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RL10_METMP
ID   RL10_METMP              Reviewed;         335 AA.
AC   Q6M0L1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=50S ribosomal protein L10 {ECO:0000255|HAMAP-Rule:MF_00280};
DE   AltName: Full=Acidic ribosomal protein P0 homolog {ECO:0000255|HAMAP-Rule:MF_00280};
GN   Name=rpl10 {ECO:0000255|HAMAP-Rule:MF_00280};
GN   Synonyms=rplP0 {ECO:0000255|HAMAP-Rule:MF_00280};
GN   OrderedLocusNames=MMP0259;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
RN   [2]
RP   SUBUNIT, STOICHIOMETRY, AND MASS SPECTROMETRY.
RX   PubMed=20467040; DOI=10.1074/mcp.m000072-mcp201;
RA   Gordiyenko Y., Videler H., Zhou M., McKay A.R., Fucini P., Biegel E.,
RA   Muller V., Robinson C.V.;
RT   "Mass spectrometry defines the stoichiometry of ribosomal stalk complexes
RT   across the phylogenetic tree.";
RL   Mol. Cell. Proteomics 9:1774-1783(2010).
CC   -!- FUNCTION: Forms part of the ribosomal stalk, playing a central role in
CC       the interaction of the ribosome with GTP-bound translation factors.
CC       {ECO:0000255|HAMAP-Rule:MF_00280}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Homodimer, it forms part of
CC       the ribosomal stalk which helps the ribosome interact with GTP-bound
CC       translation factors. Forms both a pentameric L10(L12)2(L12)2 and
CC       heptameric L10(L12)2(L12)2(L12)2 complex, where L10 forms an elongated
CC       spine to which the L12 dimers bind in a sequential fashion. The
CC       proportion of heptameric complexes increases during cell growth.
CC       {ECO:0000269|PubMed:20467040}.
CC   -!- MASS SPECTROMETRY: Mass=95159.52; Mass_error=15.63;
CC       Method=Electrospray; Note=Isolated L10(L12)6.;
CC       Evidence={ECO:0000269|PubMed:20467040};
CC   -!- MASS SPECTROMETRY: Mass=74814.80; Mass_error=4.99; Method=Electrospray;
CC       Note=Isolated L10(L12)4.; Evidence={ECO:0000269|PubMed:20467040};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00280}.
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DR   EMBL; BX950229; CAF29815.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6M0L1; -.
DR   SMR; Q6M0L1; -.
DR   STRING; 267377.MMP0259; -.
DR   EnsemblBacteria; CAF29815; CAF29815; MMP0259.
DR   KEGG; mmp:MMP0259; -.
DR   PATRIC; fig|267377.15.peg.261; -.
DR   eggNOG; arCOG04288; Archaea.
DR   HOGENOM; CLU_053173_0_0_2; -.
DR   OMA; MAHVAEW; -.
DR   BioCyc; MMAR267377:MMP_RS01400-MON; -.
DR   Proteomes; UP000000590; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.1730; -; 1.
DR   Gene3D; 3.90.105.20; -; 1.
DR   HAMAP; MF_00280; Ribosomal_L10_arch; 1.
DR   InterPro; IPR022909; 50S_L10_arch.
DR   InterPro; IPR043141; Ribosomal_L10-like_sf.
DR   InterPro; IPR001790; Ribosomal_L10P.
DR   InterPro; IPR043164; RL10_insert_sf.
DR   InterPro; IPR040637; RL10P_insert.
DR   Pfam; PF00466; Ribosomal_L10; 1.
DR   Pfam; PF17777; RL10P_insert; 1.
DR   SUPFAM; SSF160369; SSF160369; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..335
FT                   /note="50S ribosomal protein L10"
FT                   /id="PRO_1000006790"
FT   REGION          304..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..326
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   335 AA;  35805 MW;  18B57FCBD87A86B8 CRC64;
     MIEAKSEHKI APWKIEEVNA LKELLKSSNI IALIDMMEVP AVQLQEIRDK IRDQMTLKMS
     RNTLMKRAIE EVAEETGNPE FAKLVDYMDK GAAIIATEMN PFKLYKTLDE SKSPAPVKGG
     AIAPCDIEVK AGSTGMPPGP FLSELKAVGI PAAIDKGKIG IKEDKIVVKE GEVVSQKLAV
     VLSALDIKPV TVGLNVLGVY EDGVIYTESD LKIDEEEFVG KIQKAYTSAF NLSVNAVIPT
     SATVETIVQK AFNDAKAVSV ESAFVTDKTA DAILGKAYAQ MIAVAGLAGD DALDEDLKGK
     ISSGAAAPVE EAPVEEKKEE KKEEAAAPAG LGMLF
 
 
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