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Database: UniProt
Entry: A0A1H3IBF2_ALLWA
LinkDB: A0A1H3IBF2_ALLWA
Original site: A0A1H3IBF2_ALLWA 
ID   A0A1H3IBF2_ALLWA        Unreviewed;       559 AA.
AC   A0A1H3IBF2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 4.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=SAMN05421644_14116 {ECO:0000313|EMBL:SDY24224.1};
OS   Allochromatium warmingii (Chromatium warmingii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Allochromatium.
OX   NCBI_TaxID=61595 {ECO:0000313|EMBL:SDY24224.1, ECO:0000313|Proteomes:UP000198672};
RN   [1] {ECO:0000313|EMBL:SDY24224.1, ECO:0000313|Proteomes:UP000198672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 173 {ECO:0000313|EMBL:SDY24224.1,
RC   ECO:0000313|Proteomes:UP000198672};
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; FNOW01000041; SDY24224.1; -; Genomic_DNA.
DR   BioCyc; GCF_900107145:BLW10_RS11210-MONOMER; -.
DR   Proteomes; UP000198672; 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; 2.
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:UP000198672};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198672};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:SDY24224.1};
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}.
SQ   SEQUENCE   559 AA;  61927 MW;  7192B8A474820EEF CRC64;
     MTESFAELFE QSLNTTQLQP GTIVVGTVID ITADNVVINA GLKSEGIIPR SQFISPEGEL
     EVAIGDEVEV ALDAVEDGFG VTRLSREKAK RFAAWDYLEK AFENAETVKG LINGKVKGGF
     TVELGSVRAF LPGSLVDVRP VRDTTYLEGK EQEFKVIKLD RKRNNVVVSR RAVVEEEYSA
     ERDQLLKNLE EGMEVKGVVK NLTDYGAFLD LGGIDGLLHI TDMAWRRVKH PSEVVEIGDE
     INVKVLKFDR DRQRVSLGLK QMGEDPWVNI SRRYPESTRV FGKVTNIADY GCFVEIEEGV
     EGLVHVSEMD WTNKNIHPSK VVNLGDEVEV MVLDIDEERR RISLGIKQCA MNPWEEFAVT
     HKKGDHVSGK IKSITDFGIF IGLDGGIDGL VHLSDISWDE AGENALRRYK KGDELETVVL
     SVDPERERIS LGVKQLDKDP FSSFVALHEK GSVVTGVVAE VDAKGATITL GDGVEGYLRA
     SEISRDRIED ARAVLKVGEE IEAKFLGVDR KNRTLSLSMK AKDAEEEQSA IKGYAREASG
     MATLGDLLKE QMEEAQRGN
//
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