NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|41281940|ref|NP_851797|]
View 

BRISC and BRCA1-A complex member 2 isoform IV [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
BRE cd23664
BRCA1-A and BRISC complex subunit BRE; BRCA1-A and BRISC complex subunit BRE (also known as ...
 35-369 0e+00

BRCA1-A and BRISC complex subunit BRE; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. The BRCA1-A complex consists of BRE, Abraxas-1, BRCC36, MERIT40 and RAP80, and specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSB)s. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In BRCA1-A, two heteropentamers, composed of BRCC36, ABRAXAS, BRE and MERIT40, form an arc-shaped complex; the two half-arcs contact each other through BRCC36 and its scaffold partner ABRAXAS. BRCC36 is connected to this arc via the ABRAXAS MPN domain. BRE forms the central bridge between the ABRAXAS-BRCC36 MPN domain dimer and MERIT40. BRE's N-terminal ubiquitin-conjugating enzyme variants domain (UEV-N) binds the ABRAXAS MPN, and BRE's C-terminal UEV domain (UEV-C) holds MERIT40 at the extremity of the arc. Loss of BRE significantly impairs BRCA1-A function, resulting in DNA repair defects and loss of cancer suppression. The BRISC complex consists of BRE, BRCC36, MERIT40 and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. The BRISC core has the same 2-fold symmetrical arc shape and is structurally similar to BRCA1-A; however, the conformation of BRE UEV-C and MERIT40 differs markedly. BRE has different functionality in the BRCA1-A and BRISC complexes: in BRCA1, it is involved in RAP80 integration, BRCA1 sequestration and ubiquitin binding, while in BRISC, it is involved in dimerization, SHMT2 recruitment, DUB inhibition and ubiquitin binding. A BRISC complex (containing of BRE/BRCC45, BRCC36, MERIT40, and Abraxas 2/KIAA0157) has been found in insects (Camponotus floridanus) and shown to efficiently degrade 'Lys-63'-linked chains. Homologs of genes encoding components of BRCA1-A and BRISC complexes have been found in plant genomes, including for BRE/BRCC45; plant homologs of BRCC36 have been shown to be involved in DNA repair; BRCC36-Abraxas 2 complexes have been found in Arabidopsis.


:

Pssm-ID: 467821  Cd Length: 364  Bit Score: 583.38  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940  35 CTSLTPGPNCDRFKLHIPYAGETLKWDIIFNAQYPELPPDFIFG-EDAEFLPDPSALHNLASWNPSNPECLLLVVKELVQ 113
Cdd:cd23664  34 CPSLTKGPNCDRFKLVIPYAGQSLTWEVIFDASYPELPPDFIFGdDDRDFVPDIEDIKSLVNWDPSNPDSLLLVVKELLE 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 114 QYHQFQCGRLRESSRLMFEYQTLLEEPQYGENMEIYAGKKNNWtGEFSARFLLKLPVDFSNIPTYLLKDvneDPGEDVAL 193
Cdd:cd23664 114 QYKEYQISLLESYSRLQFEYSSLLEQNFSEDDIEVYVNRKNNW-GEGPVNFLIKLPVDFSNIPPYLTKD---NPGEDSAL 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 194 LSVSFEDTEATQVYPKLYLSPRIEHALGGSSALHIPAFPGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRREYIAAFLSHF 273
Cdd:cd23664 190 LLVSFPDPEGSRVTPQLYLSPRVEHALGGSSSLRIPAFPSGGCLMDYVPAVCELLKNKVELVVQGYEKRKEYIAAFLSHF 269

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 274 GTGVVEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPRDQPTLTFQSVYHFTNsGQLYSQAQKNYPYSPRWDGNEMAKRA 353
Cdd:cd23664 270 GRSVLEYDAESFSKISLLLEWNDFFFILHIELPLYFPQDQPTFTFQSIYHESN-GKPYSETVKDYPYSPRWSGNEMAERA 348

                       330
                ....*....|....*.
gi 41281940 354 KAYFKTFVPQFQEAAF 369
Cdd:cd23664 349 RAFILEYIPQFQEASV 364
 
Name Accession Description Interval E-value
BRE cd23664
BRCA1-A and BRISC complex subunit BRE; BRCA1-A and BRISC complex subunit BRE (also known as ...
 35-369 0e+00

