IF1A_PYRAB
ID IF1A_PYRAB Reviewed; 113 AA.
AC Q9V138; G8ZJ56;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Translation initiation factor 1A;
DE Short=aIF-1A;
GN Name=eIF1A; Synonyms=aif1A; OrderedLocusNames=PYRAB05910; ORFNames=PAB2441;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB49513.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ248284; CAB49513.1; ALT_INIT; Genomic_DNA.
DR EMBL; HE613800; CCE69983.1; -; Genomic_DNA.
DR PIR; B75179; B75179.
DR RefSeq; WP_048146587.1; NC_000868.1.
DR PDB; 4MNO; X-ray; 1.35 A; A=1-113.
DR PDB; 5JB3; EM; 5.34 A; 6=1-113.
DR PDB; 5JBH; EM; 5.34 A; 6=1-113.
DR PDB; 6SW9; EM; 4.20 A; 6=1-113.
DR PDB; 6SWC; EM; 3.30 A; 6=1-113.
DR PDB; 6SWD; EM; 3.20 A; 6=1-113.
DR PDB; 6SWE; EM; 3.10 A; 6=1-113.
DR PDBsum; 4MNO; -.
DR PDBsum; 5JB3; -.
DR PDBsum; 5JBH; -.
DR PDBsum; 6SW9; -.
DR PDBsum; 6SWC; -.
DR PDBsum; 6SWD; -.
DR PDBsum; 6SWE; -.
DR AlphaFoldDB; Q9V138; -.
DR SMR; Q9V138; -.
DR STRING; 272844.PAB2441; -.
DR EnsemblBacteria; CAB49513; CAB49513; PAB2441.
DR GeneID; 1495496; -.
DR KEGG; pab:PAB2441; -.
DR PATRIC; fig|272844.11.peg.629; -.
DR eggNOG; arCOG01179; Archaea.
DR HOGENOM; CLU_109098_1_2_2; -.
DR OrthoDB; 102432at2157; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 1: Evidence at protein level;
KW 3D-structure; Initiation factor; Protein biosynthesis.
FT CHAIN 1..113
FT /note="Translation initiation factor 1A"
FT /id="PRO_0000145128"
FT DOMAIN 12..87
FT /note="S1-like"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:4MNO"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:4MNO"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:4MNO"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:4MNO"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4MNO"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4MNO"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:4MNO"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:4MNO"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:4MNO"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:4MNO"
SQ SEQUENCE 113 AA; 13057 MW; A95C889DDFED6898 CRC64;
MPKKERKVEG DEVIRVPLPE GNQLFGVVEQ ALGAGWMDVR CEDGKIRRCR IPGKLRRRVW
IRVGDLVIVQ PWPVQSDKRG DIVYRYTQTQ VDWLLRKGKI TQEFLTGGSL LVE
