ID   SEY1_TALSN              Reviewed;         880 AA.
AC   B8MK20;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=TSTA_043120;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962657; EED14837.1; -; Genomic_DNA.
DR   RefSeq; XP_002484790.1; XM_002484745.1.
DR   AlphaFoldDB; B8MK20; -.
DR   SMR; B8MK20; -.
DR   STRING; 441959.B8MK20; -.
DR   EnsemblFungi; EED14837; EED14837; TSTA_043120.
DR   GeneID; 8104954; -.
DR   VEuPathDB; FungiDB:TSTA_043120; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   HOGENOM; CLU_011270_0_0_1; -.
DR   InParanoid; B8MK20; -.
DR   OMA; TNFDVMD; -.
DR   OrthoDB; 418635at2759; -.
DR   PhylomeDB; B8MK20; -.
DR   Proteomes; UP000001745; 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..880
FT                   /note="Protein sey1"
FT                   /id="PRO_0000385002"
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          68..307
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          846..880
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          463..517
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   COILED          812..839
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   COMPBIAS        859..873
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         78..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   880 AA;  99244 MW;  F63B5EC8C2D753C6 CRC64;
     MTDQRPRAES RSLTAPSLIG TNGHFASVGD AAHDPKAYEH GVQVIDEEKQ FNPNLSKYLS
     LENVANAGFN YHLISVFGSQ STGKSTLLNH LFGTQFSVMS DRERRQTTKG IWMSKNKTKH
     EDPNARMADN ILVMDVEGTD GRERGEDQDF ERKSALFALA TSEVLIVNIW EHQVGLYQGA
     NMGLLKTVFE VNLQLFLKDK NTTHRSLLFF VIRDFMGTTP LKNLEITLLE DLSRIWASLS
     KPQGLERSTI HDYFDFAFYG LPHKGYKPEE FAAEAKKLGS RFREGRRDRK EQLIGASIES
     GVFLPEYHRR IPADGFAHYA EGIWDQIVNN KDLDLPTQQE LLAQFRCDEI LREVLVAFDE
     AIVPFEEKQA AGVRAGEPTI LGGLGPAMRG ARTKAVKNFE TEASRYHKGV YQRKRTELEG
     KIDTRLKALF QGQLNAAHKS GVKDFSDAVS NAVKAGQKKG ASYDFAEIVK QETQAALERF
     EKEARATVVE GTAWSNYKQE LKLYQKDLGE VSGQLRRDEM RRLATRVERW VKSRLSHSVS
     LEFNSLGSGR GGSGAPETGD KPAENKIWDR IWNLFVQTVL DAERRFTDRA TSLDASVEEV
     DVGLWRLRRK SWSVLRLKIE EEMMEGNLLL KLRENFEDKF RYDEAGVPRI WRPTDDIEGV
     YTRARESTLT LIPLLSKFIL AENNSPPPLD RWIGHTPSSA TAADEEDLTP IGGVDAEDGR
     SLEEEMTILN DAKRQDLTVR FKKAADGVYV EAKRSAIGGI TQVPLYFYGL LLALGWNEIW
     AVLRNPAYFF LLFVCAVGAY VTYQLNLWGP MLKMADAASK QALEELKKRL REFLEASDTG
     RQAMAMSANA TGRDAGEEFE MSSLNRGGKK AEDEDENDDI