BRCA1-A and BRISC complex subunit BRE; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. The BRCA1-A complex consists of BRE, Abraxas-1, BRCC36, MERIT40 and RAP80, and specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSB)s. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In BRCA1-A, two heteropentamers, composed of BRCC36, ABRAXAS, BRE and MERIT40, form an arc-shaped complex; the two half-arcs contact each other through BRCC36 and its scaffold partner ABRAXAS. BRCC36 is connected to this arc via the ABRAXAS MPN domain. BRE forms the central bridge between the ABRAXAS-BRCC36 MPN domain dimer and MERIT40. BRE's N-terminal ubiquitin-conjugating enzyme variants domain (UEV-N) binds the ABRAXAS MPN, and BRE's C-terminal UEV domain (UEV-C) holds MERIT40 at the extremity of the arc. Loss of BRE significantly impairs BRCA1-A function, resulting in DNA repair defects and loss of cancer suppression. The BRISC complex consists of BRE, BRCC36, MERIT40 and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. The BRISC core has the same 2-fold symmetrical arc shape and is structurally similar to BRCA1-A; however, the conformation of BRE UEV-C and MERIT40 differs markedly. BRE has different functionality in the BRCA1-A and BRISC complexes: in BRCA1, it is involved in RAP80 integration, BRCA1 sequestration and ubiquitin binding, while in BRISC, it is involved in dimerization, SHMT2 recruitment, DUB inhibition and ubiquitin binding. A BRISC complex (containing of BRE/BRCC45, BRCC36, MERIT40, and Abraxas 2/KIAA0157) has been found in insects (Camponotus floridanus) and shown to efficiently degrade 'Lys-63'-linked chains. Homologs of genes encoding components of BRCA1-A and BRISC complexes have been found in plant genomes, including for BRE/BRCC45; plant homologs of BRCC36 have been shown to be involved in DNA repair; BRCC36-Abraxas 2 complexes have been found in Arabidopsis.


Pssm-ID: 467821  Cd Length: 364  Bit Score: 583.38  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940  35 CTSLTPGPNCDRFKLHIPYAGETLKWDIIFNAQYPELPPDFIFG-EDAEFLPDPSALHNLASWNPSNPECLLLVVKELVQ 113
Cdd:cd23664  34 CPSLTKGPNCDRFKLVIPYAGQSLTWEVIFDASYPELPPDFIFGdDDRDFVPDIEDIKSLVNWDPSNPDSLLLVVKELLE 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 114 QYHQFQCGRLRESSRLMFEYQTLLEEPQYGENMEIYAGKKNNWtGEFSARFLLKLPVDFSNIPTYLLKDvneDPGEDVAL 193
Cdd:cd23664 114 QYKEYQISLLESYSRLQFEYSSLLEQNFSEDDIEVYVNRKNNW-GEGPVNFLIKLPVDFSNIPPYLTKD---NPGEDSAL 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 194 LSVSFEDTEATQVYPKLYLSPRIEHALGGSSALHIPAFPGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRREYIAAFLSHF 273
Cdd:cd23664 190 LLVSFPDPEGSRVTPQLYLSPRVEHALGGSSSLRIPAFPSGGCLMDYVPAVCELLKNKVELVVQGYEKRKEYIAAFLSHF 269

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 274 GTGVVEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPRDQPTLTFQSVYHFTNsGQLYSQAQKNYPYSPRWDGNEMAKRA 353
Cdd:cd23664 270 GRSVLEYDAESFSKISLLLEWNDFFFILHIELPLYFPQDQPTFTFQSIYHESN-GKPYSETVKDYPYSPRWSGNEMAERA 348

                       330
                ....*....|....*.
gi 41281940 354 KAYFKTFVPQFQEAAF 369
Cdd:cd23664 349 RAFILEYIPQFQEASV 364
BRE pfam06113
Brain and reproductive organ-expressed protein (BRE); This family consists of several ...
 32-324 6.14e-161

Brain and reproductive organ-expressed protein (BRE); This family consists of several eukaryotic brain and reproductive organ-expressed (BRE) proteins. BRE is a putative stress-modulating gene, found able to down-regulate TNF-alpha-induced-NF-kappaB activation upon over expression. A total of six isoforms are produced by alternative splicing predominantly at either end of the gene.Compared to normal cells, immortalized human cell lines uniformly express higher levels of BRE. Peripheral blood monocytes respond to LPS by down-regulating the expression of all the BRE isoforms.It is thought that the function of BRE and its isoforms is to regulate peroxisomal activities.


