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RL4_SYNJA
ID   RL4_SYNJA               Reviewed;         326 AA.
AC   Q2JV82;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=50S ribosomal protein L4;
GN   Name=rplD; Synonyms=rpl4; OrderedLocusNames=CYA_1177;
OS   Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS   A-Prime).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=321327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-3-3Ab;
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, this protein
CC       initially binds near the 5'-end of the 23S rRNA. It is important during
CC       the early stages of 50S assembly. It makes multiple contacts with
CC       different domains of the 23S rRNA in the assembled 50S subunit and
CC       ribosome (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Forms part of the polypeptide exit tunnel. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC       {ECO:0000305}.
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DR   EMBL; CP000239; ABC99365.1; -; Genomic_DNA.
DR   RefSeq; WP_011430046.1; NC_007775.1.
DR   AlphaFoldDB; Q2JV82; -.
DR   SMR; Q2JV82; -.
DR   STRING; 321327.CYA_1177; -.
DR   EnsemblBacteria; ABC99365; ABC99365; CYA_1177.
DR   KEGG; cya:CYA_1177; -.
DR   eggNOG; COG0088; Bacteria.
DR   HOGENOM; CLU_852406_0_0_3; -.
DR   OMA; HILYLAL; -.
DR   OrthoDB; 1572673at2; -.
DR   Proteomes; UP000008818; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 3.40.1370.10; -; 1.
DR   HAMAP; MF_01328_B; Ribosomal_L4_B; 1.
DR   InterPro; IPR002136; Ribosomal_L4/L1e.
DR   InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR   InterPro; IPR013005; Ribosomal_uL4/L1e.
DR   PANTHER; PTHR10746; PTHR10746; 1.
DR   Pfam; PF00573; Ribosomal_L4; 1.
DR   SUPFAM; SSF52166; SSF52166; 1.
DR   TIGRFAMs; TIGR03953; rplD_bact; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..326
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_0000242451"
FT   REGION          1..211
FT                   /note="50S ribosomal protein L4"
FT   REGION          44..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..326
FT                   /note="Unknown"
FT   COMPBIAS        225..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   326 AA;  35864 MW;  24FFA8E4332C6757 CRC64;
     MASCVVKNWQ GETVGSAELS LKVARPETAS HILYLALRRQ MTNARQGNAH TKTRAEVRGG
     GRKPWRQKGT GRARAGSIRS PLWRKGGVIF GPRKREYNLA MNRKERQLAL RTALQSRVED
     LIVVEDFQDQ LNPPKTRAVA QALLRWGVME DQSALLIVAE RSEAVERAVR NIARVKLIGL
     DQLNVFDLLN VDWVLITTSA LEKLKARWGS GAAAAAPTQA DRLEDQAQAA EREARPVEQA
     EGQSQEQEEQ AEAQAQPEAP PAQADQANQV ALANPQVQET QEEELAQAQE REVQGQAELA
     QEAEPLAQPP AGEEAETAAA EEEDND
 
 
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