SEY1_BOTFB
ID SEY1_BOTFB Reviewed; 886 AA.
AC A6S544;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=BC1G_07815;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476885; EDN27958.1; -; Genomic_DNA.
DR RefSeq; XP_001553728.1; XM_001553678.1.
DR AlphaFoldDB; A6S544; -.
DR SMR; A6S544; -.
DR GeneID; 5434262; -.
DR KEGG; bfu:BCIN_15g01350; -.
DR VEuPathDB; FungiDB:Bcin15g01350; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
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; Transmembrane; Transmembrane helix.
FT CHAIN 1..886
FT /note="Protein sey1"
FT /id="PRO_0000384975"
FT TOPO_DOM 1..769
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 770..790
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 791..793
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 794..814
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 815..886
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 74..313
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 372..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 502..527
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COILED 722..743
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT BINDING 84..91
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 886 AA; 99373 MW; 356680AA8B1835BA CRC64;
MATANINGHG ERPSAVARFP TAPSVMTMNG NFASVGDAPT KEQYERGIQV IDEQKEFNPN
LNTYLQFTDT AHSGFNYHLI SVFGSQSTGK STLLNHLFGT QFGVMSERER RQTTKGIWMS
KNKNQSSGAS ESETMADNIL VMDVEGTDGR ERGEDQDFER KSALFALATS EVLIVNIWEH
QVGLYQGANM GLLKTVFEVN CQLFLKDKQS TPRSLLFFVI RDHLGTTPLA NLKDTLIQDL
TAIWTSLSKP AGLENSKIED YFDFAFAALP HKILQPDKFV TEVQKLGTRF RAGHKSTRAE
DAGFEGGVFL PEYHRRIPAD GFSVYAEGVW DQIVSNKDLD LPTQQELLAQ FRCDEISREV
LVSFDGKIQP LEEKQAEDTR SGKPTVIADL GSTGKTSRTS TVKNFETQAS RYHKGVYALK
RTELEGKIDT RLKALYHGQL VAAHKSGVAS FSDAVSNAVK LGQKRAASYE FADIVEREKE
TALKTFETEA KSLYIEGLAW TNFKSQYDLY EKDLNEVSGN LRKEEMRRLA TRVERWVRSR
LNDSIGVEFN KLGSGRGGSG APETGEKPAS EKDLWDRIWK TFVDTVKEAE SKFTDRAKSF
DASEDEIEVG LWRLKRKSWG VLRAKIDEEV MEGNILLKLR ENFEDKFRYD EAGVPRIWRP
SDDIEGIYTK ARESTLTLIP LLSKFKLSES SSLPELSEWI GSTPASVDPK DEEDLTPIGG
VDEEEGKSLE EEMTVLSEAK RQDLVVRFKK TADGVYVEAK RSAIGGVAQV PLYFYGLLLA
LGWNEIVAVL RNPIYFIFLI LCGIAGYVTY TLNLWGPIIR MMNAASTQGV EIGKEKLREF
LKDNEMGRQA LGMQGRDHGD SDGISLNTLD SRGKRASREE EEEEEI
