ID   IF5A_LEIDO              Reviewed;         166 AA.
AC   A4GVE9;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Eukaryotic translation initiation factor 5A {ECO:0000250|UniProtKB:Q9GU68};
DE            Short=eIF-5A {ECO:0000250|UniProtKB:Q9GU68};
OS   Leishmania donovani.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5661;
RN   [1] {ECO:0000312|EMBL:ABO34138.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Singh S., Madhubala R.;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   HYPUSINE AT LYS-53.
RX   PubMed=19880510; DOI=10.1074/jbc.m109.048850;
RA   Chawla B., Jhingran A., Singh S., Tyagi N., Park M.H., Srinivasan N.,
RA   Roberts S.C., Madhubala R.;
RT   "Identification and characterization of a novel deoxyhypusine synthase in
RT   Leishmania donovani.";
RL   J. Biol. Chem. 285:453-463(2010).
CC   -!- FUNCTION: mRNA-binding protein involved in translation elongation. Has
CC       an important function at the level of mRNA turnover, probably acting
CC       downstream of decapping. Critical for the efficient synthesis of
CC       peptide bonds between consecutive proline residues. Can resolve
CC       ribosomal stalling caused by consecutive prolines during translation
CC       (By similarity). Involved in actin dynamics and cell cycle progression,
CC       mRNA decay and probably in a pathway involved in stress response and
CC       maintenance of cell wall integrity. Functions as a regulator of
CC       apoptosis (By similarity). {ECO:0000250|UniProtKB:P63241,
CC       ECO:0000250|UniProtKB:Q9GU68}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23301}.
CC   -!- PTM: Lys-53 undergoes hypusination, a unique post-translational
CC       modification that consists in the addition of a butylamino group from
CC       spermidine to lysine side chain, leading to the formation of the
CC       unusual amino acid hypusine. eIF-5As are the only known proteins to
CC       undergo this modification, which is essential for their function.
CC       {ECO:0000269|PubMed:19880510}.
CC   -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000255}.
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DR   EMBL; EF439707; ABO34138.1; -; Genomic_DNA.
DR   RefSeq; XP_003861404.1; XM_003861356.1.
DR   RefSeq; XP_003861405.1; XM_003861357.1.
DR   AlphaFoldDB; A4GVE9; -.
DR   SMR; A4GVE9; -.
DR   GeneID; 13388650; -.
DR   GeneID; 13388651; -.
DR   KEGG; ldo:LDBPK_250740; -.
DR   KEGG; ldo:LDBPK_250750; -.
DR   VEuPathDB; TriTrypDB:LdBPK_250750.1; -.
DR   VEuPathDB; TriTrypDB:LdCL_250012700; -.
DR   VEuPathDB; TriTrypDB:LdCL_250012800; -.
DR   VEuPathDB; TriTrypDB:LdCL_250012900; -.
DR   VEuPathDB; TriTrypDB:LDHU3_25.0940; -.
DR   VEuPathDB; TriTrypDB:LDHU3_25.0950; -.
DR   VEuPathDB; TriTrypDB:LDHU3_25.0960; -.
DR   OMA; VFRNEYQ; -.
DR   SABIO-RK; A4GVE9; -.
DR   EvolutionaryTrace; A4GVE9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IDA:UniProtKB.
DR   GO; GO:0045901; P:positive regulation of translational elongation; IEA:InterPro.
DR   GO; GO:0045905; P:positive regulation of translational termination; IEA:InterPro.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR001884; IF5A-like.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR019769; Trans_elong_IF5A_hypusine_site.
DR   InterPro; IPR020189; Transl_elong_IF5A_C.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR11673; PTHR11673; 1.
DR   Pfam; PF01287; eIF-5a; 1.
DR   PIRSF; PIRSF003025; eIF5A; 1.
DR   SMART; SM01376; eIF-5a; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00037; eIF_5A; 1.
DR   PROSITE; PS00302; IF5A_HYPUSINE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Elongation factor; Hypusine; Initiation factor;
KW   Protein biosynthesis; RNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P23301"
FT   CHAIN           2..166
FT                   /note="Eukaryotic translation initiation factor 5A"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000419761"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         53
FT                   /note="Hypusine"
FT                   /evidence="ECO:0000269|PubMed:19880510"
SQ   SEQUENCE   166 AA;  17880 MW;  26687A0314544D35 CRC64;
     MSDEDHDFSH QGGGDNASKT YPLPAGALKK GGYVCINGRP CKVIDLSVSK TGKHGHAKVS
     IVATDIFTGN RLEDQAPSTH NVEVPFVKTF TYSVLDIQPN EDPSLPSHLS LMDDEGESRE
     DLDMPPDVAL ATQIKEQFDS GKEVLVVVVS AMGTEQVLQT KNAAEK