ID RS13_METAR Reviewed; 224 AA.
AC Q0W1V6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Small ribosomal subunit protein uS13 {ECO:0000255|HAMAP-Rule:MF_01315};
DE AltName: Full=30S ribosomal protein S13 {ECO:0000305};
GN Name=rps13 {ECO:0000255|HAMAP-Rule:MF_01315};
GN OrderedLocusNames=UNCMA_06190; ORFNames=RCIX2580;
OS Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=351160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX PubMed=16857943; DOI=10.1126/science.1127062;
RA Erkel C., Kube M., Reinhardt R., Liesack W.;
RT "Genome of rice cluster I archaea -- the key methane producers in the rice
RT rhizosphere.";
RL Science 313:370-372(2006).
CC -!- FUNCTION: Located at the top of the head of the 30S subunit, it
CC contacts several helices of the 16S rRNA. In the 70S ribosome it
CC contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit
CC (bridge B1b), connecting the 2 subunits; these bridges are implicated
CC in subunit movement. {ECO:0000255|HAMAP-Rule:MF_01315}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a loose heterodimer
CC with protein S19. Forms two bridges to the 50S subunit in the 70S
CC ribosome. {ECO:0000255|HAMAP-Rule:MF_01315}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC {ECO:0000255|HAMAP-Rule:MF_01315}.
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DR EMBL; AM114193; CAJ37637.1; -; Genomic_DNA.
DR RefSeq; WP_012034948.1; NC_009464.1.
DR AlphaFoldDB; Q0W1V6; -.
DR SMR; Q0W1V6; -.
DR STRING; 351160.RCIX2580; -.
DR GeneID; 5145688; -.
DR KEGG; rci:RCIX2580; -.
DR PATRIC; fig|351160.9.peg.646; -.
DR eggNOG; arCOG01722; Archaea.
DR OrthoDB; 372127at2157; -.
DR Proteomes; UP000000663; Chromosome.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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 Gene3D; 1.10.8.50; -; 1.
DR Gene3D; 4.10.910.10; 30s ribosomal protein s13, domain 2; 1.
DR HAMAP; MF_01315; Ribosomal_uS13; 1.
DR InterPro; IPR027437; Rbsml_uS13_C.
DR InterPro; IPR001892; Ribosomal_uS13.
DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR InterPro; IPR019977; Ribosomal_uS13_archaeal.
DR InterPro; IPR018269; Ribosomal_uS13_CS.
DR NCBIfam; TIGR03629; uS13_arch; 1.
DR PANTHER; PTHR10871; 30S RIBOSOMAL PROTEIN S13/40S RIBOSOMAL PROTEIN S18; 1.
DR PANTHER; PTHR10871:SF3; 40S RIBOSOMAL PROTEIN S18; 1.
DR Pfam; PF00416; Ribosomal_S13; 1.
DR SUPFAM; SSF46946; S13-like H2TH domain; 1.
DR PROSITE; PS00646; RIBOSOMAL_S13_1; 1.
DR PROSITE; PS50159; RIBOSOMAL_S13_2; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..224
FT /note="Small ribosomal subunit protein uS13"
FT /id="PRO_0000306768"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 224 AA; 24529 MW; 962E04C130F1E496 CRC64;
MSEKTDKTEK KQKKAEETVE TASAEAAPAK KGGKKQAAKP AEGAPADEAA RKGGKGKKPA
AEEKPKDEIK YIVRIANTDL DGTQTVEFAL TGIKGIGNRI SKIIARQAQV DPHATMGYLP
PEQVDKLRAV IDNLEANVPV WMLNRRRDIY TGEDKHLYGV DLTMAVKEDI NIMKKIRSYK
GIRHERGQKV RGQRTKSTGR TGATVGVVRK KGEQGGAAKK EDKK
//
