ID A8MC85_CALMQ Unreviewed; 102 AA.
AC A8MC85;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=Cmaq_0548 {ECO:0000313|EMBL:ABW01391.1};
OS Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS IC-167).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Caldivirga.
OX NCBI_TaxID=397948 {ECO:0000313|EMBL:ABW01391.1, ECO:0000313|Proteomes:UP000001137};
RN [1] {ECO:0000313|EMBL:ABW01391.1, ECO:0000313|Proteomes:UP000001137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167
RC {ECO:0000313|Proteomes:UP000001137};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Caldivirga maquilingensis IC-167.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: Belongs to the eIF-1A family.
CC {ECO:0000256|ARBA:ARBA00007392, ECO:0000256|HAMAP-Rule:MF_00216}.
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DR EMBL; CP000852; ABW01391.1; -; Genomic_DNA.
DR AlphaFoldDB; A8MC85; -.
DR STRING; 397948.Cmaq_0548; -.
DR KEGG; cma:Cmaq_0548; -.
DR eggNOG; arCOG01179; Archaea.
DR HOGENOM; CLU_109098_1_2_2; -.
DR Proteomes; UP000001137; 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 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:UP000001137}.
FT DOMAIN 5..77
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
SQ SEQUENCE 102 AA; 11802 MW; F0CD2580007B20C8 CRC64;
MSAESKVRVP DEGEMLAKVT DIVGDDRVKV VCEDGNVRIA RIPGKYRKRM WIRIGDYLIV
APWDFEPSKA DVVYKYEKGE VNELRRISKY SEVLNRLDEL AL
//
