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Conserved domains on  [gi|530413909|ref|XP_005258382|]
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DNA endonuclease RBBP8 isoform X2 [Homo sapiens]

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 ...
 20-139 2.41e-62

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: 206.06  E-value: 2.41e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413909   20 FKDLWTKLKECHDREVQGLQVKVTKLKQERILDAQRLEEFFTKNQQLREQQKVLHETIKVLEDRLRAGLCDRCAVTEEHM 99
Cdd:pfam10482   1 FEELLNKLKEIHDKEVQGLQAKVSELKKERCLDAQRLEELFSKNQQLREQQKALQENIKVLENRLRAGLCDRCAVTQELA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 530413909  100 RKKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQ 139
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 ...
 20-139 2.41e-62

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: 206.06  E-value: 2.41e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413909   20 FKDLWTKLKECHDREVQGLQVKVTKLKQERILDAQRLEEFFTKNQQLREQQKVLHETIKVLEDRLRAGLCDRCAVTEEHM 99
Cdd:pfam10482   1 FEELLNKLKEIHDKEVQGLQAKVSELKKERCLDAQRLEELFSKNQQLREQQKALQENIKVLENRLRAGLCDRCAVTQELA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 530413909  100 RKKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQ 139
Cdd:pfam10482  81 KKKQQEFENSQLQSLQHITILTNEMNTLKDENRKLKEELK 120
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
34-152 4.90e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 4.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413909  34 EVQGLQVKVTKLKQERILDAQRLEEFFTKNQQLRE---QQKVLHETIKVLEDRLRAGLCDRCAVTEEHMRKKQQEFENIR 110
Cdd:COG4717  126 QLLPLYQELEALEAELAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530413909 111 QQnlklITELMNERNTLQEENKKLSEQLQQkIENDQQHQAAE 152
Cdd:COG4717  206 QR----LAELEEELEEAQEELEELEEELEQ-LENELEAAALE 242
PRK12704 PRK12704
phosphodiesterase; Provisional
 21-153 6.45e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 6.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413909  21 KDLWTKLKECHDREV----QGLQVKVTKLKQ-ERILDaQRLEEFFTKNQQLREQQKVLHETIKVLEdrlraglcdrcavt 95
Cdd:PRK12704  63 KEEIHKLRNEFEKELrerrNELQKLEKRLLQkEENLD-RKLELLEKREEELEKKEKELEQKQQELE-------------- 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530413909  96 eehmrKKQQEFENIRQQNLKLITELMNerntLQEENKKlsEQLQQKIENDQQHQAAEL 153
Cdd:PRK12704 128 -----KKEEELEELIEEQLQELERISG----LTAEEAK--EILLEKVEEEARHEAAVL 174
 
Name Accession Description Interval E-value
CtIP_N pfam10482
Tumour-suppressor protein CtIP N-terminal domain; CtIP is predominantly a nuclear protein that ...
 20-139 2.41e-62

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: 206.06  E-value: 2.41e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413909   20 FKDLWTKLKECHDREVQGLQVKVTKLKQERILDAQRLEEFFTKNQQLREQQKVLHETIKVLEDRLRAGLCDRCAVTEEHM 99
Cdd:pfam10482   1 FEELLNKLKEIHDKEVQGLQAKVSELKKERCLDAQRLEELFSKNQQLREQQKALQENIKVLENRLRAGLCDRCAVTQELA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 530413909  100 RKKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQ 139
Cdd:pfam10482  81 KKKQQEFENSQLQSLQHITILTNEMNTLKDENRKLKEELK 120
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
34-152 4.90e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 4.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413909  34 EVQGLQVKVTKLKQERILDAQRLEEFFTKNQQLRE---QQKVLHETIKVLEDRLRAGLCDRCAVTEEHMRKKQQEFENIR 110
Cdd:COG4717  126 QLLPLYQELEALEAELAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530413909 111 QQnlklITELMNERNTLQEENKKLSEQLQQkIENDQQHQAAE 152
Cdd:COG4717  206 QR----LAELEEELEEAQEELEELEEELEQ-LENELEAAALE 242
PRK12704 PRK12704
phosphodiesterase; Provisional
 21-153 6.45e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 6.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413909  21 KDLWTKLKECHDREV----QGLQVKVTKLKQ-ERILDaQRLEEFFTKNQQLREQQKVLHETIKVLEdrlraglcdrcavt 95
Cdd:PRK12704  63 KEEIHKLRNEFEKELrerrNELQKLEKRLLQkEENLD-RKLELLEKREEELEKKEKELEQKQQELE-------------- 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530413909  96 eehmrKKQQEFENIRQQNLKLITELMNerntLQEENKKlsEQLQQKIENDQQHQAAEL 153
Cdd:PRK12704 128 -----KKEEELEELIEEQLQELERISG----LTAEEAK--EILLEKVEEEARHEAAVL 174
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
34-154 9.88e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 9.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413909  34 EVQGLQVKVTKLKQERILDAQRLEEFFTKNQQLREQQKVLHETIKVLEDRLRAGLcDRCAVTEEHMRKKQQEFENIRQQn 113
Cdd:COG4372   39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ-AELAQAQEELESLQEEAEELQEE- 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530413909 114 lklITELMNERNTLQEENKKLSEQlQQKIENDQQHQAAELE 154
Cdd:COG4372  117 ---LEELQKERQDLEQQRKQLEAQ-IAELQSEIAEREEELK 153
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
15-157 5.82e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413909  15 DTSSDFKDLWTKLKECHDREVQgLQVKVTKLKQERIL---DAQRLEEFFTKNQQLREQQKvLHETIKVLEDRLRAGLCDR 91
Cdd:COG4717  341 ELLDRIEELQELLREAEELEEE-LQLEELEQEIAALLaeaGVEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGEL 418

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530413909  92 CAVTEEHMRKK-QQEFENIRQQnlklITELMNERNTLQEENKKLSEQLQQkIENDQQHQAAELECEE 157
Cdd:COG4717  419 EELLEALDEEElEEELEELEEE----LEELEEELEELREELAELEAELEQ-LEEDGELAELLQELEE 480
 
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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