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Database: UniProt
Entry: A0A261THT0_9BORD
LinkDB: A0A261THT0_9BORD
Original site: A0A261THT0_9BORD 
ID   A0A261THT0_9BORD        Unreviewed;       570 AA.
AC   A0A261THT0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   28-FEB-2018, entry version 3.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=CAL25_14235 {ECO:0000313|EMBL:OZI49194.1};
OS   Bordetella genomosp. 5.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1395608 {ECO:0000313|EMBL:OZI49194.1, ECO:0000313|Proteomes:UP000216913};
RN   [1] {ECO:0000313|EMBL:OZI49194.1, ECO:0000313|Proteomes:UP000216913}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU10456 {ECO:0000313|EMBL:OZI49194.1,
RC   ECO:0000313|Proteomes:UP000216913};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-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:OZI49194.1}.
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DR   EMBL; NEVP01000008; OZI49194.1; -; Genomic_DNA.
DR   Proteomes; UP000216913; 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:UP000216913};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216913};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:OZI49194.1};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN       30     96       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      114    180       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      201    269       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      286    356       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      373    443       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   DOMAIN      460    529       S1 motif. {ECO:0000259|PROSITE:PS50126}.
SQ   SEQUENCE   570 AA;  62215 MW;  093DA891592E3934 CRC64;
     MSSISTQAAG GESFAALFAE SLKSQDMKSG EVISAEVVRV DHNFVVVNAG LKSEALIPLE
     EFLNDQGELE VQPGDFVSVA IDSLENGYGD TILSRDRAKR LSAWLQLEKA LENGELVTGT
     ITGKVKGGLT VMTNGIRAFL PGSLVDLRPV KDTTPYEGKT LEFKVIKLDR KRNNVVLSRR
     QVLEASMGEE RQKLLETLHE GAVVKGVVKN ITDYGAFVDL GGIDGLLHIT DMAWRRVRHP
     SEVLQVGQEV EAKVLKFDQE KSRVSLGVKQ LGEDPWVGLA RRYPQGTRLF GKVTNLTDYG
     AFVEVEAGIE GLVHVSEMDW TNKNVDPRKV VTLGEEVEVM VLEIDEDRRR ISLGMKQCRQ
     NPWEEFATNF KRGDKVRGAI KSITDFGVFV GLPGGIDGLV HLSDLSWTET GEEAVRNFKK
     GDEIEAVVLG IDTDKERISL GIKQLEGDPF NNFVATYDKG AVVPGTIKSV EPKGAVVTLS
     VDVEGYLRAS EISSGRVEDA TTVLSAGTNV EAMIINIDRK ARSIQLSIKA RDNAETADTI
     QRMSEASASS GTTNLGALLK AKLDQQRNDG
//
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