SEY1_ASPNC
ID SEY1_ASPNC Reviewed; 858 AA.
AC A2QR20;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
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; ORFNames=An08g04480;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270168; CAK45421.1; -; Genomic_DNA.
DR RefSeq; XP_001392566.1; XM_001392529.2.
DR AlphaFoldDB; A2QR20; -.
DR SMR; A2QR20; -.
DR PaxDb; A2QR20; -.
DR PRIDE; A2QR20; -.
DR EnsemblFungi; CAK45421; CAK45421; An08g04480.
DR GeneID; 4982765; -.
DR KEGG; ang:ANI_1_652074; -.
DR VEuPathDB; FungiDB:An08g04480; -.
DR HOGENOM; CLU_011270_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 8R.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:EnsemblFungi.
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:0048309; P:endoplasmic reticulum inheritance; IEA:EnsemblFungi.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IEA:EnsemblFungi.
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 Coiled coil; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..858
FT /note="Protein sey1"
FT /id="PRO_0000384972"
FT TOPO_DOM 1..742
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 743..763
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 764..766
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 767..787
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 788..858
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 50..300
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 669..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 475..504
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT BINDING 60..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 858 AA; 96379 MW; CD24EA674FCAE4A8 CRC64;
MATNGHFAAI GNGSSDKTAY EHGVQVIDEN KEFNANLSKY LTLEDVTPAG FNYHLISVFG
SQSTGKSTLL NHLFGTQFSV MSELERRQTT KGIWMSKNKN GGDSSMADNI LVMDVEGTDG
RERGEDQDFE RKSALFALAT SEVLIVNIWE HQVGLYQGAN MGLLKTVFEV NMQLFLKDRA
TSHRSLLFFV IRDFVGNTPL QNLQRTLMED MSRLWDSISK PAGLEHSSVH DYFDFQFYGL
PHKSYQPEQF VAETKKLSLR FREGQKDPSL DARKGEFSDG GVFLPEYHRR IPADGFSHYA
EGIWDQIVNN KDLDLPTQQE LLAQFRCDEI LREVMVAFDE AIVPFEDKQS QAARLGEPEI
LGGLGAAMRA SRSKAFKSFE TEASRYHKGV YQRKRAELES KIDTRLKALF QGQLDATHKS
GITEFSEAVS GAVKAGQKKG TGYDFAEIVN EEVTKAVQKF KEVAHETAVE GAAWSDSQQQ
LALYEKELAE VSARLRREEM RRLASRVERW VQSRLGESVG LEFNALGSGR AGGGAPEEGE
KPTEKKFWDR VWNVFVETVL DAERRFTDRA SSFDASLEEV DVGLWRLRRK SWGVLRAKID
EEMVEGNLLL KLRENFEDKF RYDDAGVPRI WRPTDDIEGI YTRARESTLT LIPLLSRFRL
AETSAPPPLD RWVGHTPSSA TAADEEDLPP IGGVDEEEGK SLEEEMTILS ESKRQELTVR
FKKAADGVYV EAKRSAIGGM TQVPLYFYGI LLALGWNEIV AVLRNPAYFF LLFVCLVAGY
VTYQLNLWGP IMKMTEAASN QALVEGKKRL REFLESSDTG RQAIAMSTAG GAGRGEQVEM
SRLNKQGKTT AEDEDGDL
