IF1A_METJA
ID IF1A_METJA Reviewed; 102 AA.
AC Q57887;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Translation initiation factor 1A;
DE Short=aIF-1A;
GN Name=eIF1A; OrderedLocusNames=MJ0445;
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 STRUCTURE BY NMR.
RX PubMed=11714910; DOI=10.1110/ps.18201;
RA Li W., Hoffman D.W.;
RT "Structure and dynamics of translation initiation factor aIF-1A from the
RT archaeon Methanococcus jannaschii determined by NMR spectroscopy.";
RL Protein Sci. 10:2426-2438(2001).
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eIF-1A family. {ECO:0000305}.
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DR EMBL; L77117; AAB98435.1; -; Genomic_DNA.
DR PIR; E64355; E64355.
DR RefSeq; WP_010869944.1; NC_000909.1.
DR PDB; 1JT8; NMR; -; A=1-102.
DR PDBsum; 1JT8; -.
DR AlphaFoldDB; Q57887; -.
DR SMR; Q57887; -.
DR STRING; 243232.MJ_0445; -.
DR EnsemblBacteria; AAB98435; AAB98435; MJ_0445.
DR GeneID; 1451305; -.
DR KEGG; mja:MJ_0445; -.
DR eggNOG; arCOG01179; Archaea.
DR HOGENOM; CLU_109098_1_2_2; -.
DR InParanoid; Q57887; -.
DR OMA; ADITWRY; -.
DR OrthoDB; 102432at2157; -.
DR PhylomeDB; Q57887; -.
DR EvolutionaryTrace; Q57887; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..102
FT /note="Translation initiation factor 1A"
FT /id="PRO_0000145121"
FT DOMAIN 10..85
FT /note="S1-like"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:1JT8"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:1JT8"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1JT8"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:1JT8"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1JT8"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:1JT8"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:1JT8"
SQ SEQUENCE 102 AA; 12184 MW; 8082FD686A103FC0 CRC64;
MAEQQQEQQI RVRIPRKEEN EILGIIEQML GASRVRVRCL DGKTRLGRIP GRLKNRIWVR
EGDVVIVKPW EVQGDQKCDI IWRYTKTQVE WLKRKGYLDE LL