SEY1_LACTC
ID SEY1_LACTC Reviewed; 783 AA.
AC C5DEL5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Protein SEY1 {ECO:0000255|HAMAP-Rule:MF_03109};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN Name=SEY1 {ECO:0000255|HAMAP-Rule:MF_03109};
GN OrderedLocusNames=KLTH0C10230g;
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284;
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
CC -!- FUNCTION: Cooperates with the reticulon proteins and tubule-shaping DP1
CC family proteins to generate and maintain the structure of the tubular
CC endoplasmic reticulum network. Has GTPase activity, which is required
CC for its function in ER organization. {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}. Note=Enriched in the cortical ER.
CC Concentrated in punctae along the ER tubules. {ECO:0000255|HAMAP-
CC 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}.
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DR EMBL; CU928167; CAR22226.1; -; Genomic_DNA.
DR RefSeq; XP_002552664.1; XM_002552618.1.
DR AlphaFoldDB; C5DEL5; -.
DR SMR; C5DEL5; -.
DR STRING; 559295.C5DEL5; -.
DR EnsemblFungi; CAR22226; CAR22226; KLTH0C10230g.
DR GeneID; 8291544; -.
DR KEGG; lth:KLTH0C10230g; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; C5DEL5; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000002036; Chromosome C.
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 GO; GO:0007029; P:endoplasmic reticulum organization; 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; 1.
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..783
FT /note="Protein SEY1"
FT /id="PRO_0000384984"
FT TOPO_DOM 1..679
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 680..700
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 701..703
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 704..724
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 725..783
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 35..265
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 752..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 783 AA; 89504 MW; 8E9FD17E8B38D49A CRC64;
MGETEEAIQL INEEKEFNSS TLQYFQKCVK ERDVGVDYHV ISVFGSQSSG KSTLLNALFH
TQFDTMNAKV KRQQTTKGIW LGHTTRIATL ENSLTPVKDL FVLDVEGSDG AERGEDQDFE
RKAALFAIAI SEVLIVNMWE QQVGLYQGNN MALLKTVFEV NLSLFGHQND HKVLLLFVIR
DHVGVTPLSS LQETLEAELN AIWSDLAKPE GCENSSLYDF FDLKFTALAH KVLQPDLFME
NVKELGNKFS SETPGKSFFK PEYHHNLPLD GWTMYAGNCW NQIETNKDLD LPTQQILVAK
FKTEEISNQA LALLLENYPV DLHCRELSDL AGKLQELKSL CLQEYDTYAS RYAKPVYMDN
RRDLSHKIEN KFKETISKFL DVQKEDLLSQ VEKDLTERSR STPFVTKMKE ARKKAFDAFE
ELLLQFTKLE LVASLSDENE AFSIALDEAC SNQSRKQLKQ SVNRISKSVS SGIKEDIFFL
LAHPELDLWD KVMEKFNEIV SDSTERYAVD DEKFDFQVGL SEEENQKVYK KVRSNAWTNL
YEFVHGYLNE DNVVSILRDR FENKFRYDEH DSPRLWRNEE EIDNAFRVAK EHALEVLNVL
SLASNSDHVE IVPDVPLSSG LDDEELEGEY EDEEGIYHEK GFAHILTASQ RERAVQKFKR
QANTTVIEAK RSIIRTTTHI PLYVYALLVV LGWNEFMIVI RNPLFVTLLV ILSVTAYFVH
KLNLWAPILA LVNSAVSETK ALARNKLKVI LDDDSSSSSK ASKEPTEEYE MQDLAKSSTT
GTG
