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IF5A_SPOFR
ID   IF5A_SPOFR              Reviewed;         160 AA.
AC   P62925; Q9TVJ8;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Eukaryotic translation initiation factor 5A;
DE            Short=eIF-5A;
GN   Name=eIF-5A; Synonyms=eIF5A;
OS   Spodoptera frugiperda (Fall armyworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Amphipyrinae; Spodoptera.
OX   NCBI_TaxID=7108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Midgut, and Ovary;
RX   PubMed=10620048; DOI=10.1046/j.1365-2583.1999.00148.x;
RA   van Oers M.M., van Marwijk M., Kwa M.S.G., Vlak J.M., Thomas A.A.M.;
RT   "Cloning and analysis of cDNAs encoding the hypusine-containing protein
RT   eIF5A of two lepidopteran insect species.";
RL   Insect Mol. Biol. 8:531-538(1999).
CC   -!- FUNCTION: mRNA-binding protein involved in translation elongation.
CC       Critical for the efficient synthesis of peptide bonds between
CC       consecutive proline residues. Can resolve ribosomal stalling caused by
CC       consecutive prolines during translation (By similarity). Has an
CC       important function at the level of mRNA turnover, probably acting
CC       downstream of decapping. Involved in actin dynamics and cell cycle
CC       progression, mRNA decay and probably in a pathway involved in stress
CC       response and maintenance of cell wall integrity. Functions as a
CC       regulator of apoptosis (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P63241}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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:P63241}.
CC   -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
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DR   EMBL; AF109731; AAF13316.1; -; mRNA.
DR   PDB; 5HY6; X-ray; 2.19 A; A=1-160.
DR   PDBsum; 5HY6; -.
DR   AlphaFoldDB; P62925; -.
DR   SMR; P62925; -.
DR   PRIDE; P62925; -.
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: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; Protein biosynthesis;
KW   RNA-binding.
FT   CHAIN           1..160
FT                   /note="Eukaryotic translation initiation factor 5A"
FT                   /id="PRO_0000142462"
FT   MOD_RES         52
FT                   /note="Hypusine"
FT                   /evidence="ECO:0000250|UniProtKB:P63241"
FT   STRAND          18..23
FT                   /evidence="ECO:0007829|PDB:5HY6"
FT   HELIX           24..26
FT                   /evidence="ECO:0007829|PDB:5HY6"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:5HY6"
FT   STRAND          38..47
FT                   /evidence="ECO:0007829|PDB:5HY6"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:5HY6"
FT   STRAND          58..64
FT                   /evidence="ECO:0007829|PDB:5HY6"
FT   TURN            65..67
FT                   /evidence="ECO:0007829|PDB:5HY6"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:5HY6"
FT   STRAND          77..84
FT                   /evidence="ECO:0007829|PDB:5HY6"
FT   STRAND          87..96
FT                   /evidence="ECO:0007829|PDB:5HY6"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:5HY6"
FT   HELIX           120..131
FT                   /evidence="ECO:0007829|PDB:5HY6"
FT   STRAND          135..143
FT                   /evidence="ECO:0007829|PDB:5HY6"
FT   STRAND          146..155
FT                   /evidence="ECO:0007829|PDB:5HY6"
SQ   SEQUENCE   160 AA;  17525 MW;  D3CE1E65CEA21732 CRC64;
     MADIEDTHFE TGDSGASATF PMQCSALRKN GFVMLKGRPC KIVEMSTSKT GKHGHAKVHL
     VGIDIFNGKK YEDICPSTHN MDVPHVKRED YQLTDISDDG YLTLMADNGD LREDLKIPDG
     DLGTQLRSDF DSGKELLCTV LKSCGEECVI AVKANTALDK
 
 
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