Summary: Monopolin complex subunit LRS4
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Monopolin complex subunit LRS4 Provide feedback
Monopolin is a protein complex, originally identified in Saccharomyces cerevisiae, that is required for the segregation of homologous centromeres to opposite poles of a dividing cell during meiosis I . The orthologous complex in Schizosaccharomyces pombe is not required for meiosis I chromosome segregation, but is proposed to play a similar physiological role in clamping microtubule binding sites . In S .cerevisiae this subunit is called LRS4, and in S. pombe it is known as Mde4.
Toth A, Rabitsch KP, Galova M, Schleiffer A, Buonomo SB, Nasmyth K; , Cell. 2000;103:1155-1168.: Functional genomics identifies monopolin: a kinetochore protein required for segregation of homologs during meiosis i. PUBMED:11163190 EPMC:11163190
Gregan J, Riedel CG, Pidoux AL, Katou Y, Rumpf C, Schleiffer A, Kearsey SE, Shirahige K, Allshire RC, Nasmyth K; , Curr Biol. 2007;17:1190-1200.: The kinetochore proteins Pcs1 and Mde4 and heterochromatin are required to prevent merotelic orientation. PUBMED:17627824 EPMC:17627824
Rabitsch KP, Petronczki M, Javerzat JP, Genier S, Chwalla B, Schleiffer A, Tanaka TU, Nasmyth K; , Dev Cell. 2003;4:535-548.: Kinetochore recruitment of two nucleolar proteins is required for homolog segregation in meiosis I. PUBMED:12689592 EPMC:12689592
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR018479
Monopolin is a protein complex, originally identified in Saccharomyces cerevisiae (Baker's yeast), that is required for the segregation of homologous centromeres to opposite poles of a dividing cell during meiosis I [PUBMED:11163190]. The orthologous complex in Schizosaccharomyces pombe (Fission yeast) is not required for meiosis I chromosome segregation, but is proposed to play a similar physiological role in clamping microtubule binding sites [PUBMED:17627824]. In S. cerevisiae this subunit is called LRS4, and in S. pombe it is known as Mde4 [PUBMED:12689592].
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Curation and family details
|Seed source:||Pfam-B_63451 (release 22.0)|
|Author:||Mistry J, Wood V|
|Number in seed:||5|
|Number in full:||47|
|Average length of the domain:||223.30 aa|
|Average identity of full alignment:||40 %|
|Average coverage of the sequence by the domain:||73.51 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the LRS4 domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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