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Conserved domains on  [gi|1622940350|ref|XP_014994105|]
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centromere protein C isoform X3 [Macaca mulatta]

Protein Classification

cupin domain-containing protein; cupin domain-containing carboxymuconolactone decarboxylase family protein( domain architecture ID 10390880)

cupin domain-containing protein, part of a functionally diverse superfamily with the active site generally located at the center of a conserved domain forming a beta-barrel fold| cupin domain-containing carboxymuconolactone decarboxylase family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CENP-C_mid pfam15620
Centromere assembly component CENP-C middle DNMT3B-binding region; CENP-C is a component of ...
 162-417 7.81e-128

Centromere assembly component CENP-C middle DNMT3B-binding region; CENP-C is a component of the centromere assembly complex in eukaryotes. CENP-C recruits the DNA methyltransferases DNMT3B, in order to establish the necessary epigenetic DNA-methylation essential for maintenance of chromatin structure and genomic stability. This middle region of CENP-C is the binding-domain for DNMT3B. Binding of CENP-C and DNMT3B to DNA occurs at both centromeric and peri-centromeric satellite repeats. CENP-C and DNMT3B regulate the histone code in these regions.


:

Pssm-ID: 464777  Cd Length: 260  Bit Score: 382.65  E-value: 7.81e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350 162 KVIEDEFIIDESDQSFASRSWITIPRKAGPLKQRPISPAESTALLQNGKSREKHHNILPKTLANGKHSHEPHPVEPSQSS 241
Cdd:pfam15620   2 KLLEDEFIIDESDRSFASQSWITIPRKAGPLKQRTVSPAESTALLQGKKSREKHHSVSPTTLTSDKHSDKAHPVEKSQPS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350 242 DKTVLDTSYALTGETENDCKSAKYEMCSKDAEKSSGSKRTIKQKQRRKFKAKPAEEQLDVGQSKDENIRMSHTTQDKFQR 321
Cdd:pfam15620  82 EQKKLGTSCALTDELENNCRSTKYEMYSENAEKSSGNKRTIKQKQRRKFKANVVEEQLDMEQSKDENINMSHIAQDKLQR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350 322 NSDRNIEEREEIGNDCVSKKQMSPVGNKKSS--ARKDKGEAKKKHFSNES-KNKLVPEEVISTVTRSRRISRRPSDWWVV 398
Cdd:pfam15620 162 NSDRNMEDCEEMRNDHISKKQMPPVGSKKSStsTKKDKEESKKKHFSSESkKNKLVPEEVTLTVTRSRRISRRPSDWWVV 241

                         250
                  ....*....|....*....
gi 1622940350 399 KSEESSVYSNSSIRNELPV 417
Cdd:pfam15620 242 KSEQSPVYSNSSIRNELSV 260
CENP_C_N super family cl21417
Kinetochore assembly subunit CENP-C N-terminal; CENP-C is a vertebrate family that forms a ...
 1-157 2.61e-81

Kinetochore assembly subunit CENP-C N-terminal; CENP-C is a vertebrate family that forms a core component of the centromeric chromatin. On depletion of CENP-C proper formation of both centromeres and kinetochores is prevented. The N-terminal of CENP-C is necessary for recruitment of some but not all components of the Mis12 complex of the kinetochore.


The actual alignment was detected with superfamily member pfam15622:

Pssm-ID: 464778  Cd Length: 287  Bit Score: 262.48  E-value: 2.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350   1 MSSRNINDYHSDAGEEFYLSVGSPSVLLDAKTSVSQNVIPSSAQKRETYTFENSVNTLPSSTEVSLKTKKRLNFEDKVML 80
Cdd:pfam15622 130 MSSKKLKDHHSEVDEEFYLSVGSPSVLLDAKTSVSQNAIPSIAQKRETYTFENSVNMLSSSTEISLKTKKRLNFEDKDIL 209

