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Database: UniProt
Entry: A0A1B7Z6C5_9RHOB
LinkDB: A0A1B7Z6C5_9RHOB
Original site: A0A1B7Z6C5_9RHOB 
ID   A0A1B7Z6C5_9RHOB        Unreviewed;       559 AA.
AC   A0A1B7Z6C5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   05-DEC-2018, entry version 7.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=A9199_14485 {ECO:0000313|EMBL:OBR38255.1};
OS   Donghicola sp. JL3646.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Donghicola.
OX   NCBI_TaxID=1836468 {ECO:0000313|EMBL:OBR38255.1, ECO:0000313|Proteomes:UP000092343};
RN   [1] {ECO:0000313|EMBL:OBR38255.1, ECO:0000313|Proteomes:UP000092343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL3646 {ECO:0000313|EMBL:OBR38255.1,
RC   ECO:0000313|Proteomes:UP000092343};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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:OBR38255.1}.
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DR   EMBL; LZFQ01000006; OBR38255.1; -; Genomic_DNA.
DR   RefSeq; WP_067548027.1; NZ_LZFQ01000006.1.
DR   EnsemblBacteria; OBR38255; OBR38255; A9199_14485.
DR   Proteomes; UP000092343; 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:UP000092343};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:OBR38255.1};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN       25     91       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      109    175       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      196    264       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      281    351       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      368    438       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      455    523       S1 motif. {ECO:0000259|PROSITE:PS50126}.
SQ   SEQUENCE   559 AA;  61222 MW;  1B2D1B630A902497 CRC64;
     MANVSMEEFE ALLQESFEID TPAEGSVVKG KVIAIEAGQA IIDVGYKMEG RVDLKEFANP
     GEAPSIAVGD EVEVFLRAAE NARGEAVISR EMARREEAWD RLEKAYAAEE RVEGAIFGRV
     KGGFTVDLGG AVAFLPGSQV DVRPVRDAGP LMGLKQPFQI LKMDRRRGNI VVSRRAILEE
     SRAEQRAEVI GNLTEGQAVE GVVKNITEYG AFVDLGGVDG LLHVTDMAWR RVNHPSEILS
     IGETINVQVI KINKDTHRIS LGMKQLQDDP WDAVETRYPL ESVHTGRVTN ITDYGAFVEL
     EAGVEGLVHV SEMSWTKKNV HPGKIVSTSQ EVEVMVLEID SSKRRVSLGL KQTQRNPWEV
     FAETHPEGTQ VEGEVKNITE FGLFIGLPGD IDGMVHLSDL SWDDRGEDAI QNYHKNDVVK
     AVVTEVDVEK ERISLSIKAM EGDPFAEAIG GVKRGSVITV NVTAIEDGGI EVEYEGMKSF
     IRRSDLSRDR AEQRPERFGV GDKVDVRVTN VDSKTRKLGL SIKAREIAEE KEAVEQYGSS
     ASGASLGDIL GAALKGSDE
//
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