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RL13_AQUAE
ID   RL13_AQUAE              Reviewed;         144 AA.
AC   O67722;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=50S ribosomal protein L13 {ECO:0000255|HAMAP-Rule:MF_01366};
GN   Name=rplM {ECO:0000255|HAMAP-Rule:MF_01366}; OrderedLocusNames=aq_1877;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: This protein is one of the early assembly proteins of the 50S
CC       ribosomal subunit, although it is not seen to bind rRNA by itself. It
CC       is important during the early stages of 50S assembly.
CC       {ECO:0000255|HAMAP-Rule:MF_01366}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01366}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL13 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01366}.
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DR   EMBL; AE000657; AAC07691.1; -; Genomic_DNA.
DR   PIR; H70461; H70461.
DR   RefSeq; NP_214290.1; NC_000918.1.
DR   RefSeq; WP_010881226.1; NC_000918.1.
DR   AlphaFoldDB; O67722; -.
DR   SMR; O67722; -.
DR   STRING; 224324.aq_1877; -.
DR   EnsemblBacteria; AAC07691; AAC07691; aq_1877.
DR   KEGG; aae:aq_1877; -.
DR   PATRIC; fig|224324.8.peg.1455; -.
DR   eggNOG; COG0102; Bacteria.
DR   HOGENOM; CLU_082184_2_2_0; -.
DR   InParanoid; O67722; -.
DR   OMA; DFVVIIN; -.
DR   OrthoDB; 1822215at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00392; Ribosomal_L13; 1.
DR   Gene3D; 3.90.1180.10; -; 1.
DR   HAMAP; MF_01366; Ribosomal_L13; 1.
DR   InterPro; IPR005822; Ribosomal_L13.
DR   InterPro; IPR005823; Ribosomal_L13_bac-type.
DR   InterPro; IPR023563; Ribosomal_L13_CS.
DR   InterPro; IPR036899; Ribosomal_L13_sf.
DR   PANTHER; PTHR11545; PTHR11545; 1.
DR   Pfam; PF00572; Ribosomal_L13; 1.
DR   PIRSF; PIRSF002181; Ribosomal_L13; 1.
DR   SUPFAM; SSF52161; SSF52161; 1.
DR   TIGRFAMs; TIGR01066; rplM_bact; 1.
DR   PROSITE; PS00783; RIBOSOMAL_L13; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..144
FT                   /note="50S ribosomal protein L13"
FT                   /id="PRO_0000133724"
FT   REGION          125..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   144 AA;  17068 MW;  6FC089657A6764FC CRC64;
     MKTYRIKPEE VERKWWVVDA TGKTLGRLAS EIAKILRGKH KPYYQPDVDC GDFVIVINAE
     KIRVTGKKLE QKKYYWHSRY PGGLKERTLK WMLENKPEEV IRLAVKRMLP KNRLGHRMLK
     KLKVYRGPEH PHQAQKPQPL EVKA
 
 
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