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Conserved domains on  [gi|528517270|ref|XP_005174176|]
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RBBP8 N-terminal-like protein [Danio rerio]

Protein Classification

DNA endonuclease RBBP8( domain architecture ID 10564630)

DNA endonuclease RBBP8 similar to human RBBP8 that cooperates with the MRE11-RAD50-NBN complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CtIP_N pfam10482
Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that ...
6-125 1.83e-64

Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that complexes with both BRCA1 and the BRCA1-associated RING domain protein (BARD1). At the protein level, CtIP expression varies with cell cycle progression in a pattern identical to that of BRCA1. Thus, the steady-state levels of CtIP polypeptides, which remain low in resting cells and G1 cycling cells, increase dramatically as Dividing cells traverse the G1/S boundary. CtIP can potentially modulate the functions ascribed to BRCA1 in transcriptional regulation, DNA repair, and/or cell cycle checkpoint control. This N-terminal domain carries a coiled-coil region and is essential for homodimerization of the protein. The C-terminal domain is family pfam08573.


:

Pssm-ID: 463107 [Multi-domain]  Cd Length: 120  Bit Score: 206.44  E-value: 1.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517270    6 FPELLQKLREVHDNELEGWQEKVLELTNKKNIDTKRLEELHSRNQQLREQQRILTENIKQLENRLRAGLCDRCTVTQEMA 85
Cdd:pfam10482   1 FEELLNKLKEIHDKEVQGLQAKVSELKKERCLDAQRLEELFSKNQQLREQQKALQENIKVLENRLRAGLCDRCAVTQELA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 528517270   86 KKRQQDFENSQIQSLQHISLLVSEMNTLKKENDRLRDELK 125
Cdd:pfam10482  81 KKKQQEFENSQLQSLQHITILTNEMNTLKDENRKLKEELK 120
 
Name Accession Description Interval E-value
CtIP_N pfam10482
Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that ...
6-125 1.83e-64

Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that complexes with both BRCA1 and the BRCA1-associated RING domain protein (BARD1). At the protein level, CtIP expression varies with cell cycle progression in a pattern identical to that of BRCA1. Thus, the steady-state levels of CtIP polypeptides, which remain low in resting cells and G1 cycling cells, increase dramatically as Dividing cells traverse the G1/S boundary. CtIP can potentially modulate the functions ascribed to BRCA1 in transcriptional regulation, DNA repair, and/or cell cycle checkpoint control. This N-terminal domain carries a coiled-coil region and is essential for homodimerization of the protein. The C-terminal domain is family pfam08573.


Pssm-ID: 463107 [Multi-domain]  Cd Length: 120  Bit Score: 206.44  E-value: 1.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517270    6 FPELLQKLREVHDNELEGWQEKVLELTNKKNIDTKRLEELHSRNQQLREQQRILTENIKQLENRLRAGLCDRCTVTQEMA 85
Cdd:pfam10482   1 FEELLNKLKEIHDKEVQGLQAKVSELKKERCLDAQRLEELFSKNQQLREQQKALQENIKVLENRLRAGLCDRCAVTQELA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 528517270   86 KKRQQDFENSQIQSLQHISLLVSEMNTLKKENDRLRDELK 125
Cdd:pfam10482  81 KKKQQEFENSQLQSLQHITILTNEMNTLKDENRKLKEELK 120
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
15-129 6.92e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.46  E-value: 6.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517270  15 EVHDNELEGWQEKVLELTnkknidtKRLEELHSRNQQLREQQRILTENIKQLENRLRaglcdrctvtQEMAKKRQQDFEN 94
Cdd:COG2433  402 EHEERELTEEEEEIRRLE-------EQVERLEAEVEELEAELEEKDERIERLERELS----------EARSEERREIRKD 464
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 528517270  95 SQIQSLQH-ISLLVSEMNTLKKENDRLRDELKTLRE 129
Cdd:COG2433  465 REISRLDReIERLERELEEERERIEELKRKLERLKE 500
 
Name Accession Description Interval E-value
CtIP_N pfam10482
Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that ...
6-125 1.83e-64

Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that complexes with both BRCA1 and the BRCA1-associated RING domain protein (BARD1). At the protein level, CtIP expression varies with cell cycle progression in a pattern identical to that of BRCA1. Thus, the steady-state levels of CtIP polypeptides, which remain low in resting cells and G1 cycling cells, increase dramatically as Dividing cells traverse the G1/S boundary. CtIP can potentially modulate the functions ascribed to BRCA1 in transcriptional regulation, DNA repair, and/or cell cycle checkpoint control. This N-terminal domain carries a coiled-coil region and is essential for homodimerization of the protein. The C-terminal domain is family pfam08573.


Pssm-ID: 463107 [Multi-domain]  Cd Length: 120  Bit Score: 206.44  E-value: 1.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517270    6 FPELLQKLREVHDNELEGWQEKVLELTNKKNIDTKRLEELHSRNQQLREQQRILTENIKQLENRLRAGLCDRCTVTQEMA 85
Cdd:pfam10482   1 FEELLNKLKEIHDKEVQGLQAKVSELKKERCLDAQRLEELFSKNQQLREQQKALQENIKVLENRLRAGLCDRCAVTQELA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 528517270   86 KKRQQDFENSQIQSLQHISLLVSEMNTLKKENDRLRDELK 125
Cdd:pfam10482  81 KKKQQEFENSQLQSLQHITILTNEMNTLKDENRKLKEELK 120
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
15-129 6.92e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.46  E-value: 6.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528517270  15 EVHDNELEGWQEKVLELTnkknidtKRLEELHSRNQQLREQQRILTENIKQLENRLRaglcdrctvtQEMAKKRQQDFEN 94
Cdd:COG2433  402 EHEERELTEEEEEIRRLE-------EQVERLEAEVEELEAELEEKDERIERLERELS----------EARSEERREIRKD 464
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 528517270  95 SQIQSLQH-ISLLVSEMNTLKKENDRLRDELKTLRE 129
Cdd:COG2433  465 REISRLDReIERLERELEEERERIEELKRKLERLKE 500
 
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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