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Conserved domains on  [gi|305677818]
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Chain E, Monopolin complex subunit LRS4

Protein Classification

LRS4 domain-containing protein( domain architecture ID 10564354)

LRS4 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRS4 pfam10422
Monopolin complex subunit LRS4; Monopolin is a protein complex, originally identified in ...
 5-95 2.25e-33

Monopolin complex subunit LRS4; 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.


:

Pssm-ID: 255978 [Multi-domain]  Cd Length: 211  Bit Score: 114.36  E-value: 2.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305677818    5 LQLLSNYYKAKLDSERIYNEYVQSQYEFASLDK-------PKKVVDETLFLQRQIAQLNKQLQLSFQENEKLLSVQKNQK 77
Cdd:pfam10422   1 LQLLADYYDSVLDNERIYLEYDSSQKSFLGALKtnatqsdGEKLTDETLSLQRQINQLNSDLQLQKQENEKLRKLNKTQK 80

                          90
                  ....*....|....*...
gi 305677818   78 ALYQSKLSSKDAFIDDLK 95
Cdd:pfam10422  81 ALLESKLSSKKKEVDRFK 98
 
Name Accession Description Interval E-value
LRS4 pfam10422
Monopolin complex subunit LRS4; Monopolin is a protein complex, originally identified in ...
 5-95 2.25e-33

Monopolin complex subunit LRS4; 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.


Pssm-ID: 255978 [Multi-domain]  Cd Length: 211  Bit Score: 114.36  E-value: 2.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305677818    5 LQLLSNYYKAKLDSERIYNEYVQSQYEFASLDK-------PKKVVDETLFLQRQIAQLNKQLQLSFQENEKLLSVQKNQK 77
Cdd:pfam10422   1 LQLLADYYDSVLDNERIYLEYDSSQKSFLGALKtnatqsdGEKLTDETLSLQRQINQLNSDLQLQKQENEKLRKLNKTQK 80

                          90
                  ....*....|....*...
gi 305677818   78 ALYQSKLSSKDAFIDDLK 95
Cdd:pfam10422  81 ALLESKLSSKKKEVDRFK 98
 
Name Accession Description Interval E-value
LRS4 pfam10422
Monopolin complex subunit LRS4; Monopolin is a protein complex, originally identified in ...
 5-95 2.25e-33

Monopolin complex subunit LRS4; 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.


Pssm-ID: 255978 [Multi-domain]  Cd Length: 211  Bit Score: 114.36  E-value: 2.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305677818    5 LQLLSNYYKAKLDSERIYNEYVQSQYEFASLDK-------PKKVVDETLFLQRQIAQLNKQLQLSFQENEKLLSVQKNQK 77
Cdd:pfam10422   1 LQLLADYYDSVLDNERIYLEYDSSQKSFLGALKtnatqsdGEKLTDETLSLQRQINQLNSDLQLQKQENEKLRKLNKTQK 80

                          90
                  ....*....|....*...
gi 305677818   78 ALYQSKLSSKDAFIDDLK 95
Cdd:pfam10422  81 ALLESKLSSKKKEVDRFK 98
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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