SEY1_ZYGRC
ID SEY1_ZYGRC Reviewed; 794 AA.
AC C5DTA7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
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=ZYRO0C06908g;
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229;
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; CU928175; CAR27018.1; -; Genomic_DNA.
DR RefSeq; XP_002495951.1; XM_002495906.1.
DR AlphaFoldDB; C5DTA7; -.
DR SMR; C5DTA7; -.
DR STRING; 559307.C5DTA7; -.
DR EnsemblFungi; CAR27018; CAR27018; ZYRO0C06908g.
DR GeneID; 8203157; -.
DR KEGG; zro:ZYRO0C06908g; -.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; C5DTA7; -.
DR Proteomes; UP000008536; 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 Coiled coil; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..794
FT /note="Protein SEY1"
FT /id="PRO_0000385008"
FT TOPO_DOM 1..687
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 709..711
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 712..732
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 733..794
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 43..272
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 770..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 331..352
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT BINDING 53..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 794 AA; 91948 MW; 81ECEE65AF4B75D9 CRC64;
MMEVIDSVLG DRQSAIQLID ESKKFHQDAL NYFNKCIDDR DVGLDYHVIS VFGSQSSGKS
TLLNHLFNTD FDTMDAQVKR QQTTKGIWLA HTRKVNTTHK LDGPASDLFV LDVEGSDGAE
RGEDQDFERK AALFAISVSE VLIVNMWEQQ IGLYQGNNMA LLKTVFEVNL SLFGKSHNGH
KVLLLFVIRD HVGITPLSSL KESLIAELEK VWSELNKPVE CEDSSLYDFF DLEFVGLGHK
LLQAEQFQEG VKRLGDSFAL KSANPYYFKP QYHHNLPLDG WIMYSENCWE QVENNRDLDL
PTQQILVARF KTDEVAQEAL SLFHSKYSGS VDHILDDREK LGEVLKNLKQ ECLIYYDERA
YRYAEPVYLE KRSELAAKME AEFRKTIGNF LDQLSESLMQ RLQTEVLDKK NQHLPFQKRT
KILVQSTKEE YWTAVSSFQQ LELLRSTEEI LQHFDEQVDT KIKQLKNDEV NTLIARANKS
ITLKVKEQAV HYLSNPERDT WDKILDMFEK TIQSSLSKYE ISEGHYDFQV GFTEEENDSV
YKKVCSRAWH VLNVTVHDYL KPDTIVSILR DRFETKFRYD EDDSPRLWRN EDEIDRAFRI
AKDHALEVLN VLSFAATSDH VEIVPAFGED NHEEDECYED ELGIQHSRHF AHILNELQKE
KVLQQFRRQI NLTVLDSKRS IIKTTTAIPI WMYLLVVALG WNEFVMVLRN PLLVTLVLLF
GVGFIFVNKF GLWGPVLNVA HNAVAEVRIT AKEKLRAIVM DEDEKRHLIN SAGKESYEMK
DMSDSDNEKI EKSE