Pssm-ID: 461832  Cd Length: 320  Bit Score: 453.82  E-value: 6.14e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940    32 GQNCTSltpgPNCDRFKLHIPYAGETLKWDIIFNAQYPELPPDFIF-GEDAEFLPDPSALH----NLASWNPSNPECLLL 106
Cdd:pfam06113  33 KSGCNK----PKNDRFKLHIPYAGEHLKWDVIFDSQYPEMPPDFIFnDESFLFDPDIDILStwvpSLTKWDPNNPEALLL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940   107 VVKELVQQYHQFQCGRL-RESSRLMFEYQTLLEEPQYG-ENMEIYAGKKNnwtgeFSARFLLKLPVDFSNIPTYLLKDvn 184
Cdd:pfam06113 109 VLSELLLYYKEHQIRLLgKEGSRLQFEYSTLVGETEIGeEDIEVILGGKP-----FEARFLIRLPVDYSRLPPYLNKD-- 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940   185 eDPGEDVALLSVSFEDTEATQVYPKLYLSPRIEHALGGSSALHIPAFPGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRRE 264
Cdd:pfam06113 182 -DPGEDEALLLVTFYGPEWNRVIPQLYLSPTLEHALGGPEALHIPPFPPGGCLMDYVPQVKKFLENKINHVVQGYEKRRE 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940   265 YIAAFLSHFGTGVVEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPRDQPTLTFQSVYHF 324
Cdd:pfam06113 261 YIAALIVHFGGSILEYDAEEFTKLTLLLEWNDFHFLLHIDLPSFFPKDKPQLTLQSVYHM 320
 
Name Accession Description Interval E-value
BRE cd23664
BRCA1-A and BRISC complex subunit BRE; BRCA1-A and BRISC complex subunit BRE (also known as ...
 35-369 0e+00

BRCA1-A and BRISC complex subunit BRE; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. The BRCA1-A complex consists of BRE, Abraxas-1, BRCC36, MERIT40 and RAP80, and specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSB)s. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In BRCA1-A, two heteropentamers, composed of BRCC36, ABRAXAS, BRE and MERIT40, form an arc-shaped complex; the two half-arcs contact each other through BRCC36 and its scaffold partner ABRAXAS. BRCC36 is connected to this arc via the ABRAXAS MPN domain. BRE forms the central bridge between the ABRAXAS-BRCC36 MPN domain dimer and MERIT40. BRE's N-terminal ubiquitin-conjugating enzyme variants domain (UEV-N) binds the ABRAXAS MPN, and BRE's C-terminal UEV domain (UEV-C) holds MERIT40 at the extremity of the arc. Loss of BRE significantly impairs BRCA1-A function, resulting in DNA repair defects and loss of cancer suppression. The BRISC complex consists of BRE, BRCC36, MERIT40 and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. The BRISC core has the same 2-fold symmetrical arc shape and is structurally similar to BRCA1-A; however, the conformation of BRE UEV-C and MERIT40 differs markedly. BRE has different functionality in the BRCA1-A and BRISC complexes: in BRCA1, it is involved in RAP80 integration, BRCA1 sequestration and ubiquitin binding, while in BRISC, it is involved in dimerization, SHMT2 recruitment, DUB inhibition and ubiquitin binding. A BRISC complex (containing of BRE/BRCC45, BRCC36, MERIT40, and Abraxas 2/KIAA0157) has been found in insects (Camponotus floridanus) and shown to efficiently degrade 'Lys-63'-linked chains. Homologs of genes encoding components of BRCA1-A and BRISC complexes have been found in plant genomes, including for BRE/BRCC45; plant homologs of BRCC36 have been shown to be involved in DNA repair; BRCC36-Abraxas 2 complexes have been found in Arabidopsis.


