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 24-JAN-2024, entry version 63.
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}.
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; CM000312; EEQ46568.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YS65; -.
DR SMR; C4YS65; -.
DR PaxDb; 5476-C4YS65; -.
DR VEuPathDB; FungiDB:CAWG_04924; -.
DR HOGENOM; CLU_011270_0_0_1; -.
DR OMA; YAEGVWD; -.
DR Proteomes; UP000001429; Chromosome 6.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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 CDD; cd01851; GBP; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 InterPro; IPR046758; Sey1/RHD3-like_3HB.
DR PANTHER; PTHR45923; PROTEIN SEY1; 1.
DR PANTHER; PTHR45923:SF2; PROTEIN SEY1; 1.
DR Pfam; PF05879; RHD3_GTPase; 1.
DR Pfam; PF20428; Sey1_3HB; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
