IF5A_AERPE
ID IF5A_AERPE Reviewed; 139 AA.
AC Q9YA53;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Translation initiation factor 5A;
DE AltName: Full=Hypusine-containing protein;
DE AltName: Full=eIF-5A;
GN Name=eif5a; OrderedLocusNames=APE_2085.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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; BA000002; BAA81096.2; -; Genomic_DNA.
DR PIR; H72513; H72513.
DR AlphaFoldDB; Q9YA53; -.
DR SMR; Q9YA53; -.
DR STRING; 272557.APE_2085.1; -.
DR EnsemblBacteria; BAA81096; BAA81096; APE_2085.1.
DR KEGG; ape:APE_2085.1; -.
DR PATRIC; fig|272557.25.peg.1389; -.
DR eggNOG; arCOG04277; Archaea.
DR OMA; QIMDMET; -.
DR Proteomes; UP000002518; 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;
KW Reference proteome.
FT CHAIN 1..139
FT /note="Translation initiation factor 5A"
FT /id="PRO_0000142489"
FT MOD_RES 36
FT /note="Hypusine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 139 AA; 15252 MW; 6DBB76C18D416D6E CRC64;
MSVNYATLGD LKKGSYIVID GEPCRIVEMS RAKTGKHGSA KAHVVAICVF SGQKKSLVAP
VDTRVQIPVI EKRLGQVLAD MGDMVQIMDL ETYDTFEVEK PGGNEEEEQL AAKLQPGVTV
EYWLIMGKPK IIRIRSSSS