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622940350  81 KKIEIDNKVSDEEYKTSEG-QERKPSGSSQNITRDSEYEIQRKAKKSFSTLFLETVKRKSKSSPVVRHAATAPPHSCP 157
Cdd:pfam15622 210 KKVEIENKVSEIEDKVSEGpQERKPSETSQKRIQDSEYEIQPQAKKSFSTLFLETVKRKSESSSVVRHTATAPPHSSP 287
CENP-C_C pfam11699
Mif2/CENP-C like; CENP-C_C is a C-terminal family of fungal and eukaryote proteins necessary ...
 723-807 3.72e-38

Mif2/CENP-C like; CENP-C_C is a C-terminal family of fungal and eukaryote proteins necessary for centromere formation. CENP-C is the inner-kinetochore centromere (CEN) binding protein. In the budding-yeast, Mif2, the yeast homolog, binds in the CDEIII region of the centromere, and has been shown to recruit a substantial subset of all inner and outer kinetochore proteins. Mif2 adopts a cupin fold and is extremely similar both in polypeptide chain conformation and in dimer geometry to the dimerization domain of a bacterial transcription factor. The Mif2 dimer appears to be part of an enhanceosome-like structure that nucleates kinetochore assembly in budding yeast. This C-terminal domain is the region via which CENP-C localizes to centromeres throughout the cell cycle 2,3].


:

Pssm-ID: 403028 [Multi-domain]  Cd Length: 85  Bit Score: 136.68  E-value: 3.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350 723 LKVYKTLDTPFFSTGKLILGPQEEKGKQHVGQDILVFYVNFGDLLCTLHETPYIISTGDSFYVPSGNYYNIKNLLNEESV 802
Cdd:pfam11699   1 FKFAKTLDTPFFASGILDLPPGAEKKPKNSKKMTMVFYVIQGRVEVTVHKTSFIIGKGSVFQVPRGNTYSIANLGNKEAR 80


                  ....*
gi 1622940350 803 LLFTQ 807
Cdd:pfam11699  81 LFFTQ 85
 
Name Accession Description Interval E-value
CENP-C_mid pfam15620
Centromere assembly component CENP-C middle DNMT3B-binding region; CENP-C is a component of ...
 162-417 7.81e-128

Centromere assembly component CENP-C middle DNMT3B-binding region; CENP-C is a component of the centromere assembly complex in eukaryotes. CENP-C recruits the DNA methyltransferases DNMT3B, in order to establish the necessary epigenetic DNA-methylation essential for maintenance of chromatin structure and genomic stability. This middle region of CENP-C is the binding-domain for DNMT3B. Binding of CENP-C and DNMT3B to DNA occurs at both centromeric and peri-centromeric satellite repeats. CENP-C and DNMT3B regulate the histone code in these regions.


Pssm-ID: 464777  Cd Length: 260  Bit Score: 382.65  E-value: 7.81e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350 162 KVIEDEFIIDESDQSFASRSWITIPRKAGPLKQRPISPAESTALLQNGKSREKHHNILPKTLANGKHSHEPHPVEPSQSS 241
Cdd:pfam15620   2 KLLEDEFIIDESDRSFASQSWITIPRKAGPLKQRTVSPAESTALLQGKKSREKHHSVSPTTLTSDKHSDKAHPVEKSQPS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350 242 DKTVLDTSYALTGETENDCKSAKYEMCSKDAEKSSGSKRTIKQKQRRKFKAKPAEEQLDVGQSKDENIRMSHTTQDKFQR 321
Cdd:pfam15620  82 EQKKLGTSCALTDELENNCRSTKYEMYSENAEKSSGNKRTIKQKQRRKFKANVVEEQLDMEQSKDENINMSHIAQDKLQR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350 322 NSDRNIEEREEIGNDCVSKKQMSPVGNKKSS--ARKDKGEAKKKHFSNES-KNKLVPEEVISTVTRSRRISRRPSDWWVV 398
Cdd:pfam15620 162 NSDRNMEDCEEMRNDHISKKQMPPVGSKKSStsTKKDKEESKKKHFSSESkKNKLVPEEVTLTVTRSRRISRRPSDWWVV 241

