ID   SEY1_VANPO              Reviewed;         780 AA.
AC   A7TJY3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, 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}; ORFNames=Kpol_1037p42;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS480404; EDO17445.1; -; Genomic_DNA.
DR   RefSeq; XP_001645303.1; XM_001645253.1.
DR   AlphaFoldDB; A7TJY3; -.
DR   SMR; A7TJY3; -.
DR   STRING; 436907.A7TJY3; -.
DR   EnsemblFungi; EDO17445; EDO17445; Kpol_1037p42.
DR   GeneID; 5545665; -.
DR   KEGG; vpo:Kpol_1037p42; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   HOGENOM; CLU_011270_0_0_1; -.
DR   InParanoid; A7TJY3; -.
DR   OMA; TNFDVMD; -.
DR   OrthoDB; 418635at2759; -.
DR   PhylomeDB; A7TJY3; -.
DR   Proteomes; UP000000267; 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..780
FT                   /note="Protein SEY1"
FT                   /id="PRO_0000385004"
FT   TOPO_DOM        1..680
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        681..701
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        702..704
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        705..725
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        726..780
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          35..265
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          756..780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          440..463
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   BINDING         45..52
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   780 AA;  90129 MW;  68544BCCFBC55DE9 CRC64;
     MDSKEEAIQL ITEEKHFSDD ALAYFKTCIG GRDVGVNYHV ISVFGSQSSG KSTLLNILFN
     TSFDTMDAQI KRQQTTKGIW VAHSNELLSN VDVNPEDKSD LFILDVEGSD GLERGEDQDF
     ERKAALFAIS VSEVLIVNMW EQQIGLYQGN NMALLKTVFE VNLSLFGKNK NGHKVLLLFV
     IRDHVGVTPI SSLRDTITTE LINLWETLSK PAECENKKLS DFFELQFVGL SHKLLQEERF
     VQDVKSLGDH FIMKDNEDYY FKPEYHHNLP LDGWTLYAKN CWELIEENRD LDLPTQQILV
     ARFKTEEILN DSLEVLKSKY DSNVDPVIKD KLKLIQELSV LKTECLDMYD QHASKYVSAV
     YLEKRDELEA KIYLKFLETI TLFIDSVSQD IFLQLVEDVN SESSKEPIFS KRLSNSTEVA
     KSKFEDIIEE FAAAKILSEE VKEEVVKRFE NDLKETSDKL RVTALQKLIT RSSKIINARI
     KDVVPQLLSN PDVDVWDRIM DKFHSIFSST LIKYKLDDDT YDFQFGGEDE ENNSTYKSIR
     VAAWKSLNDT IHDYLKEDTI CNILRDRFEL KFRYDDEDSP ILWKNEEEVD LAFRVAKEYA
     FKIFDVLALI KTSDNVEVVP DINFHDSDEM YEDDLGIYHS AKFSHILNEV QKEKIQIQVR
     RQINVTVLDA KRSMIKTTTH IPLWIYAIIV VLGWNEFMMV IRNPLFVTLT ILILVSFYFI
     NKFDLWGPVK SVAQTAAGET IGTIKTKLRD FVLEEHEKTP KIQSEKSNSD SEKVVENEKS