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}.
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; 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