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Conserved domains on  [gi|1063697212|ref|NP_001323102|]
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centromere protein X [Arabidopsis thaliana]

Protein Classification

CENP-X/MHF2 family protein( domain architecture ID 19224032)

CENP-X/MHF2 family protein similar to CENP-X histone-fold protein, one of the components of the constitutive centromere-associated network (CCAN) that form CENP-T-W-S-X nucleosome-like complexes and is also involved in kinetochore assembly

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HFD_CENP-X cd22921
histone-fold domain found in centromere protein X (CENP-X) and similar proteins; CENP-X, also ...
 6-104 4.07e-20

histone-fold domain found in centromere protein X (CENP-X) and similar proteins; CENP-X, also called MHF2, FANCM-associated histone fold protein 2, FANCM-interacting histone fold protein 2, Fanconi anemia-associated polypeptide of 10 kDa, retinoic acid-inducible gene D9 protein homolog, or stimulated by retinoic acid gene 13 protein homolog, is a DNA-binding component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. CENP-X, together with CENP-S, forms the MHF heterodimer, which can further assemble to form tetrameric structures. CENP-X acts as a crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. It can stabilize FANCM. CENP-X also forms a discrete complex with FANCM and CENP-S, called FANCM-MHF. This interaction leads to synergistic activation of double-stranded DNA binding and strongly stimulates FANCM-mediated DNA remodeling. In complex with CENP-T, CENP-W and CENP-S (CENP-T-W-S-X heterotetramer), CENP-X is involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of the MHF and CENP-T-W-S-X complexes, CENP-X binds DNA and bends it to form a nucleosome-like structure. Its DNA-binding function is fulfilled in the presence of CENP-S. It does not bind DNA on its own.


:

Pssm-ID: 467046  Cd Length: 73  Bit Score: 76.84  E-value: 4.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063697212   6 TFDSDLIHAIFKHIWarrfrerersdaidateaevalgttkKNRLASANANALKLSCELLKSFVSEAVQRAAIIAEAEGM 85
Cdd:cd22921     1 TFKPETIRRLLKLHF--------------------------KDKKTKINSDALKLSAELLRIFVVEAVARAARQAKAEGS 54

                          90
                  ....*....|....*....
gi 1063697212  86 EKIEATHLERILPQLLLDF 104
Cdd:cd22921    55 NTVEVEHLEKILPQLLLDF 73
 
Name Accession Description Interval E-value
HFD_CENP-X cd22921
histone-fold domain found in centromere protein X (CENP-X) and similar proteins; CENP-X, also ...
 6-104 4.07e-20

histone-fold domain found in centromere protein X (CENP-X) and similar proteins; CENP-X, also called MHF2, FANCM-associated histone fold protein 2, FANCM-interacting histone fold protein 2, Fanconi anemia-associated polypeptide of 10 kDa, retinoic acid-inducible gene D9 protein homolog, or stimulated by retinoic acid gene 13 protein homolog, is a DNA-binding component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. CENP-X, together with CENP-S, forms the MHF heterodimer, which can further assemble to form tetrameric structures. CENP-X acts as a crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. It can stabilize FANCM. CENP-X also forms a discrete complex with FANCM and CENP-S, called FANCM-MHF. This interaction leads to synergistic activation of double-stranded DNA binding and strongly stimulates FANCM-mediated DNA remodeling. In complex with CENP-T, CENP-W and CENP-S (CENP-T-W-S-X heterotetramer), CENP-X is involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of the MHF and CENP-T-W-S-X complexes, CENP-X binds DNA and bends it to form a nucleosome-like structure. Its DNA-binding function is fulfilled in the presence of CENP-S. It does not bind DNA on its own.


