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Conserved domains on  [gi|1063712662|ref|NP_001327503|]
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titan9 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RWD_DRWD_ELF-like super family cl45901
RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF ...
221-278 6.51e-04

RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF domains. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. The RWD domain (named after three major RWD-containing proteins: RING finger, WD-repeat-containing proteins and DEXD-like helicases) mediates protein-protein interactions in a variety of pathways in eukaryotes. The DRWD domain is responsible for substrate binding. It is involved in interactions with other kinetochore proteins. The ELF (N-terminal E2-like fold) domain is found in all Fanconi anemia group L protein (FANCL) homologs. It is required to promote efficient DNA damage-induced FANCD2 (Fanconi anemia group D2 protein) monoubiquitination in vertebrate cells.


The actual alignment was detected with superfamily member cd23787:

Pssm-ID: 480265  Cd Length: 102  Bit Score: 38.47  E-value: 6.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712662 221 LSFSLTFINNPNGEEsELLYKP----ASLGTFQRVAPEWMREVIKFSTSMCPIFFERVSRVI 278
Cdd:cd23787    42 LHFKLTFPKDEDLDD-EVIYTPllddRRDAELLSKLPEYLKEEITFPRDQLPKFFWRLSKSL 102
 
Name Accession Description Interval E-value
RWD_CSM1 cd23787
RWD domain of Saccharomyces cerevisiae chromosome segregation in meiosis protein 1 (CSM1) and ...
221-278 6.51e-04

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: 38.47  E-value: 6.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712662 221 LSFSLTFINNPNGEEsELLYKP----ASLGTFQRVAPEWMREVIKFSTSMCPIFFERVSRVI 278
Cdd:cd23787    42 LHFKLTFPKDEDLDD-EVIYTPllddRRDAELLSKLPEYLKEEITFPRDQLPKFFWRLSKSL 102
 
Name Accession Description Interval E-value
RWD_CSM1 cd23787
RWD domain of Saccharomyces cerevisiae chromosome segregation in meiosis protein 1 (CSM1) and ...
221-278 6.51e-04

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: 38.47  E-value: 6.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712662 221 LSFSLTFINNPNGEEsELLYKP----ASLGTFQRVAPEWMREVIKFSTSMCPIFFERVSRVI 278
Cdd:cd23787    42 LHFKLTFPKDEDLDD-EVIYTPllddRRDAELLSKLPEYLKEEITFPRDQLPKFFWRLSKSL 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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