ID A0A8E0S1I0_9TREM Unreviewed; 420 AA.
AC A0A8E0S1I0;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE SubName: Full=Eukaryotic translation initiation factor 5B {ECO:0000313|EMBL:KAA0199052.1};
GN ORFNames=FBUS_10045 {ECO:0000313|EMBL:KAA0199052.1};
OS Fasciolopsis buskii.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Fasciolidae;
OC Fasciolopsis.
OX NCBI_TaxID=27845 {ECO:0000313|EMBL:KAA0199052.1, ECO:0000313|Proteomes:UP000728185};
RN [1] {ECO:0000313|EMBL:KAA0199052.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HT {ECO:0000313|EMBL:KAA0199052.1};
RC TISSUE=Whole worm {ECO:0000313|EMBL:KAA0199052.1};
RA Choi Y.-J.;
RT "Annotation for the trematode Fasciolopsis buski.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in translation initiation. Ribosome-dependent
CC GTPase that promotes the joining of the 60S ribosomal subunit to the
CC pre-initiation complex to form the 80S initiation complex with the
CC initiator methionine-tRNA in the P-site base paired to the start codon.
CC Together with eIF1A (EIF1AX), actively orients the initiator
CC methionine-tRNA in a conformation that allows 60S ribosomal subunit
CC joining to form the 80S initiation complex. Is released after formation
CC of the 80S initiation complex. Its GTPase activity is not essential for
CC ribosomal subunits joining, but GTP hydrolysis is needed for eIF1A
CC (EIF1AX) ejection quickly followed by EIF5B release to form elongation-
CC competent ribosomes. In contrast to its procaryotic homolog, does not
CC promote recruitment of Met-rRNA to the small ribosomal subunit.
CC {ECO:0000256|ARBA:ARBA00053410}.
CC -!- COFACTOR:
CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC Evidence={ECO:0000256|ARBA:ARBA00001944};
CC -!- SUBUNIT: Interacts through its C-terminal domain (CTD) with the CTD of
CC eIF1A (EIF1AX) or with the CTD of EIF5 (mutually exclusive) through a
CC common binding site. Interacts with eIF1A (EIF1AX) from the location of
CC the start codon by the 43S complex until the formation of the 80S
CC complex. Interacts with ANXA5 in a calcium and phospholipid-dependent
CC manner. {ECO:0000256|ARBA:ARBA00061781}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAA0199052.1}.
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DR EMBL; LUCM01001351; KAA0199052.1; -; Genomic_DNA.
DR OrthoDB; 4928at2759; -.
DR Proteomes; UP000728185; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd03703; aeIF5B_II; 1.
DR CDD; cd16266; IF2_aeIF5B_IV; 1.
DR FunFam; 2.40.30.10:FF:000013; eukaryotic translation initiation factor 5B; 1.
DR FunFam; 2.40.30.10:FF:000026; Eukaryotic translation initiation factor 5B; 1.
DR FunFam; 3.40.50.10050:FF:000002; Eukaryotic translation initiation factor 5B; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR InterPro; IPR029459; EFTU-type.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF14578; GTP_EFTU_D4; 1.
DR Pfam; PF11987; IF-2; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000313|EMBL:KAA0199052.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000728185}.
FT DOMAIN 170..269
FT /note="Translation initiation factor IF- 2"
FT /evidence="ECO:0000259|Pfam:PF11987"
FT DOMAIN 291..380
FT /note="Elongation factor Tu-type"
FT /evidence="ECO:0000259|Pfam:PF14578"
SQ SEQUENCE 420 AA; 46963 MW; 2488D47DBA646204 CRC64;
MELNVELFYR NSNQDEYISM VPTSAHSGDG MGDLLASLCL YLQNKLSKRL AFSEELHASV
MEVKELHGLG TTIDVIVVNG FIKEGDTIVL AGQEGPIATQ VRGLLQPAPM AELRVKGSYQ
HLKEIQGAQG VKLIAKDLEK ALAGLPLHVA TDLGEELYFK DEVSRGLKAA LKAIAVSPLG
VYVVASTLGS LESLLVYLKS VDIPYSGINI GTVHKKDVMK ASVMVEREQK WAVILAFDVR
VDKDAQRLAA ELGVRIFTSD IIYRLQSQME EYVEDLKRGN RRKHRDLAVY PCKLRILPDM
VFNSRAPIVV GVHVEAGVVR EGTPLCVPSK DNINLGRIFS IEFNHKPVQE ARTGQEVCVR
IDPLDGETPK LYGRHFDHND LMVSKISRES IDIMKEHFRS DLTKEDWKLM LELKKLFDIF
//
