ID A0A139CIS1_9EURY Unreviewed; 210 AA.
AC A0A139CIS1;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Small ribosomal subunit protein uS5 {ECO:0000256|ARBA:ARBA00035255, ECO:0000256|HAMAP-Rule:MF_01307};
GN Name=rps5 {ECO:0000256|HAMAP-Rule:MF_01307};
GN ORFNames=AWU59_2268 {ECO:0000313|EMBL:KXS41092.1};
OS Methanolobus sp. T82-4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX NCBI_TaxID=1794908 {ECO:0000313|EMBL:KXS41092.1, ECO:0000313|Proteomes:UP000074030};
RN [1] {ECO:0000313|EMBL:KXS41092.1, ECO:0000313|Proteomes:UP000074030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T82-4 {ECO:0000313|EMBL:KXS41092.1};
RA Wolfe R., Daly R., Wrighton K.;
RT "Methanolobus T82 Annotated.";
RL Submitted (FEB-2016) 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}.
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:KXS41092.1}.
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DR EMBL; LSRV01000093; KXS41092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139CIS1; -.
DR STRING; 1794908.AWU59_2268; -.
DR PATRIC; fig|1794908.3.peg.1704; -.
DR Proteomes; UP000074030; Unassembled WGS sequence.
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; IPR018192; Ribosomal_uS5_N_CS.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR01020; uS5_euk_arch; 1.
DR PANTHER; PTHR13718:SF4; 40S RIBOSOMAL PROTEIN S2; 1.
DR PANTHER; PTHR13718; RIBOSOMAL S SUBUNIT; 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; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 3: Inferred from homology;
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}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01307};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01307}.
FT DOMAIN 50..113
FT /note="S5 DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50881"
SQ SEQUENCE 210 AA; 22933 MW; 42AAA5B0F77B5E97 CRC64;
MAYNYEEEWV PQTRLGKLVH EGQITSMDEA IDSGLPVRES KVIDILLPDL EDEVLDINMV
QRMTDSGRRV KFRATVIVGN GDGFVGLGQA KDVQVGPAIR KAIDNAKINI LKVKRGCGSW
ECACGREHTV PSEVRGKAGS VIVELKPAPR GLGLAAGDTA RKVLEKAGIK DVWTRTEGTT
RTTLNFAKAT FNALHNTGTV RQPIRLEEEA
//