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Database: UniProt
Entry: A6FVB8_9RHOB
LinkDB: A6FVB8_9RHOB
Original site: A6FVB8_9RHOB 
ID   A6FVB8_9RHOB            Unreviewed;       562 AA.
AC   A6FVB8;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   08-MAY-2019, entry version 41.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   Name=rpsA {ECO:0000313|EMBL:EDM69820.1};
GN   ORFNames=RAZWK3B_10672 {ECO:0000313|EMBL:EDM69820.1};
OS   Roseobacter sp. AzwK-3b.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Roseobacter.
OX   NCBI_TaxID=351016 {ECO:0000313|EMBL:EDM69820.1, ECO:0000313|Proteomes:UP000004119};
RN   [1] {ECO:0000313|EMBL:EDM69820.1, ECO:0000313|Proteomes:UP000004119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AzwK-3b {ECO:0000313|EMBL:EDM69820.1,
RC   ECO:0000313|Proteomes:UP000004119};
RA   Francis C., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) 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:EDM69820.1}.
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DR   EMBL; ABCR01000013; EDM69820.1; -; Genomic_DNA.
DR   STRING; 351016.RAZWK3B_10672; -.
DR   EnsemblBacteria; EDM69820; EDM69820; RAZWK3B_10672.
DR   eggNOG; ENOG4105CAV; Bacteria.
DR   eggNOG; COG0539; LUCA.
DR   Proteomes; UP000004119; 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   Complete proteome {ECO:0000313|Proteomes:UP000004119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004119};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:EDM69820.1};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN       26     92       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      110    176       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      197    265       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      282    352       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      369    439       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      456    524       S1 motif. {ECO:0000259|PROSITE:PS50126}.
SQ   SEQUENCE   562 AA;  61673 MW;  C6829FA97504268E CRC64;
     MAHNASMEEF ETLLNESLEM DTPDEGSVVK GKVIAIEAGQ AIIDVGYKME GRVDLKEFAN
     PGEAPEIAVG DEVEVFLRAA ENSRGEAVIS REMARREEAW DRLEKAYADE ERVDGAIFGR
     VKGGFTVDLG GAVAFLPGSQ VDVRPVRDAG PLMGLKQPFQ ILKMDRRRGN IVVSRRAILE
     ESRAEQRAEV ISQLTEGDTV DGVVKNITEY GAFVDLGGVD GLLHVTDMAW RRVNHPSEIL
     SIGETVKVQV IKINKETHRI SLGMKQLQED PWDLVAAKYP LASVHTGRVT NITDYGAFVE
     LEPGVEGLVH VSEMSWTKKN VHPGKIVSTS QEVEVMVLEI DQAKRRVSLG LKQTQRNPWE
     VFAETHPVGT EVEGEVKNIT EFGLFIGLPG DIDGMVHLSD LSWDERGEEA IQNYKKGDIV
     KAVVSEVDVE KERISLSIKA LDGDPFADAV GGVKRGSIIT VEVTSIEDGG IEVQYDGLKS
     FIRRSDLSRD RSEQRPERFT VGDKVDVRVT NVDSKTRRLG LSIKAREIAE EKEAVQQYGS
     SDSGASLGDI LGAALKGDDD KG
//
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