IF5A_PYRAB
ID IF5A_PYRAB Reviewed; 138 AA.
AC Q9V0M2; G8ZGW8;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Translation initiation factor 5A;
DE AltName: Full=Hypusine-containing protein;
DE AltName: Full=eIF-5A;
GN Name=eif5a; Synonyms=aif5A; OrderedLocusNames=PYRAB07670; ORFNames=PAB1854;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
CC -!- FUNCTION: Functions by promoting the formation of the first peptide
CC bond. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
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DR EMBL; AJ248285; CAB49681.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70163.1; -; Genomic_DNA.
DR PIR; H75120; H75120.
DR RefSeq; WP_010867889.1; NC_000868.1.
DR AlphaFoldDB; Q9V0M2; -.
DR SMR; Q9V0M2; -.
DR STRING; 272844.PAB1854; -.
DR EnsemblBacteria; CAB49681; CAB49681; PAB1854.
DR GeneID; 1496107; -.
DR KEGG; pab:PAB1854; -.
DR PATRIC; fig|272844.11.peg.807; -.
DR eggNOG; arCOG04277; Archaea.
DR HOGENOM; CLU_102600_3_0_2; -.
DR OMA; QIMDMET; -.
DR OrthoDB; 98221at2157; -.
DR PhylomeDB; Q9V0M2; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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..138
FT /note="Translation initiation factor 5A"
FT /id="PRO_0000142498"
FT MOD_RES 37
FT /note="Hypusine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 138 AA; 15315 MW; AC2C92FE5E0C29B1 CRC64;
MGDKTKVQVS KLKPGRYIII DDEPCRIVNI TVSSPGKHGS AKARIEAVGI FDGKVRSIVK
PTSAEVDVPI IDKKTAQVIA ITPDTVQIMD METYEMFEVP IDTGVAEEIR DQLKEGINVE
YWETLGRVKI MRIKGEGE
