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Database: UniProt
Entry: A0A1V9DQA6_9GAMM
LinkDB: A0A1V9DQA6_9GAMM
Original site: A0A1V9DQA6_9GAMM 
ID   A0A1V9DQA6_9GAMM        Unreviewed;       557 AA.
AC   A0A1V9DQA6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   16-JAN-2019, entry version 6.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=B2J69_02140 {ECO:0000313|EMBL:OQP36031.1};
OS   Pantoea latae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=1964541 {ECO:0000313|EMBL:OQP36031.1, ECO:0000313|Proteomes:UP000192769};
RN   [1] {ECO:0000313|EMBL:OQP36031.1, ECO:0000313|Proteomes:UP000192769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS1 {ECO:0000313|EMBL:OQP36031.1,
RC   ECO:0000313|Proteomes:UP000192769};
RA   Lata P., Govindarajan S., Qi F., Li J.-L., Maurya S.K., Sahoo M.K.;
RT   "Whole genome shotgun sequence of Pantoea agglomerans strain AS1
RT   isolated from a cycad, Zamia floridana in Central Florida, USA.";
RL   Submitted (FEB-2017) 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:OQP36031.1}.
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DR   EMBL; MWUE01000004; OQP36031.1; -; Genomic_DNA.
DR   Proteomes; UP000192769; 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:UP000192769};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:OQP36031.1};
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   557 AA;  61195 MW;  0E090063E968A557 CRC64;
     MTESFAQLFE ESLKEIETRP GSIVRGVVVS IDKDVVLVDA GLKSESAIPA EQFKNAAGEL
     EIQVGDEVDV ALDAVEDGFG ETLLSREKAK RHEAWITLEK AYEDAETVTG VINGKVKGGF
     TVELNGIRAF LPGSLVDVRP VRDTLHLEGK ELEFKVIKLD QKRNNVVVSR RAVIESENSA
     ERDQLLENLQ EGMEVKGIVK NLTDYGAFVD LGGVDGLLHI TDMAWKRVKH PSEIVNVGDE
     ITVKVLKFDR ERTRVSLGLK QLGEDPWVAI AKRYPEGTRL TGRVTNLTDY GCFVEIEEGV
     EGLVHVSEMD WTNKNIHPSK VVNVGDVVEV MVLDIDEERR RISLGLKQCK ANPWQQFAET
     HNKGDRVEGK IKSITDFGIF IGLDGGIDGL VHLSDISWNA TGEEAVREYK KGDEIAAVVL
     QVDAERERIS LGVKQLAEDP FNNYITLNKK GAIVTGKVTA VDAKGATVEL ADGVEGYLRA
     SEASRDRVED ATLVLNVGDD VEAKFTGVDR KNRVVSLSVR AKDEADEKDA IATVNNKQEE
     GNFSNAMAEA FKAAKGE
//
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