SEY1_SCLS1
ID SEY1_SCLS1 Reviewed; 888 AA.
AC A7ERA6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-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; ORFNames=SS1G_07860;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
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; CH476630; EDN91998.1; -; Genomic_DNA.
DR RefSeq; XP_001591234.1; XM_001591184.1.
DR AlphaFoldDB; A7ERA6; -.
DR SMR; A7ERA6; -.
DR STRING; 665079.A7ERA6; -.
DR PRIDE; A7ERA6; -.
DR GeneID; 5487333; -.
DR KEGG; ssl:SS1G_07860; -.
DR VEuPathDB; FungiDB:sscle_11g082800; -.
DR InParanoid; A7ERA6; -.
DR OMA; TNFDVMD; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
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 Coiled coil; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..888
FT /note="Protein sey1"
FT /id="PRO_0000385001"
FT TOPO_DOM 1..771
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 772..792
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 793..795
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 796..816
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 817..888
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 76..315
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 724..745
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 709..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86..93
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 888 AA; 99696 MW; 0E1267CD88A98024 CRC64;
MDMATSNING HGDRPSPAAR FPTAPSVMTM NGNFASVGDA PTKEQYEHGI QVIDEQKEFN
PNLNEYLQYT DTAHSGFNYH LISVFGSQST GKSTLLNHLF GTQFGVMSER ERRQTTKGIW
MSKNKNQSSG ASESETMADN ILVMDVEGTD GRERGEDQDF ERKSALFALA TSEVLIVNIW
EHQVGLYQGA NMGLLKTVFE VNCQLFLKDK QSTPRSLLFF VIRDHLGTTP LANLKETLIQ
DLSAIWTSLS KPAGLENSKI EDYFDFAFAA LPHKILQPDK FITEVQKLGT RFRAGRKSAR
AEDAGFEGGV FLPEYHRRIP ADGFAVYTEG VWDQIVNNKD LDLPTQQELL AQFRCDEISR
EVLISFDAKI HPLEEKQGED VRSGKPTVIA DLGVTGKTAR TSTIKHFETQ ASRYHKAVYT
LKRTELEGKI DTRLKLLFHG QLLAAHKSGV ASFSDAVSTA VKNGQKRAAS YEFADIVERE
KEVALKTFEA EMKSLYIEEL SWTNFSSSYD LFEKDLNEVS GNLRKEEMRR LATHVERWVR
SRLNDSIGVE FNKLGSGRGG SGAPETGEKP ATEKDLWDRI WKTFTGTVKE AESKFIERAK
SFDASEDEIE IGLWRLRRKS WGVLRAKIDE EVMEGNILLK LRENFEDKFR YDEAGVPRIW
RPSDDIEGIY TKARESTLTL IPLLAKFKLL ETSSPPELPE WIGNTPASVD PKDEEDLTPI
GGVDEEEGKS LEEEMTVLSE AKRQDLVVRF KKTADGVYVE AKRSAIGGVA QVPLYFYGLL
LALGWNEIVA VLRNPIYFVF LILCGVAGYV TYTLNLWGPI IRMLNAASTQ GVEIGKEKLR
EFLKDSEVGR QALGMQGRDA GDSDAISLNT LDSRGKRVVR EDEDVDEI
