ID   IF5A_METM7              Reviewed;         131 AA.
AC   A6VFP3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=MmarC7_0199;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000745; ABR65269.1; -; Genomic_DNA.
DR   RefSeq; WP_011976606.1; NC_009637.1.
DR   AlphaFoldDB; A6VFP3; -.
DR   SMR; A6VFP3; -.
DR   STRING; 426368.MmarC7_0199; -.
DR   EnsemblBacteria; ABR65269; ABR65269; MmarC7_0199.
DR   GeneID; 5329104; -.
DR   KEGG; mmz:MmarC7_0199; -.
DR   eggNOG; arCOG04277; Archaea.
DR   HOGENOM; CLU_102600_3_0_2; -.
DR   OMA; QIMDMET; -.
DR   OrthoDB; 98221at2157; -.
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   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..131
FT                   /note="Translation initiation factor 5A"
FT                   /id="PRO_1000007911"
FT   MOD_RES         37
FT                   /note="Hypusine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00085"
SQ   SEQUENCE   131 AA;  14213 MW;  C9E44A4A3FD4A010 CRC64;
     MAGTKPGDLG GVKVGQYVVI EGVACKVMDT AHSKPGKHGG AKVRLVAVGI FEPVKKEHVG
     PASSRIDIPL IDKRKGQVLA LMGDNVQIMD METYETLEIP MPDDVEGIES GVEVEYFEAM
     DRYKITRVIS K