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Database: UniProt
Entry: A0A162GQ57_9MICO
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ID   A0A162GQ57_9MICO        Unreviewed;        73 AA.
AC   A0A162GQ57;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Translation initiation factor IF-1 {ECO:0000256|HAMAP-Rule:MF_00075};
GN   Name=infA {ECO:0000256|HAMAP-Rule:MF_00075,
GN   ECO:0000313|EMBL:KZX21028.1};
GN   ORFNames=ACH61_01863 {ECO:0000313|EMBL:KZX21028.1}, EV639_105209
GN   {ECO:0000313|EMBL:TCO37121.1};
OS   Rathayibacter tanaceti.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=1671680 {ECO:0000313|EMBL:KZX21028.1, ECO:0000313|Proteomes:UP000076717};
RN   [1] {ECO:0000313|EMBL:TCO37121.1, ECO:0000313|Proteomes:UP000295366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:TCO37121.1,
RC   ECO:0000313|Proteomes:UP000295366};
RX   PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA   Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA   De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA   Kyrpides N.C.;
RT   "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT   the genomes of soil and plant-associated and newly described type
RT   strains.";
RL   Stand. Genomic Sci. 10:26-26(2015).
RN   [2] {ECO:0000313|EMBL:KZX21028.1, ECO:0000313|Proteomes:UP000076717}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:KZX21028.1,
RC   ECO:0000313|Proteomes:UP000076717};
RA   Vasilenko O.V., Starodumova I.P., Tarlachkov S.V., Dorofeeva L.V.,
RA   Evtushenko L.I.;
RT   "Draft Genome Sequence of Rathayibacter sp. Strain VKM Ac-2596 Isolated
RT   from Leaf Gall Induced by Plant-Parasitic Nematodes.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:TCO37121.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:TCO37121.1};
RA   Whitman W., Huntemann M., Clum A., Pillay M., Palaniappan K., Varghese N.,
RA   Mikhailova N., Stamatis D., Reddy T., Daum C., Shapiro N., Ivanova N.,
RA   Kyrpides N., Woyke T.;
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZX21028.1}.
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DR   EMBL; LIIN01000058; KZX21028.1; -; Genomic_DNA.
DR   EMBL; SLWP01000005; TCO37121.1; -; Genomic_DNA.
DR   RefSeq; WP_022883252.1; NZ_SLWP01000005.1.
DR   AlphaFoldDB; A0A162GQ57; -.
DR   GeneID; 66874903; -.
DR   PATRIC; fig|1671680.3.peg.1978; -.
DR   OrthoDB; 9803250at2; -.
DR   Proteomes; UP000076717; Unassembled WGS sequence.
DR   Proteomes; UP000295366; Unassembled WGS sequence.
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; 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   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:UP000076717};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00075};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00075}.
FT   DOMAIN          1..73
FT                   /note="S1-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50832"
SQ   SEQUENCE   73 AA;  8406 MW;  16E21FF61C9F0E40 CRC64;
     MAKKDGVIEI EGAVVEALPN AMFRVELTNG HKVLAHISGK MRQHYIRILP EDRVIVELSP
     YDLTRGRIVY RYK
//
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