ID   SEY1_CANAW              Reviewed;         790 AA.
AC   C4YS65;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=CAWG_04924;
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1;
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}.
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DR   EMBL; CM000312; EEQ46568.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4YS65; -.
DR   SMR; C4YS65; -.
DR   STRING; 5476.C4YS65; -.
DR   EnsemblFungi; EEQ46568; EEQ46568; CAWG_04924.
DR   VEuPathDB; FungiDB:CAWG_04924; -.
DR   HOGENOM; CLU_011270_0_0_1; -.
DR   OMA; TNFDVMD; -.
DR   Proteomes; UP000001429; 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_0000384976"
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;  90211 MW;  CAE6F08A21FE7A47 CRC64;
     MELSEGELSH TSSSSSFVPV DQRQLQDAIQ IIDENKHFNT GILDYINKTS PADVGNNYHI
     ISVFGSQSTG KSTLLNRLFN TNFDVMDESN RQQTTKGIWL AYSPVVSTTL GHTTSKSNIL
     VMDVEGTDGR ERGEDQDFER KAALFALSTS EVLIINIWET QVGLYQGANM GLLKTVFEVN
     LSLFGKSKLE THNDHKVLLL IVIRDHVGVT PVESLAKTFT SDLQNMWSSL AKPAELEHLQ
     FADFFDVTFH ALNHKVLQPK EFGEGINRLG DRLVVSNELF KPEYHHDVPI DGWTMYAERC
     WEQIETNKDL DLPTQQILVA QFKCDEIVES VFQEFLAKYQ HHFKEVDAAP DFEELGALFA
     DLRQDAFEDY DASASRYNKA VYEQKRKKLR WLINDKLKEV FDVHAKNLCN TLLEKFEKDL
     VALKGKDFAV NVKTLSTKLV EDVNFQVSLM SLQGDLSLDE IILALTKDID AIVAKQQVIE
     LNSIVNKSVK KLSASLSKSI QFELGDPNEE TWDNVLQQFK GVYEKFGGDF GLGTSSTQNQ
     QAIEKFKFKS WCQFYDVTHK LISREKLLAL LQDRFDDKFR YDENGLPKLY LNEQDLEKTF
     AVAKQHALQV LPILTFAKLT DGSEIVPDYD IFDSKLREQF LGGYDDSDDE EDHCFAEIIT
     EQEKSEVLAK FKKEVDAKYI ETKRSIVQHI TQIPYYIYLI ILVLGWNEFM AIIRNPLFFS
     LSIVLGATVY VLYYLGLLRP ALVVAQRTMD EVIVMAKTKL REVLIDDHEV TGRQLNKMAG
     SKENIELDDM