The domain within your query sequence starts at position 12 and ends at position 213; the E-value for the Ribosomal_L1 domain shown below is 3.5e-49.

EAVREVLHGNQRKRRKFLETVELQISLKNYDPQKDKRFSGTVRLKSTPRPKFSVCVLGDQ
QHCDEAKAVDIPHMDIEALKKLNKNKKLVKKLAKKYDAFLASESLIKQIPRILGPGLNKA
GKFPSLLTHNENMVAKVDEVKSTIKFQMKKVLCLAVAVGHVKMTDDELVYNIHLAVNFLV
SLLKKNWQNVRALYIKSTMGKP

Ribosomal_L1

Ribosomal_L1
PFAM accession number:PF00687
Interpro abstract (IPR028364):

Ribosomal protein L1 is the largest protein from the large ribosomal subunit. The L1 protein contains two domains: 2-layer alpha/beta domain and a 3-layer alpha/beta domain (interrupts the first domain). The two domains cycle between open and closed conformations via a hinge motion. In Escherichia coli, L1 is known to bind to the 23S rRNA. The RNA-binding site of L1 is highly conserved, with both mRNA and rRNA binding the same binding site. Like several other large ribosomal subunit proteins, L1 displays RNA chaperone activity [(PUBMED:17517772),(PUBMED:15659579),(PUBMED:16330048),(PUBMED:12037305), (PUBMED:10801481),(PUBMED:12514741)]. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities [(PUBMED:8635468), (PUBMED:8607874)], groups:

  • Eubacterial L1
  • Algal and plant chloroplast L1
  • Cyanelle L1
  • Archaebacterial L1
  • Vertebrate L10A
  • Yeast Utp30, Rpl1a, Rpl1b and Mrpl1.
This entry also matches ribosome biogenesis proteins, such as Cic1, which associates with the proteasome and is required for the degradation of specific substrates [(PUBMED:11500370)], and for the synthesis of 60S ribosome subunits [(PUBMED:14623999)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Ribosomal_L1