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Conserved domains on  [gi|1958769256|ref|XP_038963429|]
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protein DBF4 homolog A isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ZnF_DBF super family cl46924
Zinc finger in DBF-like proteins;
287-334 8.32e-19

Zinc finger in DBF-like proteins;


The actual alignment was detected with superfamily member smart00586:

Pssm-ID: 128854 [Multi-domain]  Cd Length: 49  Bit Score: 80.21  E-value: 8.32e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958769256  287 EKRKKGYCECCLQKYEDLETHLLSEKHRNFAQSN-QYQVVDDIVSKLIF 334
Cdd:smart00586   1 EEKKPGYCENCREKYDDLETHLLSEKHRRFAENNdNFQALDDLISQLRR 49
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
42-109 3.28e-03

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


:

Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 36.89  E-value: 3.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958769256  42 KYKPLWGKIFYL-DLPSITiCEKLQKDIKELGGRVEEFLSKDISYLVSNKKEAKYAQTLGRVSPVPSPE 109
Cdd:pfam00533   2 KEKLFSGKTFVItGLDGLE-RDELKELIEKLGGKVTDSLSKKTTHVIVEARTKKYLKAKELGIPIVTEE 69
 
Name Accession Description Interval E-value
ZnF_DBF smart00586
Zinc finger in DBF-like proteins;
287-334 8.32e-19

Zinc finger in DBF-like proteins;


Pssm-ID: 128854 [Multi-domain]  Cd Length: 49  Bit Score: 80.21  E-value: 8.32e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958769256  287 EKRKKGYCECCLQKYEDLETHLLSEKHRNFAQSN-QYQVVDDIVSKLIF 334
Cdd:smart00586   1 EEKKPGYCENCREKYDDLETHLLSEKHRRFAENNdNFQALDDLISQLRR 49
zf-DBF pfam07535
DBF zinc finger; This domain is predicted to bind metal ions and is often found associated ...
292-332 1.15e-15

DBF zinc finger; This domain is predicted to bind metal ions and is often found associated with pfam00533 and pfam02178. It was first identified in the Drosophila chiffon gene product, and is associated with initiation of DNA replication.


Pssm-ID: 462197  Cd Length: 42  Bit Score: 70.99  E-value: 1.15e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958769256 292 GYCECCLQKYEDLETHLLSEKHRNFAQ-SNQYQVVDDIVSKL 332
Cdd:pfam07535   1 GYCENCRVKYEDLEEHIVSEKHRKFAEnDSNFKELDELISKL 42
DBF4 COG5067
Protein kinase essential for the initiation of DNA replication [DNA replication, recombination, ...
284-334 1.05e-07

Protein kinase essential for the initiation of DNA replication [DNA replication, recombination, and repair / Cell division and chromosome partitioning];


Pssm-ID: 227399 [Multi-domain]  Cd Length: 468  Bit Score: 54.95  E-value: 1.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958769256 284 QLKEKRKKGYCECCLQKYEDLETHLLSEKHRNFAQSNQ-YQVVDDIVSKLIF 334
Cdd:COG5067   415 KVKKETKKGYCENCREKYESLEQHIVSEKHRRFAENDLnFEALDSLFELLRR 466
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
42-109 3.28e-03

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 36.89  E-value: 3.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958769256  42 KYKPLWGKIFYL-DLPSITiCEKLQKDIKELGGRVEEFLSKDISYLVSNKKEAKYAQTLGRVSPVPSPE 109
Cdd:pfam00533   2 KEKLFSGKTFVItGLDGLE-RDELKELIEKLGGKVTDSLSKKTTHVIVEARTKKYLKAKELGIPIVTEE 69
 
Name Accession Description Interval E-value
ZnF_DBF smart00586
Zinc finger in DBF-like proteins;
287-334 8.32e-19

Zinc finger in DBF-like proteins;


Pssm-ID: 128854 [Multi-domain]  Cd Length: 49  Bit Score: 80.21  E-value: 8.32e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958769256  287 EKRKKGYCECCLQKYEDLETHLLSEKHRNFAQSN-QYQVVDDIVSKLIF 334
Cdd:smart00586   1 EEKKPGYCENCREKYDDLETHLLSEKHRRFAENNdNFQALDDLISQLRR 49
zf-DBF pfam07535
DBF zinc finger; This domain is predicted to bind metal ions and is often found associated ...
292-332 1.15e-15

DBF zinc finger; This domain is predicted to bind metal ions and is often found associated with pfam00533 and pfam02178. It was first identified in the Drosophila chiffon gene product, and is associated with initiation of DNA replication.


Pssm-ID: 462197  Cd Length: 42  Bit Score: 70.99  E-value: 1.15e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1958769256 292 GYCECCLQKYEDLETHLLSEKHRNFAQ-SNQYQVVDDIVSKL 332
Cdd:pfam07535   1 GYCENCRVKYEDLEEHIVSEKHRKFAEnDSNFKELDELISKL 42
DBF4 COG5067
Protein kinase essential for the initiation of DNA replication [DNA replication, recombination, ...
284-334 1.05e-07

Protein kinase essential for the initiation of DNA replication [DNA replication, recombination, and repair / Cell division and chromosome partitioning];


Pssm-ID: 227399 [Multi-domain]  Cd Length: 468  Bit Score: 54.95  E-value: 1.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958769256 284 QLKEKRKKGYCECCLQKYEDLETHLLSEKHRNFAQSNQ-YQVVDDIVSKLIF 334
Cdd:COG5067   415 KVKKETKKGYCENCREKYESLEQHIVSEKHRRFAENDLnFEALDSLFELLRR 466
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
42-109 3.28e-03

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 36.89  E-value: 3.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958769256  42 KYKPLWGKIFYL-DLPSITiCEKLQKDIKELGGRVEEFLSKDISYLVSNKKEAKYAQTLGRVSPVPSPE 109
Cdd:pfam00533   2 KEKLFSGKTFVItGLDGLE-RDELKELIEKLGGKVTDSLSKKTTHVIVEARTKKYLKAKELGIPIVTEE 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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