IF5A_PYRIL
ID IF5A_PYRIL Reviewed; 132 AA.
AC A1RS27;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Pisl_0581;
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000504; ABL87759.1; -; Genomic_DNA.
DR RefSeq; WP_011762335.1; NC_008701.1.
DR AlphaFoldDB; A1RS27; -.
DR SMR; A1RS27; -.
DR STRING; 384616.Pisl_0581; -.
DR EnsemblBacteria; ABL87759; ABL87759; Pisl_0581.
DR GeneID; 4617552; -.
DR KEGG; pis:Pisl_0581; -.
DR eggNOG; arCOG04277; Archaea.
DR HOGENOM; CLU_102600_3_0_2; -.
DR OMA; QIMDMET; -.
DR OrthoDB; 98221at2157; -.
DR Proteomes; UP000002595; 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..132
FT /note="Translation initiation factor 5A"
FT /id="PRO_1000007918"
FT MOD_RES 36
FT /note="Hypusine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00085"
SQ SEQUENCE 132 AA; 14693 MW; C8BBABCAE28B90D1 CRC64;
MSTKYVEVGE LKEGSYVVID GEPCRVVEIE KSKTGKHGSA KARIVAIGVF DGGKRTLSLP
VDAQIEVPII EKFTAQVLSI SGNVIQLMDM RDYKTIEVPI DYVEEEAKGR LAPGVEVEVW
QILNRYKITR VK
