ID   SEY11_ENTDS             Reviewed;         956 AA.
AC   B0E843;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Protein SEY1 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03109};
DE            EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN   ORFNames=EDI_213660;
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; DS548107; EDR29291.1; -; Genomic_DNA.
DR   RefSeq; XP_001734534.1; XM_001734482.1.
DR   AlphaFoldDB; B0E843; -.
DR   SMR; B0E843; -.
DR   STRING; 46681.XP_001734534.1; -.
DR   EnsemblProtists; EDR29291; EDR29291; EDI_213660.
DR   GeneID; 5879449; -.
DR   KEGG; edi:EDI_213660; -.
DR   VEuPathDB; AmoebaDB:EDI_213660; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   OMA; TNFDVMD; -.
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..956
FT                   /note="Protein SEY1 homolog 1"
FT                   /id="PRO_0000384944"
FT   TOPO_DOM        1..764
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        765..785
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        786..788
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        789..809
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        810..956
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          120..358
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          906..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          8..84
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   COMPBIAS        915..929
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         130..137
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   956 AA;  111873 MW;  960646B705615FBB CRC64;
     MQESELLHNQ LKVEELKKEE EIENNLEKKK TPGIDMKRVN LIKKRDEDII AENIQGELKE
     EERENIKVKE KEIKEEKKEK ENYPCMQIID QEGIFADENQ KERITFEEFI QENTKFKELG
     FNYNMLSILG PQNSGKSTLL NYLFDTDFTV LNEKNGRQRT TRGVWLGLVG DRKDIIIMDL
     EGSDGSIRED DLSFERKISL FSLSVCSVLM VNIWSHDVGR YGASNMSLLK NIFELNLQLF
     QKEDSPKTLI LFVIRDRDQK KPFENTKSVL LEDIMKIWDN VARPECFKRA PIDKFFDLEF
     TSLPHFKHDK ELFIQEVKEL KKRFDCKNQN TYFRSIYNKE IPADGLALFT KQVWSSIKSN
     KDLDLPSQKE MLARFRCDEL IENIFNEFEK EIEEIKIKHS EKHIFNNFKI FCDCLYDKKM
     KEFMNIASKY LDRVVKEKAD LLSEKMLNEI SYLFQTQMTL AINYIKTMLT TSYVTLKNQY
     ITEQSSLFDP TKYAGYAEQM DDFNITIKNE WEKISTQSVP SNIENNFEIE INTLDRFINK
     LYEIGRRDLI EALMTHFKKH LQNIMKPLLL PLFEQSNKNM WEQVRKIVLE TTSQNLQELE
     NGMINSLKMN KDDVEKKLNE LQVYIIDAVR STILERPGFV SNLMENKFIS IFRLDNEGLP
     KKWKQNEDLS KPYFKAKAEA EKILDLFSYI RMDPKDDNFS FISINPATGK KMIIEEPENG
     VIDQTKVLFS LSERLSIYEG FQNMAEANFM RAQQELAAIT VHSKTPMWLI LLIAFLSFDN
     IVYVLKSPTL LALTLIIIAI IYSLNKFGYA YLIDSVISFI LSISWSSVLY LIQDLGLFKN
     LLPKPEAPKR KRPQKKIQDD KPKSPLLVTH KKLPSVMGDV TIDNIDSLNS FDDAFKLVGH
     DEKPIRKPFR PLPNRETQSM RNIPTSASFT KSQSMFIKRN ITTASSLNKP NETKEF