(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHT8_GEOS0

ID   A0A0F6BHT8_GEOS0        Unreviewed;        72 AA.
AC   A0A0F6BHT8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, 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   OrderedLocusNames=GY4MC1_0133 {ECO:0000313|EMBL:ADP72989.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72989.1};
RN   [1] {ECO:0000313|EMBL:ADP72989.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72989.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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, ECO:0000256|SAAS:SAAS01209831}.
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       ECO:0000256|SAAS:SAAS00326798}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00075}.
CC   -!- SIMILARITY: Belongs to the IF-1 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00075, ECO:0000256|SAAS:SAAS00571750}.
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DR   EMBL; CP002293; ADP72989.1; -; Genomic_DNA.
DR   RefSeq; WP_003247618.1; NC_014650.1.
DR   EnsemblBacteria; ADP72989; ADP72989; GY4MC1_0133.
DR   GeneID; 29574169; -.
DR   KEGG; gmc:GY4MC1_0133; -.
DR   KO; K02518; -.
DR   OMA; AHVSGKM; -.
DR   OrthoDB; 2066663at2; -.
DR   BioCyc; GSP581103:G1GOQ-160-MONOMER; -.
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   HAMAP; MF_00075; IF_1; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR004368; TIF_IF1.
DR   PANTHER; PTHR33370; PTHR33370; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00008; infA; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHT8.
DR   SWISS-2DPAGE; A0A0F6BHT8.
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00075};
KW   Initiation factor {ECO:0000256|HAMAP-Rule:MF_00075, ECO:0000256|PROSITE-
KW   ProRule:PRU00181, ECO:0000256|SAAS:SAAS00462727,
KW   ECO:0000313|EMBL:ADP72989.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00075};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00075, ECO:0000256|PROSITE-
KW   ProRule:PRU00181, ECO:0000256|SAAS:SAAS00462770};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00075,
KW   ECO:0000256|SAAS:SAAS00571734};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00075,
KW   ECO:0000256|SAAS:SAAS00571792}.
FT   DOMAIN          1..72
FT                   /note="S1-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50832"
FT   MOD_RES         60
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00075"
SQ   SEQUENCE   72 AA;  8228 MW;  57C0C615BBE97D8E CRC64;
     MAKDDVIEVE GTVVETLPNA MFRVELENGH TVLAHVSGKI RMHFIRILPG DKVTVELSPY
     DLTRGRITYR YK
//

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