ID A0A3M7TCD8_9FLAO Unreviewed; 71 AA.
AC A0A3M7TCD8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=D1631_01305 {ECO:0000313|EMBL:RNA60664.1}, D1632_04035
GN {ECO:0000313|EMBL:RMZ61140.1};
OS Chryseobacterium nematophagum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=2305228 {ECO:0000313|EMBL:RNA60664.1, ECO:0000313|Proteomes:UP000278775};
RN [1] {ECO:0000313|Proteomes:UP000267524, ECO:0000313|Proteomes:UP000278775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUb129 {ECO:0000313|EMBL:RNA60664.1,
RC ECO:0000313|Proteomes:UP000278775}, and JUb275
RC {ECO:0000313|EMBL:RMZ61140.1, ECO:0000313|Proteomes:UP000267524};
RA Page A., Roberts M., Felix M.-A., Weir W.;
RT "Chryseobacterium nematophagum: a novel matrix digesting pathogen of
RT nematodes.";
RL Submitted (AUG-2018) 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:RNA60664.1}.
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DR EMBL; QWIV01000005; RMZ61140.1; -; Genomic_DNA.
DR EMBL; QWIU01000002; RNA60664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M7TCD8; -.
DR OrthoDB; 9803250at2; -.
DR Proteomes; UP000267524; Unassembled WGS sequence.
DR Proteomes; UP000278775; 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}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_00075};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00075}.
FT DOMAIN 1..71
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
SQ SEQUENCE 71 AA; 8198 MW; ED9DC3E84DFFEDE8 CRC64;
MAKQKHIEQD GVIVEALSNA MFRVELENGH VLIAHISGKM RMHYIKLLPG DKVKLEMSPY
DLTKGRITFR Y
//