ID   SEY11_PARTE             Reviewed;         752 AA.
AC   A0BKG2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Protein SEY1 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03109};
DE            EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN   ORFNames=GSPATT00029660001;
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2;
RX   PubMed=17086204; DOI=10.1038/nature05230;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
CC   -!- FUNCTION: Probable GTP-binding protein that may be involved in cell
CC       development. {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}.
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; CT868000; CAK59029.1; -; Genomic_DNA.
DR   RefSeq; XP_001426427.1; XM_001426390.1.
DR   AlphaFoldDB; A0BKG2; -.
DR   SMR; A0BKG2; -.
DR   STRING; 5888.CAK59029; -.
DR   PRIDE; A0BKG2; -.
DR   EnsemblProtists; CAK59029; CAK59029; GSPATT00029660001.
DR   GeneID; 5012211; -.
DR   KEGG; ptm:GSPATT00029660001; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   HOGENOM; CLU_378813_0_0_1; -.
DR   InParanoid; A0BKG2; -.
DR   OMA; TNFDVMD; -.
DR   Proteomes; UP000000600; Partially assembled 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   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..752
FT                   /note="Protein SEY1 homolog 1"
FT                   /id="PRO_0000384952"
FT   TOPO_DOM        1..674
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        675..695
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        696..698
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        699..719
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        720..752
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          40..265
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   COILED          445..465
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   752 AA;  88194 MW;  39FB9EC1F5BCF531 CRC64;
     MIKNQGDRYH LIDKNALEEK KLDSNELTEF VKSSGLIDIG KKYNIVSIIG SQSTGKSTLL
     NYLFGTQFDV QNRQQSVGQT TVGIWISKDV KNNVVVLDVE GSDSVERKSG ENMVENQTAL
     MALAMSHCFI INVFVNALGQ HTSCQLSIIK IIMQQNLKLF QQDTVKHIIF VVRDWDEEYN
     YDEASRKLNG YLLNIWNEIP KPDQYRETDF HELFSVQVVT LVYYKLKNEF AEQTNQLHSK
     LANQQDPNFI FKDFDYEKNV RWSDMPQYLS NIWVVIANNK DLNLPNEKIL ISNMRCQQIK
     LEALEGVKDL TEDLQNRVRT QFVENFGQQC LSILGVAQKI YDKDAKDYHA DVYKEKEKEL
     RDELMNKFYT YFQRQTESLK QHYMNRLSEN LETLKRESIY DLPDKLNEVD LLKVNFEESL
     SKSVIEKGLW QEQDHVGFFN QQFDNQLKSF VEAQLASFKQ QLDNIIKSEC DKIVSQQVLN
     ISPKFWSQID ADYYTMISDK YSKYDALLSG LRVQWKQIDD YLSKFEEDSF HNLKQVIAVA
     SGRFKDQLFQ QFKAQFVRTE DGQPRNWQKT TEEEIFHIYT EARDKVFSFL DILRIRKVKF
     IRIQQTMKKI AKTHLAPFTP LKEKISYQIS ADTDSDDVVL NEVFYTQVKM QLAEDIDVQY
     QDAIQKHKQD FLQNIPKPFW FLLLFFMYDD VLRWMGNPLF LYPILIILCF IGFCIAIGLH
     SLPKLAFQTV FRTINQALLP LIFGGISKLK TS