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Database: UniProt
Entry: A0A4U0U6T9_9PEZI
LinkDB: A0A4U0U6T9_9PEZI
Original site: A0A4U0U6T9_9PEZI 
ID   A0A4U0U6T9_9PEZI        Unreviewed;       164 AA.
AC   A0A4U0U6T9;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   18-JUN-2025, entry version 18.
DE   RecName: Full=Eukaryotic translation initiation factor 5A {ECO:0000256|RuleBase:RU362005};
DE            Short=eIF-5A {ECO:0000256|RuleBase:RU362005};
GN   ORFNames=B0A50_02885 {ECO:0000313|EMBL:TKA30166.1};
OS   Salinomyces thailandicus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Salinomyces.
OX   NCBI_TaxID=706561 {ECO:0000313|EMBL:TKA30166.1, ECO:0000313|Proteomes:UP000308549};
RN   [1] {ECO:0000313|EMBL:TKA30166.1, ECO:0000313|Proteomes:UP000308549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 6315 {ECO:0000313|EMBL:TKA30166.1,
RC   ECO:0000313|Proteomes:UP000308549};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) 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   -!- 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:TKA30166.1}.
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DR   EMBL; NAJL01000012; TKA30166.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4U0U6T9; -.
DR   OrthoDB; 9975114at2759; -.
DR   Proteomes; UP000308549; 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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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   Initiation factor {ECO:0000313|EMBL:TKA30166.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU362005};
KW   Reference proteome {ECO:0000313|Proteomes:UP000308549};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          89..158
FT                   /note="Translation elongation factor IF5A C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01376"
SQ   SEQUENCE   164 AA;  17893 MW;  3A4857D5A0DC1F3D CRC64;
     MAENNDAQHE LTFESADAGA SLTYPMQCSA LRKNGFVCIK NRPCKIVDMS TSKTGKHGHA
     KVHLVAIDLF TGKKLEDLSP STHNMDVPNV RRQEYQLLDI SEDGFLNLLT DNGEEKNDVK
     VPDGDVGDKI TKLFTDEGKD VNVIVLTAMG EESAMDAKEA PKGA
//
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