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Conserved domains on  [gi|1039770379|ref|XP_017176127|]
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centromere protein C isoform X5 [Mus musculus]

Protein Classification

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 ...
 1-255 2.91e-119

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: 355.30  E-value: 2.91e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379   1 MKLLEDEFIIDRSDRSFSSRLWVMIPSKDRHLSAHKPSP-ENTALLQGKKSREKSHSLSAMTFARNTQSDKAHPIEEAQL 79
Cdd:pfam15620   1 MKLLEDEFIIDESDRSFASQSWITIPRKAGPLKQRTVSPaESTALLQGKKSREKHHSVSPTTLTSDKHSDKAHPVEKSQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379  80 SVEENPATTC--TDELENDCRSPENKMQSETAKTPPAWERTTKQSQRRVSKPKAAEE-LRKGQSSWENSNVSNTGQDKLQ 156
Cdd:pfam15620  81 SEQKKLGTSCalTDELENNCRSTKYEMYSENAEKSSGNKRTIKQKQRRKFKANVVEEqLDMEQSKDENINMSHIAQDKLQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379 157 INSKRNMKDCEEVRNEPNPKKQKPALENKKKTNSTQTNKEKSGKKFFSGGS-KNKFVPKKVTLTSRRSCRISQRPSEWWR 235
Cdd:pfam15620 161 RNSDRNMEDCEEMRNDHISKKQMPPVGSKKSSTSTKKDKEESKKKHFSSESkKNKLVPEEVTLTVTRSRRISRRPSDWWV 240

                         250       260
                  ....*....|....*....|
gi 1039770379 236 VKSDESSVDRNPSKENNSPV 255
Cdd:pfam15620 241 VKSEQSPVYSNSSIRNELSV 260
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 555-639 1.48e-31

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


The actual alignment was detected with superfamily member pfam11699:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 85  Bit Score: 117.42  E-value: 1.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379 555 LKVFKTLDTIYFSTGKLVLGPYEEKGKQHVGQDILVFYVNFGDLLCTLHETPYKLTTGDSFYVPSGNHYNIKNLLNVESS 634
Cdd:pfam11699   1 FKFAKTLDTPFFASGILDLPPGAEKKPKNSKKMTMVFYVIQGRVEVTVHKTSFIIGKGSVFQVPRGNTYSIANLGNKEAR 80


                  ....*
gi 1039770379 635 LLFTQ 639
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 ...
 1-255 2.91e-119

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: 355.30  E-value: 2.91e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379   1 MKLLEDEFIIDRSDRSFSSRLWVMIPSKDRHLSAHKPSP-ENTALLQGKKSREKSHSLSAMTFARNTQSDKAHPIEEAQL 79
Cdd:pfam15620   1 MKLLEDEFIIDESDRSFASQSWITIPRKAGPLKQRTVSPaESTALLQGKKSREKHHSVSPTTLTSDKHSDKAHPVEKSQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379  80 SVEENPATTC--TDELENDCRSPENKMQSETAKTPPAWERTTKQSQRRVSKPKAAEE-LRKGQSSWENSNVSNTGQDKLQ 156
Cdd:pfam15620  81 SEQKKLGTSCalTDELENNCRSTKYEMYSENAEKSSGNKRTIKQKQRRKFKANVVEEqLDMEQSKDENINMSHIAQDKLQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379 157 INSKRNMKDCEEVRNEPNPKKQKPALENKKKTNSTQTNKEKSGKKFFSGGS-KNKFVPKKVTLTSRRSCRISQRPSEWWR 235
Cdd:pfam15620 161 RNSDRNMEDCEEMRNDHISKKQMPPVGSKKSSTSTKKDKEESKKKHFSSESkKNKLVPEEVTLTVTRSRRISRRPSDWWV 240

                         250       260
                  ....*....|....*....|
gi 1039770379 236 VKSDESSVDRNPSKENNSPV 255
Cdd:pfam15620 241 VKSEQSPVYSNSSIRNELSV 260
CENP-C_C pfam11699
Mif2/CENP-C like; CENP-C_C is a C-terminal family of fungal and eukaryote proteins necessary ...
 555-639 1.48e-31

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: 117.42  E-value: 1.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379 555 LKVFKTLDTIYFSTGKLVLGPYEEKGKQHVGQDILVFYVNFGDLLCTLHETPYKLTTGDSFYVPSGNHYNIKNLLNVESS 634
Cdd:pfam11699   1 FKFAKTLDTPFFASGILDLPPGAEKKPKNSKKMTMVFYVIQGRVEVTVHKTSFIIGKGSVFQVPRGNTYSIANLGNKEAR 80


                  ....*
gi 1039770379 635 LLFTQ 639
Cdd:pfam11699  81 LFFTQ 85
cupin_CENP-C_C cd06993
centromere-binding protein CENP-C, C-terminal cupin domain; This family includes centromeric ...
 565-640 3.12e-27

