SEY1_CANTT
ID SEY1_CANTT Reviewed; 808 AA.
AC C5MCD3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 55.
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}; ORFNames=CTRG_03725;
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG692398; EER33300.1; -; Genomic_DNA.
DR RefSeq; XP_002549428.1; XM_002549382.1.
DR AlphaFoldDB; C5MCD3; -.
DR SMR; C5MCD3; -.
DR STRING; 5482.XP_002549428.1; -.
DR EnsemblFungi; EER33300; EER33300; CTRG_03725.
DR GeneID; 8297859; -.
DR KEGG; ctp:CTRG_03725; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
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 Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..808
FT /note="Protein SEY1"
FT /id="PRO_0000384978"
FT TOPO_DOM 1..701
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 723..725
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 726..746
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 747..808
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 57..286
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 808 AA; 91668 MW; C6E276AA1074614D CRC64;
MSSELSEGEL SHTSSSSSFV PVDQRQLQDA IQIINEEKRF NQSVLEYINK TAPADVGNNY
HIISVFGSQS TGKSTLLNKL FNTNFDVMDE SNRQQTTKGI WLAFSPVVST TSGHTSSKSN
ILVMDVEGTD GRERGEDQDF ERKAALFALS TSEILIINIW ETQVGLYQGA NMGLLKTVFE
VNLSLFGKSK LEKHDDHKVL LLIVIRDYVG VTPVESLAKT FTQDLINMWA SLAKPAELEH
LQFADFFDVD FHALNHKVLQ PKEFSEGINK LGDRLVVGDE LFKPEYHHQV PIDGWVMYAG
NCWEQIETNK DLDLPTQQIL VAQFKCDEIV ENVFQEFLKK FEQLFGEPQA EPDYEQIGAL
FSDLRNDTLE DYDISASKYN KSVYEQKRVK LISLVNEKFK EVFDFYAKEL SSTMLKKFHS
DVVALKGKNF AASVKELSTG LIASIVTTLG LISLQGDLSS NEVTTALSKD IADIVSKQQV
IELNSIVNRA VKKLTNSLSK SIQFELGDPN ENTWDTVLQQ FNSLSQEVLT KYDGDFGLGT
TDEQNKQALD RFQFKSWTSF YESMHKLISK EKLLVLLQDR FDDVFRYDEN GLPKLYLNEA
DLEKTFTESK QHALKVLPIL TIAKLSDGSE IVPEIDIFDH KLREKYLGVA DEDSDDEDDD
EHCFAEIVTE QEKSEVLAKF KKEVDAKYIE TKRSIVQHIT QIPYYIYLVI VFLGWNEFMA
IIRNPLLFSL ALLLGASVYI LYKLNLLKPA IVVAQRTFDE TVAMGKEKLR EILIDDHETQ
GRNLGKIAGK NPSAPAEEYS DNIELDDM
