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Conserved domains on  [gi|305677814|pdb|3N7N|A]
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Chain A, Monopolin complex subunit CSM1

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Csm1_N pfam18504
Csm1 N-terminal domain; In the budding yeast Saccharomyces cerevisiae, sister chromatid ...
 1-70 4.31e-27

Csm1 N-terminal domain; In the budding yeast Saccharomyces cerevisiae, sister chromatid co-orientation in meiosis I depends on the four-protein monopolin complex (Mam1, Csm1, Lrs4, and Hrr25/casein kinase 1), which localizes to centromeres from meiotic prophase through metaphase I. Csm1 and Lrs4, form a complex that resides in the nucleolus during interphase and relocalizes to centromeres during meiotic prophase, accompanied by phosphorylation of Lrs4. This is the N-terminal domain of Csm1 which forms a coiled-coil.


:

Pssm-ID: 375930  Cd Length: 70  Bit Score: 97.39  E-value: 4.31e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3N7N_A          1 MDPLTVYKNSVKQQIDSADLLVANLVNENFVLSEKLDTKATEIKQLQKQIDSLNAQVKELKTQTSQQAEN 70
Cdd:pfam18504   1 MDPLTEYKESVQERLDSADLLVSKLVHENSVLSQKLETKDQEIESLKEQLASLEEQVKELEERRKKQEEN 70
Csm1 pfam12539
Chromosome segregation protein Csm1/Pcs1; Saccharomyces cerevisiae Csm1 is part of the ...
 72-165 1.49e-25

Chromosome segregation protein Csm1/Pcs1; Saccharomyces cerevisiae Csm1 is part of the monopolin complex. Csm1 forms a complex with Mde4 and promotes monoorientation during meiosis. Csm1 also plays a mitotic role in DNA replication. This family also contains the Schizosaccharomyces pombe homolog to Csm1, Pcs1. Pcs1 forms a complex with Mde4 and acts in the central kinetochore domain to clamp microtubule binding sites together. The two complexes (Csm1/Lrs4 and Pcs1/Mde4) contribute to the prevention of merotelic attachment.


:

Pssm-ID: 432621  Cd Length: 84  Bit Score: 94.11  E-value: 1.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3N7N_A         72 EVIKDLYEYLCNVRVHKSYEDDSGLWFDISQGTHSGgssddysIMDYKLGFVKGQAQvTEVIYAPVLKQRSTEElysLQS 151
Cdd:pfam12539   1 QLKEDLYEDLTGLIVRNVKEDDGEDVFDCIQTGRNG-------TLHYKLGIDKSFEE-AEFTYVPLLDESRDRE---LIK 69

                          90
                  ....*....|....
3N7N_A        152 KLPEYLFETLSFPL 165
Cdd:pfam12539  70 ILPDYLCEEITFPR 83
 
Name Accession Description Interval E-value
Csm1_N pfam18504
Csm1 N-terminal domain; In the budding yeast Saccharomyces cerevisiae, sister chromatid ...
 1-70 4.31e-27

Csm1 N-terminal domain; In the budding yeast Saccharomyces cerevisiae, sister chromatid co-orientation in meiosis I depends on the four-protein monopolin complex (Mam1, Csm1, Lrs4, and Hrr25/casein kinase 1), which localizes to centromeres from meiotic prophase through metaphase I. Csm1 and Lrs4, form a complex that resides in the nucleolus during interphase and relocalizes to centromeres during meiotic prophase, accompanied by phosphorylation of Lrs4. This is the N-terminal domain of Csm1 which forms a coiled-coil.


Pssm-ID: 375930  Cd Length: 70  Bit Score: 97.39  E-value: 4.31e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3N7N_A          1 MDPLTVYKNSVKQQIDSADLLVANLVNENFVLSEKLDTKATEIKQLQKQIDSLNAQVKELKTQTSQQAEN 70
Cdd:pfam18504   1 MDPLTEYKESVQERLDSADLLVSKLVHENSVLSQKLETKDQEIESLKEQLASLEEQVKELEERRKKQEEN 70
Csm1 pfam12539
Chromosome segregation protein Csm1/Pcs1; Saccharomyces cerevisiae Csm1 is part of the ...
 72-165 1.49e-25

Chromosome segregation protein Csm1/Pcs1; Saccharomyces cerevisiae Csm1 is part of the monopolin complex. Csm1 forms a complex with Mde4 and promotes monoorientation during meiosis. Csm1 also plays a mitotic role in DNA replication. This family also contains the Schizosaccharomyces pombe homolog to Csm1, Pcs1. Pcs1 forms a complex with Mde4 and acts in the central kinetochore domain to clamp microtubule binding sites together. The two complexes (Csm1/Lrs4 and Pcs1/Mde4) contribute to the prevention of merotelic attachment.


