SEY1_DEBHA
ID SEY1_DEBHA Reviewed; 847 AA.
AC Q6BK59;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 92.
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=DEHA2F24640g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382138; CAG89823.2; -; Genomic_DNA.
DR RefSeq; XP_461412.2; XM_461412.1.
DR AlphaFoldDB; Q6BK59; -.
DR SMR; Q6BK59; -.
DR STRING; 4959.XP_461412.2; -.
DR EnsemblFungi; CAG89823; CAG89823; DEHA2F24640g.
DR GeneID; 2903782; -.
DR KEGG; dha:DEHA2F24640g; -.
DR VEuPathDB; FungiDB:DEHA2F24640g; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; Q6BK59; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000000599; Chromosome F.
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..847
FT /note="Protein SEY1"
FT /id="PRO_0000155132"
FT TOPO_DOM 1..741
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 742..762
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 763..765
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 766..786
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 787..847
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 66..297
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76..83
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 847 AA; 96057 MW; 4E503EA6492B1A09 CRC64;
MSTGHKSLSP SDFVNDENQS VGSSSSSFVP VEQNSENAIQ MINENKQFNE SILNYIEKST
SSSDIGNNYH IISVFGSQST GKSTLLNHLF NTNFDVMDES KRQQTTKGIW MAHSPLVSST
LTNGSKSEEN IFVMDVEGTD GRERGEDQDF ERKAALFALS TSEILIINIW ETQVGLYQGA
NMGLLKTVFE VNLSLFGKSK LDKNDHKVLL LFVIRDHIGV TPLENLAATL TQDLVAMWDS
LNIPPELSHL QFQDFFDIAF HTLGHKVLQP EKFTDDIKLL GNKIIDMHDS GYLFKKNYHH
NIPVDGWTMY AESCWNQIDN NKDLDLPTQQ ILVAKFKCDE ILNLVYDEFV LGFNEHLLAD
APSKSSDTET SIDYSELGLS FMQMRNATLE NFELAASKYN QSVYEQKRAA LSLKINNKFS
ELFEIYVKDL VDKYTKSFTD TVSFGKKKLQ GNTFHEGITN LQESIFQEFS QNIALISLNG
DLEYDNHVKG LQLKLEQMVS KQQIVELNSI ITKSLKKLNN GLGKVIVEEL NDPKSDTWDN
ILEKFKSYVD STVSKYEVGA GEYDFGLGTS LQSNIGAINK FKYKSWVSFH ELIHKYISKD
NVLNSLKDRF DDKFRYDENG LPRLYQNGHE LDNSFNESKS YAMDILPVLT IAKLSDGTEI
LPDYDIFDKR LRNQYGGASV VTADDQQISI DTDSEDEEEE NPCFAEILSE SDKAAILAKF
KKEINAKFVE TKRSIIQNVT QIPYYIYLVI LVLGWNEFMA IIRNPLFFTL ALLLGAGAYV
MYHLNLLKPA SIVAQRMIDE SIVLAKQKLK EFLLDEPETH GHNLNKISGN KTPPEDESIE
LDNLDPK
