ID M7T8C7_9ARCH Unreviewed; 214 AA.
AC M7T8C7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=MCGE09_00140 {ECO:0000313|EMBL:EMR73118.1};
OS Thaumarchaeota archaeon SCGC AB-539-E09.
OC Archaea; Nitrososphaerota.
OX NCBI_TaxID=1198115 {ECO:0000313|EMBL:EMR73118.1, ECO:0000313|Proteomes:UP000031483};
RN [1] {ECO:0000313|EMBL:EMR73118.1, ECO:0000313|Proteomes:UP000031483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC AB-539-E09 {ECO:0000313|EMBL:EMR73118.1,
RC ECO:0000313|Proteomes:UP000031483};
RX PubMed=23535597; DOI=10.1038/nature12033;
RA Lloyd K.G., Schreiber L., Petersen D.G., Kjeldsen K.U., Lever M.A.,
RA Steen A.D., Stepanauskas R., Richter M., Kleindienst S., Lenk S.,
RA Schramm A., Jorgensen B.B.;
RT "Predominant archaea in marine sediments degrade detrital proteins.";
RL Nature 496:215-218(2013).
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}.
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:EMR73118.1}.
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DR EMBL; ALXK01000078; EMR73118.1; -; Genomic_DNA.
DR AlphaFoldDB; M7T8C7; -.
DR PATRIC; fig|1198115.4.peg.495; -.
DR Proteomes; UP000031483; Unassembled WGS sequence.
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:UP000031483};
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 56..119
FT /note="S5 DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50881"
SQ SEQUENCE 214 AA; 23389 MW; 5034B8A1DA1D3930 CRC64;
MSGRRRPREN PLDNWVPKTR LGRMVREGQI SSIYEIFEEG YRIKEVEIID VLVPDLRDEV
IDINLVQKQT DAGERSRFRA VVAMGNSDGL IGLGAGKAPR VRNAIEKGIR EAKLNLYPIR
RGCGSWECDC GEPHTIPFKV TGKSGSVVVT LMPAAKGLGL VAGDTAKTVL SMAGVKDCWS
KTTGATQTAT SFSFATFEAL KNTMKIMTPA DWSA
//
