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IF5A_PYRAR
ID   IF5A_PYRAR              Reviewed;         132 AA.
AC   A4WLN5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Pars_1751;
OS   Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=340102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL   Submitted (APR-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; CP000660; ABP51302.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WLN5; -.
DR   SMR; A4WLN5; -.
DR   STRING; 340102.Pars_1751; -.
DR   EnsemblBacteria; ABP51302; ABP51302; Pars_1751.
DR   KEGG; pas:Pars_1751; -.
DR   HOGENOM; CLU_102600_3_0_2; -.
DR   OMA; QIMDMET; -.
DR   PhylomeDB; A4WLN5; -.
DR   Proteomes; UP000001567; 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   3: Inferred from homology;
KW   Cytoplasm; Hypusine; Initiation factor; Protein biosynthesis.
FT   CHAIN           1..132
FT                   /note="Translation initiation factor 5A"
FT                   /id="PRO_1000007916"
FT   MOD_RES         36
FT                   /note="Hypusine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00085"
SQ   SEQUENCE   132 AA;  14728 MW;  2F73A095E9EF7B68 CRC64;
     MSTKFVEVGE LKEGSYVVID GEPCRVVEIE KSKTGKHGSA KARIVAVGMF DGGKRTLSLP
     VDAQIEVPII EKFTAQILSI SGDIIQLMDM RDYKTIEVPM KYVEDEAKGR LAPGSEVEVW
     QILDRYKIVR VK
 
 
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