SEY1_ARTOC
ID SEY1_ARTOC Reviewed; 862 AA.
AC C5FJT2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 57.
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=MCYG_03762;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS995703; EEQ30943.1; -; Genomic_DNA.
DR RefSeq; XP_002848256.1; XM_002848210.1.
DR AlphaFoldDB; C5FJT2; -.
DR SMR; C5FJT2; -.
DR STRING; 63405.XP_002848256.1; -.
DR EnsemblFungi; EEQ30943; EEQ30943; MCYG_03762.
DR GeneID; 9229580; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000002035; Unassembled WGS sequence.
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..862
FT /note="Protein SEY1"
FT /id="PRO_0000384987"
FT TOPO_DOM 1..743
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 744..764
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 765..767
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 768..788
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 789..862
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 48..301
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 818..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 476..500
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 840..855
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 862 AA; 97154 MW; AC6BDE5833A671AF CRC64;
MASNGHFSSV GDVDGGNYQH GVQVVDGDKE FNPNLSKYLA HENVTPAGFN YHLISVFGSQ
STGKSTLLNT LFKTDFSVMS ETERRQTTKG IWLSKNKRTA SNEKEKMADN VLVMDVEGTD
GRERGEDQDF ERKSALFALA TSEVLIVNIW EHQVGLYQGA NMGLLKTVFE VNLQLFLKDT
KSTPRSLLFF VIRDFVGTTP LENLRNTLMQ DLQRIWMSLS KPEGTENSTI EDYFDFEFAG
LPHKSFQPEK FASEVDKLST RFRDGHRDPS STSAKGTAVE GGVFLPEYHR RIPADGFAVY
AEGIWDQIVN NKDLDLPTQQ ELLAQFRCDE IAREVLILFD ETIGPFEVQQ AEGVRSGIPL
ILGSLGVAMR AARGKTMTSF ETEASRYHKR VFMTKKSELE EKIDTRLKAL FSGQLSAAHK
SGVTQFSEAV SAAVKAGQKK GASYDFAEIV TRERKLAIEK FENEASTTMV EGAPWSDYKQ
ELSLFQKDLE KISSQLRKDE MRRLATRVER WVRSRLGDSI DLEFNALGSG RGGSRAPENG
DKPSEKTIWD RIWSLFVNTV LDAERRFTER ARSFDASLEE VDVGLWRLRR KSWGVLRSKI
EEEMMEGNIL HKLRENFEDK FRYDDVGVPR IWRPTDDIEG IYTTARESTL SLIPLLARFR
LNETSAPPPL DKWVGHMPSS ASAADEEDLA PIGGVDEDDG KSLEEEMTML SEAKRQDLTV
RFKKAADGVY VEAKRSAIGG ITQVPLYFYG LLLALGWNEI IAVLRNPIYF IFLLLIGVGA
YVTFRLNLWG PMINMAEAAS RQAVEEGKRR LREFLESSDS GRQAMAMSGR NARGTEEYEM
SSNLKSKGRR TDTSDDDNDD DL
