ID A0A9E7L6G0_9LILI Unreviewed; 151 AA.
AC A0A9E7L6G0;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 18-JUN-2025, entry version 8.
DE RecName: Full=Eukaryotic translation initiation factor 5A {ECO:0000256|RuleBase:RU362005};
DE Short=eIF-5A {ECO:0000256|RuleBase:RU362005};
GN ORFNames=MUK42_15126 {ECO:0000313|EMBL:URE47618.1};
OS Musa troglodytarum.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa.
OX NCBI_TaxID=320322 {ECO:0000313|EMBL:URE47618.1, ECO:0000313|Proteomes:UP001055439};
RN [1] {ECO:0000313|EMBL:URE47618.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:URE47618.1};
RA Wang J.;
RT "The Musa troglodytarum L. genome provides insights into the mechanism of
RT non-climacteric behaviour and enrichment of carotenoids.";
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Translation factor that promotes translation elongation and
CC termination, particularly upon ribosome stalling at specific amino acid
CC sequence contexts. Binds between the exit (E) and peptidyl (P) site of
CC the ribosome and promotes rescue of stalled ribosome: specifically
CC required for efficient translation of polyproline-containing peptides
CC as well as other motifs that stall the ribosome. Acts as ribosome
CC quality control (RQC) cofactor by joining the RQC complex to facilitate
CC peptidyl transfer during CAT tailing step.
CC {ECO:0000256|RuleBase:RU362005}.
CC -!- PTM: eIF-5A seems to be the only eukaryotic protein to have a hypusine
CC residue which is a post-translational modification of a lysine by the
CC addition of a butylamino group. {ECO:0000256|RuleBase:RU362005}.
CC -!- SIMILARITY: Belongs to the eIF-5A family.
CC {ECO:0000256|ARBA:ARBA00006016, ECO:0000256|RuleBase:RU362005}.
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; CP097511; URE47618.1; -; Genomic_DNA.
DR OrthoDB; 9975114at2759; -.
DR Proteomes; UP001055439; Chromosome 9.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045901; P:positive regulation of translational elongation; IEA:UniProtKB-UniRule.
DR GO; GO:0045905; P:positive regulation of translational termination; IEA:UniProtKB-UniRule.
DR CDD; cd04468; S1_eIF5A; 1.
DR FunFam; 2.30.30.30:FF:000012; Eukaryotic translation initiation factor 5A; 1.
DR FunFam; 2.40.50.140:FF:000034; Eukaryotic translation initiation factor 5A; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR001884; IF5A-like.
DR InterPro; IPR048670; IF5A-like_N.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014722; Rib_uL2_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 NCBIfam; TIGR00037; eIF_5A; 1.
DR PANTHER; PTHR11673; TRANSLATION INITIATION FACTOR 5A FAMILY MEMBER; 1.
DR Pfam; PF01287; eIF-5a; 1.
DR Pfam; PF21485; IF5A-like_N; 1.
DR PIRSF; PIRSF003025; eIF5A; 1.
DR SMART; SM01376; eIF-5a; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR PROSITE; PS00302; IF5A_HYPUSINE; 1.
PE 3: Inferred from homology;
KW Hypusine {ECO:0000256|ARBA:ARBA00023071, ECO:0000256|RuleBase:RU362005};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU362005};
KW Reference proteome {ECO:0000313|Proteomes:UP001055439}.
FT DOMAIN 77..146
FT /note="Translation elongation factor IF5A C-terminal"
FT /evidence="ECO:0000259|SMART:SM01376"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 151 AA; 16486 MW; 1179A5DB6970BE5B CRC64;
MSDEEHHFES KADAGASKTY PQQAGTIRKN GYIVVEVSTS KTGKHGHAKC HFVAIDIFNA
KKLEDIVPSS HNCDVPHVNR TDYQLIDISE DGFVSLLTES GNTKDDLKLP TDENLLAQLK
DGFAEGKDLV VTVMSAMGEE QICALKDIGP K
//
