ID A7AQ73_BABBO Unreviewed; 154 AA.
AC A7AQ73;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=Eukaryotic translation initiation factor 4C {ECO:0000256|ARBA:ARBA00032507};
GN ORFNames=BBOV_III011550 {ECO:0000313|EMBL:BAN65238.1,
GN ECO:0000313|EMBL:EDO08707.1};
OS Babesia bovis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5865 {ECO:0000313|EMBL:EDO08707.1, ECO:0000313|Proteomes:UP000002173};
RN [1] {ECO:0000313|EMBL:EDO08707.1, ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T2Bo {ECO:0000313|EMBL:EDO08707.1};
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).
RN [2] {ECO:0000313|EMBL:EDO08707.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T2Bo {ECO:0000313|EMBL:EDO08707.1};
RA Nene V.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:BAN65238.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Texas {ECO:0000313|EMBL:BAN65238.1};
RX PubMed=25124460; DOI=10.1186/1471-2164-15-678;
RA Yamagishi J., Wakaguri H., Yokoyama N., Yamashita R., Suzuki Y., Xuan X.,
RA Igarashi I.;
RT "The Babesia bovis gene and promoter model: an update from full-length EST
RT analysis.";
RL BMC Genomics 15:678-678(2014).
RN [4] {ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33294524; DOI=10.1016/j.dib.2020.106533;
RA Ueti M.W., Johnson W.C., Kappmeyer L.S., Herndon D.R., Mousel M.R.,
RA Reif K.E., Taus N.S., Ifeonu O.O., Silva J.C., Suarez C.E., Brayton K.A.;
RT "Transcriptome dataset of Babesia bovis life stages within vertebrate and
RT invertebrate hosts.";
RL Data Brief 33:106533-106533(2020).
RN [5] {ECO:0000313|Proteomes:UP000002173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33069745;
RA Ueti M.W., Johnson W.C., Kappmeyer L.S., Herndon D.R., Mousel M.R.,
RA Reif K.E., Taus N.S., Ifeonu O.O., Silva J.C., Suarez C.E., Brayton K.A.;
RT "Comparative analysis of gene expression between Babesia bovis blood stages
RT and kinetes allowed by improved genome annotation.";
RL Int. J. Parasitol. 51:123-136(2021).
CC -!- FUNCTION: Seems to be required for maximal rate of protein
CC biosynthesis. Enhances ribosome dissociation into subunits and
CC stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal
CC subunits. {ECO:0000256|ARBA:ARBA00025502,
CC ECO:0000256|RuleBase:RU004365}.
CC -!- SIMILARITY: Belongs to the eIF-1A family.
CC {ECO:0000256|ARBA:ARBA00007392, ECO:0000256|RuleBase:RU004364}.
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DR EMBL; AK441444; BAN65238.1; -; mRNA.
DR EMBL; AAXT01000001; EDO08707.1; -; Genomic_DNA.
DR RefSeq; XP_001612275.1; XM_001612225.1.
DR STRING; 5865.A7AQ73; -.
DR EnsemblProtists; EDO08707; EDO08707; BBOV_III011550.
DR GeneID; 5480535; -.
DR KEGG; bbo:BBOV_III011550; -.
DR VEuPathDB; PiroplasmaDB:BBOV_III011550; -.
DR eggNOG; KOG3403; Eukaryota.
DR OMA; KMEDQEY; -.
DR Proteomes; UP000002173; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd05793; S1_IF1A; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00216; aIF_1A; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR InterPro; IPR001253; TIF_eIF-1A.
DR InterPro; IPR018104; TIF_eIF-1A_CS.
DR NCBIfam; TIGR00523; eIF-1A; 1.
DR PANTHER; PTHR21668; EIF-1A; 1.
DR PANTHER; PTHR21668:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 4C; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SMART; SM00652; eIF1a; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS01262; IF1A; 1.
DR PROSITE; PS50832; S1_IF1_TYPE; 1.
PE 2: Evidence at transcript level;
KW Initiation factor {ECO:0000256|PROSITE-ProRule:PRU00181,
KW ECO:0000256|RuleBase:RU004365};
KW Protein biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00181,
KW ECO:0000256|RuleBase:RU004365};
KW Reference proteome {ECO:0000313|Proteomes:UP000002173}.
FT DOMAIN 22..96
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..154
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 154 AA; 17523 MW; 9DD34A817B5E9109 CRC64;
MPKNKGKGGK NRRRGKNDND GEKRELVFKM EDQEYAQVLR MLGNGRLEAY CFDGNKRLCH
IRGKMRKRVW VNAGDIILVS LRDYQDSKAD VIAKYTADEA RSLKAYGELP ESTKITETDL
YDDEGDGGIE FQDESSGSDS EDDKEDAKFD IDDL
//
