ID A0A0U3FLW8_9CREN Unreviewed; 217 AA.
AC A0A0U3FLW8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Small ribosomal subunit protein uS5 {ECO:0000256|HAMAP-Rule:MF_01307};
GN Name=rps5 {ECO:0000256|HAMAP-Rule:MF_01307};
GN ORFNames=EYM_00360 {ECO:0000313|EMBL:ALU11375.1};
OS Ignicoccus islandicus DSM 13165.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignicoccus.
OX NCBI_TaxID=940295 {ECO:0000313|EMBL:ALU11375.1, ECO:0000313|Proteomes:UP000060778};
RN [1] {ECO:0000313|EMBL:ALU11375.1, ECO:0000313|Proteomes:UP000060778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13165 {ECO:0000313|EMBL:ALU11375.1,
RC ECO:0000313|Proteomes:UP000060778};
RA Podar M.;
RT "Comparative genomics of Ignicoccus.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: With S4 and S12 plays an important role in translational
CC accuracy. {ECO:0000256|HAMAP-Rule:MF_01307}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S4.
CC {ECO:0000256|HAMAP-Rule:MF_01307}.
CC -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC subunit; the C-terminal domain interacts with the body and contacts
CC protein S4. The interaction surface between S4 and S5 is involved in
CC control of translational fidelity. {ECO:0000256|HAMAP-Rule:MF_01307}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000256|ARBA:ARBA00008945, ECO:0000256|HAMAP-Rule:MF_01307,
CC ECO:0000256|RuleBase:RU003823}.
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DR EMBL; CP006867; ALU11375.1; -; Genomic_DNA.
DR RefSeq; WP_075049156.1; NZ_CP006867.1.
DR AlphaFoldDB; A0A0U3FLW8; -.
DR STRING; 940295.EYM_00360; -.
DR GeneID; 30679492; -.
DR KEGG; iis:EYM_00360; -.
DR PATRIC; fig|940295.4.peg.72; -.
DR OrthoDB; 38155at2157; -.
DR Proteomes; UP000060778; Chromosome.
DR GO; GO:0022626; C:cytosolic ribosome; IEA:UniProt.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_01307_A; Ribosomal_S5_A; 1.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR000851; Ribosomal_uS5.
DR InterPro; IPR047866; Ribosomal_uS5_arc.
DR InterPro; IPR005324; Ribosomal_uS5_C.
DR InterPro; IPR005711; Ribosomal_uS5_euk/arc.
DR InterPro; IPR013810; Ribosomal_uS5_N.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR01020; uS5_euk_arch; 1.
DR PANTHER; PTHR48277; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1.
DR PANTHER; PTHR48277:SF1; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000060778};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01307};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01307};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01307}; rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01307}.
FT DOMAIN 55..118
FT /note="S5 DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50881"
SQ SEQUENCE 217 AA; 24101 MW; 71F4E9ED99C0AAD1 CRC64;
MSVRVDQTES LETWVPKTRV GKMVKEGKIT SIYEIFEKNL PILEPEIVDF LVPDLKHEVL
DVSLVQKVTD AGRITRLRVL IVVGNENGLV GLGMGKARQM RFAIQKALTN AKLNIIPVRR
GCGSWECTCG EPHSVPFTVH GKSGSVRITL KPAPRGTGLV AGDVARTVLK YAGLKDVWTH
TEGETRTTHN FAKATLEALK QTYRFLAPWD WTQPQEG
//
