ID   IF5A_METS3              Reviewed;         129 AA.
AC   A5ULK4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Translation initiation factor 5A {ECO:0000255|HAMAP-Rule:MF_00085};
DE   AltName: Full=Hypusine-containing protein {ECO:0000255|HAMAP-Rule:MF_00085};
DE   AltName: Full=eIF-5A {ECO:0000255|HAMAP-Rule:MF_00085};
GN   Name=eIF5A; OrderedLocusNames=Msm_0877;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
CC   -!- FUNCTION: Functions by promoting the formation of the first peptide
CC       bond. {ECO:0000255|HAMAP-Rule:MF_00085}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00085}.
CC   -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000255|HAMAP-
CC       Rule:MF_00085}.
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DR   EMBL; CP000678; ABQ87082.1; -; Genomic_DNA.
DR   RefSeq; WP_004033052.1; NC_009515.1.
DR   AlphaFoldDB; A5ULK4; -.
DR   SMR; A5ULK4; -.
DR   STRING; 420247.Msm_0877; -.
DR   EnsemblBacteria; ABQ87082; ABQ87082; Msm_0877.
DR   GeneID; 5217336; -.
DR   KEGG; msi:Msm_0877; -.
DR   PATRIC; fig|420247.28.peg.874; -.
DR   eggNOG; arCOG04277; Archaea.
DR   HOGENOM; CLU_102600_3_0_2; -.
DR   OMA; QIMDMET; -.
DR   Proteomes; UP000001992; Chromosome.
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:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00085; eIF_5A; 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; IPR022847; Transl_elong_IF5A_arc.
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   3: Inferred from homology;
KW   Cytoplasm; Hypusine; Initiation factor; Protein biosynthesis.
FT   CHAIN           1..129
FT                   /note="Translation initiation factor 5A"
FT                   /id="PRO_1000007913"
FT   MOD_RES         36
FT                   /note="Hypusine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00085"
SQ   SEQUENCE   129 AA;  14172 MW;  F7DCF3A48ADCC0BC CRC64;
     MSTKVVEIKT LKVGKYIVLG GEASKITSLT TSSPGKHGAA KARLEAVGIF DNQKRSIVKP
     VDTKVDIPII DKRVGQVLSI QGNNVQLMDM ENYDTLDLPM PEELKDQITE GIEVDYIVAL
     GNMKIMRTK