SEY1_KLULA
ID SEY1_KLULA Reviewed; 786 AA.
AC Q6CJ97;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=KLLA0F20317g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG98700.1; -; Genomic_DNA.
DR RefSeq; XP_455992.1; XM_455992.1.
DR AlphaFoldDB; Q6CJ97; -.
DR SMR; Q6CJ97; -.
DR STRING; 28985.XP_455992.1; -.
DR EnsemblFungi; CAG98700; CAG98700; KLLA0_F20317g.
DR GeneID; 2895475; -.
DR KEGG; kla:KLLA0_F20317g; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; Q6CJ97; -.
DR OMA; TNFDVMD; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:EnsemblFungi.
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:0048309; P:endoplasmic reticulum inheritance; IEA:EnsemblFungi.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IEA:EnsemblFungi.
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..786
FT /note="Protein SEY1"
FT /id="PRO_0000155134"
FT TOPO_DOM 1..684
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 685..705
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 706..708
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 709..729
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 730..786
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 35..262
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 765..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 355..375
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT BINDING 45..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 786 AA; 89177 MW; 97D50D5828665670 CRC64;
MSDLKEAIQL IDENKQFNPS TLNYFTKCLG DKNVGVKYHV ISVFGSQSSG KSTLLNKLFD
TKFDTMDAQV KRQQTTRGIW LSHSANIYSS GAANQSIPDF FVLDVEGSDG AERGEDQDFE
RKAALFALSV SEVLIVNMWE NQVGLYQGNN MGLLKTVFEV NLSLFGKNEN RHKVALLFVI
RDFTGQTPLE SLEASLVLEL EKMWSQLSKP EGCEDTSFHD FFVPNFFGLG HKVFQPEQFD
NDVKSLGDLF VDQDASFFKD EYHTHLPLDG WSLYAENCWE QIENNKDLDL PTQQILVARF
KTDEIAAAAY NKFLNDYQSQ VTDSLDGKEL ATVLKTLQST CIDVDYDPFA SRYAKKVYEE
RRDDLIKQLN TIIDETITNF VTRTTSSLIE TFHKNARDRS LKGPFKLKIQ SALEKASRTF
KTNLAPFSEL ELLSSMDAYI SKFEARVNTE VADLQERELN AIVARFNKGL TIKLKDTILH
LLAKPTINVW DDVMKEFTSF LDGSLKKYTN EDGKIDFQTG ATTDANDKTE HTLKRNAWSF
LDHTVHGYLT EDNVVDIMRN VFNDKFRYDD DGMPKFWKNE AEVDASYRLA KSQALSVLDA
LAIVKNKDNV EILIPEALLE SDGDGSDYEE NGGQEEEEAG LYHQQRFSHV LSALQKDKII
TKFKQFTDLV IIEAKRSIVN TTERIPLYMY ALVVALGWGR IITILRNPAT IILSIIVLAG
AYFVHKLNLW GPLLQFANQA TGQATAVLKQ TVRSLVVDEE PKRKILVEPH ESEGVDKEPS
KNDQHL
