ID RS5_HALMA Reviewed; 212 AA.
AC P26815; Q5V1U2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 01-MAY-2013, entry version 78.
DE RecName: Full=30S ribosomal protein S5;
DE AltName: Full=HmaS5;
GN Name=rps5; OrderedLocusNames=rrnAC1592;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1832208; DOI=10.1007/BF00282450;
RA Scholzen T., Arndt E.;
RT "Organization and nucleotide sequence of ten ribosomal protein genes
RT from the region equivalent to the spectinomycin operon in the
RT archaebacterium Halobacterium marismortui.";
RL Mol. Gen. Genet. 228:70-80(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G.,
RA Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P.,
RA Date S.V., Marcotte E., Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from
RT the Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
CC -!- FUNCTION: With S4 and S12 plays an important role in translational
CC accuracy (By similarity).
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S4
CC (By similarity).
CC -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC subunit; the C-terminal domain interacts with the body and
CC contacts protein S4. The interaction surface between S4 and S5 is
CC involved in control of translational fidelity.
CC -!- SIMILARITY: Belongs to the ribosomal protein S5P family.
CC -!- SIMILARITY: Contains 1 S5 DRBM domain.
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DR EMBL; X58395; CAA41291.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46510.1; -; Genomic_DNA.
DR PIR; S16542; S16542.
DR RefSeq; YP_136216.1; NC_006396.1.
DR ProteinModelPortal; P26815; -.
DR STRING; 272569.rrnAC1592; -.
DR EnsemblBacteria; AAV46510; AAV46510; rrnAC1592.
DR GeneID; 3128557; -.
DR KEGG; hma:rrnAC1592; -.
DR eggNOG; COG0098; -.
DR HOGENOM; HOG000072596; -.
DR KO; K02988; -.
DR OMA; GIKDVWT; -.
DR ProtClustDB; PRK04044; -.
DR BioCyc; HMAR272569:GJDH-1448-MONOMER; -.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:HAMAP.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:HAMAP.
DR GO; GO:0006412; P:translation; IEA:HAMAP.
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; IPR014720; dsRNA-bd-like_dom.
DR InterPro; IPR000851; Ribosomal_S5.
DR InterPro; IPR005324; Ribosomal_S5_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005711; Ribosomal_S5_euk/arc.
DR InterPro; IPR013810; Ribosomal_S5_N.
DR InterPro; IPR018192; Ribosomal_S5_N_CS.
DR PANTHER; PTHR13718; PTHR13718; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR TIGRFAMs; TIGR01020; rpsE_arch; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 3: Inferred from homology;
KW Complete proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1 212 30S ribosomal protein S5.
FT /FTId=PRO_0000131645.
FT DOMAIN 48 111 S5 DRBM.
SQ SEQUENCE 212 AA; 23048 MW; 461F9C6472B0F5FC CRC64;
MSANNGWEPR TRLGKQVVEG EIDSMQEALN SGLPLKESEV VDQLVPDLED EVLDINMVQR
MTDSGRRVKF RCVVAVGNRD GLIGYAEGRD DQVGGAIQKA IDIAKLNIID VSRGCGSWEC
GCGRPHTVAL RTEGKAGSVE VELQPAPRGL GLAGGETVRK VLELAGIEDI WTRSSGNTRT
TVNFAKATFN ALQNTAEARV PERTFEKREV IE
//
