ID IF1A_SACS2 Reviewed; 108 AA.
AC Q97W62;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Translation initiation factor 1A;
DE Short=aIF-1A;
GN Name=eIF1A; OrderedLocusNames=SSO2375;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE006641; AAK42526.1; -; Genomic_DNA.
DR PIR; G90408; G90408.
DR RefSeq; WP_009989464.1; NC_002754.1.
DR AlphaFoldDB; Q97W62; -.
DR SMR; Q97W62; -.
DR STRING; 273057.SSO2375; -.
DR PaxDb; 273057-SSO2375; -.
DR EnsemblBacteria; AAK42526; AAK42526; SSO2375.
DR GeneID; 72910954; -.
DR KEGG; sso:SSO2375; -.
DR PATRIC; fig|273057.12.peg.2460; -.
DR eggNOG; arCOG01179; Archaea.
DR HOGENOM; CLU_109098_1_2_2; -.
DR InParanoid; Q97W62; -.
DR PhylomeDB; Q97W62; -.
DR Proteomes; UP000001974; 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 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; Protein biosynthesis; Reference proteome.
FT CHAIN 1..108
FT /note="Translation initiation factor 1A"
FT /id="PRO_0000145134"
FT DOMAIN 11..85
FT /note="S1-like"
SQ SEQUENCE 108 AA; 12518 MW; EC6ADC11A358B3D8 CRC64;
MPKKDRAQEA PSRDVPRPEE GQTICVVKKM LGGDHLIVLC MDGKERLARI PGKIRKKMWM
REGDVVLVGI WDFQPNRCDI LYKYGNDEIK RLVNENIISR EVIDQLRG
//
