ID   SEY1_PLACH              Reviewed;         913 AA.
AC   Q4XZY3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Protein SEY1 homolog {ECO:0000255|HAMAP-Rule:MF_03109};
DE            EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN   Name=SEY1 {ECO:0000250|UniProtKB:A0A509AN59}; ORFNames=PC000321.02.0;
OS   Plasmodium chabaudi.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=5825;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS;
RX   PubMed=15637271; DOI=10.1126/science.1103717;
RA   Hall N., Karras M., Raine J.D., Carlton J.M., Kooij T.W.A., Berriman M.,
RA   Florens L., Janssen C.S., Pain A., Christophides G.K., James K.,
RA   Rutherford K., Harris B., Harris D., Churcher C.M., Quail M.A., Ormond D.,
RA   Doggett J., Trueman H.E., Mendoza J., Bidwell S.L., Rajandream M.A.,
RA   Carucci D.J., Yates J.R. III, Kafatos F.C., Janse C.J., Barrell B.G.,
RA   Turner C.M.R., Waters A.P., Sinden R.S.;
RT   "A comprehensive survey of the Plasmodium life cycle by genomic,
RT   transcriptomic, and proteomic analyses.";
RL   Science 307:82-86(2005).
CC   -!- FUNCTION: Probable GTP-binding protein involved in generating and
CC       maintaining the structure of the tubular endoplasmic reticulum network.
CC       {ECO:0000250|UniProtKB:A0A509AN59}.
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; CAAJ01002020; CAH77527.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4XZY3; -.
DR   SMR; Q4XZY3; -.
DR   PRIDE; Q4XZY3; -.
DR   VEuPathDB; PlasmoDB:PCHAS_1027400; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   HOGENOM; CLU_312978_0_0_1; -.
DR   InParanoid; Q4XZY3; -.
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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..913
FT                   /note="Protein SEY1 homolog"
FT                   /id="PRO_0000384954"
FT   TOPO_DOM        1..825
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        826..846
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        847..849
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        850..870
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        871..913
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          33..288
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          89..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          636..659
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   COILED          703..727
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   BINDING         43..50
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   913 AA;  105963 MW;  763DCDB7066ABF10 CRC64;
     MANASKTQII DYEGHIIDDL KEWMSDNGLS KLGFNYNVIA ILGSQSSGKS TLLNNLFKTS
     FEVMNTKLGH SQTTQGLWLS YDKFEDELAG GSSEGTDAES KNKSGDKPVV NPTLILDVEG
     NDSKERGENR LTFEHRSALF SLALADCVIV NLWYHSLGNF TASNYGLLKT VMEVHLELFH
     QNVNCPKTIL MFTVRDWFEE FAPLDVIREK IIEEYVNKIW QELKKPKSSK NAKVDDYFII
     EVVGLSHGII KKDEFLKDIK RLRHRWVYEL RPVNYSRNIP ADGFAQYCHN IWNTIVKQSQ
     LDIPSQQEML ATFRCQEIKN NVLNSISGMI KEKIIDSKNR YIENFKTWAE TDIIEKSVNE
     YLIDASRYQR SICLKTLEEL LEAIFIQLQT IVDNNLNYTQ RILSSKFSKE LNSMYSVCTT
     DKGYFLLSSD KNADATEQDD NLSNMDKSGE SAKKGNQSKC INLWSNFLYN ADMLEYTTIS
     NFYDQYKKCT IEIVEGSMAS NESKDSQEKK NHDFNYKNSL TILATSIYKD TNRIRSVQCN
     ILIERIRATI KEELKNVDNM LVTVKCSKDY WDYILKVTNK LEDYIYTNLS KCFVNLKIGI
     NTTHLNNGDN IYARLNTNSD YGFVYSHNDH MYDFSDDENN NFDEIDTEID QSKNDMESLF
     NSKKFEIITK QNKKEKYVSS INNDLTKEMN NKKLILELKN FYIEIIIDAL KIKLDEISND
     IANVIINRFE SVFNYDEIEQ PRQWRNVSVV ELKNIFRVSK DYAFLIVEIL QKNIKIDKLD
     KHLPNNFINT DIIEKGKSKA KKRIQEICRD AQYIQETGGQ MSLKNVPFAF WVILLILGWN
     EILMFTRLFF RLNIILPMFM AFIIIVGSCL YTGNAQVLSY LNKIAFIVIK HSYNFYKHLQ
     TVGNQPTKPE KVD