SEY1_PENRW
ID SEY1_PENRW Reviewed; 880 AA.
AC B6GX67;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=Pc12g14980;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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; AM920427; CAP81125.1; -; Genomic_DNA.
DR RefSeq; XP_002558301.1; XM_002558255.1.
DR AlphaFoldDB; B6GX67; -.
DR SMR; B6GX67; -.
DR STRING; 1108849.XP_002558301.1; -.
DR EnsemblFungi; CAP81125; CAP81125; PCH_Pc12g14980.
DR GeneID; 8308318; -.
DR KEGG; pcs:Pc12g14980; -.
DR VEuPathDB; FungiDB:PCH_Pc12g14980; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
DR BioCyc; PCHR:PC12G14980-MON; -.
DR Proteomes; UP000000724; Contig Pc00c12.
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:0007029; P:endoplasmic reticulum organization; IEA:UniProtKB-UniRule.
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..880
FT /note="Protein sey1"
FT /id="PRO_0000384992"
FT TOPO_DOM 1..762
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 763..783
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 784..786
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 808..880
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 66..320
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 496..519
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COILED 856..880
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 853..880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76..83
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 880 AA; 99102 MW; 6958256990B57E57 CRC64;
MAERRPSGLE RSPTAPPVLS NGHFASIGAE GDASSYEHGV QVIDENKEFN PDLSKYLSLE
NVTPAGFNYH LISVFGSQST GKSTLLNHLF GTQFSVMSEL ERRQTTKGIW LSNNKKQGDA
GSAERMADNI LVMDVEGTDG RERGEDQDFE RKSALFALAT SEVLIVNIWE HQVGLYQGAN
MGLLKTVFEV NLQLFLKDKH TTHRSLLFFV IRDFIGTTPL KNLQKTLLED LSRLWDTISK
PAGLEKSTIH DYFDFQFYGL PHKGYQPDQF VTEANKLGLR FREGHRDPKR DALKGEFSEG
GVFLPEYHRR IPADGFSHYA EGIWDQIVNN KDLDLPTQQE LLAQFRCDEI LREVMIGFDE
AITAFEDKQA ESVRVGAPEV LGGLGVAMRA ARVKTLKSFE TEASRYHKGV YQRKSAELQG
KVDTRLKALF HGQLSAAHKS GIRDFSDSVS AAVKDGQKKG GSYDFAEIVA KETQSSLEKF
EEVAHSTLVD GASWSNCTQE LSLFKKELAE VSARLRRDEM RRLATRVERW VQSRLGESVG
LEFNALGSGR AGGGAPENGE KPTEKDFWDR IWNLFEETVL DAERRFTDRA SSFDASIDEV
DVGLWRLRRK SWGVLRAKIE EEMIEGNLLL KLRENFEDKF RYDEAGVPRI WRPTDDIEGI
YTRARESTLT VIPLLSRFRL ERTTAPPPLD RWIGHTPSTA TPADEEDLAP IGGVDEHEGK
SLEEEMTILS DAKRQELTVR FKKAADGVYV EAKRSAIGGM TQVPLYFYGL LLALGWNEIW
AVLRNPAYFI LLFAFAIGAY ITYQLNLWGP MLKMTEAASQ QALEEGKRRL REFLESSDTG
RQAIAMSAGE RAGSSGRKEE YEMSDMQKRA SNANDDLDDM
