SEY1_ASHGO
ID SEY1_ASHGO Reviewed; 791 AA.
AC Q74ZD5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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}; OrderedLocusNames=AGR264C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54754.1; -; Genomic_DNA.
DR RefSeq; NP_986930.1; NM_211992.1.
DR AlphaFoldDB; Q74ZD5; -.
DR SMR; Q74ZD5; -.
DR STRING; 33169.AAS54754; -.
DR EnsemblFungi; AAS54754; AAS54754; AGOS_AGR264C.
DR GeneID; 4623232; -.
DR KEGG; ago:AGOS_AGR264C; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; Q74ZD5; -.
DR OMA; TNFDVMD; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IBA:GO_Central.
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..791
FT /note="Protein SEY1"
FT /id="PRO_0000155127"
FT TOPO_DOM 1..685
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 686..706
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 707..709
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 731..791
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 40..268
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 763..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..57
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 791 AA; 90062 MW; 60C4FCB6F8E45213 CRC64;
MSEDGASKCQ DSIQLIDEQK QFNEKTLEYF KRCIGERDVG LDYHVISVFG SQSSGKSTLL
NALFNTKFDT MNAQVKRQQT TKGIWIAHTR EVQTTANTGK GVDFFVLDVE GSDGAERGED
KDFERKAALF ALATSEVLIV NMWEQQVGLY QGNNMGLLKT VFEVNLSLFG HKKDKQKILL
LFVVRDFTGF TPLSSLQETL TNELQAMWSE LNKPAGAEGS SLDDFFDFAF TGLSHKLFKP
EEFASDVAKL GDKFTDLKRE DYYLSGKYHQ GLPLDGWSFY ADSCWEQIEN NKDLDLPTQQ
TLVANFKTEE IANNAFEHFS TAFSKLSSSL PGPELAASMK ELKDQCTKEY DNYGSRYMKA
VYLEKRGELL DKIKTKFSDA IAVHMSKLFN SLVSTFQSTV AQNAACQPLS ERLKVGKERV
MQVFEQETSD FVALELIPSV DADASALLEK IDELAERERG KEMKAIILRA KKYQFTHTRD
DIVHLLSHPQ DNVWQLVMDH FDDVFRRSVL KYKLPNLGDV TDESTAYDFQ LDLIEEDNYA
LYLKIRSNAW TILYDIIHQY LKEDNVVSIL RERFESKFRY DQNDVPRLWK NEEEVDAGFK
VAREHALNML NTLSIASCDG VEIVPDVPLA SDEDEAQDEQ GLYNEKRFGH ILTAIQKEKI
IQHFKRFANV AVVEAKRSTI KSHTHIPMWI YAIIAVLGWN EFMLVLRNPL FIALMLLIVG
AAYTVHRLNL WTPLATFASA AVNETTHAVK AKLRTILLDD EHPKNASSKP VESFEMQDLS
VNETKENANE S
