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Database: UniProt
Entry: A0A1V6SK99_9EURO
LinkDB: A0A1V6SK99_9EURO
Original site: A0A1V6SK99_9EURO 
ID   A0A1V6SK99_9EURO        Unreviewed;       158 AA.
AC   A0A1V6SK99;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   18-JUN-2025, entry version 22.
DE   RecName: Full=Eukaryotic translation initiation factor 5A {ECO:0000256|RuleBase:RU362005};
DE            Short=eIF-5A {ECO:0000256|RuleBase:RU362005};
GN   ORFNames=PENSTE_c036G07050 {ECO:0000313|EMBL:OQE14338.1};
OS   Penicillium steckii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE14338.1, ECO:0000313|Proteomes:UP000191285};
RN   [1] {ECO:0000313|Proteomes:UP000191285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQE14338.1}.
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DR   EMBL; MLKD01000036; OQE14338.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6SK99; -.
DR   STRING; 303698.A0A1V6SK99; -.
DR   OrthoDB; 9975114at2759; -.
DR   Proteomes; UP000191285; Unassembled WGS sequence.
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:000007; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768};
KW   Hypusine {ECO:0000256|ARBA:ARBA00023071, ECO:0000256|RuleBase:RU362005};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU362005};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191285};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          85..154
FT                   /note="Translation elongation factor IF5A C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01376"
SQ   SEQUENCE   158 AA;  17383 MW;  15B74CDB2EDA388A CRC64;
     MADEHDVTFE SADAGASTTF PMQCSALRKN GHVVIKGRPC KIVDMSTSKT GKHGHAKVHI
     VAIDIFTGKK LEDLSPSTHN MDVPNVGRKE YQLLDITDDD FLSLMKDDGD TKDDVKVPDN
     DLGARIVKMF REEEKDVNVI IQTAMGEEVA IDAKEAPK
//
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