IF5A_METJA
ID IF5A_METJA Reviewed; 132 AA.
AC Q58625;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Translation initiation factor 5A;
DE AltName: Full=Hypusine-containing protein;
DE AltName: Full=eIF-5A;
GN Name=eif5a; OrderedLocusNames=MJ1228;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP SIMILARITY.
RX PubMed=9419357; DOI=10.1073/pnas.95.1.224;
RA Kyrpides N.C., Woese C.R.;
RT "Universally conserved translation initiation factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:224-228(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND HYPUSINE AT LYS-37.
RX PubMed=9724718; DOI=10.1073/pnas.95.18.10419;
RA Kim K.K., Hung L.W., Yokota H., Kim R., Kim S.H.;
RT "Crystal structures of eukaryotic translation initiation factor 5A from
RT Methanococcus jannaschii at 1.8-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10419-10424(1998).
CC -!- FUNCTION: Functions by promoting the formation of the first peptide
CC bond.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
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DR EMBL; L77117; AAB99231.1; -; Genomic_DNA.
DR RefSeq; WP_010870740.1; NC_000909.1.
DR PDB; 1EIF; X-ray; 1.90 A; A=1-132.
DR PDB; 2EIF; X-ray; 1.80 A; A=1-132.
DR PDBsum; 1EIF; -.
DR PDBsum; 2EIF; -.
DR AlphaFoldDB; Q58625; -.
DR SMR; Q58625; -.
DR STRING; 243232.MJ_1228; -.
DR EnsemblBacteria; AAB99231; AAB99231; MJ_1228.
DR GeneID; 1452124; -.
DR KEGG; mja:MJ_1228; -.
DR eggNOG; arCOG04277; Archaea.
DR HOGENOM; CLU_102600_3_0_2; -.
DR InParanoid; Q58625; -.
DR OMA; QIMDMET; -.
DR OrthoDB; 98221at2157; -.
DR PhylomeDB; Q58625; -.
DR EvolutionaryTrace; Q58625; -.
DR Proteomes; UP000000805; 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; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045901; P:positive regulation of translational elongation; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hypusine; Initiation factor; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..132
FT /note="Translation initiation factor 5A"
FT /id="PRO_0000142493"
FT MOD_RES 37
FT /note="Hypusine"
FT /evidence="ECO:0000269|PubMed:9724718"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2EIF"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:2EIF"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:2EIF"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:2EIF"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2EIF"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:2EIF"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:2EIF"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:2EIF"
FT STRAND 71..82
FT /evidence="ECO:0007829|PDB:2EIF"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:2EIF"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2EIF"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2EIF"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:2EIF"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:2EIF"
SQ SEQUENCE 132 AA; 14180 MW; 5B0F48905B0DCF69 CRC64;
MPGTKQVNVG SLKVGQYVMI DGVPCEIVDI SVSKPGKHGG AKARVVGIGI FEKVKKEFVA
PTSSKVEVPI IDRRKGQVLA IMGDMVQIMD LQTYETLELP IPEGIEGLEP GGEVEYIEAV
GQYKITRVIG GK
