ID B8D5W4_DESA1 Unreviewed; 223 AA.
AC B8D5W4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Small ribosomal subunit protein uS3 {ECO:0000256|HAMAP-Rule:MF_01309};
GN Name=rps3 {ECO:0000256|HAMAP-Rule:MF_01309};
GN OrderedLocusNames=DKAM_1169 {ECO:0000313|EMBL:ACL11495.1};
OS Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 /
OS 1221n) (Desulfurococcus kamchatkensis).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Desulfurococcus.
OX NCBI_TaxID=490899 {ECO:0000313|EMBL:ACL11495.1, ECO:0000313|Proteomes:UP000006903};
RN [1] {ECO:0000313|EMBL:ACL11495.1, ECO:0000313|Proteomes:UP000006903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18924 / JCM 16383 / VKM B-2413 / 1221n
RC {ECO:0000313|Proteomes:UP000006903};
RX PubMed=19114480; DOI=10.1128/JB.01525-08;
RA Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V.,
RA Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Complete genome sequence of the anaerobic, protein-degrading
RT hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.";
RL J. Bacteriol. 191:2371-2379(2009).
CC -!- FUNCTION: Binds the lower part of the 30S subunit head.
CC {ECO:0000256|HAMAP-Rule:MF_01309}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01309}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC {ECO:0000256|ARBA:ARBA00010761, ECO:0000256|HAMAP-Rule:MF_01309}.
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DR EMBL; CP001140; ACL11495.1; -; Genomic_DNA.
DR RefSeq; WP_012608836.1; NC_011766.1.
DR AlphaFoldDB; B8D5W4; -.
DR STRING; 490899.DKAM_1169; -.
DR GeneID; 7171829; -.
DR KEGG; dka:DKAM_1169; -.
DR eggNOG; arCOG04097; Archaea.
DR HOGENOM; CLU_058591_1_1_2; -.
DR Proteomes; UP000006903; Chromosome.
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:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd02411; KH-II_30S_S3_arch; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.30.1140.32; Ribosomal protein S3, C-terminal domain; 1.
DR HAMAP; MF_01309_A; Ribosomal_S3_A; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR036419; Ribosomal_S3_C_sf.
DR InterPro; IPR027488; Ribosomal_uS3_arc.
DR InterPro; IPR001351; Ribosomal_uS3_C.
DR InterPro; IPR005703; Ribosomal_uS3_euk/arc.
DR NCBIfam; TIGR01008; uS3_euk_arch; 1.
DR PANTHER; PTHR11760; 30S/40S RIBOSOMAL PROTEIN S3; 1.
DR PANTHER; PTHR11760:SF32; 40S RIBOSOMAL PROTEIN S3; 1.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF00189; Ribosomal_S3_C; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR SUPFAM; SSF54821; Ribosomal protein S3 C-terminal domain; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01309};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01309};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01309};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01309}.
FT DOMAIN 20..99
FT /note="KH type-2"
FT /evidence="ECO:0000259|PROSITE:PS50823"
SQ SEQUENCE 223 AA; 24810 MW; 2E86D044E515A8A5 CRC64;
MVGPRVKSYF LEYGLKKLMI DEFLAHYFKD AGYADVELYR TPTGYRVVIH AEYPGRLIGR
GGSVIKKLST ILQNKFGLDN VNITISPVID PDLNARVVAF RIVRALEKEI PFRRVMMYML
KRVMDAGAIG AEIIISGKLR GERATYEKLK AGKVYKAGEP VEYMVDRAVV KALLKPGIFG
VEVVIVKPGI KMPDHVEIKT LKPEELEALK PAKTTEGGGS EGK
//