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Database: UniProt
Entry: E9B2F8_LEIMU
LinkDB: E9B2F8_LEIMU
Original site: E9B2F8_LEIMU 
ID   E9B2F8_LEIMU            Unreviewed;       893 AA.
AC   E9B2F8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Protein SEY1 homolog {ECO:0000256|HAMAP-Rule:MF_03109};
DE            EC=3.6.5.- {ECO:0000256|HAMAP-Rule:MF_03109};
GN   ORFNames=LMXM_31_0370 {ECO:0000313|EMBL:CBZ29421.1};
OS   Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ29421.1, ECO:0000313|Proteomes:UP000007259};
RN   [1] {ECO:0000313|EMBL:CBZ29421.1, ECO:0000313|Proteomes:UP000007259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|EMBL:CBZ29421.1,
RC   ECO:0000313|Proteomes:UP000007259};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
CC   -!- FUNCTION: Probable GTP-binding protein that may be involved in cell
CC       development. {ECO:0000256|HAMAP-Rule:MF_03109}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|HAMAP-Rule:MF_03109}; Multi-pass membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_03109}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03109}.
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DR   EMBL; FR799584; CBZ29421.1; -; Genomic_DNA.
DR   RefSeq; XP_003877877.1; XM_003877828.1.
DR   AlphaFoldDB; E9B2F8; -.
DR   GeneID; 13453466; -.
DR   KEGG; lmi:LMXM_31_0370; -.
DR   VEuPathDB; TriTrypDB:LmxM.31.0370; -.
DR   OMA; YHVVGVF; -.
DR   OrthoDB; 1606at2759; -.
DR   PhylomeDB; E9B2F8; -.
DR   Proteomes; UP000007259; Chromosome 31.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01851; GBP; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   InterPro; IPR046758; Sey1/RHD3-like_3HB.
DR   PANTHER; PTHR45923; PROTEIN SEY1; 1.
DR   PANTHER; PTHR45923:SF2; PROTEIN SEY1; 1.
DR   Pfam; PF05879; RHD3_GTPase; 1.
DR   Pfam; PF20428; Sey1_3HB; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51715; G_GB1_RHD3; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW   Rule:MF_03109};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_03109};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03109};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03109};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03109};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_03109};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_03109}.
FT   TOPO_DOM        1..757
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT   TRANSMEM        774..795
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        779..781
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        803..893
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT   DOMAIN          52..321
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51715"
FT   REGION          135..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         62..69
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   893 AA;  97929 MW;  FFEFB5313166D4AC CRC64;
     MGLYLVDSDG HLQSEKRLKE YLTTIVAPSV SQSGSVATAD DGDDDSALEA IGVNYHVVGV
     FGGQSSGKST LLNHLFGTDF QTLDETVRRG QTTKGAFMAR ASNSLAGFEA SSAAVGADRL
     ASGAADRSSR LNRAAAAAET KDAADGERGE PHTASPLLVL DFEGTDGLER GEDQWFERQL
     SLFGLSIADI LIINMWAVDV GRFNAANLSL LRTIFEVNLQ LFSHDNYKAE EMPTLLIVLR
     DFTDGDPAPS LATMRKSFDK IWEGITRPAQ FSGASIDALF HLKYYVMPHY KLQRTEFMTS
     VETLRRWFGD SQCPDYLFSH HAMFRGVPLE GLPAYLTNCW EAIRTSKDLD IPTQREMLAQ
     HRCKEAKVQE LKTFRHFAQH YEDRLLRGEM LLRLSEVLEE EMETRLTSFY RQTKLYKSDV
     VGQYANELET ELVDATMQVL NRLSKAIATE VLSNVESRVL NSVEESLRQL LKSAQTLPFS
     AGEGPSAAEA AEANDVEGGA APLVGAQRMD SPSCQKLVRG FWRSLSSHVN EVVAEVAALP
     PRAHVYGRYV ALIAQDPTAR LNVLNIVTDA LFQKVKSRMV SMADSACDTM HTGFERSLTH
     NSDGTARFFA TTKGLQKAVP AAMQAGVVVL GSLFYFRLKL VAASADDDGI GADADGAALP
     QSRSARRVRH DRHRIVFSDN DAEAAFYLSY STLDTVPKYP YDVPVTCVDC GGEEVGAATD
     CILLSQQGTV RAYELYKQKC DFTTQLQLRA VEAGKQRLPA WVIPALFILG WNELLYVLTS
     PALLVLVVVI CAVFFKQFFV SQWRAFEETG PASVVIPTKA VIHTLSTLVR PLLDYGTGPC
     RESTERGHDA AGAGERAMSH AGGAPTHVDP TPGNANVPTA PATIRHRTSR KLD
//
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