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Database: UniProt
Entry: A0A178GF89_9GAMM
LinkDB: A0A178GF89_9GAMM
Original site: A0A178GF89_9GAMM 
ID   A0A178GF89_9GAMM        Unreviewed;       558 AA.
AC   A0A178GF89;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   05-JUN-2019, entry version 10.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   Name=rpsA {ECO:0000313|EMBL:OAL83421.1};
GN   ORFNames=AY605_10230 {ECO:0000313|EMBL:OAL83421.1};
OS   Acinetobacter sp. SFD.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=1805635 {ECO:0000313|EMBL:OAL83421.1, ECO:0000313|Proteomes:UP000186186};
RN   [1] {ECO:0000313|EMBL:OAL83421.1, ECO:0000313|Proteomes:UP000186186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SFD {ECO:0000313|EMBL:OAL83421.1,
RC   ECO:0000313|Proteomes:UP000186186};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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:OAL83421.1}.
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DR   EMBL; LSZJ01000014; OAL83421.1; -; Genomic_DNA.
DR   RefSeq; WP_064096561.1; NZ_LSZJ01000014.1.
DR   Proteomes; UP000186186; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000186186};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:OAL83421.1};
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      536    558       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A178GF89}.
FT   COILED      471    491       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   558 AA;  61077 MW;  9CD1C5EE0F73EA5F CRC64;
     MTESFAALFE ASELNLNVEK GAVIQGVVVS IDSDWVTVDT GLKSEGVVDR AEFLNEQREL
     EVQVGDTVDV VVEALDNGMG QTVLSREKAK RAETWTKLEK IFEDGEIVTG VISGKVKGGF
     TVDIGPVRAF LPGSLVDTRP IRDTTHLEGK ELEFKVIKLD AKRNNVVVSR RAVMEAESSA
     DREALLAQLE EGQTVTGTIK NLTDYGAFVD LGGIDGLLHI TDMAWKRIKH PSEVVEVGQE
     VTVKVLKFDR ERNRVSLGLK QLGEDPWLAI MNRYPKGSIV KARVTNLTDY GCFAEIAEGV
     EGLVHVSEMD HTNKNIHPSK VVQIGDEVDV MVLEVDEERR RISLGIKQTR ANPWEEFAKE
     HDKGEKVSGT IKSITDFGIF IGLPGGIDGL VHLSDISWNE QGEEAIRRYK KGDTVEAVIL
     SVDAEGNRIS LGIKQMNNDP FNDFLAANER GALVKGTVTA VDAKGATVKL ADEVEATLKA
     SEINRDRVED ATKFLEVGQE VEAKIINVDR KSRAINLSIK AKDEAEEKEA VANLKTAPAG
     QDNGPKTIGD LIKAQMSN
//
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