ID   SEY1_KOMPG              Reviewed;         785 AA.
AC   C4R432;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
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};
GN   OrderedLocusNames=PAS_chr3_0279;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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; FN392321; CAY70318.1; -; Genomic_DNA.
DR   RefSeq; XP_002492497.1; XM_002492452.1.
DR   AlphaFoldDB; C4R432; -.
DR   SMR; C4R432; -.
DR   STRING; 644223.C4R432; -.
DR   PRIDE; C4R432; -.
DR   EnsemblFungi; CAY70318; CAY70318; PAS_chr3_0279.
DR   GeneID; 8200107; -.
DR   KEGG; ppa:PAS_chr3_0279; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   HOGENOM; CLU_011270_0_0_1; -.
DR   InParanoid; C4R432; -.
DR   OMA; TNFDVMD; -.
DR   Proteomes; UP000000314; Chromosome 3.
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..785
FT                   /note="Protein SEY1"
FT                   /id="PRO_0000384996"
FT   TOPO_DOM        1..690
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        691..711
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        712..714
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        715..735
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        736..785
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          40..266
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   COILED          451..479
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   BINDING         50..57
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   785 AA;  90507 MW;  FEEAEB2711EB6ECB CRC64;
     MTDLEVSAIQ VIDENKVFNS LLVDYMKQFY SQNNSSDDKG LNYHIVSVFG SQSTGKSTLL
     NHLFHTKFDV MDESQRQQTT KGIWLAHANH ISSSNESGDF ANNTKNVFVM DVEGTDGRER
     GEDQDFERKA ALFALSTSEI LIINIWEHQV GLYQGANLGL LRTVFEVNLS LFAKNKQRCL
     LLFVIRDHVG NTSLESLSDV LTLDLQNIWS QLNKPQGTEG FELDDFFDLK FVALAHKLLQ
     PDKFIEDISV LGDKFISEDQ LFNEGYHRAI PIDGWSMYAE QVWEQIETNQ DLDLPTQQIL
     VARFRCDEIS SQVYESFHEQ FVKSNWDDLS FTEIGNSLKE LRQNAVQQYD ILAGRYSESV
     YLQRKKLLVQ KVDLSILEVY TSVLQKLIRQ SRDLYLKQIE SSLTKKEAGI IFYQVLDNAE
     RESLKYFNEN TSLISFVDVD DSEARSYDPS PKLRELEEEL SNLRTELVNK EQENIKTKIP
     RKFKSHFKLI VQDELSNIKP SSWEELLDQF RQVSEKLLAK YKSPDSNYDF HLGLSKEKNK
     ELHEQVLIKF WIKFKEILND FVTETNVLRL LVSKFEDEFR YDEEGLPVVW KNSAEIDVKF
     AKARNSALDL LPLFSLAHTA EGEILPDYDI AHDEAEAESD NEEDDGFKES HKFAHLLSAR
     DQDAIRNKFK KQTDALYVET KRSVINSKTE VPLYIYALLL VLGWNEFMII LRNPLLITLL
     LIGLTGLYLG YKTKLLGPIV QVVQAMIQEL QDQAKNKLRD VLVSEPEAPS QVRIGKEVDA
     TKDED