Pssm-ID: 432621  Cd Length: 84  Bit Score: 94.11  E-value: 1.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3N7N_A         72 EVIKDLYEYLCNVRVHKSYEDDSGLWFDISQGTHSGgssddysIMDYKLGFVKGQAQvTEVIYAPVLKQRSTEElysLQS 151
Cdd:pfam12539   1 QLKEDLYEDLTGLIVRNVKEDDGEDVFDCIQTGRNG-------TLHYKLGIDKSFEE-AEFTYVPLLDESRDRE---LIK 69

                          90
                  ....*....|....
3N7N_A        152 KLPEYLFETLSFPL 165
Cdd:pfam12539  70 ILPDYLCEEITFPR 83
RWD_CSM1 cd23787
RWD domain of Saccharomyces cerevisiae chromosome segregation in meiosis protein 1 (CSM1) and ...
 69-179 8.15e-23

RWD domain of Saccharomyces cerevisiae chromosome segregation in meiosis protein 1 (CSM1) and related proteins; Saccharomyces cerevisiae CSM1 is a component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. It also plays a mitotic role in DNA replication. The family also includes Schizosaccharomyces pombe chromosome segregation protein 1 (PCS1), which is a component of a monopolin-like complex composed of PCS1 and MDE4. The PCS1/MDE4 complex associates with the kinetochore and is essential for accurate chromosome segregation during mitosis and meiosis II. PCS1 may clamp together microtubule binding sites on the same kinetochore, preventing merotelic attachment of microtubules. In contrast to its S. cerevisiae ortholog CSM1, PCS1 is not required for mono-orientation during meiosis I.


Pssm-ID: 467649  Cd Length: 102  Bit Score: 87.78  E-value: 8.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3N7N_A       69 ENSEVIKDLYEYLCNVRVHKSYEDDS-GLWFDISQgTHSGGSsddysiMDYKLGFVKGQAQVTEVIYAPVLKQRSTEELy 147
Cdd:cd23787   1 EKLEAILRLYEDLTGLRITDVKEDDDdGLTFDCIQ-TGRNGT------LHFKLTFPKDEDLDDEVIYTPLLDDRRDAEL- 72

                        90       100       110
                ....*....|....*....|....*....|..
3N7N_A      148 slQSKLPEYLFETLSFPLSSLNQFYNKIAKSL 179
Cdd:cd23787  73 --LSKLPEYLKEEITFPRDQLPKFFWRLSKSL 102
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 9-79 2.59e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.89  E-value: 2.59e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3N7N_A        9 NSVKQQIDSADLLVANLVNENFVLSEKLDTKATEIKQLQKQIDSLNAQVKELKTQ-TSQQAENSEVIKDLYE 79
Cdd:COG3883  26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERARALYR 97
 
Name Accession Description Interval E-value
Csm1_N pfam18504
Csm1 N-terminal domain; In the budding yeast Saccharomyces cerevisiae, sister chromatid ...
 1-70 4.31e-27

Csm1 N-terminal domain; In the budding yeast Saccharomyces cerevisiae, sister chromatid co-orientation in meiosis I depends on the four-protein monopolin complex (Mam1, Csm1, Lrs4, and Hrr25/casein kinase 1), which localizes to centromeres from meiotic prophase through metaphase I. Csm1 and Lrs4, form a complex that resides in the nucleolus during interphase and relocalizes to centromeres during meiotic prophase, accompanied by phosphorylation of Lrs4. This is the N-terminal domain of Csm1 which forms a coiled-coil.