                         250
                  ....*....|....*....
gi 1622940350 399 KSEESSVYSNSSIRNELPV 417
Cdd:pfam15620 242 KSEQSPVYSNSSIRNELSV 260
CENP_C_N pfam15622
Kinetochore assembly subunit CENP-C N-terminal; CENP-C is a vertebrate family that forms a ...
 1-157 2.61e-81

Kinetochore assembly subunit CENP-C N-terminal; CENP-C is a vertebrate family that forms a core component of the centromeric chromatin. On depletion of CENP-C proper formation of both centromeres and kinetochores is prevented. The N-terminal of CENP-C is necessary for recruitment of some but not all components of the Mis12 complex of the kinetochore.


Pssm-ID: 464778  Cd Length: 287  Bit Score: 262.48  E-value: 2.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350   1 MSSRNINDYHSDAGEEFYLSVGSPSVLLDAKTSVSQNVIPSSAQKRETYTFENSVNTLPSSTEVSLKTKKRLNFEDKVML 80
Cdd:pfam15622 130 MSSKKLKDHHSEVDEEFYLSVGSPSVLLDAKTSVSQNAIPSIAQKRETYTFENSVNMLSSSTEISLKTKKRLNFEDKDIL 209

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622940350  81 KKIEIDNKVSDEEYKTSEG-QERKPSGSSQNITRDSEYEIQRKAKKSFSTLFLETVKRKSKSSPVVRHAATAPPHSCP 157
Cdd:pfam15622 210 KKVEIENKVSEIEDKVSEGpQERKPSETSQKRIQDSEYEIQPQAKKSFSTLFLETVKRKSESSSVVRHTATAPPHSSP 287
CENP-C_C pfam11699
Mif2/CENP-C like; CENP-C_C is a C-terminal family of fungal and eukaryote proteins necessary ...
 723-807 3.72e-38

Mif2/CENP-C like; CENP-C_C is a C-terminal family of fungal and eukaryote proteins necessary for centromere formation. CENP-C is the inner-kinetochore centromere (CEN) binding protein. In the budding-yeast, Mif2, the yeast homolog, binds in the CDEIII region of the centromere, and has been shown to recruit a substantial subset of all inner and outer kinetochore proteins. Mif2 adopts a cupin fold and is extremely similar both in polypeptide chain conformation and in dimer geometry to the dimerization domain of a bacterial transcription factor. The Mif2 dimer appears to be part of an enhanceosome-like structure that nucleates kinetochore assembly in budding yeast. This C-terminal domain is the region via which CENP-C localizes to centromeres throughout the cell cycle 2,3].


Pssm-ID: 403028 [Multi-domain]  Cd Length: 85  Bit Score: 136.68  E-value: 3.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350 723 LKVYKTLDTPFFSTGKLILGPQEEKGKQHVGQDILVFYVNFGDLLCTLHETPYIISTGDSFYVPSGNYYNIKNLLNEESV 802
Cdd:pfam11699   1 FKFAKTLDTPFFASGILDLPPGAEKKPKNSKKMTMVFYVIQGRVEVTVHKTSFIIGKGSVFQVPRGNTYSIANLGNKEAR 80


                  ....*
gi 1622940350 803 LLFTQ 807
Cdd:pfam11699  81 LFFTQ 85
cupin_CENP-C_C cd06993
centromere-binding protein CENP-C, C-terminal cupin domain; This family includes centromeric ...
 732-808 2.85e-30

