SEY1_LODEL
ID SEY1_LODEL Reviewed; 847 AA.
AC A5E240;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=LELG_03677;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
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; CH981527; EDK45498.1; -; Genomic_DNA.
DR RefSeq; XP_001525749.1; XM_001525699.1.
DR AlphaFoldDB; A5E240; -.
DR SMR; A5E240; -.
DR STRING; 379508.A5E240; -.
DR EnsemblFungi; EDK45498; EDK45498; LELG_03677.
DR GeneID; 5232322; -.
DR KEGG; lel:LELG_03677; -.
DR VEuPathDB; FungiDB:LELG_03677; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; A5E240; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
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; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..847
FT /note="Protein SEY1"
FT /id="PRO_0000384985"
FT TOPO_DOM 1..720
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 721..741
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 742..744
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 745..765
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 766..847
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 55..290
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 847 AA; 96261 MW; 740135CEF4220519 CRC64;
MSSGEPLSET SSSSSSFVPV DQVHLQDAIQ VIDENKHFNK DILGYINKTC PPNIGHNYHI
VAVFGSQSTG KSTLLNRLFN TNFDVMNEQS RQQTTKGIWL AQSPVLSTSH GHGASKSSIL
VMDVEGTDGR ERGEDQDFER KAALFALSTS EVLILNIWET QVGLYQGANM GLLKTVFEVN
LTLFGKSKLE SKNNLQSKSS HKVLLLVVIR DHVGNTPVEN LASTITIDLK KMWDSLLKPT
ELKELAFEDF FDLDFHALNH KILQPKEFTA GVGRLGDRLV VENDIFKPEY HHNIPIDGWT
LYAEKCWEQI ETNKDLDLPT QQILVAQFKC DEVVDTVFKE FSNKFKELFA VIEESPDYEN
VGALFSDLKS EVLEDYDQVA AKYNQSVYLQ KRQKLDDLVN TKLKEVFDVH AKNLLQHSLT
KYKKDLVALK GKDFAARSKS LSDEALELVM LNLSHISLSG AFATEILLHQ FASDIKAITS
QQQFIELNNI VSKAVKKLSQ SLSKLMQLQL NDPTEKTWDN ILYNFHQLQK EFTSKHNGDF
GLNTTEAENE NAFAKFKFQS WDAFYQLIHK LITKEKVLQQ LQTRFDDKFR YDVNGLPKLY
QNSRELEESF AVAKEHALGV LPILTIAKLS DDSEIIPDVD IFTKLLRVKY SASNRVGNYN
EEGGEEEEDE DEDEDDDVAL NGFADIIDEV EKAEIMAKFR KEIDAKFMET KRSIVQHVTQ
IPYYIYIIIL LLGWNEFMAV VRNPFTFSLA IILGASLYIL YTMNLLKPAL TVTQRLVDEV
IAVGKEKLRE VLIDDHHIQA HNLDKMTGKV KVGIHEENAK EDEDATDFLK PKPTQVDVTS
LNVVEEE
