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Database: UniProt
Entry: A8AAA6_IGNH4
LinkDB: A8AAA6_IGNH4
Original site: A8AAA6_IGNH4 
ID   A8AAA6_IGNH4            Unreviewed;       132 AA.
AC   A8AAA6;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 81.
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=Igni_0676 {ECO:0000313|EMBL:ABU81858.1};
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591 {ECO:0000313|EMBL:ABU81858.1, ECO:0000313|Proteomes:UP000000262};
RN   [1] {ECO:0000313|EMBL:ABU81858.1, ECO:0000313|Proteomes:UP000000262}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125
RC   {ECO:0000313|Proteomes:UP000000262};
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H.Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
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. {ECO:0000256|HAMAP-
CC       Rule:MF_00216}.
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DR   EMBL; CP000816; ABU81858.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8AAA6; -.
DR   STRING; 453591.Igni_0676; -.
DR   KEGG; iho:Igni_0676; -.
DR   eggNOG; arCOG01179; Archaea.
DR   HOGENOM; CLU_109098_1_2_2; -.
DR   OMA; NGQETIC; -.
DR   OrthoDB; 2586at2157; -.
DR   PhylomeDB; A8AAA6; -.
DR   Proteomes; UP000000262; 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   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; 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:UP000000262}.
FT   DOMAIN          11..87
FT                   /note="S1-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50832"
SQ   SEQUENCE   132 AA;  14905 MW;  3B901E7B527B55D7 CRC64;
     MAKRKGTRSE KSKEVVLPGE GEVLCVVERI VGADHALIRC LDNPELVRDG RIPGKLRRRV
     WIREGDIVIA TVWDFQPKKA DIVYRYSRDE LKRLIVKGLL PKEIAELAGI TEEEIALTAQ
     QMAQEEAEGE EA
//
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