ID   SEY12_PARTE             Reviewed;         749 AA.
AC   A0E2L1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Protein SEY1 homolog 2 {ECO:0000255|HAMAP-Rule:MF_03109};
DE            EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN   ORFNames=GSPATT00022700001;
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; CT868655; CAK89528.1; -; Genomic_DNA.
DR   RefSeq; XP_001456925.1; XM_001456888.1.
DR   AlphaFoldDB; A0E2L1; -.
DR   SMR; A0E2L1; -.
DR   STRING; 5888.CAK89528; -.
DR   PRIDE; A0E2L1; -.
DR   EnsemblProtists; CAK89528; CAK89528; GSPATT00022700001.
DR   GeneID; 5042710; -.
DR   KEGG; ptm:GSPATT00022700001; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   HOGENOM; CLU_378813_0_0_1; -.
DR   InParanoid; A0E2L1; -.
DR   OMA; DERPDNI; -.
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..749
FT                   /note="Protein SEY1 homolog 2"
FT                   /id="PRO_0000384953"
FT   TOPO_DOM        1..671
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        672..692
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        693..695
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        696..716
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        717..749
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   749 AA;  88274 MW;  A397A41BAE823159 CRC64;
     MIKNYGDRYH LIDKKALEDK KLDKDQLVEF VRTSGISDIG KNYNIVSIIG SQSTGKSTLL
     NQLFGTKFDV QNRQQSVGQT TVGIWLSKDV QNNVVVLDVE GSDSVERKSG ENMVENQTAL
     MALAMSHCFI INVFLNALGQ HTSCQLSIIK IIMQQNLKLF QQDTVKHIIF VVRDWDEDAN
     YEEASRRLNG YLLNIWNEIP KPDHYKETDF HQLFSVQVVT LVYYKMKKEF IEQTNDLHAK
     LSNQQDPNFI FKDFDYEKNV RWSDMPQYLS NIWEVISNNK DLNLPNEKIL ISNMRCQQIK
     LEALDGVKQL NEDLQNRVRT KLVDNFAQEC QTIMNLAFKL YDKDARDYHI EVYKEKEKEL
     KDELVNRFYT YFQKQTEQLK QHYMNTLTEN LETLKRESIY NLPDKLNELD LFKLQFEEQL
     AKSVIQKGLW QEEDHIRYFR QQFDNQLKAF VEAQLATFKQ QLDNIIKSEC DKIVSSQVLN
     ISSKFWQQIE SDYYAMISEK YQKYEVLLTG LRVQQKQIED YLNKFEEDSF HNLKQVIAVA
     SGRFKDQLFQ QFKAQFVRAP DGQPRNWQKL TEEEIFHCYT DARDKVFQLL DSLRIRKIKF
     IRQQVVLKKK AQTLIISSSQ KVQYQISSDA DSDDVVLNDV FYTQVKMQLA EDIDVQYQDA
     IQKHKQDFLQ NIPKPFWFLL LFFMYDDVLR WMGNPLFLYP ILIILCFVGF CIAIGLHSLP
     KLAFQWVFRT LNQAVIPIIF GGISKLKGS