Pssm-ID: 467821  Cd Length: 364  Bit Score: 583.38  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940  35 CTSLTPGPNCDRFKLHIPYAGETLKWDIIFNAQYPELPPDFIFG-EDAEFLPDPSALHNLASWNPSNPECLLLVVKELVQ 113
Cdd:cd23664  34 CPSLTKGPNCDRFKLVIPYAGQSLTWEVIFDASYPELPPDFIFGdDDRDFVPDIEDIKSLVNWDPSNPDSLLLVVKELLE 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 114 QYHQFQCGRLRESSRLMFEYQTLLEEPQYGENMEIYAGKKNNWtGEFSARFLLKLPVDFSNIPTYLLKDvneDPGEDVAL 193
Cdd:cd23664 114 QYKEYQISLLESYSRLQFEYSSLLEQNFSEDDIEVYVNRKNNW-GEGPVNFLIKLPVDFSNIPPYLTKD---NPGEDSAL 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 194 LSVSFEDTEATQVYPKLYLSPRIEHALGGSSALHIPAFPGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRREYIAAFLSHF 273
Cdd:cd23664 190 LLVSFPDPEGSRVTPQLYLSPRVEHALGGSSSLRIPAFPSGGCLMDYVPAVCELLKNKVELVVQGYEKRKEYIAAFLSHF 269

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 274 GTGVVEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPRDQPTLTFQSVYHFTNsGQLYSQAQKNYPYSPRWDGNEMAKRA 353
Cdd:cd23664 270 GRSVLEYDAESFSKISLLLEWNDFFFILHIELPLYFPQDQPTFTFQSIYHESN-GKPYSETVKDYPYSPRWSGNEMAERA 348

                       330
                ....*....|....*.
gi 41281940 354 KAYFKTFVPQFQEAAF 369
Cdd:cd23664 349 RAFILEYIPQFQEASV 364
BRE pfam06113
Brain and reproductive organ-expressed protein (BRE); This family consists of several ...
 32-324 6.14e-161

Brain and reproductive organ-expressed protein (BRE); This family consists of several eukaryotic brain and reproductive organ-expressed (BRE) proteins. BRE is a putative stress-modulating gene, found able to down-regulate TNF-alpha-induced-NF-kappaB activation upon over expression. A total of six isoforms are produced by alternative splicing predominantly at either end of the gene.Compared to normal cells, immortalized human cell lines uniformly express higher levels of BRE. Peripheral blood monocytes respond to LPS by down-regulating the expression of all the BRE isoforms.It is thought that the function of BRE and its isoforms is to regulate peroxisomal activities.


Pssm-ID: 461832  Cd Length: 320  Bit Score: 453.82  E-value: 6.14e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940    32 GQNCTSltpgPNCDRFKLHIPYAGETLKWDIIFNAQYPELPPDFIF-GEDAEFLPDPSALH----NLASWNPSNPECLLL 106
Cdd:pfam06113  33 KSGCNK----PKNDRFKLHIPYAGEHLKWDVIFDSQYPEMPPDFIFnDESFLFDPDIDILStwvpSLTKWDPNNPEALLL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940   107 VVKELVQQYHQFQCGRL-RESSRLMFEYQTLLEEPQYG-ENMEIYAGKKNnwtgeFSARFLLKLPVDFSNIPTYLLKDvn 184
Cdd:pfam06113 109 VLSELLLYYKEHQIRLLgKEGSRLQFEYSTLVGETEIGeEDIEVILGGKP-----FEARFLIRLPVDYSRLPPYLNKD-- 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940   185 eDPGEDVALLSVSFEDTEATQVYPKLYLSPRIEHALGGSSALHIPAFPGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRRE 264
Cdd:pfam06113 182 -DPGEDEALLLVTFYGPEWNRVIPQLYLSPTLEHALGGPEALHIPPFPPGGCLMDYVPQVKKFLENKINHVVQGYEKRRE 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940   265 YIAAFLSHFGTGVVEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPRDQPTLTFQSVYHF 324
Cdd:pfam06113 261 YIAALIVHFGGSILEYDAEEFTKLTLLLEWNDFHFLLHIDLPSFFPKDKPQLTLQSVYHM 320
BRE-like cd23520
BRCA1-A and BRISC complex subunit BRE and related proteins; BRCA1-A and BRISC complex subunit ...
 34-368 6.67e-158

