SEY12_ENTHI
ID SEY12_ENTHI Reviewed; 825 AA.
AC C4M6U3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 57.
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=EHI_054180;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=15729342; DOI=10.1038/nature03291;
RA Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J., Amedeo P.,
RA Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T., Suh B., Pop M.,
RA Duchene M., Ackers J., Tannich E., Leippe M., Hofer M., Bruchhaus I.,
RA Willhoeft U., Bhattacharya A., Chillingworth T., Churcher C.M., Hance Z.,
RA Harris B., Harris D., Jagels K., Moule S., Mungall K.L., Ormond D.,
RA Squares R., Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H.,
RA Price C., Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S.,
RA Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U.,
RA Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M.,
RA Barrell B.G., Fraser C.M., Hall N.;
RT "The genome of the protist parasite Entamoeba histolytica.";
RL Nature 433:865-868(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RA Lorenzi H., Amedeo P., Inman J., Schobel S., Caler E.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; DS571309; EAL44464.2; -; Genomic_DNA.
DR RefSeq; XP_649850.2; XM_644758.2.
DR AlphaFoldDB; C4M6U3; -.
DR SMR; C4M6U3; -.
DR STRING; 5759.rna_EHI_054180-1; -.
DR GeneID; 3404147; -.
DR KEGG; ehi:EHI_054180; -.
DR VEuPathDB; AmoebaDB:EHI5A_040760; -.
DR VEuPathDB; AmoebaDB:EHI7A_145120; -.
DR VEuPathDB; AmoebaDB:EHI8A_163750; -.
DR VEuPathDB; AmoebaDB:EHI_054180; -.
DR VEuPathDB; AmoebaDB:KM1_233570; -.
DR eggNOG; KOG2203; Eukaryota.
DR InParanoid; C4M6U3; -.
DR OMA; DIMEDIM; -.
DR Proteomes; UP000001926; Partially assembled 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; 1.
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..825
FT /note="Protein SEY1 homolog 2"
FT /id="PRO_0000384947"
FT TOPO_DOM 1..728
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 729..749
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 750..752
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 753..773
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 774..825
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 83..305
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 373..397
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT BINDING 93..100
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 825 AA; 96601 MW; C27901710908A0A2 CRC64;
MDEVSPTKHF TSKPLLPTKT PRDKAISHYV NALNSPRNVV KTETPECGIQ IIDGDGNFAS
TDTRERPSLK NYILSKPEFL KRGMDYNAVG ILGAQSSGKS TLLNYLFNTK FRILNEVMGR
SRTTHGVWMA LSGKESNIVV FDLEGTDGSA REDDYSFERK TSLFSLSVCS VLMVNLWSHD
VGRFQASNMS LLKTVFELNL QLFVKEETPK TLIVFVIRDR EADTPFDQIE RDIMEDIMRI
WDTVIPPEEF INSPINRFFD FQFTSLPHYE HFYENFVEEV NLMKKKFDPK NKDTYFLPQY
NKEIPADGLS CFCEQIWETI KDNKDLDLPS QREMLSRYRC TEISNQIYKE FNDSIKGEMK
ILKKGNIIED FKKVFTKQID AALERYKEVT ERYMETIVEE IEEQLKKQLC GLVESLFERQ
AELMEKAIGK RVKGEFTIIR NEYALLYNKK EFNPMKYQKY SQELSRTKAV IERDWRKQFD
DSVPKFLAEK TKEKFNSVCK DIGIAYEDSV SKMTEVMKQH FGDYLESTIK PKITPYLEAC
KKDMWKNIRN VINIQFTNGF NKLEEGFKTC SNMNKDTIEE EIKKSKTDIL NSIKELVIKR
KIELPYLLER KFNNMFRFDN KGLPRKWEPT DDVDTLYFAA RDETEDILDM YCYFRIEESD
DQYKFTINYR DGDLPSESIE TLPKGADEEK VILNHEERKE LIETLNGFFE KGYLIALREK
ENSEIKYQIP LYLIVLVVFF GFDEFIAILT NPLLFILTLI IGGGVYIGYK LNLGGVAKNY
IQYLLSMSLS STMEYLRTIP FFTPLIDKVW PKDDNNTEET QEEIK