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: 104.93  E-value: 3.12e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770379 565 YFSTGKLVLGPYEEKGKQHVGQDILVFYVNFGDLLCTLHETPYKLTTGDSFYVPSGNHYNIKNLLNVESSLLFTQI 640
Cdd:cd06993     2 FFASGMLELPPGGEKPLKNSKDNTYVFYVIQGAVEVTLHETTFVVTKGCSFQVPRGNYYSIKNIGNKEARLFFVQS 77
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 91-324 5.28e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 40.03  E-value: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379   91 DELENDCRSPENKMQSETAKTPPAWERTTKQSQRRVSKPKAAEELRKGQSSWENSNVSNTGQDKLQINSKRNMKDceevr 170
Cdd:PTZ00108  1135 DKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKL----- 1209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379  171 nepnpkKQKPALENKKKTNSTQTNKEKSGKKFFSGGSKN-KFVPKKVTLTSRRSCRISQRPSEWW------------RVK 237
Cdd:PTZ00108  1210 ------DDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRlKSKKNNSSKSSEDNDEFSSDDLSKEgkpknapkrvsaVQY 1283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379  238 SDESSVDRNPSKENNSPVVYPNKKKQTKRNHVSKRAGKKPGSSKRQKTemSPRVQKSLNVKDSGGTVSGHDDTSRSQRKP 317
Cdd:PTZ00108  1284 SPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKT--ARKKKSKTRVKQASASQSSRLLRRPRKKKS 1361


                   ....*..
gi 1039770379  318 LKIIEAD 324
Cdd:PTZ00108  1362 DSSSEDD 1368
 
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 ...
 1-255 2.91e-119

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: 355.30  E-value: 2.91e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379   1 MKLLEDEFIIDRSDRSFSSRLWVMIPSKDRHLSAHKPSP-ENTALLQGKKSREKSHSLSAMTFARNTQSDKAHPIEEAQL 79
Cdd:pfam15620   1 MKLLEDEFIIDESDRSFASQSWITIPRKAGPLKQRTVSPaESTALLQGKKSREKHHSVSPTTLTSDKHSDKAHPVEKSQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379  80 SVEENPATTC--TDELENDCRSPENKMQSETAKTPPAWERTTKQSQRRVSKPKAAEE-LRKGQSSWENSNVSNTGQDKLQ 156
Cdd:pfam15620  81 SEQKKLGTSCalTDELENNCRSTKYEMYSENAEKSSGNKRTIKQKQRRKFKANVVEEqLDMEQSKDENINMSHIAQDKLQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379 157 INSKRNMKDCEEVRNEPNPKKQKPALENKKKTNSTQTNKEKSGKKFFSGGS-KNKFVPKKVTLTSRRSCRISQRPSEWWR 235
Cdd:pfam15620 161 RNSDRNMEDCEEMRNDHISKKQMPPVGSKKSSTSTKKDKEESKKKHFSSESkKNKLVPEEVTLTVTRSRRISRRPSDWWV 240

                         250       260
                  ....*....|....*....|
gi 1039770379 236 VKSDESSVDRNPSKENNSPV 255
Cdd:pfam15620 241 VKSEQSPVYSNSSIRNELSV 260
CENP-C_C pfam11699
Mif2/CENP-C like; CENP-C_C is a C-terminal family of fungal and eukaryote proteins necessary ...
 555-639 1.48e-31

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: 117.42  E-value: 1.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379 555 LKVFKTLDTIYFSTGKLVLGPYEEKGKQHVGQDILVFYVNFGDLLCTLHETPYKLTTGDSFYVPSGNHYNIKNLLNVESS 634
Cdd:pfam11699   1 FKFAKTLDTPFFASGILDLPPGAEKKPKNSKKMTMVFYVIQGRVEVTVHKTSFIIGKGSVFQVPRGNTYSIANLGNKEAR 80


                  ....*
gi 1039770379 635 LLFTQ 639
Cdd:pfam11699  81 LFFTQ 85
cupin_CENP-C_C cd06993
centromere-binding protein CENP-C, C-terminal cupin domain; This family includes centromeric ...
 565-640 3.12e-27

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: 104.93  E-value: 3.12e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770379 565 YFSTGKLVLGPYEEKGKQHVGQDILVFYVNFGDLLCTLHETPYKLTTGDSFYVPSGNHYNIKNLLNVESSLLFTQI 640
Cdd:cd06993     2 FFASGMLELPPGGEKPLKNSKDNTYVFYVIQGAVEVTLHETTFVVTKGCSFQVPRGNYYSIKNIGNKEARLFFVQS 77
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 91-324 5.28e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 40.03  E-value: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379   91 DELENDCRSPENKMQSETAKTPPAWERTTKQSQRRVSKPKAAEELRKGQSSWENSNVSNTGQDKLQINSKRNMKDceevr 170
Cdd:PTZ00108  1135 DKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKL----- 1209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379  171 nepnpkKQKPALENKKKTNSTQTNKEKSGKKFFSGGSKN-KFVPKKVTLTSRRSCRISQRPSEWW------------RVK 237
Cdd:PTZ00108  1210 ------DDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRlKSKKNNSSKSSEDNDEFSSDDLSKEgkpknapkrvsaVQY 1283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770379  238 SDESSVDRNPSKENNSPVVYPNKKKQTKRNHVSKRAGKKPGSSKRQKTemSPRVQKSLNVKDSGGTVSGHDDTSRSQRKP 317
Cdd:PTZ00108  1284 SPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKT--ARKKKSKTRVKQASASQSSRLLRRPRKKKS 1361


                   ....*..
gi 1039770379  318 LKIIEAD 324
Cdd:PTZ00108  1362 DSSSEDD 1368
 
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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