BRCA1-A and BRISC complex subunit BRE and related proteins; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. The BRCA1-A complex consists of BRE, Abraxas-1, BRCC36, MERIT40 and RAP80, and specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSB)s. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In BRCA1-A, two heteropentamers, composed of BRCC36, ABRAXAS, BRE and MERIT40, form an arc-shaped complex; the two half-arcs contact each other through BRCC36 and its scaffold partner ABRAXAS. BRCC36 is connected to this arc via the ABRAXAS MPN domain. BRE forms the central bridge between the ABRAXAS-BRCC36 MPN domain dimer and MERIT40. BRE's N-terminal ubiquitin-conjugating enzyme variants domain (UEV-N) binds the ABRAXAS MPN, and BRE's C-terminal UEV domain (UEV-C) holds MERIT40 at the extremity of the arc. Loss of BRE significantly impairs BRCA1-A function, resulting in DNA repair defects and loss of cancer suppression. The BRISC complex consists of BRE, BRCC36, MERIT40 and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. The BRISC core has the same 2-fold symmetrical arc shape and is structurally similar to BRCA1-A; however, the conformation of BRE UEV-C and MERIT40 differs markedly. BRE has different functionality in the BRCA1-A and BRISC complexes: in BRCA1, it is involved in RAP80 integration, BRCA1 sequestration and ubiquitin binding, while in BRISC, it is involved in dimerization, SHMT2 recruitment, DUB inhibition and ubiquitin binding. A BRISC complex (consisting of BRE/BRCC45, BRCC36, MERIT40 and Abraxas 2/KIAA0157) has been found in insects (Camponotus floridanus) and shown to efficiently degrade 'Lys-63'-linked chains. Homologs of genes encoding components of BRCA1-A and BRISC complexes have been found in plant genomes, including for BRE/BRCC45; plant homologs of BRCC36 have been shown to be involved in DNA repair; BRCC36-Abraxas 2 complexes have been found in Arabidopsis.


Pssm-ID: 467820  Cd Length: 352  Bit Score: 447.28  E-value: 6.67e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940  34 NCTSLTPGPNCDRFKLHIPYAGETLKWDIIFNAQYPELPPDFIFGEDaEFLPDPSALHNLASWNPSNPECLLLVVKELVQ 113
Cdd:cd23520  30 GCGQLEGTPKADRFKLSIPYAGESVDWDIIFNSQDPELPPDFIFHDD-FFLPDLTALTSLASWDPSDPNSLLKVLKELIS 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 114 QYHQFQCGRLRE-SSRLMFEYQTLLEEPqYGENMEIYAGKKNNwtgeFSARFLLKLPVDFSNIPTYllkdvneDPGEDVA 192
Cdd:cd23520 109 MYQQHQRRRLERqNERIRFEYETLLAEP-YGEEMDISASVKND----LSEKVEFAIPVDFDNQPQG-------VNQDIVL 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 193 LLSVSFEDTEATQVYPKLYL--SPRIEHALGgSSALHIPAFPGGgCLIDYVPQVCHLLTNKVQYVIQGYHKRREYIAAFL 270
Cdd:cd23520 177 LLQVQFLLSSADVRAPKLTLepSPSLFDALG-KLRLVPPETPHE-CLMEYVPRVKEHITEKVDKEIRSREKRREFIEALL 254

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 271 SHFGTGVVEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPRDQPTLTFQSVYHFTNSGQLYSQAQKNYPYSPRWDGNEMA 350
Cdd:cd23520 255 SLFGDSLLEYDMENFRFISLLLKHEDFYFLVHIYLPLSFPKKQPTLTFQSVYHMTSSGKLYSREERNVPFSPRWEAERMA 334

