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RL10_HALVD
ID   RL10_HALVD              Reviewed;         348 AA.
AC   P41198; D4GWB8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   25-MAY-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};
DE   AltName: Full=L10e;
GN   Name=rpl10 {ECO:0000255|HAMAP-Rule:MF_00280};
GN   Synonyms=rplP0 {ECO:0000255|HAMAP-Rule:MF_00280};
GN   OrderedLocusNames=HVO_2756;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=8755911; DOI=10.1128/jb.178.15.4737-4741.1996;
RA   Shimmin L.C., Dennis P.P.;
RT   "Conserved sequence elements involved in regulation of ribosomal protein
RT   gene expression in halophilic archaea.";
RL   J. Bacteriol. 178:4737-4741(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(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. Forms part of the ribosomal
CC       stalk which helps the ribosome interact with GTP-bound translation
CC       factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10
CC       forms an elongated spine to which the L12 dimers bind in a sequential
CC       fashion. {ECO:0000255|HAMAP-Rule:MF_00280}.
CC   -!- MISCELLANEOUS: Was called L10e in this organism; in this case 'e' is
CC       for E.coli-like, not eukaryotic-type protein.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00280}.
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DR   EMBL; X58924; CAA41724.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE02429.1; -; Genomic_DNA.
DR   PIR; S34136; S34136.
DR   RefSeq; WP_004043002.1; NZ_AOHU01000047.1.
DR   AlphaFoldDB; P41198; -.
DR   SMR; P41198; -.
DR   IntAct; P41198; 7.
DR   STRING; 309800.C498_09069; -.
DR   EnsemblBacteria; ADE02429; ADE02429; HVO_2756.
DR   GeneID; 8926688; -.
DR   KEGG; hvo:HVO_2756; -.
DR   eggNOG; arCOG04288; Archaea.
DR   HOGENOM; CLU_053173_0_0_2; -.
DR   OMA; MAHVAEW; -.
DR   OrthoDB; 73593at2157; -.
DR   Proteomes; UP000008243; 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   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..348
FT                   /note="50S ribosomal protein L10"
FT                   /id="PRO_0000154791"
FT   REGION          291..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..341
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        223..224
FT                   /note="VS -> SP (in Ref. 1; CAA41724)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="N -> NHS (in Ref. 1; CAA41724)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="D -> E (in Ref. 1; CAA41724)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        297
FT                   /note="G -> A (in Ref. 1; CAA41724)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   348 AA;  36916 MW;  BD8115765520B4FB CRC64;
     MSESEVRQTE VIPQWKREEV DELVDFIESY ESVGVVGVAG IPSRQLQSMR RELHGSAAVR
     MSRNTLVNRA LDEVNDGFEE LKEYIAGQVA LIGTNDNPFA LFKELEASKT PAPINAGEVA
     PNDIVIPEGD TGVDPGPFVG ELQQVGASAR IMDGSIMVTE DSNVLSEGEE VSEELANVLA
     ELGIEPKEVG LDLRGVFSEG VLFEPDELAI DVDEYRADIQ SAVSAATNLS VNAVYPTAQT
     APTLIAKATS EAKAVGLFAN IESPDFMPEL ISKADAQLRA LAANIDDEEA LPEELRGVSA
     ADTGAAEEEE STDEEAADAD QADAAEDDDA ADDDGDDEDA GDALGSLF
 
 
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