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Database: UniProt
Entry: A0A240U189_9BURK
LinkDB: A0A240U189_9BURK
Original site: A0A240U189_9BURK 
ID   A0A240U189_9BURK        Unreviewed;       561 AA.
AC   A0A240U189;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   05-JUN-2019, entry version 7.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=CBP34_08175 {ECO:0000313|EMBL:ART51639.1};
OS   Acidovorax carolinensis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=553814 {ECO:0000313|EMBL:ART51639.1, ECO:0000313|Proteomes:UP000194432};
RN   [1] {ECO:0000313|EMBL:ART51639.1, ECO:0000313|Proteomes:UP000194432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA3 {ECO:0000313|EMBL:ART51639.1};
RA   Singleton D.R., Lee J., Dickey A.N., Stroud A., Scholl E.H.,
RA   Wright F.A., Aitken M.D.;
RT   "Polyphasic characterization of four soil-derived phenanthrene-
RT   degrading Acidovorax strains and proposal of Acidovorax
RT   phenanthrenivorans sp. nov.";
RL   Submitted (MAY-2017) 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; CP021361; ART51639.1; -; Genomic_DNA.
DR   RefSeq; WP_008905636.1; NZ_CP021361.1.
DR   KEGG; acin:CBP34_08175; -.
DR   KO; K02945; -.
DR   BioCyc; GCF_002157145:CBP34_RS08195-MONOMER; -.
DR   Proteomes; UP000194432; 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:UP000194432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194432};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:ART51639.1};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN       21     87       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      105    171       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      192    260       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      277    347       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      364    434       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      451    520       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      529    551       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A240U189}.
FT   COMPBIAS    530    546       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A240U189}.
SQ   SEQUENCE   561 AA;  61623 MW;  69646EA5602530BC CRC64;
     MSESFAALFE ESLTRTEMRP GEVITAEVVR VEHNFVVVNA GLKSEAYVPL EEFKNDKGEV
     EVQVGDFVSV AIGSIENGYG DTILSRDTAK RLASWMSLEK ALESGEFVTG TTSGKVKGGL
     TVLVNGIRAF LPGSLIDTRP IKDLTPYENK TMEFKVIKLD RKRNNVVLSR RAVVEASMGE
     ERAKLMETLK EGSIVQGVVK NITEYGAFVD LGGIDGLLHI TDMAWRRVRH PSEVVTAGQE
     ITAKILKFDT EKNRVSLGLK QMGDDPWMGV NRRYPQGTRL FGKITNIADY GAFVELEPGI
     EGLVHVSEMD WTNKNIAPAK LVSLGDEVEV MVLEIDEDKR RISLGMKQCK ANPWQEFAQD
     TKRGDRVKGP IKSITDFGVF VGLAAGIDGL VHLSDLSWNE AGEAAVRNYK KGQEVEAIVL
     AVDVDRERIS LGIKQLDGDP FTTFVTVNDK GQTVTGKVKT VDARGAEIDL GEDIVGYLRA
     SEISRDRVED ARNVLKEGDE VTAVVVNVDR KTRNIQLSIK QKDMADEQGA MANLSQQSSR
     ESAGTTSLGA LLRAKLDNSE K
//
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