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SEY1_BABBO
ID   SEY1_BABBO              Reviewed;         828 AA.
AC   A7AT07;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Protein SEY1 homolog {ECO:0000255|HAMAP-Rule:MF_03109};
DE            EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN   ORFNames=BBOV_II001090;
OS   Babesia bovis.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Babesiidae; Babesia.
OX   NCBI_TaxID=5865;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T2Bo;
RX   PubMed=17953480; DOI=10.1371/journal.ppat.0030148;
RA   Brayton K.A., Lau A.O.T., Herndon D.R., Hannick L., Kappmeyer L.S.,
RA   Berens S.J., Bidwell S.L., Brown W.C., Crabtree J., Fadrosh D.,
RA   Feldblum T., Forberger H.A., Haas B.J., Howell J.M., Khouri H., Koo H.,
RA   Mann D.J., Norimine J., Paulsen I.T., Radune D., Ren Q., Smith R.K. Jr.,
RA   Suarez C.E., White O., Wortman J.R., Knowles D.P. Jr., McElwain T.F.,
RA   Nene V.M.;
RT   "Genome sequence of Babesia bovis and comparative analysis of apicomplexan
RT   hemoprotozoa.";
RL   PLoS Pathog. 3:1401-1413(2007).
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; AAXT01000003; EDO06068.1; -; Genomic_DNA.
DR   RefSeq; XP_001609636.1; XM_001609586.1.
DR   AlphaFoldDB; A7AT07; -.
DR   SMR; A7AT07; -.
DR   STRING; 5865.XP_001609636.1; -.
DR   PRIDE; A7AT07; -.
DR   EnsemblProtists; EDO06068; EDO06068; BBOV_II001090.
DR   GeneID; 5477861; -.
DR   KEGG; bbo:BBOV_II001090; -.
DR   VEuPathDB; PiroplasmaDB:BBOV_II001090; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   InParanoid; A7AT07; -.
DR   OMA; TNFDVMD; -.
DR   Proteomes; UP000002173; 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   Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..828
FT                   /note="Protein SEY1 homolog"
FT                   /id="PRO_0000384941"
FT   TOPO_DOM        1..718
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        719..739
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        740..742
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        743..763
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        764..828
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          44..284
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   BINDING         54..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   828 AA;  92854 MW;  408D413926C40D9E CRC64;
     MTEDVMNDDF DSLVTKPTEF IDYNCDINNG FNDLLKSQKF DKLGFNYNVL SILGCQSSGK
     SSLLNSVFGL DFDVMNTKLG HSQTTKGLWG ALVIPKDTGS GNVTIVIDVE GTDSRERGEG
     RLTFEHRSAL LCLAISDCVV INLWYHSLGN LTGSNYGLLK TVVEANLELA EASENTLASG
     DYKTVLCFCI RDWFPELAPL ETVRQKVVNE YMLGIWNDIN KPDKFKNSKL EDIFRFELYG
     FNHALVHPDE FAKDSSRFRL AWATSISPKS YSRAVPSDGF FYYASNILQT VKDQSHLDIP
     NQREMLANFR CQEIKGGVLD EMVPSISSML TDAQSGVMDD FQHRAVELVD VAVGKYLELA
     SRYDKTTSNK IGNELVISVF SKLQPVFDAI ISHHCSDLAV RATVRLNEKF AISGKERSPM
     VGGQKAADVW PKFNMLTDEI KAELYNSLNS HILSCAINYS HESGIQAQSD FDTSAAVDMF
     NVTFKNEVES VRARHIRALL GQITDLVDSG FKVIGEALLE RNVTSDKYWG DVNDLIDRAY
     STCLDTMGPC YTGLVPSVQP NEFEYLAFMI LLQATKCNLE RTESRITDII LERFEQFFQY
     QEFNGETVPR DWGSYTEEEL KQTYTQCKKE ALNIVAVLRD CSPPTLEVPA FEVSSLKPNH
     VLYQELSAGV DSLRATTTSL SDEVLVDTVK ACRKRFQEFF RTAQQIQSSS KNGISWKNIP
     PPFWILLLLC SWNELCSVLR IVFKVQVLIP LIILGFIVVQ YFSHLVFGTS ADAVFRPFKR
     QARELAMVGT KWIFKVATST AAAAVNAGAK TTFLSDDDND SGKKAEEN
 
 
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