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Database: UniProt
Entry: A0A140E5I3_9GAMM
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ID   A0A140E5I3_9GAMM        Unreviewed;        72 AA.
AC   A0A140E5I3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Translation initiation factor IF-1 {ECO:0000256|HAMAP-Rule:MF_00075};
GN   Name=infA {ECO:0000256|HAMAP-Rule:MF_00075};
GN   ORFNames=JT25_004005 {ECO:0000313|EMBL:AMK75657.1};
OS   Methylomonas denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=1538553 {ECO:0000313|EMBL:AMK75657.1, ECO:0000313|Proteomes:UP000030512};
RN   [1] {ECO:0000313|EMBL:AMK75657.1, ECO:0000313|Proteomes:UP000030512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJG1 {ECO:0000313|EMBL:AMK75657.1,
RC   ECO:0000313|Proteomes:UP000030512};
RX   PubMed=25580993; DOI=10.1111/1462-2920.12772;
RA   Kits K.D., Klotz M.G., Stein L.Y.;
RT   "Methane oxidation coupled to nitrate reduction under hypoxia by the
RT   Gammaproteobacterium Methylomonas denitrificans, sp. nov. type strain
RT   FJG1.";
RL   Environ. Microbiol. 17:3219-3232(2015).
CC   -!- FUNCTION: One of the essential components for the initiation of protein
CC       synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit
CC       to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps
CC       modulate mRNA selection, yielding the 30S pre-initiation complex (PIC).
CC       Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are
CC       released leaving the mature 70S translation initiation complex.
CC       {ECO:0000256|HAMAP-Rule:MF_00075}.
CC   -!- SUBUNIT: Component of the 30S ribosomal translation pre-initiation
CC       complex which assembles on the 30S ribosome in the order IF-2 and IF-3,
CC       IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at
CC       any time during PIC assembly. {ECO:0000256|HAMAP-Rule:MF_00075}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00075}.
CC   -!- SIMILARITY: Belongs to the IF-1 family. {ECO:0000256|ARBA:ARBA00010939,
CC       ECO:0000256|HAMAP-Rule:MF_00075}.
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DR   EMBL; CP014476; AMK75657.1; -; Genomic_DNA.
DR   RefSeq; WP_013819653.1; NZ_CP014476.1.
DR   AlphaFoldDB; A0A140E5I3; -.
DR   STRING; 1538553.JT25_004005; -.
DR   KEGG; mdn:JT25_004005; -.
DR   OrthoDB; 9803250at2; -.
DR   Proteomes; UP000030512; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04451; S1_IF1; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00075; IF_1; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR   InterPro; IPR003029; S1_domain.
DR   InterPro; IPR004368; TIF_IF1.
DR   NCBIfam; TIGR00008; infA; 1.
DR   PANTHER; PTHR33370; TRANSLATION INITIATION FACTOR IF-1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR33370:SF1; TRANSLATION INITIATION FACTOR IF-1, CHLOROPLASTIC; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00075};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_00075};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00075}; Reference proteome {ECO:0000313|Proteomes:UP000030512};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00075};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00075}.
FT   DOMAIN          1..72
FT                   /note="S1-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50832"
SQ   SEQUENCE   72 AA;  8417 MW;  B40D75CBFAA413BA CRC64;
     MAKEDQIEMD GKVIDTLPNT MFRVELENGH IVTAHISGKM RKHYIRILTG DKVRVEMTPY
     DLTKGRITFR NR
//
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