IF5A_METBF
ID IF5A_METBF Reviewed; 128 AA.
AC Q46EL9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=Mbar_A0695;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ69673.1; -; Genomic_DNA.
DR RefSeq; WP_011305723.1; NC_007355.1.
DR AlphaFoldDB; Q46EL9; -.
DR SMR; Q46EL9; -.
DR STRING; 269797.Mbar_A0695; -.
DR EnsemblBacteria; AAZ69673; AAZ69673; Mbar_A0695.
DR GeneID; 3625762; -.
DR KEGG; mba:Mbar_A0695; -.
DR eggNOG; arCOG04277; Archaea.
DR HOGENOM; CLU_102600_3_0_2; -.
DR OMA; QIMDMET; -.
DR OrthoDB; 98221at2157; -.
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..128
FT /note="Translation initiation factor 5A"
FT /id="PRO_0000259437"
FT MOD_RES 35
FT /note="Hypusine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00085"
SQ SEQUENCE 128 AA; 14238 MW; 3A6467D6506BC5F4 CRC64;
MKQQVEVKEL KEGKYVIIDD EACVIKSITK SKPGKHGAAK ARVEAIGLFD GQKRSYIGSV
ANKIYVPIVE RKTAQVISIT GDITQLMDMG DFSTFEIVVP DEYKDKIKEG EEVSYITALG
KIKLDIRT
