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Database: UniProt
Entry: A0A176YLZ6_9BRAD
LinkDB: A0A176YLZ6_9BRAD
Original site: A0A176YLZ6_9BRAD 
ID   A0A176YLZ6_9BRAD        Unreviewed;       568 AA.
AC   A0A176YLZ6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   03-JUL-2019, entry version 9.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=AYJ54_15560 {ECO:0000313|EMBL:OAF08155.1};
OS   Bradyrhizobium centrolobii.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=1505087 {ECO:0000313|EMBL:OAF08155.1, ECO:0000313|Proteomes:UP000076959};
RN   [1] {ECO:0000313|EMBL:OAF08155.1, ECO:0000313|Proteomes:UP000076959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR 10245 {ECO:0000313|EMBL:OAF08155.1,
RC   ECO:0000313|Proteomes:UP000076959};
RA   Simoes-Araujo J.L.Sr., Barauna A.C., Silva K., Zilli J.E.;
RT   "Draft Genome Sequence of the Strain BR 10245 (Bradyrhizobium sp.)
RT   isolated from nodules of Centrolobium paraense.";
RL   Submitted (MAR-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OAF08155.1}.
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DR   EMBL; LUUB01000063; OAF08155.1; -; Genomic_DNA.
DR   RefSeq; WP_063701556.1; NZ_LUUB01000063.1.
DR   EnsemblBacteria; OAF08155; OAF08155; AYJ54_15560.
DR   Proteomes; UP000076959; Unassembled WGS sequence.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000076959};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:OAF08155.1};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN       32     98       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      116    182       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      203    271       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      288    358       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      375    445       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      456    531       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   COILED       83    103       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   568 AA;  62931 MW;  DFA15904FB580A48 CRC64;
     MASISADTYS PSRDDFAAML DESFAGGNLQ ESSVVKGKVV AIEKDMAVID VGLKTEGRVA
     LREFSGPGRE SDLKVGDEVE VFLDRIENAL GEAVLSRDKA RREESWGKLE KAFQNNEKVT
     GVIFNQVKGG FTVDLDGAVA FLPRSQVDIR PIRDVAPLMN NAQPFQILKM DRRRGNIVVS
     RRTVLEETRA EQRQELVQNL EEGQVIDGVV KNITDYGAFV DLGGIDGLLH VTDIAWRRVN
     HPTEVLSIGQ TVKVKIIKIN HETHRISLGM KQLLDDPWQG IEAKYPLGAR FTGRVTNITD
     YGAFVELEPG IEGLIHVSEM SWTKKNMHPG KIVSTSQEVE VQVLEVDSVK RRISLGLKQT
     MRNPWEVFVE KHPTGSVVEG EVKNKTEFGL FLGLEGDVDG MVHLSDLDWK LPGEQVIDNY
     KKGDMVKAVV LDVDVEKERI SLGIKQLEGD PFAEPGDVKK GAVVTCEVLE VKESGIEVKI
     VGTDFTTFIK RSELARDRND QRAERFAVGE KVDARVIQFD KKARKVQVSI KALEVAEEKE
     AIAQYGSSDS GATLGDILGT ALKNRDNK
//
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