                       330
                ....*....|....*...
gi 41281940 351 KRAKAYFKTFVPQFQEAA 368
Cdd:cd23520 335 VEIAEFIYDEVPKFLTKA 352
BRE-like_insects cd23665
BRCA1-A and BRISC complex subunit BRE-like protein found in insects; BRCA1-A and BRISC complex ...
 45-366 4.96e-108

BRCA1-A and BRISC complex subunit BRE-like protein found in insects; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. The BRCA1-A complex consists of BRE, Abraxas-1, BRCC36, MERIT40 and RAP80, and specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSB)s. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In BRCA1-A, two heteropentamers, composed of BRCC36, ABRAXAS, BRE and MERIT40, form an arc-shaped complex; the two half-arcs contact each other through BRCC36 and its scaffold partner ABRAXAS. BRCC36 is connected to this arc via the ABRAXAS MPN domain. BRE forms the central bridge between the ABRAXAS-BRCC36 MPN domain dimer and MERIT40. BRE's N-terminal ubiquitin-conjugating enzyme variants domain (UEV-N) binds the ABRAXAS MPN, and BRE's C-terminal UEV domain (UEV-C) holds MERIT40 at the extremity of the arc. Loss of BRE significantly impairs BRCA1-A function, resulting in DNA repair defects and loss of cancer suppression. The BRISC complex consists of BRE, BRCC36, MERIT40 and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. The BRISC core has the same 2-fold symmetrical arc shape and is structurally similar to BRCA1-A; however, the conformation of BRE UEV-C and MERIT40 differs markedly. BRE has different functionality in the BRCA1-A and BRISC complexes: in BRCA1, it is involved in RAP80 integration, BRCA1 sequestration and ubiquitin binding; in BRISC, it is involved in dimerization, SHMT2 recruitment, DUB inhibition and ubiquitin binding. A BRISC complex (containing of BRE/BRCC45, BRCC36, MERIT40, and Abraxas 2/KIAA0157) has been found in insects (Camponotus floridanus) and shown to efficiently degrade 'Lys-63'-linked chains. This model contains the BRE domain of BRISC complexes found in insects.


Pssm-ID: 467822  Cd Length: 364  Bit Score: 321.07  E-value: 4.96e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940  45 DRFKLHIPYAGETLKWDIIFNAQYPELPPDFIFGeDAEFLPDPSA------LHNLASWNPSNPECLLLVVKELVQQY--H 116
Cdd:cd23665  36 DRFKLSIPYAGKNLNWEVIFDSEDPEFGPDFIFN-DDTFLADPDIdtisknVPSLAKWNPNDPKALLNVLNELLVLYkkH 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 117 QFQCGRLRESSRLMFEYQTLLEEPQYG-ENMEIYAGkkNNWTGEFSARFLLKLPVDFSNIPTYLLKDVNEDPGEDVALLS 195
Cdd:cd23665 115 QIEKLQKQNYSRLQLEYSMLLTETEITpEDVEVILL--PNGSKPTEARFLIRLSVDFSQLPEYIQPIILLNPGNDTAMLL 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 196 VSFEDTEATQVYPKLYLSPRIEHALGGSSALHIPAFPGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRREYIAAFLSHFGT 275
Cdd:cd23665 193 VTFSGPDWNRITPSLQLSPRLEEILGGSTTLHLPPFPKDKTLMEYVPEVKKLIEEKINSIAQHFKKKKEFISALLSLQRG 272

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 276 GVVEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPRDQPTLTFQSVYHFTnSGQLYSQAQKNYPYSPRWDGNEMAKRAKA 355
Cdd:cd23665 273 SIIEYDSINFSKITFLLEVDDFHCLVHITLPPKFPQEKPKVTLQSIYHMT-SKKPYSEELDDYPYSPRWEPEMMVKKLLH 351

                       330
                ....*....|.
gi 41281940 356 YFKTFVPQFQE 366
Cdd:cd23665 352 ILEEAVPKFKN 362
BRE-like_plant cd23666
BRCA1-A and BRISC complex subunit BRE-like protein found in plants; BRCA1-A and BRISC complex ...
 45-360 4.50e-51

