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
//