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Database: UniProt
Entry: A0A1R0HF79_9BURK
LinkDB: A0A1R0HF79_9BURK
Original site: A0A1R0HF79_9BURK 
ID   A0A1R0HF79_9BURK        Unreviewed;       557 AA.
AC   A0A1R0HF79;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   05-JUN-2019, entry version 7.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=BOQ04_00355 {ECO:0000313|EMBL:OLY97179.1};
OS   Polynucleobacter sphagniphilus.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=1743169 {ECO:0000313|EMBL:OLY97179.1, ECO:0000313|Proteomes:UP000187156};
RN   [1] {ECO:0000313|EMBL:OLY97179.1, ECO:0000313|Proteomes:UP000187156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWH-Weng1-1 {ECO:0000313|EMBL:OLY97179.1,
RC   ECO:0000313|Proteomes:UP000187156};
RA   Hahn M.W.;
RT   "Polynucleobacter sphagniphilus sp. nov. a planktonic freshwater
RT   bacterium isolated from an acidic and humic freshwater habitat.";
RL   Submitted (NOV-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:OLY97179.1}.
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DR   EMBL; MPIY01000001; OLY97179.1; -; Genomic_DNA.
DR   RefSeq; WP_076022800.1; NZ_MPIY01000001.1.
DR   Proteomes; UP000187156; 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:UP000187156};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:OLY97179.1};
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}.
FT   REGION      521    541       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1R0HF79}.
SQ   SEQUENCE   557 AA;  60694 MW;  8F39301EB37ED819 CRC64;
     MSESFAELFE ESLTRSNMKT GQVISAEVLR IDHNFVVVNA GLKSEAFIPV EEFHNDAGEI
     EVSPGDFVSV AIDALENGYG DTILSRDKAK RLASWMNLEK ALEQAEIVTG TVTGKVKGGL
     TVMVNGIRAF LPGSLVDTRP IKDTSPYEGK TMEFKVIKLD RKRNNVVLSR RAVVEASQGE
     ERAKLMSNLK EGSVVQGIVK NITDYGAFVD LGGIDGLLHI TDLAWRRVRH PSEMLTVGQE
     VTAKILKFDQ DKNRVSLGVK QLGDDPWVGI ARRYPPNTRL FGKVTNLTDY GAFVEIESGI
     EGLVHVSEMD WTNKNVAPSK ATALGTEVEV MVLDIDEDKR RISLGIKQCK ANPWEEFSRA
     QQKGDKLSGA IKSITDFGVF IGLPGGIDGL VHLSDLSWNE PGEEAVKKYK KGDEVEATVL
     AIDVEKERIS LGIKQLSGDP FNNYTSVSDK GSLVTGTVKA VDAKGATIHL ADEVEAYLRA
     SEISTDRVED ARNVLKEGDS VTAMIINIDR KSRAINLSIK AKDSSDQQDA MSKLQGDAQS
     GTTNLGALLK AKLDNQG
//
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