BRCA1-A and BRISC complex subunit BRE-like protein found in plants; BRCA1-A and BRISC complex subunit BRE (also known as BRISC and BRCA1 A complex member 2; BRCC4; BRCC45) is a core component of both the BRCA1-A and BRISC complexes. BRCA1-A and BRISC are separate complexes with diverging function; they use the same core of subunits to perform very distinct biological tasks, and are found in all vertebrates. The BRCA1-A complex consists of BRE, Abraxas-1, BRCC36, MERIT40, and RAP80 and specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSB)s. This complex also possesses deubiquitinase (DUB) activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In BRCA1-A, two heteropentamers composed of BRCC36, ABRAXAS, BRE, and MERIT40 form an arc-shaped complex; the two half-arcs contact each other through BRCC36 and its scaffold partner ABRAXAS. BRCC36 is connected to this arc via the ABRAXAS MPN domain. BRE forms the central bridge between the ABRAXAS-BRCC36 MPN domain dimer and MERIT40. BRE's N-terminal ubiquitin-conjugating enzyme variants domain (UEV-N) binds the ABRAXAS MPN, and BRE's C-terminal UEV domain (UEV-C) holds MERIT40 at the extremity of the arc. Loss of BRE significantly impairs BRCA1-A function, resulting in DNA repair defects and loss of cancer suppression. The BRISC complex consists of BRE, BRCC36, MERIT40, and Abraxas 2, and serves cellular stress response and immune signaling functions; it specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. The BRISC core has the same 2-fold symmetrical arc shape and is structurally similar to BRCA1-A, however the conformation of BRE UEV-C and MERIT40 differs markedly. BRE has different functionality in the BRCA1-A and BRISC complexes: in BRCA1 it is involved in RAP80 integration, BRCA1 sequestration, and ubiquitin binding; in BRISC it is involved in dimerization, SHMT2 recruitment, DUB inhibition, and ubiquitin binding. Homologs of genes encoding components of BRCA1-A and BRISC complexes have been found in plant genomes, including for BRE/BRCC45; plant homologs of BRCC36 have been shown to be involved in DNA repair, and BRCC36-Abraxas 2 complexes have been found in Arabidopsis. This model contains the BRE domain of BRISC complexes found in plants.


Pssm-ID: 467823  Cd Length: 370  Bit Score: 174.47  E-value: 4.50e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940  45 DRFKLHIPYAGETLKWDIIFNAQYPELPPDFIFG-EDAEFLP------DP----SALHNLASWNPSNPECLLLVVKELVQ 113
Cdd:cd23666  36 DRFTLLIPCCLEYIKWDVIYNAQYPTVPPDVVFGaDDEDFQPllfmpeGPagkvSLWGILRDWNVKDPSRLLRLLLELRN 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 114 QYHQFQCGRLRE--SSRLMFEYQTLLeePQYGENMEIYAGkknnwtGEFSARFLLKLP-VDFSNIPTYLLKDVNEDPGED 190
Cdd:cd23666 116 LYLQYQRKRVEEldDDRVKFEISTIL--AREGLEMCLVTG------PDRPEEVKFAIPlVDVDLSNKLVLGCSPWKPQQK 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 191 VaLLSVSFEDTEATQVYP-----KLYLSPRIEHALGgSSALHIPAFPGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRREY 265
Cdd:cd23666 188 I-YLQVKFPVQRGQTSLPsapqlKLVAPPALREVFD-VEDVKLPAWTDGMCLAEYLPNLEEQLKAQVVEAVASVGLRRRF 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281940 266 IAAFLSHFGTGVvEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPRDQPTLTFQSVYHFTNSGQ-LYSQAQKNYPYSPRW 344
Cdd:cd23666 266 IEALPPVFGRPL-EADTVYCRRASILASSGVFTFLVHFSLPTQFPKQQPTLTLQSSQHFDSQGVpIVSRLYDDYPWSPRW 344

                       330       340
                ....*....|....*....|...
gi 41281940 345 DGNEMAKR-------AKAYFKTF 360
Cdd:cd23666 345 EPSEMVERifefiaeEALAFKKY 367
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH