ID A0A498GXR7_9EURY Unreviewed; 71 AA.
AC A0A498GXR7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
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 ORFNames=ABH15_11115 {ECO:0000313|EMBL:RXE55313.1};
OS Methanoculleus taiwanensis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=1550565 {ECO:0000313|EMBL:RXE55313.1, ECO:0000313|Proteomes:UP000290932};
RN [1] {ECO:0000313|EMBL:RXE55313.1, ECO:0000313|Proteomes:UP000290932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CYW4 {ECO:0000313|EMBL:RXE55313.1,
RC ECO:0000313|Proteomes:UP000290932};
RX PubMed=25575827; DOI=.1099/ijs.0.000062;
RA Weng C.Y., Chen S.C., Lai M.C., Wu S.Y., Lin S., Yang T.F., Chen P.C.;
RT "Methanoculleus taiwanensis sp. nov., a methanogen isolated from deep
RT marine sediment at the deformation front area near Taiwan.";
RL Int. J. Syst. Evol. Microbiol. 65:1044-1049(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXE55313.1}.
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DR EMBL; LHQS01000003; RXE55313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498GXR7; -.
DR Proteomes; UP000290932; Unassembled WGS sequence.
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:UP000290932}.
FT DOMAIN 1..56
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
SQ SEQUENCE 71 AA; 8619 MW; E31D4AA5A21668EF CRC64;
MLGSNHIRVR CEDGVTRMGR IKGKIKKRLW IREGDLLIVV PWDFQDEKCD IIYRYIRPQV
EWLQKNNYLS K
//
