ID   IF5A_SENVE              Reviewed;         159 AA.
AC   Q9SC12;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Eukaryotic translation initiation factor 5A;
DE            Short=eIF-5A;
GN   Name=EIFSV1;
OS   Senecio vernalis (Spring groundsel).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Senecioneae;
OC   Senecioninae; Senecio.
OX   NCBI_TaxID=93496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10611289; DOI=10.1073/pnas.96.26.14777;
RA   Ober D., Hartmann T.;
RT   "Homospermidine synthase, the first pathway-specific enzyme of
RT   pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:14777-14782(1999).
CC   -!- FUNCTION: The precise role of eIF-5A in protein biosynthesis is not
CC       known but it functions by promoting the formation of the first peptide
CC       bond.
CC   -!- PTM: Lys-52 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:Q9XI91}.
CC   -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
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DR   EMBL; AJ238624; CAB65463.1; -; mRNA.
DR   AlphaFoldDB; Q9SC12; -.
DR   SMR; Q9SC12; -.
DR   GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Hypusine; Initiation factor; Protein biosynthesis.
FT   CHAIN           1..159
FT                   /note="Eukaryotic translation initiation factor 5A"
FT                   /id="PRO_0000142477"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         52
FT                   /note="Hypusine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XI91"
SQ   SEQUENCE   159 AA;  17265 MW;  7BC45DA7AFAB73AC CRC64;
     MSDEEHQFES KADAGASKTY PQQAGTIRKG GHIVIKNRAC KVVEVSTSKT GKHGHAKCHF
     VAIDIFNGKK LEDIVPSSHN CDVPHVNRTD YQLIDISEDG FVSLLTENGN TKDDLKLPTD
     DALLTQIKDG FGEGKDLVVS VMSAMGEEQI CALKDIGPK