Type |
Details |
Score |
Gene |
Type: |
gene |
Organism: |
macaque, rhesus |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
macaque, rhesus |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
macaque, rhesus |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
macaque, rhesus |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
dog, domestic |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
chimpanzee |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
chimpanzee |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
chimpanzee |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
chimpanzee |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
chimpanzee |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
chimpanzee |
|
•
•
•
•
•
|
DO Term |
|
•
•
•
•
•
|
Publication |
First Author: |
Karbstein K |
Year: |
2006 |
Journal: |
J Mol Biol |
Title: |
GTP-dependent formation of a ribonucleoprotein subcomplex required for ribosome biogenesis. |
Volume: |
356 |
Issue: |
2 |
Pages: |
432-43 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subunit []. The N terminus of Bms1 contains a guanine nucleotide-binding (G) domain that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes [].This entry represents the N-terminal domain of Bms1. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This domain is found at the C terminus of the ribosome biogenesis protein BMS1 and TSR1 families, which may act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus. |
|
•
•
•
•
•
|
Publication |
First Author: |
Wegierski T |
Year: |
2001 |
Journal: |
RNA |
Title: |
Bms1p, a G-domain-containing protein, associates with Rcl1p and is required for 18S rRNA biogenesis in yeast. |
Volume: |
7 |
Issue: |
9 |
Pages: |
1254-67 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
803
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1284
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1287
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1223
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
Bms1p and Tsr1p represent a new family of factors required for ribosomebiogenesis. They are each independently required for 40S ribosomal subunitbiogenesis. Bms1p, a protein required for pre-rRNA processing, contains anevolutionarily conserved guanine nucleotide-binding (G) domain with five conserved polypeptide loopsdesignated G1 through G5, which form contact sites with the guanine nucleotideor coordinate the Mg(2+) ion. Sequences resembling G1 (consensus [GA]-x(4)-G-K-[ST]; also known as a P-loop), G4 (consensus [NT]-K-x-D), and G5 (consensusS-[AG]are present in all Bms1 proteins, and either fully conform with theconsensus or contain, at most, single conservative substitutions. The G2 motif(consensus G-P-[IV]-T) contains a T residue involved in the coordination ofthe Mg(2+) required for GTP hydrolysis. The G3 motif diverges from theconsensus found in G proteins, D-x(2)-G; however, the D residue is replacedwith the conserved E residue. In contrast, Tsr1p lacks a P-loop and is notpredicted to bind GTP. It functions at a later step of 40S ribosomeproduction, possibly in assembly and/or export of 43S pre-ribosomal subunitsto the cytosol [, , ].This entry represents a domain found in Bms1 and Tsr1, and includes cases, such as Tsr1, where it may not function as a guanine nucleotide-binding domain. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
830
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
416
|
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Gelperin D |
Year: |
2001 |
Journal: |
RNA |
Title: |
Bms1p, a novel GTP-binding protein, and the related Tsr1p are required for distinct steps of 40S ribosome biogenesis in yeast. |
Volume: |
7 |
Issue: |
9 |
Pages: |
1268-83 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Bms1p and Tsr1p represent a new family of factors required for ribosomebiogenesis. They are each independently required for 40S ribosomal subunitbiogenesis. Bms1p, a protein required for pre-rRNA processing, contains anevolutionarily conserved guanine nucleotide-binding (G) domain with five conserved polypeptide loopsdesignated G1 through G5, which form contact sites with the guanine nucleotideor coordinate the Mg(2+) ion. Sequences resembling G1 (consensus [GA]-x(4)-G-K-[ST]; also known as a P-loop), G4 (consensus [NT]-K-x-D), and G5 (consensusS-[AG]are present in all Bms1 proteins, and either fully conform with theconsensus or contain, at most, single conservative substitutions. The G2 motif(consensus G-P-[IV]-T) contains a T residue involved in the coordination ofthe Mg(2+) required for GTP hydrolysis. The G3 motif diverges from theconsensus found in G proteins, D-x(2)-G; however, the D residue is replacedwith the conserved E residue. In contrast, Tsr1p lacks a P-loop and is notpredicted to bind GTP. It functions at a later step of 40S ribosomeproduction, possibly in assembly and/or export of 43S pre-ribosomal subunitsto the cytosol [, , ]. |
|
•
•
•
•
•
|
Publication |
First Author: |
Leipe DD |
Year: |
2002 |
Journal: |
J Mol Biol |
Title: |
Classification and evolution of P-loop GTPases and related ATPases. |
Volume: |
317 |
Issue: |
1 |
Pages: |
41-72 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gerhard DS |
Year: |
2004 |
Journal: |
Genome Res |
Title: |
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |
Volume: |
14 |
Issue: |
10B |
Pages: |
2121-7 |
|
•
•
•
•
•
|