ID   SEY12_ENTDS             Reviewed;         829 AA.
AC   B0EKR0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=EDI_026070;
OS   Entamoeba dispar (strain ATCC PRA-260 / SAW760).
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC PRA-260 / SAW760;
RA   Lorenzi H., Inman J., Schobel S., Amedeo P., Caler E.;
RT   "Annotation of Entamoeba dispar SAW760.";
RL   Submitted (DEC-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; DS549788; EDR24883.1; -; Genomic_DNA.
DR   RefSeq; XP_001738770.1; XM_001738718.1.
DR   AlphaFoldDB; B0EKR0; -.
DR   SMR; B0EKR0; -.
DR   STRING; 46681.XP_001738770.1; -.
DR   EnsemblProtists; EDR24883; EDR24883; EDI_026070.
DR   GeneID; 5883871; -.
DR   KEGG; edi:EDI_026070; -.
DR   VEuPathDB; AmoebaDB:EDI_026070; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   OMA; DIMEDIM; -.
DR   OrthoDB; 418635at2759; -.
DR   Proteomes; UP000008076; 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; 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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..829
FT                   /note="Protein SEY1 homolog 2"
FT                   /id="PRO_0000384945"
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..829
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          372..396
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   COILED          576..596
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   829 AA;  97184 MW;  D57B492E69603905 CRC64;
     MDEVSPTKHF TSKPLLPTKT PRDKAISHYV NALNSPRNVV KTEIPECGIQ IIDGDGNFAS
     TDTRERPSLK NYILSKPEFL KRGMDYNAVG ILGAQSSGKS TLLNYLFNTK FRILNEVMGR
     SRTTHGVWMA LSGKESNIVV FDLEGTDGSA REDDYSFERK TSLFSLSVCS VLMVNLWSHD
     VGRFQASNMS LLKTVFELNL QLFVKEETPK TLIVFVIRDR EADTPFDQIE RDIMEDIMRI
     WDSVIPPEKF INSPINRFFD FQFTSLPHYE HFYENFVEEV NLMKKKFDPK NKETYFLPQY
     NKEIPADGLS CFCEQIWETI KDNKDLDLPS QREMLSRYRC TEISNQIYKE FNDSIKGEMK
     TLKKGNIIEE FKKIMTKEID TAIEKYKEVT ERYMESIVEE IEEQLKKQLY GLVESLFERQ
     AELMEKAIGK RVKGEFTIIR NEYALLYNKK EFNPMKYQKY SQELSRTKAV IERDWRKQFD
     ESVPKFLAEK TKEKFNSVCK DIGIAYEDAV SKMAEVMKQH FGDYLESTIK PKITPYLEAC
     KKDMWKNIRN VINTQFTNGF NKLEEGFKTC SNMNKDTIEE EIKKSKIDIL NIIKELVIKR
     KTELPYLLER KFNNIFRFDN KGLPRKWEPT DDVDTLYFTA RDETEDILDM YCYFRIEEND
     DQFKFTINYR DGDLPSESIE ALPEGADEDK IILNHQERKE LIETLNEFFE KGYLIALREK
     ENSEIKYQIP LYLIVLVIFF GFDEFIAILT NPLLFILTLI IGGGIYIGYK LNLGGVAKNY
     IQYLLSMSLS STMEYLRTIP FFTPLIDKIW PKDDNKDDDS TEETQEETK