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Conserved domains on  [gi|126276407|ref|XP_001387000|]
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CSM1-like protein [Scheffersomyces stipitis CBS 6054]

Protein Classification

PRK06975 and Csm1 domain-containing protein( domain architecture ID 10576117)

protein containing domains Smc, PRK06975, and Csm1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Csm1 pfam12539
Chromosome segregation protein Csm1/Pcs1; Saccharomyces cerevisiae Csm1 is part of the ...
 215-315 1.77e-29

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: 107.98  E-value: 1.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126276407  215 GFTLDMLELLTGLRIVNFEEDESKYFFDVKQSGSNGQdeiyINYQLVISKSFaTTAEINYIPTFlealeNDDEDQEqvdn 294
Cdd:pfam12539   1 QLKEDLYEDLTGLIVRNVKEDDGEDVFDCIQTGRNGT----LHYKLGIDKSF-EEAEFTYVPLL-----DESRDRE---- 66

                          90       100
                  ....*....|....*....|.
gi 126276407  295 anlLKEILPDYLCENLSFPYD 315
Cdd:pfam12539  67 ---LIKILPDYLCEEITFPRD 84
 
Name Accession Description Interval E-value
Csm1 pfam12539
Chromosome segregation protein Csm1/Pcs1; Saccharomyces cerevisiae Csm1 is part of the ...
 215-315 1.77e-29

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: 107.98  E-value: 1.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126276407  215 GFTLDMLELLTGLRIVNFEEDESKYFFDVKQSGSNGQdeiyINYQLVISKSFaTTAEINYIPTFlealeNDDEDQEqvdn 294
Cdd:pfam12539   1 QLKEDLYEDLTGLIVRNVKEDDGEDVFDCIQTGRNGT----LHYKLGIDKSF-EEAEFTYVPLL-----DESRDRE---- 66

                          90       100
                  ....*....|....*....|.
gi 126276407  295 anlLKEILPDYLCENLSFPYD 315
Cdd:pfam12539  67 ---LIKILPDYLCEEITFPRD 84
RWD_CSM1 cd23787
RWD domain of Saccharomyces cerevisiae chromosome segregation in meiosis protein 1 (CSM1) and ...
 212-328 2.07e-22

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: 90.09  E-value: 2.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126276407 212 ENIGFTLDMLELLTGLRIVNFEEDESKYF-FDVKQSGSNGQdeiyINYQLVISKSFATTAEINYIPTFLEalenddedqe 290
Cdd:cd23787    1 EKLEAILRLYEDLTGLRITDVKEDDDDGLtFDCIQTGRNGT----LHFKLTFPKDEDLDDEVIYTPLLDD---------- 66

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 126276407 291 qvDNANLLKEILPDYLCENLSFPYDTLSQFYSKVNRAV 328
Cdd:cd23787   67 --RRDAELLSKLPEYLKEEITFPRDQLPKFFWRLSKSL 102
 
Name Accession Description Interval E-value
Csm1 pfam12539
Chromosome segregation protein Csm1/Pcs1; Saccharomyces cerevisiae Csm1 is part of the ...
 215-315 1.77e-29

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: 107.98  E-value: 1.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126276407  215 GFTLDMLELLTGLRIVNFEEDESKYFFDVKQSGSNGQdeiyINYQLVISKSFaTTAEINYIPTFlealeNDDEDQEqvdn 294
Cdd:pfam12539   1 QLKEDLYEDLTGLIVRNVKEDDGEDVFDCIQTGRNGT----LHYKLGIDKSF-EEAEFTYVPLL-----DESRDRE---- 66

                          90       100
                  ....*....|....*....|.
gi 126276407  295 anlLKEILPDYLCENLSFPYD 315
Cdd:pfam12539  67 ---LIKILPDYLCEEITFPRD 84
RWD_CSM1 cd23787
RWD domain of Saccharomyces cerevisiae chromosome segregation in meiosis protein 1 (CSM1) and ...
 212-328 2.07e-22

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: 90.09  E-value: 2.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126276407 212 ENIGFTLDMLELLTGLRIVNFEEDESKYF-FDVKQSGSNGQdeiyINYQLVISKSFATTAEINYIPTFLEalenddedqe 290
Cdd:cd23787    1 EKLEAILRLYEDLTGLRITDVKEDDDDGLtFDCIQTGRNGT----LHFKLTFPKDEDLDDEVIYTPLLDD---------- 66

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 126276407 291 qvDNANLLKEILPDYLCENLSFPYDTLSQFYSKVNRAV 328
Cdd:cd23787   67 --RRDAELLSKLPEYLKEEITFPRDQLPKFFWRLSKSL 102
 
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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