centromere-binding protein CENP-C, C-terminal cupin domain; This family includes centromeric protein C (CENP-C; known as Mif2 in budding yeast and centromere protein 3 or cnp3 in fission yeast), which is an inner kinetochore centromere (CEN)-binding protein found in fungi and metazoans. CENP-C is a component of the CENP-A nucleosome-associated complex (NAC) that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. CENP-C localizes to the inner kinetochore plates adjacent to the centromeric DNA and is known to have DNA-binding ability. CENP-C, along with CENP-H, provides a platform onto which the mitotic kinetochore is assembled and thus plays a critical role in the structuring of kinethocore chromatin. The cupin domain at the C-terminus forms a homodimer which is part of an enhanceosome-like structure that nucleates kinetochore assembly in budding yeast. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380398 [Multi-domain]  Cd Length: 77  Bit Score: 113.79  E-value: 2.85e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622940350 732 PFFSTGKLILGPQEEKGKQHVGQDILVFYVNFGDLLCTLHETPYIISTGDSFYVPSGNYYNIKNLLNEESVLLFTQI 808
Cdd:cd06993     1 DFFASGMLELPPGGEKPLKNSKDNTYVFYVIQGAVEVTLHETTFVVTKGCSFQVPRGNYYSIKNIGNKEARLFFVQS 77
 
Name Accession Description Interval E-value
CENP-C_mid pfam15620
Centromere assembly component CENP-C middle DNMT3B-binding region; CENP-C is a component of ...
 162-417 7.81e-128

Centromere assembly component CENP-C middle DNMT3B-binding region; CENP-C is a component of the centromere assembly complex in eukaryotes. CENP-C recruits the DNA methyltransferases DNMT3B, in order to establish the necessary epigenetic DNA-methylation essential for maintenance of chromatin structure and genomic stability. This middle region of CENP-C is the binding-domain for DNMT3B. Binding of CENP-C and DNMT3B to DNA occurs at both centromeric and peri-centromeric satellite repeats. CENP-C and DNMT3B regulate the histone code in these regions.


Pssm-ID: 464777  Cd Length: 260  Bit Score: 382.65  E-value: 7.81e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350 162 KVIEDEFIIDESDQSFASRSWITIPRKAGPLKQRPISPAESTALLQNGKSREKHHNILPKTLANGKHSHEPHPVEPSQSS 241
Cdd:pfam15620   2 KLLEDEFIIDESDRSFASQSWITIPRKAGPLKQRTVSPAESTALLQGKKSREKHHSVSPTTLTSDKHSDKAHPVEKSQPS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350 242 DKTVLDTSYALTGETENDCKSAKYEMCSKDAEKSSGSKRTIKQKQRRKFKAKPAEEQLDVGQSKDENIRMSHTTQDKFQR 321
Cdd:pfam15620  82 EQKKLGTSCALTDELENNCRSTKYEMYSENAEKSSGNKRTIKQKQRRKFKANVVEEQLDMEQSKDENINMSHIAQDKLQR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350 322 NSDRNIEEREEIGNDCVSKKQMSPVGNKKSS--ARKDKGEAKKKHFSNES-KNKLVPEEVISTVTRSRRISRRPSDWWVV 398
Cdd:pfam15620 162 NSDRNMEDCEEMRNDHISKKQMPPVGSKKSStsTKKDKEESKKKHFSSESkKNKLVPEEVTLTVTRSRRISRRPSDWWVV 241

                         250
                  ....*....|....*....
gi 1622940350 399 KSEESSVYSNSSIRNELPV 417
Cdd:pfam15620 242 KSEQSPVYSNSSIRNELSV 260
CENP_C_N pfam15622
Kinetochore assembly subunit CENP-C N-terminal; CENP-C is a vertebrate family that forms a ...
 1-157 2.61e-81

Kinetochore assembly subunit CENP-C N-terminal; CENP-C is a vertebrate family that forms a core component of the centromeric chromatin. On depletion of CENP-C proper formation of both centromeres and kinetochores is prevented. The N-terminal of CENP-C is necessary for recruitment of some but not all components of the Mis12 complex of the kinetochore.


