IF1A_METBU
ID IF1A_METBU Reviewed; 106 AA.
AC Q12YN5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Translation initiation factor 1A {ECO:0000255|HAMAP-Rule:MF_00216};
DE Short=aIF-1A {ECO:0000255|HAMAP-Rule:MF_00216};
GN Name=eif1a {ECO:0000255|HAMAP-Rule:MF_00216}; OrderedLocusNames=Mbur_0456;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
CC -!- FUNCTION: Seems to be required for maximal rate of protein
CC biosynthesis. Enhances ribosome dissociation into subunits and
CC stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal
CC subunits. {ECO:0000255|HAMAP-Rule:MF_00216}.
CC -!- SIMILARITY: Belongs to the eIF-1A family. {ECO:0000255|HAMAP-
CC Rule:MF_00216}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000300; ABE51441.1; -; Genomic_DNA.
DR RefSeq; WP_011498603.1; NC_007955.1.
DR AlphaFoldDB; Q12YN5; -.
DR SMR; Q12YN5; -.
DR STRING; 259564.Mbur_0456; -.
DR EnsemblBacteria; ABE51441; ABE51441; Mbur_0456.
DR GeneID; 3998258; -.
DR KEGG; mbu:Mbur_0456; -.
DR HOGENOM; CLU_109098_1_2_2; -.
DR OMA; ADITWRY; -.
DR OrthoDB; 102432at2157; -.
DR Proteomes; UP000001979; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd05793; S1_IF1A; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00216; aIF_1A; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR InterPro; IPR001253; TIF_eIF-1A.
DR InterPro; IPR018104; TIF_eIF-1A_CS.
DR PANTHER; PTHR21668; PTHR21668; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SMART; SM00652; eIF1a; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00523; eIF-1A; 1.
DR PROSITE; PS01262; IF1A; 1.
DR PROSITE; PS50832; S1_IF1_TYPE; 1.
PE 3: Inferred from homology;
KW Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..106
FT /note="Translation initiation factor 1A"
FT /id="PRO_0000259366"
FT DOMAIN 18..92
FT /note="S1-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00216"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 106 AA; 12154 MW; A46213A57E5C89F8 CRC64;
MKKNNGGRGS KTDAPAVTRV RTPRRENNEI LATVSALLGG KRVTLQCMDG IVRMGRIPGS
KKKRMWVREG DIVIITPWDF QDSKAEVIWK YTRPQVEWLE RKGFLK