IF5A_LEIMU
ID IF5A_LEIMU Reviewed; 166 AA.
AC E9AXF0;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Eukaryotic translation initiation factor 5A {ECO:0000250|UniProtKB:Q9GU68};
DE Short=eIF-5A {ECO:0000250|UniProtKB:Q9GU68};
GN ORFNames=LMXM_25_0720, LMXM_25_0730;
OS Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=929439;
RN [1] {ECO:0000312|EMBL:CBZ27641.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000312|EMBL:CBZ27641.1};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
RN [2] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RA Bosch J., Hol W.G.J.;
RT "Structural analysis of Leishmania mexicana eukaryotic initiation factor
RT 5a.";
RL Submitted (OCT-2004) to the PDB data bank.
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:0000250|UniProtKB:A4GVE9}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000255}.
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; FR799578; CBZ27641.1; -; Genomic_DNA.
DR EMBL; FR799578; CBZ27642.1; -; Genomic_DNA.
DR RefSeq; XP_003876126.1; XM_003876077.1.
DR RefSeq; XP_003876127.1; XM_003876078.1.
DR PDB; 1XTD; X-ray; 2.70 A; A=1-166.
DR PDBsum; 1XTD; -.
DR AlphaFoldDB; E9AXF0; -.
DR SMR; E9AXF0; -.
DR GeneID; 13449242; -.
DR GeneID; 13449243; -.
DR KEGG; lmi:LMXM_25_0720; -.
DR KEGG; lmi:LMXM_25_0730; -.
DR VEuPathDB; TriTrypDB:LmxM.25.0720; -.
DR VEuPathDB; TriTrypDB:LmxM.25.0730; -.
DR OMA; VFRNEYQ; -.
DR PhylomeDB; E9AXF0; -.
DR Proteomes; UP000007259; Chromosome 25.
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; ISS: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 3D-structure; 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_0000419762"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Hypusine"
FT /evidence="ECO:0000250|UniProtKB:A4GVE9"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:1XTD"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1XTD"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1XTD"
FT STRAND 39..48
FT /evidence="ECO:0007829|PDB:1XTD"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1XTD"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:1XTD"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1XTD"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1XTD"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1XTD"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:1XTD"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:1XTD"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:1XTD"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:1XTD"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:1XTD"
SQ SEQUENCE 166 AA; 17828 MW; 57C1B16AEFAD5763 CRC64;
MSDEDHDFAH QGGGDNASKT YPMAAGALKK GGYVCINGRP CKVIDLSVSK TGKHGHAKVS
IVATDIFTGN RLEDQAPSTH NVEVPFVKTF TYSVLDIQPN EDPSLPSHLS LMDDEGESRE
DLDMPPDAAL ATQIKEQFDS GKEVLVVVVS AMGTEQVLQT KNAAEK
