IF5A_NATPD
ID IF5A_NATPD Reviewed; 124 AA.
AC Q3IN38;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 {ECO:0000255|HAMAP-Rule:MF_00085}; OrderedLocusNames=NP_4752A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI50467.1; -; Genomic_DNA.
DR RefSeq; WP_011324080.1; NC_007426.1.
DR AlphaFoldDB; Q3IN38; -.
DR SMR; Q3IN38; -.
DR STRING; 348780.NP_4752A; -.
DR EnsemblBacteria; CAI50467; CAI50467; NP_4752A.
DR GeneID; 3703270; -.
DR KEGG; nph:NP_4752A; -.
DR eggNOG; arCOG04277; Archaea.
DR HOGENOM; CLU_102600_3_0_2; -.
DR OMA; QIMDMET; -.
DR OrthoDB; 98221at2157; -.
DR Proteomes; UP000002698; 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; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11673; PTHR11673; 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..124
FT /note="Translation initiation factor 5A"
FT /id="PRO_0000259441"
FT REGION 27..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Hypusine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00085"
SQ SEQUENCE 124 AA; 14008 MW; EF1A567638535593 CRC64;
MPKEQKEVRD LQEGNYVMIE DVPSKITSYS TSKPGKHGSA KARVEGTGVF DGQKRNFTQP
VDAKVWVPIV NRKQGQVVSV SGDDMQVMDL ETYETITMRI PEDLAPESDD EIEYLEFEGQ
RKVV
