IF5A_SULIN
ID IF5A_SULIN Reviewed; 131 AA.
AC C3NHT8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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; OrderedLocusNames=YN1551_1610;
OS Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=419942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y.N.15.51 / Yellowstone #2;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001404; ACP48698.1; -; Genomic_DNA.
DR RefSeq; WP_012711261.1; NC_012623.1.
DR AlphaFoldDB; C3NHT8; -.
DR SMR; C3NHT8; -.
DR EnsemblBacteria; ACP48698; ACP48698; YN1551_1610.
DR GeneID; 7814462; -.
DR GeneID; 7940577; -.
DR GeneID; 8761181; -.
DR KEGG; sin:YN1551_1610; -.
DR HOGENOM; CLU_102600_3_0_2; -.
DR OMA; QIMDMET; -.
DR Proteomes; UP000006818; 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..131
FT /note="Translation initiation factor 5A"
FT /id="PRO_1000202607"
FT MOD_RES 36
FT /note="Hypusine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00085"
SQ SEQUENCE 131 AA; 14535 MW; ABA5ED21F75645F1 CRC64;
MSITYTTVGE LKVGSYVVID GEPCRVVEVT KAKTGKHGSA KANVVAIGVF SGAKKTLMAP
VDQQVEVPII EKHIGQIIAD MGDKIQVMDL ETYETFEIEK PTEDELASKI RPNAELEYWE
IMGRRKIVRV K