SEY1_LEIMA
ID SEY1_LEIMA Reviewed; 891 AA.
AC Q4Q5P8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 66.
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=LmjF32.0370, LmjF_32_0370;
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin;
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B.G., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
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=CAJ08501.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; FR796428; CAJ08501.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001685350.1; XM_001685298.1.
DR AlphaFoldDB; Q4Q5P8; -.
DR SMR; Q4Q5P8; -.
DR STRING; 5664.LmjF.32.0370; -.
DR EnsemblProtists; CAJ08501; CAJ08501; LMJF_32_0370.
DR GeneID; 5656146; -.
DR KEGG; lma:LMJF_32_0370; -.
DR VEuPathDB; TriTrypDB:LmjF.32.0370; -.
DR VEuPathDB; TriTrypDB:LMJLV39_320008900; -.
DR VEuPathDB; TriTrypDB:LMJSD75_320008900; -.
DR eggNOG; KOG2203; Eukaryota.
DR InParanoid; Q4Q5P8; -.
DR Proteomes; UP000000542; Chromosome 32.
DR GO; GO:0005737; C:cytoplasm; ISO:GeneDB.
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:0005739; C:mitochondrion; ISO:GeneDB.
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..891
FT /note="Protein SEY1 homolog"
FT /id="PRO_0000384951"
FT TOPO_DOM 1..756
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 757..777
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 778..780
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 781..801
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 802..891
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 52..321
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT BINDING 62..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 891 AA; 97934 MW; B42AB853748A6A0D CRC64;
MSLHLVDADG HLHSEKRLKE YLTTIVAPSV SQSGSAATAD DGDGDSTLEA IGVNYHVVGV
FGGQSSGKST LLNHLFGTDF QTLNEAVRRG QTTKGAFMAR ANDALAGVEA SSAAVVADRL
ASGAADRSSC LNRAAAAAAT KDVADGAHGA SRTASLMLVL DFEGTDGLER GEDQCFERQL
SLFGLSIADT LIINMWAVDV GRFNAANLNL LRTIFEVNLQ LFSHDKYEAE EKPTLLIVLR
DFTEDDPAPS LATVRKSFDT IWEGITRPAQ FAGASIDALF HLKYYVMPHY KLQKTEFMTS
VETLQRWFSD SQCPDYLFSH RAMFRGVPLE GLPAYLTSCW EAIRTSKDLD IPTQREMLAQ
HRCKEAKMQE LKAFRHFARN YEDRLLHGEM LLRLSEVLDE EMETRLTSFY RQTKLYNSDV
VGQYANELET ELVNATMRVL NRLSKAIAAE VLSNAEPRVL NSVEESLRQL LKSAQTLPFS
AGEGPGAAEA AEVNDVEGDA AHLVGAQRMD SPACQKLVRS FWRSLSRHVN EVVAEVAAMP
PRAHLYGRYV ALIAQDPTTR LNVLNIVTDA LFQKVKSRMV SMADSACDTM HAGFERSLTH
NSDGTARFFA TTKGLQKAVP AATQAGVVVL GSLFYFRLKL VAAADDDGIG ADAAGTALPQ
SRSARRVRQD RHRILFNDND AEAAFYLSYS TFDTAPKYPY DVPVRSADCD GEEAGAAADC
ILLSQQATVR AYELYRQKCD FTTQLQLRTI EAGKQRLPAW VIPALFILGW NELLYVLTSP
ALLVLVVVIC AVFFKQFFVS QWHAFEETGP ASVVIPTKTV IHTLSTLVRP LLDYGPGPRT
ERTERSHDAA AAVEEMSHVE ATCTHVDPTL GSANLPAAPA TMRHRTSRKL D
