ID   IF5A_SULAC              Reviewed;         131 AA.
AC   P28461; Q4J981;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Translation initiation factor 5A;
DE   AltName: Full=Hypusine-containing protein;
DE   AltName: Full=SHP;
DE   AltName: Full=eIF-5A;
GN   Name=eif5a; OrderedLocusNames=Saci_1311;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND HYPUSINE
RP   AT LYS-36.
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=1541288; DOI=10.1111/j.1432-1033.1992.tb16690.x;
RA   Bartig D., Lemkemeier K., Frank J., Lottspeich F., Klink F.;
RT   "The archaebacterial hypusine-containing protein. Structural features
RT   suggest common ancestry with eukaryotic translation initiation factor 5A.";
RL   Eur. J. Biochem. 204:751-758(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: Functions by promoting the formation of the first peptide
CC       bond. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA44842.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X63132; CAA44842.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000077; AAY80649.1; -; Genomic_DNA.
DR   PIR; S22380; S22380.
DR   RefSeq; WP_011278151.1; NC_007181.1.
DR   AlphaFoldDB; P28461; -.
DR   SMR; P28461; -.
DR   STRING; 330779.Saci_1311; -.
DR   EnsemblBacteria; AAY80649; AAY80649; Saci_1311.
DR   GeneID; 3473388; -.
DR   KEGG; sai:Saci_1311; -.
DR   PATRIC; fig|330779.12.peg.1265; -.
DR   eggNOG; arCOG04277; Archaea.
DR   HOGENOM; CLU_102600_3_0_2; -.
DR   OMA; QIMDMET; -.
DR   Proteomes; UP000001018; 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; IPR013185; Transl_elong_KOW-like.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR11673; PTHR11673; 1.
DR   Pfam; PF08207; EFP_N; 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   Cytoplasm; Direct protein sequencing; Hypusine; Initiation factor;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..131
FT                   /note="Translation initiation factor 5A"
FT                   /id="PRO_0000142503"
FT   MOD_RES         36
FT                   /note="Hypusine"
FT                   /evidence="ECO:0000269|PubMed:1541288"
FT   CONFLICT        129
FT                   /note="R -> Y (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   131 AA;  14535 MW;  3857AE86925DDC11 CRC64;
     MSIQYTTVGD LKVGSYVMID GEPCRVVEIT KAKTGKHGSA KANVVAIGLF TGQKRSLMAP
     VDQQVEVPII EKHVGQILAD KGDNLTIMDL ESYETFDLEK PTENEIVSKI RPGAEIEYWS
     VMGRRKIVRV K