Pssm-ID: 467046  Cd Length: 73  Bit Score: 76.84  E-value: 4.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063697212   6 TFDSDLIHAIFKHIWarrfrerersdaidateaevalgttkKNRLASANANALKLSCELLKSFVSEAVQRAAIIAEAEGM 85
Cdd:cd22921     1 TFKPETIRRLLKLHF--------------------------KDKKTKINSDALKLSAELLRIFVVEAVARAARQAKAEGS 54

                          90
                  ....*....|....*....
gi 1063697212  86 EKIEATHLERILPQLLLDF 104
Cdd:cd22921    55 NTVEVEHLEKILPQLLLDF 73
CENP-X pfam09415
CENP-S associating Centromere protein X; The centromere, essential for faithful chromosome ...
 54-103 5.51e-14

CENP-S associating Centromere protein X; The centromere, essential for faithful chromosome segregation during mitosis, has a network of constitutive centromere-associated (CCAN) proteins associating with it during mitosis. So far in vertebrates at least 15 centromere proteins have been identified, which are divided into several subclasses based on functional and biochemical analyses. These provide a platform for the formation of a functional kinetochore during mitosis. CENP-S is one that does not associate with the CENP-H-containing complex but rather interacts with CENP-X to form a stable assembly of outer kinetochore proteins that functions downstream of other components of the CCAN. This complex may directly allow efficient and stable formation of the outer kinetochore on the CCAN platform.


Pssm-ID: 462793  Cd Length: 72  Bit Score: 61.03  E-value: 5.51e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063697212  54 NANALKLSCELLKSFVSEAVQRAAIIAEAEGMEK---IEATHLERILPQLLLD 103
Cdd:pfam09415  20 TKDALALVAEYLEIFVREAVARAAEQARAEGSEGggfLEVEDLEKIAPQLLLD 72
 
Name Accession Description Interval E-value
HFD_CENP-X cd22921
histone-fold domain found in centromere protein X (CENP-X) and similar proteins; CENP-X, also ...
 6-104 4.07e-20

histone-fold domain found in centromere protein X (CENP-X) and similar proteins; CENP-X, also called MHF2, FANCM-associated histone fold protein 2, FANCM-interacting histone fold protein 2, Fanconi anemia-associated polypeptide of 10 kDa, retinoic acid-inducible gene D9 protein homolog, or stimulated by retinoic acid gene 13 protein homolog, is a DNA-binding component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. CENP-X, together with CENP-S, forms the MHF heterodimer, which can further assemble to form tetrameric structures. CENP-X acts as a crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. It can stabilize FANCM. CENP-X also forms a discrete complex with FANCM and CENP-S, called FANCM-MHF. This interaction leads to synergistic activation of double-stranded DNA binding and strongly stimulates FANCM-mediated DNA remodeling. In complex with CENP-T, CENP-W and CENP-S (CENP-T-W-S-X heterotetramer), CENP-X is involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of the MHF and CENP-T-W-S-X complexes, CENP-X binds DNA and bends it to form a nucleosome-like structure. Its DNA-binding function is fulfilled in the presence of CENP-S. It does not bind DNA on its own.


Pssm-ID: 467046  Cd Length: 73  Bit Score: 76.84  E-value: 4.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063697212   6 TFDSDLIHAIFKHIWarrfrerersdaidateaevalgttkKNRLASANANALKLSCELLKSFVSEAVQRAAIIAEAEGM 85
Cdd:cd22921     1 TFKPETIRRLLKLHF--------------------------KDKKTKINSDALKLSAELLRIFVVEAVARAARQAKAEGS 54

                          90
                  ....*....|....*....
gi 1063697212  86 EKIEATHLERILPQLLLDF 104
Cdd:cd22921    55 NTVEVEHLEKILPQLLLDF 73
CENP-X pfam09415
CENP-S associating Centromere protein X; The centromere, essential for faithful chromosome ...
 54-103 5.51e-14

CENP-S associating Centromere protein X; The centromere, essential for faithful chromosome segregation during mitosis, has a network of constitutive centromere-associated (CCAN) proteins associating with it during mitosis. So far in vertebrates at least 15 centromere proteins have been identified, which are divided into several subclasses based on functional and biochemical analyses. These provide a platform for the formation of a functional kinetochore during mitosis. CENP-S is one that does not associate with the CENP-H-containing complex but rather interacts with CENP-X to form a stable assembly of outer kinetochore proteins that functions downstream of other components of the CCAN. This complex may directly allow efficient and stable formation of the outer kinetochore on the CCAN platform.


Pssm-ID: 462793  Cd Length: 72  Bit Score: 61.03  E-value: 5.51e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063697212  54 NANALKLSCELLKSFVSEAVQRAAIIAEAEGMEK---IEATHLERILPQLLLD 103
Cdd:pfam09415  20 TKDALALVAEYLEIFVREAVARAAEQARAEGSEGggfLEVEDLEKIAPQLLLD 72
 
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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