ID   SEY1_TALMQ              Reviewed;         873 AA.
AC   B6QIM3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 60.
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=PMAA_098060;
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEA23218.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DS995902; EEA23218.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002149385.1; XM_002149349.1.
DR   AlphaFoldDB; B6QIM3; -.
DR   SMR; B6QIM3; -.
DR   STRING; 441960.B6QIM3; -.
DR   EnsemblFungi; EEA23218; EEA23218; PMAA_098060.
DR   GeneID; 7026923; -.
DR   KEGG; tmf:PMAA_098060; -.
DR   HOGENOM; CLU_260035_0_0_1; -.
DR   OrthoDB; 418635at2759; -.
DR   Proteomes; UP000001294; 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..873
FT                   /note="Protein sey1"
FT                   /id="PRO_0000384993"
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..873
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          68..320
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          691..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..873
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          462..519
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   COILED          812..839
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   BINDING         78..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   873 AA;  98535 MW;  56C812CB47890EFF CRC64;
     MVDQRPRAGS RSFTAPSLIG TNGHFASVGD AAHDPKAYEH GVQVIDEEKE FNPNLSKYLS
     LEDVTNAGFN YHLISVFGSQ STGKSTLLNH LFGTQFSVMS DKERRQTTKG IWMSKNKTKH
     EDPNARMADN ILVMDVEGTD GRERGEDQDF ERKSALFALA TSEVLIVNIW EHQVGLYQGA
     NMGLLKTVFE VNLQLFLKDK NTTHRSLLFF VIRDFMGNTP LKNLETTLLE DLSRIWASLS
     KPQGLERSTI HDYFDFAFYG LPHKGYKPDE FAAEAKKLGS RFREGRRDRK EQLMGASIEN
     GVFLPEYHRR IPADGFAHYA NGIWDQIVNN KDLDLPTQQE LLAQFRCDEI SREVIAAFDE
     AIAPFEEKQA AGVRAGELVI LGGLGAAMRG ARVKAVKNFE TEASRYHKGV YQRKRAELEG
     KIDTRLKALF QGQLNAAHKS GVKDFSDAVS NAVKAGQKKG ASYDFAEIVK QETKAALERY
     EKEARASLVE GTSWSNYKQE LKLYQKDLAE VSGQLRRDEM RRLATRVERW VRSRLSDSVS
     LEFNSLGSGR GGSGAPETGE KPSESKIWDR IWNLFVETVL DAERRFTDRA TSFDASVDEV
     DVGLWRLRRK SWGVLRLKVE EEMMEGNLLL KLRENFEDKF RYDEAGVPRI WRPTDDIEGI
     YTRARESTLT LIPLLSKFHL AENNAPPPLD RWVGHTPSSA TAADEEDLTP IGGVDEEDGK
     SLEEEVTILN DAKRQDLTVR FKKAADGVYV EAKRSAIGGI TQVPLYFYGL LLALGWNEIW
     AVLRNPAYFF LLFVCAIGAY VTYQLNLWGP ILKMADAASR QALEELKKKL REFLEASDTG
     RQAMAMSSGE EYEMSSLNRG GKRVEDEDEN DDI