SEY1_TRYCC
ID SEY1_TRYCC Reviewed; 877 AA.
AC Q4DHA1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Protein SEY1 homolog {ECO:0000255|HAMAP-Rule:MF_03109};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN ORFNames=Tc00.1047053511285.50;
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener;
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
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; AAHK01000479; EAN91902.1; -; Genomic_DNA.
DR RefSeq; XP_813753.1; XM_808660.1.
DR AlphaFoldDB; Q4DHA1; -.
DR SMR; Q4DHA1; -.
DR STRING; 5693.XP_813753.1; -.
DR PaxDb; Q4DHA1; -.
DR EnsemblProtists; EAN91902; EAN91902; Tc00.1047053511285.50.
DR GeneID; 3545203; -.
DR KEGG; tcr:511285.50; -.
DR eggNOG; KOG2203; Eukaryota.
DR OMA; YHVVGVF; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000002296; 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..877
FT /note="Protein SEY1 homolog"
FT /id="PRO_0000384964"
FT TOPO_DOM 1..735
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 736..756
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 757..759
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 781..877
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 49..307
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 850..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 388..410
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 863..877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 877 AA; 99185 MW; 6C2181238212C42A CRC64;
MVAFAGGART EDAHLIDDEG QLLPVNGIEE YLFTALGASR GGDALHRVGI TYHVVGVLGG
QSSGKSTLLN CLFGTKFQTM DETKRRGQTT KGAFISRANF EVLRGDDGEM DAGASALMES
CAGKSLPLFV VDFEGTDGFE RGEDQSFERQ LSLFALSVAD VLLINMWAVD VGRFNAANMS
LLRTIFEVNL QLFSHDSYTK EEKPTLLVVL RDFTEVETRT HFETVRKSFD KIWDNIVKPE
AFKNSTIDTL FDLRYHVLPH FKLQRAAFDK ETAKFRQWFY LSTCDEYLFH TRGMFRGVPL
DGIPSYLSSC WEMIRKSKDL DIPTQREMLA RHRCLEVKKQ ILQLFTEFCS NYTERLQRGE
LVTHLTSLLE QDVDDKLRDF HQQTRLYRID IVRKTEAELE EELLKVELKL VGEYAKFISS
KVLEELETAV SGTVDGALRW LLHQAQSIPF LSAEAGDAGG GTEHMSHLKS VERASSNDVY
ITDNETCNVL VHSFWKRLCR ALQAEIELLY CDFSQQHQRQ RESQTLNLYD RYASLVAEDP
ALQEAIAHFV SDAVFQKVSR RFASMAENAA ETIHQAFEGV LNRNQDGTVR FFHTTKALQR
IEPQARQAGL VLLGCLLYYR VKVVADRVVY KLEDTDGLSR AAVHLLGERR KLIVRENSEE
QKFFLHYATI SEAPRYPIGA PVAETDSADT SDNVVDRDCV LLSQQAVQRA FDLYTQKCEF
TMQLQLRSIE GEKQNLPAWV LPVLLLLGWN EIWYVLSSPV LLVVVVIIAA VFLRGFLLTQ
WAIFEETGPT CVVVGVRVVV QQIRNIYKAL VPMMPDDVKS NVARHRDPGS FSDVTASAVG
TSWPYAAAEP TVLPPSTTSA TLTRRLKKEE EVPTQKE
