RBBP8 N-terminal-like protein [Danio rerio]
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
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
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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
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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
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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
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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
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Blast search parameters | ||||
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