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Conserved domains on  [gi|2462557893|ref|XP_054173343|]
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protein DBF4 homolog B isoform X18 [Homo sapiens]

Protein Classification

BRCT domain-containing protein( domain architecture ID 10455335)

BRCT (BRCA1 C-terminus) domain-containing protein may interact with DNA, and participate in DNA-damage checkpoint or DNA-repair pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-DBF pfam07535
DBF zinc finger; This domain is predicted to bind metal ions and is often found associated ...
 260-301 1.14e-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: 70.22  E-value: 1.14e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462557893 260 GYCECCQEAFEELHVHLQSAQHRSFALEAHLYAEVDRIIAQL 301
Cdd:pfam07535   1 GYCENCRVKYEDLEEHIVSEKHRKFAENDSNFKELDELISKL 42
DBF4 super family cl34887
Protein kinase essential for the initiation of DNA replication [DNA replication, recombination, ...
 214-301 1.03e-05

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


The actual alignment was detected with superfamily member COG5067:

Pssm-ID: 227399 [Multi-domain]  Cd Length: 468  Bit Score: 47.64  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557893 214 PAAESRTRKVARLKApfLKIEDESRESKDgePSPRSAAHTMPRR--KKGYCECCQEAFEELHVHLQSAQHRSFALEAHLY 291
Cdd:COG5067   379 PLCTLKTRLIVDRKL--GVKQTNGAPSKE--TGKDSAVHQKVKKetKKGYCENCREKYESLEQHIVSEKHRRFAENDLNF 454

                          90
                  ....*....|
gi 2462557893 292 AEVDRIIAQL 301
Cdd:COG5067   455 EALDSLFELL 464
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 47-93 7.92e-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: 34.96  E-value: 7.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462557893  47 PFSGKSFYLDLPAGKNLQFLTGAIQQLGGVIEGFLSKEVSYIVSSRR 93
Cdd:pfam00533   5 LFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEAR 51
 
Name Accession Description Interval E-value
zf-DBF pfam07535
DBF zinc finger; This domain is predicted to bind metal ions and is often found associated ...
 260-301 1.14e-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: 70.22  E-value: 1.14e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462557893 260 GYCECCQEAFEELHVHLQSAQHRSFALEAHLYAEVDRIIAQL 301
Cdd:pfam07535   1 GYCENCRVKYEDLEEHIVSEKHRKFAENDSNFKELDELISKL 42
ZnF_DBF smart00586
Zinc finger in DBF-like proteins;
257-301 8.11e-12

Zinc finger in DBF-like proteins;


Pssm-ID: 128854 [Multi-domain]  Cd Length: 49  Bit Score: 59.80  E-value: 8.11e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462557893  257 RKKGYCECCQEAFEELHVHLQSAQHRSFALEAHLYAEVDRIIAQL 301
Cdd:smart00586   3 KKPGYCENCREKYDDLETHLLSEKHRRFAENNDNFQALDDLISQL 47
DBF4 COG5067
Protein kinase essential for the initiation of DNA replication [DNA replication, recombination, ...
 214-301 1.03e-05

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: 47.64  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557893 214 PAAESRTRKVARLKApfLKIEDESRESKDgePSPRSAAHTMPRR--KKGYCECCQEAFEELHVHLQSAQHRSFALEAHLY 291
Cdd:COG5067   379 PLCTLKTRLIVDRKL--GVKQTNGAPSKE--TGKDSAVHQKVKKetKKGYCENCREKYESLEQHIVSEKHRRFAENDLNF 454

                          90
                  ....*....|
gi 2462557893 292 AEVDRIIAQL 301
Cdd:COG5067   455 EALDSLFELL 464
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 47-93 7.92e-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: 34.96  E-value: 7.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462557893  47 PFSGKSFYLDLPAGKNLQFLTGAIQQLGGVIEGFLSKEVSYIVSSRR 93
Cdd:pfam00533   5 LFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEAR 51
 
Name Accession Description Interval E-value
zf-DBF pfam07535
DBF zinc finger; This domain is predicted to bind metal ions and is often found associated ...
 260-301 1.14e-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: 70.22  E-value: 1.14e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462557893 260 GYCECCQEAFEELHVHLQSAQHRSFALEAHLYAEVDRIIAQL 301
Cdd:pfam07535   1 GYCENCRVKYEDLEEHIVSEKHRKFAENDSNFKELDELISKL 42
ZnF_DBF smart00586
Zinc finger in DBF-like proteins;
257-301 8.11e-12

Zinc finger in DBF-like proteins;


Pssm-ID: 128854 [Multi-domain]  Cd Length: 49  Bit Score: 59.80  E-value: 8.11e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2462557893  257 RKKGYCECCQEAFEELHVHLQSAQHRSFALEAHLYAEVDRIIAQL 301
Cdd:smart00586   3 KKPGYCENCREKYDDLETHLLSEKHRRFAENNDNFQALDDLISQL 47
DBF4 COG5067
Protein kinase essential for the initiation of DNA replication [DNA replication, recombination, ...
 214-301 1.03e-05

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: 47.64  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557893 214 PAAESRTRKVARLKApfLKIEDESRESKDgePSPRSAAHTMPRR--KKGYCECCQEAFEELHVHLQSAQHRSFALEAHLY 291
Cdd:COG5067   379 PLCTLKTRLIVDRKL--GVKQTNGAPSKE--TGKDSAVHQKVKKetKKGYCENCREKYESLEQHIVSEKHRRFAENDLNF 454

                          90
                  ....*....|
gi 2462557893 292 AEVDRIIAQL 301
Cdd:COG5067   455 EALDSLFELL 464
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 47-93 7.92e-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: 34.96  E-value: 7.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462557893  47 PFSGKSFYLDLPAGKNLQFLTGAIQQLGGVIEGFLSKEVSYIVSSRR 93
Cdd:pfam00533   5 LFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEAR 51
 
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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