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IF5A_PYRNV
ID   IF5A_PYRNV              Reviewed;         132 AA.
AC   B1Y9U5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Tneu_1571;
OS   Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 /
OS   V24Sta) (Thermoproteus neutrophilus).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=444157;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL   Submitted (MAR-2008) 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; CP001014; ACB40495.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1Y9U5; -.
DR   SMR; B1Y9U5; -.
DR   STRING; 444157.Tneu_1571; -.
DR   EnsemblBacteria; ACB40495; ACB40495; Tneu_1571.
DR   KEGG; tne:Tneu_1571; -.
DR   eggNOG; arCOG04277; Archaea.
DR   HOGENOM; CLU_102600_3_0_2; -.
DR   OMA; QIMDMET; -.
DR   Proteomes; UP000001694; 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_1000093010"
FT   MOD_RES         36
FT                   /note="Hypusine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00085"
SQ   SEQUENCE   132 AA;  14597 MW;  E3AAB178637DFD69 CRC64;
     MSTKYVEAGE LKEGSYVVID GEPCRVVEIE KSKTGKHGSA KARIVAVGVF DGGKRTLSLP
     VDAQVEVPII EKFTAQVLSI SGDIIQLMDM RDYKTIEVPM SYVEEEAKGR LAPGAEVEVW
     QILDRFKIVR VK
 
 
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