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RL24_CENSY
ID   RL24_CENSY              Reviewed;         167 AA.
AC   A0RVY4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=50S ribosomal protein L24 {ECO:0000255|HAMAP-Rule:MF_01326};
GN   Name=rpl24 {ECO:0000255|HAMAP-Rule:MF_01326};
GN   OrderedLocusNames=CENSYa_0868;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
CC   -!- FUNCTION: One of two assembly initiator proteins, it binds directly to
CC       the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_01326}.
CC   -!- FUNCTION: Located at the polypeptide exit tunnel on the outside of the
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_01326}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01326}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01326}.
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DR   EMBL; DP000238; ABK77501.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0RVY4; -.
DR   SMR; A0RVY4; -.
DR   STRING; 414004.CENSYa_0868; -.
DR   EnsemblBacteria; ABK77501; ABK77501; CENSYa_0868.
DR   KEGG; csy:CENSYa_0868; -.
DR   HOGENOM; CLU_093240_2_0_2; -.
DR   OMA; VRIMRGD; -.
DR   Proteomes; UP000000758; Chromosome.
DR   GO; GO:0015934; C:large 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; cd06089; KOW_RPL26; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   HAMAP; MF_01326_A; Ribosomal_L24_A; 1.
DR   InterPro; IPR041988; KOW_RPL26/RPL24.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR005756; Ribosomal_L26/L24P_euk/arc.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR11143; PTHR11143; 1.
DR   Pfam; PF16906; Ribosomal_L26; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   TIGRFAMs; TIGR01080; rplX_A_E; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..167
FT                   /note="50S ribosomal protein L24"
FT                   /id="PRO_0000355733"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          107..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   167 AA;  17809 MW;  22F3D098550F1237 CRC64;
     MKATKMRNRQ IYQASTRTRS MQVGSPLSKE LRAKYGKRSV RVVEGDTVSV VRGEYKDIDG
     KVSHVDTESG SVAIEGIKKE KGKGDKFDVL IRASKVVVTG LNASDSWRMK KLGGTAEPAA
     KADSEDAASV GKAEPEDSGI DDATEPEQAG AAGAESHDAE APREESK
 
 
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