Pssm-ID: 464778  Cd Length: 287  Bit Score: 262.48  E-value: 2.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350   1 MSSRNINDYHSDAGEEFYLSVGSPSVLLDAKTSVSQNVIPSSAQKRETYTFENSVNTLPSSTEVSLKTKKRLNFEDKVML 80
Cdd:pfam15622 130 MSSKKLKDHHSEVDEEFYLSVGSPSVLLDAKTSVSQNAIPSIAQKRETYTFENSVNMLSSSTEISLKTKKRLNFEDKDIL 209

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622940350  81 KKIEIDNKVSDEEYKTSEG-QERKPSGSSQNITRDSEYEIQRKAKKSFSTLFLETVKRKSKSSPVVRHAATAPPHSCP 157
Cdd:pfam15622 210 KKVEIENKVSEIEDKVSEGpQERKPSETSQKRIQDSEYEIQPQAKKSFSTLFLETVKRKSESSSVVRHTATAPPHSSP 287
CENP-C_C pfam11699
Mif2/CENP-C like; CENP-C_C is a C-terminal family of fungal and eukaryote proteins necessary ...
 723-807 3.72e-38

Mif2/CENP-C like; CENP-C_C is a C-terminal family of fungal and eukaryote proteins necessary for centromere formation. CENP-C is the inner-kinetochore centromere (CEN) binding protein. In the budding-yeast, Mif2, the yeast homolog, binds in the CDEIII region of the centromere, and has been shown to recruit a substantial subset of all inner and outer kinetochore proteins. Mif2 adopts a cupin fold and is extremely similar both in polypeptide chain conformation and in dimer geometry to the dimerization domain of a bacterial transcription factor. The Mif2 dimer appears to be part of an enhanceosome-like structure that nucleates kinetochore assembly in budding yeast. This C-terminal domain is the region via which CENP-C localizes to centromeres throughout the cell cycle 2,3].


Pssm-ID: 403028 [Multi-domain]  Cd Length: 85  Bit Score: 136.68  E-value: 3.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622940350 723 LKVYKTLDTPFFSTGKLILGPQEEKGKQHVGQDILVFYVNFGDLLCTLHETPYIISTGDSFYVPSGNYYNIKNLLNEESV 802
Cdd:pfam11699   1 FKFAKTLDTPFFASGILDLPPGAEKKPKNSKKMTMVFYVIQGRVEVTVHKTSFIIGKGSVFQVPRGNTYSIANLGNKEAR 80


                  ....*
gi 1622940350 803 LLFTQ 807
Cdd:pfam11699  81 LFFTQ 85
cupin_CENP-C_C cd06993
centromere-binding protein CENP-C, C-terminal cupin domain; This family includes centromeric ...
 732-808 2.85e-30

centromere-binding protein CENP-C, C-terminal cupin domain; This family includes centromeric protein C (CENP-C; known as Mif2 in budding yeast and centromere protein 3 or cnp3 in fission yeast), which is an inner kinetochore centromere (CEN)-binding protein found in fungi and metazoans. CENP-C is a component of the CENP-A nucleosome-associated complex (NAC) that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. CENP-C localizes to the inner kinetochore plates adjacent to the centromeric DNA and is known to have DNA-binding ability. CENP-C, along with CENP-H, provides a platform onto which the mitotic kinetochore is assembled and thus plays a critical role in the structuring of kinethocore chromatin. The cupin domain at the C-terminus forms a homodimer which is part of an enhanceosome-like structure that nucleates kinetochore assembly in budding yeast. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380398 [Multi-domain]  Cd Length: 77  Bit Score: 113.79  E-value: 2.85e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622940350 732 PFFSTGKLILGPQEEKGKQHVGQDILVFYVNFGDLLCTLHETPYIISTGDSFYVPSGNYYNIKNLLNEESVLLFTQI 808
Cdd:cd06993     1 DFFASGMLELPPGGEKPLKNSKDNTYVFYVIQGAVEVTLHETTFVVTKGCSFQVPRGNYYSIKNIGNKEARLFFVQS 77
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 751-805 3.07e-03

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 36.85  E-value: 3.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622940350 751 HVGQDILvFYVNFGDLLCTLHETPYIISTGDSFYVPSGNYYNIKNLLNEESVLLF 805
Cdd:pfam07883  16 HPGEDEF-FYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLD 69
 
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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