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Database: UniProt
Entry: M4R5N0_BIBTR
LinkDB: M4R5N0_BIBTR
Original site: M4R5N0_BIBTR 
ID   M4R5N0_BIBTR            Unreviewed;       548 AA.
AC   M4R5N0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   16-JAN-2019, entry version 24.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=WQG_11280 {ECO:0000313|EMBL:AGH38405.1};
OS   Bibersteinia trehalosi USDA-ARS-USMARC-192.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Bibersteinia.
OX   NCBI_TaxID=1171377 {ECO:0000313|EMBL:AGH38405.1, ECO:0000313|Proteomes:UP000011846};
RN   [1] {ECO:0000313|EMBL:AGH38405.1, ECO:0000313|Proteomes:UP000011846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=192 {ECO:0000313|Proteomes:UP000011846};
RA   Harhay G.P., Koren S., Phillippy A., McVey D.S., Kuszak J.,
RA   Clawson M., Harhay D.M., Heaton M., Chitko-Mckown C., Smith T.P.L.;
RT   "Annotation of the Bibersteinia trehalsoi USDA-ARS-USMARC-192 complete
RT   genome.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds mRNA; thus facilitating recognition of the
CC       initiation point. It is needed to translate mRNA with a short
CC       Shine-Dalgarno (SD) purine-rich sequence.
CC       {ECO:0000256|PIRNR:PIRNR002111}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC       {ECO:0000256|PIRNR:PIRNR002111}.
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DR   EMBL; CP003745; AGH38405.1; -; Genomic_DNA.
DR   RefSeq; WP_015432543.1; NC_020515.1.
DR   EnsemblBacteria; AGH38405; AGH38405; WQG_11280.
DR   KEGG; bto:WQG_11280; -.
DR   PATRIC; fig|1171377.3.peg.1122; -.
DR   KO; K02945; -.
DR   BioCyc; BTRE1171377:G1HFQ-1148-MONOMER; -.
DR   Proteomes; UP000011846; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000110; Ribosomal_S1.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   Pfam; PF00575; S1; 6.
DR   PIRSF; PIRSF002111; RpsA; 1.
DR   SMART; SM00316; S1; 6.
DR   SUPFAM; SSF50249; SSF50249; 6.
DR   TIGRFAMs; TIGR00717; rpsA; 1.
DR   PROSITE; PS50126; S1; 6.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000011846};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011846};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:AGH38405.1};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN       22     88       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      106    172       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      193    261       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      278    348       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      365    435       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      452    513       S1 motif. {ECO:0000259|PROSITE:PS50126}.
SQ   SEQUENCE   548 AA;  59850 MW;  A7F5B356D41EC026 CRC64;
     MSELSFAELF EESLKGQETR LGSIVKGTVV KIQKGLVFVD AGLKSESAIP AEEFFNAQGE
     LEVQVGDVVD VALDAVEDGF GETKLSREKA KRNESWAALE KAFEEQATVT GYVNGKVKGG
     FTVELNGVRA FLPGSLVDTR PVRSEVNLEG QTLELKVIKL DQKRNNVVVS RRAVIESTSS
     ADREEVLANL VEGSEVKGTV KNLTEYGAFV DLGGVDGLLH ITDMAWKRVK HPSEVVNVGD
     ELTVKVLKFD KEKTRVSLGL KQLGQDPWVA IAQNHPVNSK LTGKVTNLTD YGCFVEILDG
     VEGLVHVSEM DWTNKNIHPS KVVNVGDVVE VMVLEVDEER RRISLGLKQC KANPWEHFAE
     THNKNDKVKG KIKSITDFGI FIGLEGGIDG LVHLSDISWN VAGEEAVRNY KKGDEVEAVV
     LQVDAVKERI SLGIKQLESD PFTNFVDSTK KGEIVSAKVV EVDAKGAKVE LIEGVEGFIR
     AADLTEEVAV NDTVEAKYTG VDRKSRIVHL SVRAKDQAEE SAAIAQVNKE EVVMPNAFAE
     AFKAAKGE
//
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