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Database: UniProt
Entry: A0A0S8C5X4_9CHLR
LinkDB: A0A0S8C5X4_9CHLR
Original site: A0A0S8C5X4_9CHLR 
ID   A0A0S8C5X4_9CHLR        Unreviewed;       132 AA.
AC   A0A0S8C5X4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Small ribosomal subunit protein uS8 {ECO:0000256|ARBA:ARBA00035258, ECO:0000256|HAMAP-Rule:MF_01302};
GN   Name=rpsH {ECO:0000256|HAMAP-Rule:MF_01302};
GN   ORFNames=AMJ70_09135 {ECO:0000313|EMBL:KPK19262.1};
OS   Dehalococcoidia bacterium SG8_51_3.
OC   Bacteria; Chloroflexota; Dehalococcoidia.
OX   NCBI_TaxID=1703394 {ECO:0000313|EMBL:KPK19262.1, ECO:0000313|Proteomes:UP000051285};
RN   [1] {ECO:0000313|EMBL:KPK19262.1, ECO:0000313|Proteomes:UP000051285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_51_3 {ECO:0000313|EMBL:KPK19262.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       to 16S rRNA central domain where it helps coordinate assembly of the
CC       platform of the 30S subunit. {ECO:0000256|HAMAP-Rule:MF_01302}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S5 and
CC       S12. {ECO:0000256|HAMAP-Rule:MF_01302}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS8 family.
CC       {ECO:0000256|ARBA:ARBA00006471, ECO:0000256|HAMAP-Rule:MF_01302}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPK19262.1}.
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DR   EMBL; LJTX01000202; KPK19262.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8C5X4; -.
DR   PATRIC; fig|1703394.3.peg.1550; -.
DR   Proteomes; UP000051285; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1370.30; -; 1.
DR   Gene3D; 3.30.1490.10; -; 1.
DR   HAMAP; MF_01302_B; Ribosomal_S8_B; 1.
DR   InterPro; IPR000630; Ribosomal_uS8.
DR   InterPro; IPR035987; Ribosomal_uS8_sf.
DR   PANTHER; PTHR11758:SF4; 37S RIBOSOMAL PROTEIN S8, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11758; 40S RIBOSOMAL PROTEIN S15A; 1.
DR   Pfam; PF00410; Ribosomal_S8; 1.
DR   SUPFAM; SSF56047; Ribosomal protein S8; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_01302};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_01302}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01302};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01302}.
SQ   SEQUENCE   132 AA;  14788 MW;  0ACC97B8DDE039F9 CRC64;
     MTVSDPIADM LTRIRNALMA KHEQVLVPSS RMKLSIARIL KEEGFITDYE VVREKPQRVI
     KVQLKYHDRN KPAITGMKRV SKPGLRVYVG GKEIPRVFGG LGIAIVSTSK GVRTGQQAWR
     QGIGGEVLCF VW
//
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