ID   SEY1_YEAS1              Reviewed;         776 AA.
AC   B3LJJ8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Protein SEY1 {ECO:0000255|HAMAP-Rule:MF_03109};
DE            EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
DE   AltName: Full=Synthetic enhancer of YOP1 protein {ECO:0000255|HAMAP-Rule:MF_03109};
GN   Name=SEY1 {ECO:0000255|HAMAP-Rule:MF_03109}; ORFNames=SCRG_01558;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cooperates with the reticulon proteins RTN1 and RTN2 and the
CC       tubule-shaping DP1 family protein YOP1 to generate and maintain the
CC       structure of the tubular endoplasmic reticulum network. Has GTPase
CC       activity, which is required for its function in ER organization.
CC       {ECO:0000255|HAMAP-Rule:MF_03109}.
CC   -!- SUBUNIT: Interacts with RTN1 and YOP1; GTP binding is not required for
CC       these interactions.
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; CH408045; EDV10751.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LJJ8; -.
DR   SMR; B3LJJ8; -.
DR   EnsemblFungi; EDV10751; EDV10751; SCRG_01558.
DR   HOGENOM; CLU_011270_0_0_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..776
FT                   /note="Protein SEY1"
FT                   /id="PRO_0000385005"
FT   TOPO_DOM        1..681
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        682..702
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        703..705
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        706..726
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        727..776
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          34..263
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   BINDING         44..51
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   776 AA;  89438 MW;  68AC66F440CE7202 CRC64;
     MADRSAIQLI DEEKEFHQSA LQYFQQCIGN RDVGLDYHVI SVFGSQSSGK STLLNVLFNT
     NFDTMDAQVK RQQTTKGIWL AHTKQVNTTI EIDNDRPDIF VLDVEGSDGS ERGEDQDFER
     KAALFAIAVS EVLIVNMWEQ QIGLYQGNNM ALLKTVFEVN LSLFGKNDND HKVLLLFVIR
     DHVGVTPLSS LSDSVTRELE KIWTELSKPA GCEGSSLYDY FDLKFVGLAH KLLQEDKFTQ
     DVKKLGDSFV MKGTENYYFK PQYHHRLPLD GWTMYAENCW DQIERNKDLD LPTQQILVAR
     FKTEEISNEA LEEFISKYDE SIAPLKGNLG SLTSQLVKLK EECLTKYDEQ ASRYARNVYM
     EKREALNTNL NSHISGTINE FLESLMEKLW DDLKLEVSSR DKATTSFVES VAAGKSKIEK
     EFNESMETFK KLGLLISNEE ITCKFSDDIE ERIKQLRDAE LKAKIGRIKK NLVPELKDHV
     IHLLSHPSKK VWDDIMNDFE STIKDNISAY QVEKDKYDFK IGLSESENAK IYKNIRILAW
     RTLDTTVHDY LKIDTIVSIL RDRFEDVFRY DAEGSPRLWK TEEEIDGTFR VAKEHALEVF
     EVLSLAVTSD NVEIIPDVPM AEEESGEDNE IYRDNEGVFH SRRFAHILTE LQKENVLDQF
     RRQINITVLD SKRSIITTRT HIPPWIYVLL AVLGWNEFVA VIRNPLFVTL TLILGATFFV
     IHKFGLWGPV VNVVQSAVGE TRTAIKDKLR QFVVEDHEVK ESFEMKDFSK NEQKEK