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Database: UniProt
Entry: A0A1D9BA82_9NEIS
LinkDB: A0A1D9BA82_9NEIS
Original site: A0A1D9BA82_9NEIS 
ID   A0A1D9BA82_9NEIS        Unreviewed;       557 AA.
AC   A0A1D9BA82;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   16-JAN-2019, entry version 7.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=BJP62_01945 {ECO:0000313|EMBL:AOX99320.1};
OS   Jeongeupia sp. USM3.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Jeongeupia.
OX   NCBI_TaxID=1906741 {ECO:0000313|EMBL:AOX99320.1, ECO:0000313|Proteomes:UP000176825};
RN   [1] {ECO:0000313|EMBL:AOX99320.1, ECO:0000313|Proteomes:UP000176825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USM3 {ECO:0000313|EMBL:AOX99320.1,
RC   ECO:0000313|Proteomes:UP000176825};
RA   Kho H.P.;
RT   "Jeongeupia sp. strain USM3 Genome sequencing and assembly.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AOX99320.1, ECO:0000313|Proteomes:UP000176825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USM3 {ECO:0000313|EMBL:AOX99320.1,
RC   ECO:0000313|Proteomes:UP000176825};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; CP017668; AOX99320.1; -; Genomic_DNA.
DR   RefSeq; WP_070525960.1; NZ_CP017668.1.
DR   KEGG; jeu:BJP62_01945; -.
DR   KO; K02945; -.
DR   OrthoDB; 1235756at2; -.
DR   Proteomes; UP000176825; 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:UP000176825};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176825};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:AOX99320.1};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN       20     86       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      104    170       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      191    259       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      276    346       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      363    433       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      450    519       S1 motif. {ECO:0000259|PROSITE:PS50126}.
SQ   SEQUENCE   557 AA;  61120 MW;  3E0F3CD44BB8BDC0 CRC64;
     MESFAALFEE SLQNQEMRSG EVITAEVVAI DHNFVTVNAG LKSESLIPVE EFKSDAGELD
     VKIGDFVTVA IDSIENGYGE TKLSREKAKR LAAWIELEDT LEKGLVMTGV ISGKVKGGLT
     VMVNGLRAFL PGSLVDIRPV KDTTPYEGKQ IEFKVIKLDR KRNNVVVSRR AVLEESLGEE
     RQKLMETLRE GAVIKGIVKN ITDYGAFVDL GGIDGLLHIT DLAWRRVKHP SEVLAVGDEI
     EAKVLKFDQE KNRVSLGLKQ LGEDPWVGLS RRYPSGTRLF GKVTNLTDYG AFVEIEQGIE
     GLVHVSEMDW TNKNVHPSKV VSLGDEVEVM ILDIDEEKRR ISLGMKQCMA NPWDEFGQNF
     KKGDKLQGAI KSITDFGVFV GLPGGIDGLV HLSDLSWHAT GEEAVRNFKK GDEVEAVVLS
     IDIDKERISL GIKQLEGDPF NNYVSTSDKG TIVRGTVKSL DAKGAVIGLT DEVEGYLRAT
     EVSRDRVEDI RTVLKEGDEV EAMIINVDRK NRSINLSIKS KDMGEEKAAM SQLSADASAG
     TTNLGALLKA KLSGSQE
//
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