ID   SEY1_LEIBR              Reviewed;         891 AA.
AC   A4HK17;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 2.
DT   03-AUG-2022, entry version 64.
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=LbrM32_V2.0440;
OS   Leishmania braziliensis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC   Leishmania braziliensis species complex.
OX   NCBI_TaxID=5660;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904;
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FR799007; CAM42839.2; -; Genomic_DNA.
DR   RefSeq; XP_001567402.2; XM_001567352.2.
DR   AlphaFoldDB; A4HK17; -.
DR   SMR; A4HK17; -.
DR   STRING; 5660.A4HK17; -.
DR   GeneID; 5418325; -.
DR   KEGG; lbz:LBRM_32_0440; -.
DR   VEuPathDB; TriTrypDB:LbrM.32.0440; -.
DR   VEuPathDB; TriTrypDB:LBRM2903_320009100; -.
DR   VEuPathDB; TriTrypDB:LBRM2903_320009200; -.
DR   InParanoid; A4HK17; -.
DR   Proteomes; UP000007258; 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   PANTHER; PTHR45923; PTHR45923; 1.
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_0000384949"
FT   TOPO_DOM        1..754
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        755..775
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        776..778
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        779..799
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        800..891
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          52..318
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          863..891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..883
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   891 AA;  98289 MW;  90B66C6D73DF844B CRC64;
     MNLHLVDSDG HLEAEKKLTE YLTSIVAPSV SPSRGSATAD GDYGNGALEA VGLNYHVVGV
     FGGQSSGKST LLNHLFGTHF QMLDETVRRG QTTKGAFMAL ANTALAGLEA SDVAVVAPRL
     APSAADRSSR LNHAVAAAVT NNTTGGAPPT GSPLLVLDFE GTDGLERGED QCFERQLSLF
     GLSIVDTLII NMWAVDVGRF NAANLSLLRT IFEVNLQLFS HSNYEAEEKP TLLVVLRDFT
     EDDPLPSLTT VRKSFDTIWE SITRPAQFED TSIDALFHLK YYVMPHYRLQ KEEFMASVET
     LRRWFGDSRC SDYLFSYHSM FRGVPLDGLP AYLTNCWAAI RTSKDLDIPT QREMLAQHRC
     KEAKEQELMT YRDFARGYED RLLRGEMLLR LSEVLDEEME TRLTAFYRQT KLYSSAVVGQ
     YANELETELV DATMQVLNRL SKAIATEVLS NVESRVLNSV EESLRQLLKS AQTLPFSAGE
     DSSTTEPAEA HDADEDAARL LGAQRMDSAA CQRLVRGFWR TLSIQVKEVV AEVAAMPPRA
     HLYGRYAVLI VQDPTTRLNV LNIVTDAFFQ KVKSRLVSMA NSACDTMHSG FERSLTYNSD
     GTVRFFATTR GLQKAVPAAV QAGLVVLGSL FYFRLKLVSA AVSDDDDLDT GATAALPQSR
     SARRVRHNRC HIVFDDNDAE AAFYLSYSTL DTAPKYPCDV PVPTLDCDRE EVGVAADCVL
     LSQQATVRAY ELYKQKCDFT TQLQLRAAEA GNQRLPAWVI PALFILGWNE LLYVLTSPAL
     LVLVVVICAV FFRQFFVSQW HAFEETGPAS VVIPVRTVVH ALSALVRSLL GDGQGSCPER
     AARNGSDVVA SGEREMAHVK VTSTHADPAP SNTTVPTAQA TMRHRTTHKL D