ID   SEY1_LEIIN              Reviewed;         895 AA.
AC   A4I7K1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Protein SEY1 homolog {ECO:0000255|HAMAP-Rule:MF_03109};
DE            EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN   ORFNames=LinJ32.0740, LinJ_32_0380;
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5;
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Sqaures R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM70785.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; FR796464; CAM70785.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001467720.1; XM_001467683.1.
DR   AlphaFoldDB; A4I7K1; -.
DR   SMR; A4I7K1; -.
DR   STRING; 5671.XP_001467720.1; -.
DR   GeneID; 5071778; -.
DR   KEGG; lif:LINJ_32_0380; -.
DR   VEuPathDB; TriTrypDB:LINF_320008800; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   InParanoid; A4I7K1; -.
DR   Proteomes; UP000008153; Chromosome 32.
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   Pfam; PF05879; RHD3; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51715; G_GB1_RHD3; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..895
FT                   /note="Protein SEY1 homolog"
FT                   /id="PRO_0000384950"
FT   TOPO_DOM        1..759
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        760..780
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        781..783
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        784..804
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        805..895
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          52..323
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          839..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..857
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..887
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         62..69
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   895 AA;  98351 MW;  3E0F2B3367C5C8B9 CRC64;
     MSLHLVDSDG HLQSEKRLKE YLTTIVAPSV SQSGSAATAD DGDGDSALEA IGVNYHVVGV
     FGGQSSGKST LLNHLFGTDF QTLNEAVRRG QTTKGAFIAR ANDALAGFEA SGASVVADQL
     ASGAADHSSC LNRAAAAAAA ATKDAAYGEH GAPHTVPPLL VLDFEGTDGL ERGEDQCFER
     QLSLFGLSIA DTLIINMWAV DVGRFNAANL SLLRTIFEVN LQLFSHDNYE AEEKPTLLIV
     LRDFTEDDPA PSLATVRKSF DTIWEGITRP AQFAGASIDA LFHLKYYVMP HYKLQKTEFM
     PSVETLRRWF GDSQCPDYLF SHRAMFRGVP LEGLPAYLTN CWEAIRTSKD LDIPTQREML
     AQHRCKEAKV QELKTFRHFA RHYEDRLLHG EMLLRLSEVL DEEMETRLAS FYRQTKLYNS
     DVVGQYANEL ETELVDATLR VLNRLSKAIA AEVLSNTEPR VLNSVEESLR QLLKSAQTLP
     FSAGEGPSAA EAEEANDVER DAAHLVGAQR MDSPACQKLV RSFWRSLSSY VNEVVAEVAA
     MPPRAHLYGR YVALIAQDPT TRLNVLNIVT DALFQKVKSR VVSMADSACD TMHAGFERSL
     THNSDGTARF FATTKGLQKA VPAAMQAGVV VLGSLFYFRL KLVAAGADDD GIGADVAGTA
     LPQSRSARRV RHDQHRIVFS DNDAEAAFYL SYSTLDTAPK YPYDVPVTSA DCEGEEAGAV
     ADCILLSQQA IVRAYELYRQ KCDFTTQLQL RTVEAAKQRL PAWVIPALFI LGWNELLYVL
     TSPALLVLVV VICAVFFKQF FVSQWHAFEE TGPASVVIPT KTVIHTLSTL VRSLLDYRPG
     PRTERTERSH DAAAAAEKEM PHVAATATHV DPTLGNANVP TAPSTMRHRT SRKLD