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Database: UniProt
Entry: A0A151EFW6_9EURY
LinkDB: A0A151EFW6_9EURY
Original site: A0A151EFW6_9EURY 
ID   A0A151EFW6_9EURY        Unreviewed;       107 AA.
AC   A0A151EFW6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   08-NOV-2023, entry version 25.
DE   RecName: Full=Small ribosomal subunit protein uS17 {ECO:0000256|HAMAP-Rule:MF_01345};
GN   Name=rps17 {ECO:0000256|HAMAP-Rule:MF_01345};
GN   ORFNames=AYK23_05870 {ECO:0000313|EMBL:KYK27520.1};
OS   Candidatus Proteinoplasmatales archaeon SG8-5.
OC   Archaea; Euryarchaeota; Candidatus Proteinoplasmatales.
OX   NCBI_TaxID=1803822 {ECO:0000313|EMBL:KYK27520.1, ECO:0000313|Proteomes:UP000075319};
RN   [1] {ECO:0000313|Proteomes:UP000075319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds
CC       specifically to the 5'-end of 16S ribosomal RNA. {ECO:0000256|HAMAP-
CC       Rule:MF_01345}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01345}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS17 family.
CC       {ECO:0000256|ARBA:ARBA00010254, ECO:0000256|HAMAP-Rule:MF_01345,
CC       ECO:0000256|RuleBase:RU003872}.
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:KYK27520.1}.
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DR   EMBL; LSSH01000078; KYK27520.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151EFW6; -.
DR   Proteomes; UP000075319; Unassembled WGS sequence.
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; 2.40.50.1000; -; 1.
DR   HAMAP; MF_01345_A; Ribosomal_S17_A; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000266; Ribosomal_uS17.
DR   InterPro; IPR028333; Ribosomal_uS17_arc/euk.
DR   InterPro; IPR019978; Ribosomal_uS17_archaeal.
DR   InterPro; IPR019979; Ribosomal_uS17_CS.
DR   NCBIfam; TIGR03630; uS17_arch; 1.
DR   PANTHER; PTHR10744:SF9; 40S RIBOSOMAL PROTEIN S11; 1.
DR   PANTHER; PTHR10744; 40S RIBOSOMAL PROTEIN S11 FAMILY MEMBER; 1.
DR   Pfam; PF00366; Ribosomal_S17; 1.
DR   PRINTS; PR00973; RIBOSOMALS17.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00056; RIBOSOMAL_S17; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01345,
KW   ECO:0000256|RuleBase:RU003872};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01345,
KW   ECO:0000256|RuleBase:RU003872};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01345};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01345}.
SQ   SEQUENCE   107 AA;  12354 MW;  48F48CB5E3CB2701 CRC64;
     MDIGIDVELP KKECKDRFCP FHGTLPVRGQ ILEGIVVSDR MQQSVVVKRE YMRLNKKYER
     LEKRSGKYLA HSPPCLGTKS GDRVRIMECR PLSKTISYVV IEKRTGE
//
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