Pssm-ID: 375930  Cd Length: 70  Bit Score: 97.39  E-value: 4.31e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3N7N_A          1 MDPLTVYKNSVKQQIDSADLLVANLVNENFVLSEKLDTKATEIKQLQKQIDSLNAQVKELKTQTSQQAEN 70
Cdd:pfam18504   1 MDPLTEYKESVQERLDSADLLVSKLVHENSVLSQKLETKDQEIESLKEQLASLEEQVKELEERRKKQEEN 70
Csm1 pfam12539
Chromosome segregation protein Csm1/Pcs1; Saccharomyces cerevisiae Csm1 is part of the ...
 72-165 1.49e-25

Chromosome segregation protein Csm1/Pcs1; Saccharomyces cerevisiae Csm1 is part of the monopolin complex. Csm1 forms a complex with Mde4 and promotes monoorientation during meiosis. Csm1 also plays a mitotic role in DNA replication. This family also contains the Schizosaccharomyces pombe homolog to Csm1, Pcs1. Pcs1 forms a complex with Mde4 and acts in the central kinetochore domain to clamp microtubule binding sites together. The two complexes (Csm1/Lrs4 and Pcs1/Mde4) contribute to the prevention of merotelic attachment.


Pssm-ID: 432621  Cd Length: 84  Bit Score: 94.11  E-value: 1.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3N7N_A         72 EVIKDLYEYLCNVRVHKSYEDDSGLWFDISQGTHSGgssddysIMDYKLGFVKGQAQvTEVIYAPVLKQRSTEElysLQS 151
Cdd:pfam12539   1 QLKEDLYEDLTGLIVRNVKEDDGEDVFDCIQTGRNG-------TLHYKLGIDKSFEE-AEFTYVPLLDESRDRE---LIK 69

                          90
                  ....*....|....
3N7N_A        152 KLPEYLFETLSFPL 165
Cdd:pfam12539  70 ILPDYLCEEITFPR 83
RWD_CSM1 cd23787
RWD domain of Saccharomyces cerevisiae chromosome segregation in meiosis protein 1 (CSM1) and ...
 69-179 8.15e-23

RWD domain of Saccharomyces cerevisiae chromosome segregation in meiosis protein 1 (CSM1) and related proteins; Saccharomyces cerevisiae CSM1 is a component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. It also plays a mitotic role in DNA replication. The family also includes Schizosaccharomyces pombe chromosome segregation protein 1 (PCS1), which is a component of a monopolin-like complex composed of PCS1 and MDE4. The PCS1/MDE4 complex associates with the kinetochore and is essential for accurate chromosome segregation during mitosis and meiosis II. PCS1 may clamp together microtubule binding sites on the same kinetochore, preventing merotelic attachment of microtubules. In contrast to its S. cerevisiae ortholog CSM1, PCS1 is not required for mono-orientation during meiosis I.


Pssm-ID: 467649  Cd Length: 102  Bit Score: 87.78  E-value: 8.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3N7N_A       69 ENSEVIKDLYEYLCNVRVHKSYEDDS-GLWFDISQgTHSGGSsddysiMDYKLGFVKGQAQVTEVIYAPVLKQRSTEELy 147
Cdd:cd23787   1 EKLEAILRLYEDLTGLRITDVKEDDDdGLTFDCIQ-TGRNGT------LHFKLTFPKDEDLDDEVIYTPLLDDRRDAEL- 72

                        90       100       110
                ....*....|....*....|....*....|..
3N7N_A      148 slQSKLPEYLFETLSFPLSSLNQFYNKIAKSL 179
Cdd:cd23787  73 --LSKLPEYLKEEITFPRDQLPKFFWRLSKSL 102
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 9-79 2.59e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.89  E-value: 2.59e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3N7N_A        9 NSVKQQIDSADLLVANLVNENFVLSEKLDTKATEIKQLQKQIDSLNAQVKELKTQ-TSQQAENSEVIKDLYE 79
Cdd:COG3883  26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERARALYR 97
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 8-68 2.76e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.50  E-value: 2.76e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
3N7N_A        8 KNSVKQQIDSADLLVANLVNENFVLSEKLDTKATEIKQLQKQIDSLNAQVKELKTQTSQQA 68
Cdd:COG3883  32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
 
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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