ID A0A0F7FIS1_9CREN Unreviewed; 108 AA.
AC A0A0F7FIS1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=MA03_07820 {ECO:0000313|EMBL:AKG39160.1};
OS Infirmifilum uzonense.
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Infirmifilum.
OX NCBI_TaxID=1550241 {ECO:0000313|EMBL:AKG39160.1, ECO:0000313|Proteomes:UP000067434};
RN [1] {ECO:0000313|EMBL:AKG39160.1, ECO:0000313|Proteomes:UP000067434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1807-2 {ECO:0000313|EMBL:AKG39160.1,
RC ECO:0000313|Proteomes:UP000067434};
RX PubMed=26664700; DOI=10.1186/s40793-015-0105-y;
RA Toshchakov S.V., Korzhenkov A.A., Samarov N.I., Mazunin I.O., Mozhey O.I.,
RA Shmyr I.S., Derbikova K.S., Taranov E.A., Dominova I.N.,
RA Bonch-Osmolovskaya E.A., Patrushev M.V., Podosokorskaya O.A.,
RA Kublanov I.V.;
RT "Complete genome sequence of and proposal of Thermofilum uzonense sp. nov.
RT a novel hyperthermophilic crenarchaeon and emended description of the genus
RT Thermofilum.";
RL Stand. Genomic Sci. 10:122-122(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}.
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DR EMBL; CP009961; AKG39160.1; -; Genomic_DNA.
DR RefSeq; WP_052884711.1; NZ_CP009961.1.
DR AlphaFoldDB; A0A0F7FIS1; -.
DR STRING; 1550241.MA03_07820; -.
DR GeneID; 25402129; -.
DR KEGG; thf:MA03_07820; -.
DR PATRIC; fig|1550241.5.peg.1621; -.
DR HOGENOM; CLU_109098_1_2_2; -.
DR OrthoDB; 2586at2157; -.
DR Proteomes; UP000067434; 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:UP000067434}.
FT DOMAIN 12..87
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
SQ SEQUENCE 108 AA; 12454 MW; AD69D0120663E9BF CRC64;
MSKNPKEPEE TEESEIPLPD GQTTLLCVIQ QLLGFDRARV FCSDGKIRLC RIPGKLKKRM
WMKVGDLVLV APWDFQPDKG DILYRYTGTE IQRLERKGLL KDLHQLLG
//
