ID   SEY1_CANDC              Reviewed;         790 AA.
AC   B9WJF2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=CD36_65490;
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(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; FM992693; CAX41375.1; -; Genomic_DNA.
DR   RefSeq; XP_002421214.1; XM_002421169.1.
DR   AlphaFoldDB; B9WJF2; -.
DR   SMR; B9WJF2; -.
DR   STRING; 42374.XP_002421214.1; -.
DR   EnsemblFungi; CAX41375; CAX41375; CD36_65490.
DR   GeneID; 8048665; -.
DR   KEGG; cdu:CD36_65490; -.
DR   CGD; CAL0000164118; Cd36_65490.
DR   VEuPathDB; FungiDB:CD36_65490; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   HOGENOM; CLU_011270_0_0_1; -.
DR   OrthoDB; 418635at2759; -.
DR   Proteomes; UP000002605; Chromosome 6.
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..790
FT                   /note="Protein SEY1"
FT                   /id="PRO_0000384977"
FT   TOPO_DOM        1..692
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        693..713
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        714..716
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        717..737
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        738..790
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          55..284
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   BINDING         65..72
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   790 AA;  89983 MW;  FEE0B236A9F97D20 CRC64;
     MELSEGELSH TSSSSSFVPV DQRQLQDAIQ IIDEDKHFNT GILDYINKTS PADVGNNYHI
     ISVFGSQSTG KSTLLNRLFN TNFDVMDESN RQQTTKGIWL AYSPVVSTTS GHTTSKSNIL
     VMDVEGTDGR ERGEDQDFER KAALFALSTS EILIINIWET QVGLYQGANM GLLKTVFEVN
     LSLFGKSKLE KHNEHKVLLL IVIRDHVGVT PVESLAKTFT SDLQNMWGSL SKPAELEHLR
     FADFFDVSFH ALNHKVLQPK EFGEGINKLG DRLVVNNELF KPEYHHDVPI DGWTMYAERC
     WEQIETNKDL DLPTQQILVA QFKCDEIVEG VFQEFLSKYQ HHFKEVDVDV DFAELGELFV
     DLRSDSLEDY DVSASRYNKA VYEQKRAKLR GLINDKLKEV FDVHAKKLCD TLLETFQKDL
     VALKGKDFAV NVKALSTKLV EQVVDTLSLM SLHGDISSNE ITSGLSKEID ATIAKQQVIE
     LNSIVNKSVK KLSGSLSKSI QFELGDPNDE TWDNVLQMFK ESYDKFGGDF GLGTSTTQNE
     QAIERFKFKS WCQFYDVTRK LISKEKLLAL LQDRFDDKFR YDENGLPKLY LNEQDLEKTF
     AVAKQYALQV LPILTLAKLA DGSEIVPEYD IFDSKLREEF LGAYDDSDDE DDHCFAEVVT
     EQEKSEVLAK FKKEVDAKYI ETKRSIVQHI TQIPYYIYLI ILVLGWNEFM AIIRNPLFFS
     LSIVLGATVY VLYYLNLLKP AMLVAQRTMD EVIIMAKTKL REVLIDDHEV TGRQLNKIAG
     GKENIELDDM