ID Q2FSC8_METHJ Unreviewed; 113 AA.
AC Q2FSC8;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Translation initiation factor 1A {ECO:0000256|HAMAP-Rule:MF_00216};
DE Short=aIF-1A {ECO:0000256|HAMAP-Rule:MF_00216};
GN Name=eif1a {ECO:0000256|HAMAP-Rule:MF_00216};
GN OrderedLocusNames=Mhun_2969 {ECO:0000313|EMBL:ABD42657.1};
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259 {ECO:0000313|EMBL:ABD42657.1, ECO:0000313|Proteomes:UP000001941};
RN [1] {ECO:0000313|Proteomes:UP000001941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1
RC {ECO:0000313|Proteomes:UP000001941};
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
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:0000256|ARBA:ARBA00025502, ECO:0000256|HAMAP-
CC Rule:MF_00216, ECO:0000256|RuleBase:RU004365}.
CC -!- SIMILARITY: Belongs to the eIF-1A family.
CC {ECO:0000256|ARBA:ARBA00007392, ECO:0000256|HAMAP-Rule:MF_00216,
CC ECO:0000256|RuleBase:RU004364}.
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DR EMBL; CP000254; ABD42657.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2FSC8; -.
DR STRING; 323259.Mhun_2969; -.
DR EnsemblBacteria; ABD42657; ABD42657; Mhun_2969.
DR KEGG; mhu:Mhun_2969; -.
DR eggNOG; arCOG01179; Archaea.
DR HOGENOM; CLU_109098_1_2_2; -.
DR InParanoid; Q2FSC8; -.
DR Proteomes; UP000001941; 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; Nucleic acid-binding proteins; 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 NCBIfam; TIGR00523; eIF-1A; 1.
DR PANTHER; PTHR21668; EIF-1A; 1.
DR PANTHER; PTHR21668:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 4C; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SMART; SM00652; eIF1a; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS01262; IF1A; 1.
DR PROSITE; PS50832; S1_IF1_TYPE; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_00216, ECO:0000256|PROSITE-
KW ProRule:PRU00181};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00216, ECO:0000256|PROSITE-
KW ProRule:PRU00181}; Reference proteome {ECO:0000313|Proteomes:UP000001941}.
FT DOMAIN 26..100
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 113 AA; 13279 MW; 0BAE175317567603 CRC64;
MISNIDDEWE EEVGASEKAG PDDEIIRVRL PKKSNNEQFA IAELMMGANH IRVRCSDGVT
RLGRIKGKMK KRAWIREGDI IIIVPWSFQD DKCDITYRYT PPQRDWLRRN NYL
//
