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Conserved domains on  [gi|1034650191|ref|XP_016866334|]
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centromere protein W isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CENP-W super family cl21317
CENP-W protein; CENP-W is a family of vertebral kinetochore proteins that associates directly ...
 1-42 1.18e-13

CENP-W protein; CENP-W is a family of vertebral kinetochore proteins that associates directly with CENP-T. CENP-W members are histone-fold proteins. The histone fold region is critical for binding to centromeric DNA. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes.


The actual alignment was detected with superfamily member pfam15510:

Pssm-ID: 434767  Cd Length: 88  Bit Score: 59.24  E-value: 1.18e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 1034650191  1 MALSTIVSQRKQIKRKAPRGFLKRVFKRKKPQLRLEKSGDLL 42
Cdd:pfam15510  1 MAPAATISQRKRIKRKAPRAFLKRTFKQKKPHLGLEACCDLL 42
 
Name Accession Description Interval E-value
CENP-W pfam15510
CENP-W protein; CENP-W is a family of vertebral kinetochore proteins that associates directly ...
 1-42 1.18e-13

CENP-W protein; CENP-W is a family of vertebral kinetochore proteins that associates directly with CENP-T. CENP-W members are histone-fold proteins. The histone fold region is critical for binding to centromeric DNA. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes.


Pssm-ID: 434767  Cd Length: 88  Bit Score: 59.24  E-value: 1.18e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 1034650191  1 MALSTIVSQRKQIKRKAPRGFLKRVFKRKKPQLRLEKSGDLL 42
Cdd:pfam15510  1 MAPAATISQRKRIKRKAPRAFLKRTFKQKKPHLGLEACCDLL 42
 
Name Accession Description Interval E-value
CENP-W pfam15510
CENP-W protein; CENP-W is a family of vertebral kinetochore proteins that associates directly ...
 1-42 1.18e-13

CENP-W protein; CENP-W is a family of vertebral kinetochore proteins that associates directly with CENP-T. CENP-W members are histone-fold proteins. The histone fold region is critical for binding to centromeric DNA. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes.


Pssm-ID: 434767  Cd Length: 88  Bit Score: 59.24  E-value: 1.18e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 1034650191  1 MALSTIVSQRKQIKRKAPRGFLKRVFKRKKPQLRLEKSGDLL 42
Cdd:pfam15510  1 MAPAATISQRKRIKRKAPRAFLKRTFKQKKPHLGLEACCDLL 42
 
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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