IF5A_PYRCJ
ID IF5A_PYRCJ Reviewed; 132 AA.
AC A3MTA0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Pcal_0434;
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
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 calidifontis JCM 11548.";
RL Submitted (FEB-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; CP000561; ABO07867.1; -; Genomic_DNA.
DR AlphaFoldDB; A3MTA0; -.
DR SMR; A3MTA0; -.
DR STRING; 410359.Pcal_0434; -.
DR EnsemblBacteria; ABO07867; ABO07867; Pcal_0434.
DR KEGG; pcl:Pcal_0434; -.
DR eggNOG; arCOG04277; Archaea.
DR HOGENOM; CLU_102600_3_0_2; -.
DR OMA; QIMDMET; -.
DR Proteomes; UP000001431; 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_1000007917"
FT MOD_RES 36
FT /note="Hypusine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00085"
SQ SEQUENCE 132 AA; 14666 MW; 3FCB79F52DC317F5 CRC64;
MSTKYVEVGE LKEGSYVVID GEPCRVVEIE KSKTGKHGSA KARVVAVGVF DGAKRTLSLP
VDAQIEVPII EKFTAQVLSI SGDVIQLMDM RDYKTIEVPM KYVEEEAKGR LAPGAEVEVW
QILDRFKIVR VK
