SEY1_MAGO7
ID SEY1_MAGO7 Reviewed; 848 AA.
AC Q525S7; A4R1C1; G4MNV9;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=MGG_06979;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; CM001231; EHA57116.1; -; Genomic_DNA.
DR RefSeq; XP_003709728.1; XM_003709680.1.
DR AlphaFoldDB; Q525S7; -.
DR SMR; Q525S7; -.
DR STRING; 318829.MGG_06979T0; -.
DR EnsemblFungi; MGG_06979T0; MGG_06979T0; MGG_06979.
DR GeneID; 2685152; -.
DR KEGG; mgr:MGG_06979; -.
DR VEuPathDB; FungiDB:MGG_06979; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; Q525S7; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000009058; Chromosome 1.
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 Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..848
FT /note="Protein SEY1"
FT /id="PRO_0000155135"
FT TOPO_DOM 1..733
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 734..754
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 755..757
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 758..778
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 779..848
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 47..277
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 815..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 848 AA; 95441 MW; 93E390C2455C2F15 CRC64;
MNGNFAAVGS EPTDAQFEHG IQVIDEDKQY NGLVNDYLRR THVAEAGFNY HLISVFGSQS
TGKSTLLNNL FGTEFSVMSE SERRQTTKGI WMSKNKREGK MAENILVMDV EGTDGRERGE
DQDFERKSAL FALATSEVLI VNIWEHQVGL YQGANMGLLK TVFEVNLQLF LKDKQSSPRS
LLFFVIRDHI GNTPLSNLRN TLVQDLTKIW SSISKPPALE NAKIEDYFDF AFAALPHKIL
QPEKFVTEVE NLGTRFVAGH RSTQDQEFVG GVFLPEYHRR IPADGFSIYA EGIWDQIVNN
KDLDLPTQQE LLAQFRCDEI SRDVLNAFDE AITPLEDKQA EASRLGKPFV LPDLGDTARS
ARSKAVEAFK VQASRYHKGV YTRKQAELEG KMDSRLKALY QGQLAAAHKA GVAAFSDAVT
GAVKAGQKSG GSYEFAEIVD KQKRKTLDIF AKEAQGLEIE GLAWTNFKPQ FLLFEKELDE
VSARLRKDEM RRLATRVERW VKSRLGDSIG LEFNKLGSGR GGSGAPETGE KPATEKDLWD
RIWTVFVAVV KEAQERFAER AKSFEASSEE VEIGLWRLRR KSWVALRERI DEEVMEGNIL
LKLRENFEDK FRYDEAGVPR IWRPTDDIEG IYTRARESTL TLIPLLSRFR LAETYASPDL
PGWIGNQPPG VEPDDEEDLT PIGGIDEEEG KSLEEEMTVL SESKRQDLVV RFKKTADGVY
VEAKRGALGG MTQVPLYFWI ALFAFGWNEI WMVIRNPFLF ILLLLSAGGT YVAYNLSLLG
PMMQMTNAAA NQASEIGKQK LREFLENNET ARQALAMPAS SKSSGGEQVR MDTLDSKGKK
KDYDDDGI
