.
DR SMR; A2FJ32; -.
DR STRING; 5722.XP_001308026.1; -.
DR PRIDE; A2FJ32; -.
DR GeneID; 4752840; -.
DR KEGG; tva:TVAG_204380; -.
DR VEuPathDB; TrichDB:TVAG_204380; -.
DR eggNOG; KOG2203; Eukaryota.
DR InParanoid; A2FJ32; -.
DR OMA; DIMEDIM; -.
DR Proteomes; UP000001542; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IBA:GO_Central.
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..827
FT /note="Protein SEY1 homolog 3"
FT /id="PRO_0000384962"
FT TOPO_DOM 1..634
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 635..655
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 656..658
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 659..679
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 680..827
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 28..242
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 745..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 322..346
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COILED 384..407
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COILED 475..501
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COILED 805..826
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 749..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..808
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 827 AA; 95416 MW; 2CFE26F65FA720B4 CRC64;
MAQIIDENAK VCETLEGYLD SIGITTAGLN YHTLSIIGPQ SSGKSTLLNN LFHTTFETMN
DQIGRQQTTK GIHAAFNNQN VLIFDIEGSD SRERGDADAL FERKAALFGL ALSEVVMVNM
WEKDIGRYNA SSIPLLRTVF EVNLQLFSSS QEAKCHLLFV IRDSTHPGEI IENQVRRDLD
MIWKDVILPQ NLQGKKFDDF FVFHFFQLPH LKLEPEKFKE QAAKLASMFT NKDEPGFFFA
QPMGKLIPGD GLAQYIHSVW DAISENRELN LPSQRKTLSN FRCEEFANQA YKEFETNATE
QIVSKIDAKP FTEFKEIGQK LFETAIHNYN QQANKYVRDI ANEKRQSLQE RISSFLAPSF
QRNCTIFKES AEKKFTEYIE KLPTELEESN EWEQNANKKL EETIKSIDEF VKSTMIPEFK
WQFDVSDIED NLHTLITNKL DTAISEMEQR VFERRNIEYK ERINAILDSA EPNMWERLRS
EMRNEITQTT SEINNILKKN TVDRHPSPKI ANMYYRSTDS QITSASQFIQ QKMIIRFEEK
FLQDEEHKSR VWKPDDDISA IFESARENGL HILNMFTNSQ LREPGTPVPL NDILTRQILT
QIRREQILTE FNDTIEKSYI SAVQIRESLI VRNTVPLWMW IVIAIGGYQQ LVSVVEHPWK
TLFLLAAIGL VYWLWSNQKL DKVIKVVKNY ITRVLCIIVK LLQSTTQEME VAPSILQASK
KSAANDMELI KKGLDDKKIE DEKTLETADT LDTMTTEVSE SNSTSASTNS PSKSEDSKEP
APAPKPRHRK RVSTSNNPYA TLQPNRINQA ELLKMKEMIQ KRQAEKH
