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Conserved domains on  [gi|60302883|ref|NP_001012525|]
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centromere protein W isoform b [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 ...
 1-88 8.72e-38

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: 121.26  E-value: 8.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60302883    1 MALSTIVSQRKQIKRKAPRGFLKRVFKRKKPQLRLEKSGDLLVHLNCLLFVHRLAEESRTNACASKCRVINKEHVLAAAK 80
Cdd:pfam15510  1 MAPAATISQRKRIKRKAPRAFLKRTFKQKKPHLGLEACCDLLIHLNCLLFIQRLAEEARTDACENKCGIIKDDHVLAAAK 80


                 ....*...
gi 60302883   81 VILKKSRG 88
Cdd:pfam15510 81 VILKKSRG 88
 
Name Accession Description Interval E-value
CENP-W pfam15510
CENP-W protein; CENP-W is a family of vertebral kinetochore proteins that associates directly ...
 1-88 8.72e-38

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: 121.26  E-value: 8.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60302883    1 MALSTIVSQRKQIKRKAPRGFLKRVFKRKKPQLRLEKSGDLLVHLNCLLFVHRLAEESRTNACASKCRVINKEHVLAAAK 80
Cdd:pfam15510  1 MAPAATISQRKRIKRKAPRAFLKRTFKQKKPHLGLEACCDLLIHLNCLLFIQRLAEEARTDACENKCGIIKDDHVLAAAK 80


                 ....*...
gi 60302883   81 VILKKSRG 88
Cdd:pfam15510 81 VILKKSRG 88
HFD_CENP-W cd13732
histone-fold domain found in centromere protein W (CENP-W) and similar proteins; CENP-W, also ...
 15-88 1.14e-24

histone-fold domain found in centromere protein W (CENP-W) and similar proteins; CENP-W, also called cancer-up-regulated gene 2 protein (CUG2), is a component of the CENPA-NAC (nucleosome-associated) complex, which plays a central role in the assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENP-A into centromeres. CENP-W is also part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENP-A. Moreover, CENP-W forms a heterodimer with CENP-T. This dimer co-assembles with CENP-S-CENP-X heterodimers at centromeres to form the tetrameric CENP-T-W-S-X complex, which is a subcomplex of the large constitutive centromere-associated network (CCAN, also known as the interphase centromere complex or ICEN). The heterotetrameric CENP-T-W-S-X complex binds and supercoils DNA and plays an important role in kinetochore assembly. CENP-W has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. It is required for normal chromosome organization and normal progress through mitosis.


Pssm-ID: 467029  Cd Length: 74  Bit Score: 87.66  E-value: 1.14e-24
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60302883 15 RKAPRGFLKRVFKRKKPQLRLEKSGDLLVHLNCLLFVHRLAEESRTNACASKCRVINKEHVLAAAKVILKKSRG 88
Cdd:cd13732  1 KLYPRSTLKKIIKKHLPGLRLAKNADILVYLDYLLFLQRLAEEARTEARESGSKTIKPEHVRKAAKKVLKKFRG 74
 
Name Accession Description Interval E-value
CENP-W pfam15510
CENP-W protein; CENP-W is a family of vertebral kinetochore proteins that associates directly ...
 1-88 8.72e-38

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: 121.26  E-value: 8.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60302883    1 MALSTIVSQRKQIKRKAPRGFLKRVFKRKKPQLRLEKSGDLLVHLNCLLFVHRLAEESRTNACASKCRVINKEHVLAAAK 80
Cdd:pfam15510  1 MAPAATISQRKRIKRKAPRAFLKRTFKQKKPHLGLEACCDLLIHLNCLLFIQRLAEEARTDACENKCGIIKDDHVLAAAK 80


                 ....*...
gi 60302883   81 VILKKSRG 88
Cdd:pfam15510 81 VILKKSRG 88
HFD_CENP-W cd13732
histone-fold domain found in centromere protein W (CENP-W) and similar proteins; CENP-W, also ...
 15-88 1.14e-24

histone-fold domain found in centromere protein W (CENP-W) and similar proteins; CENP-W, also called cancer-up-regulated gene 2 protein (CUG2), is a component of the CENPA-NAC (nucleosome-associated) complex, which plays a central role in the assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENP-A into centromeres. CENP-W is also part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENP-A. Moreover, CENP-W forms a heterodimer with CENP-T. This dimer co-assembles with CENP-S-CENP-X heterodimers at centromeres to form the tetrameric CENP-T-W-S-X complex, which is a subcomplex of the large constitutive centromere-associated network (CCAN, also known as the interphase centromere complex or ICEN). The heterotetrameric CENP-T-W-S-X complex binds and supercoils DNA and plays an important role in kinetochore assembly. CENP-W has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. It is required for normal chromosome organization and normal progress through mitosis.


Pssm-ID: 467029  Cd Length: 74  Bit Score: 87.66  E-value: 1.14e-24
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60302883 15 RKAPRGFLKRVFKRKKPQLRLEKSGDLLVHLNCLLFVHRLAEESRTNACASKCRVINKEHVLAAAKVILKKSRG 88
Cdd:cd13732  1 KLYPRSTLKKIIKKHLPGLRLAKNADILVYLDYLLFLQRLAEEARTEARESGSKTIKPEHVRKAAKKVLKKFRG 74
 
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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