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Conserved domains on  [gi|1117368316|ref|XP_019376141|]
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PREDICTED: microcephalin isoform X1 [Gavialis gangeticus]

Protein Classification

BRCT domain-containing protein( domain architecture ID 13026389)

BRCT (BRCA1 C-terminus) domain-containing protein may interact with DNA, and participate in DNA-damage checkpoint or DNA-repair pathways; similar to vertebrate microcephalin implicated in chromosome condensation and DNA damage induced cellular responses

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 664-739 1.44e-38

second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the second repeat.


:

Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 137.72  E-value: 1.44e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1117368316 664 RTLVMTSMSSEKQNTVIQVVNKLGGFSFSNDVCETTSHVVAGSPRRTLNVMLGIARGCWIVCYEWVLWSLEFGCWI 739
Cdd:cd17736     1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
 7-85 1.59e-34

first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the first repeat.


:

Pssm-ID: 349348 [Multi-domain]  Cd Length: 78  Bit Score: 126.15  E-value: 1.59e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1117368316   7 GVSAYVEVWSANRtENYSKTFAQQLQDMGAQVSKTFNKHVTHVIFKEGHLATWRKAQQTGVKLVSILWVEKCRETGVRV 85
Cdd:cd17716     1 GVVAYVDVRSGDG-ADRSSAFRSILEELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEACKETGKRV 78
BRCT_microcephalin_rpt3 cd17751
third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 765-841 3.46e-30

third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the third repeat.


:

Pssm-ID: 349382  Cd Length: 75  Bit Score: 113.87  E-value: 3.46e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1117368316 765 EKYQQNLFKNQPVMFISLTSQPPCDKLSELVRLCGGKVCKTLRQAKICIGEYlgKQQPEIKYLSEKWILDSVTQHKI 841
Cdd:cd17751     1 SRYRQNLFADGGPIYVSSNSVPPKDKLEELVLLCGGKVVKSSRKADICIGKT--PPNPDKPSVSEKWLLDSITNHKL 75
Microcephalin super family cl13665
Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family ...
 222-614 2.00e-23

Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 384 and 835 amino acids in length. Microcephalin is involved in determining the size of the brain in animals. It is a protein, which if expressed homozygously causes the organizm to have the condition microcephaly. organizms expressing the mutated form of this protein in a homozygous manner develop a condition called microcephaly - a drastically reduced brain mass and volume. Microcephalin is predicted to contain three BRCA1 C-terminal domains, the first of which is the probable microcephaly mutation site.


The actual alignment was detected with superfamily member pfam12258:

Pssm-ID: 463511 [Multi-domain]  Cd Length: 390  Bit Score: 103.26  E-value: 2.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 222 EQINDSLNSSFDDLWGNCKLKRQKIESLECINAAQSDIYVSTPALEDSSFCS----NDRENLTPKQCnRKQLNKKLI-LQ 296
Cdd:pfam12258   1 ESFAGGLHSSFDDLCGNSECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSsassGCLSQLTPQKS-KSNLSKEEInWQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 297 HSLGGDL--SEKGESETSPNKKQDYDDNLT-SLSIATNISFLQEKDLSHSASSQRtvqleaaagtkdshsdllvsskdfn 373
Cdd:pfam12258  80 RDAVGEVvtPDRKQAEGVSKGMFDEKDSLSpALSATKGHPLGHSRPKSSSAKRKR------------------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 374 mCSVDVSVPvdlrdcavghkTKGKSKRKRSSTKLTT--SVLCKSGaenEFLEAMTTRNKISHA-EKGSYEDFFSSSDLNK 450
Cdd:pfam12258 135 -TSEDLNSP-----------PKEKLKKKRSSRKSAMprLQLFKSE---NSLQLMTRPAVETPDcEESSYDDYFSPDNLKE 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 451 seiQESHFVLGVQQKSSCSPEVTYKTGSSRRESN--EQC--SALSKKKRKTVQTNGTlLKSDCKLSELLESTKSVTLNCM 526
Cdd:pfam12258 200 ---RNSENLPPGSQPLSSPAQLSCRSLSKRERKSilEMSdfSCIGKKPRSVDITDLT-AKTSSSLQKPTNDEGNTTLSCL 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 527 VDGKNAQTAEDLVSSslNQLHQNTRENNCRTNVNCSPFPSGATLQD-----------DNTAMMVSLSLKSENKGTAEPK- 594
Cdd:pfam12258 276 TSEGTPAAEETPGCC--RQAGPQKREDAGPEGNSHSHTTDEPALPSghhgdltplkgSSEEMRESVDVKSTQKEGATSKt 353

                         410       420       430
                  ....*....|....*....|....*....|
gi 1117368316 595 ----------EHPLIFPDSASMEKSTDDKK 614
Cdd:pfam12258 354 lnssegeaqsDYKLNFVGDCNVEKSTEEKE 383
 
Name Accession Description Interval E-value
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 664-739 1.44e-38

second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the second repeat.


Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 137.72  E-value: 1.44e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1117368316 664 RTLVMTSMSSEKQNTVIQVVNKLGGFSFSNDVCETTSHVVAGSPRRTLNVMLGIARGCWIVCYEWVLWSLEFGCWI 739
Cdd:cd17736     1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
 7-85 1.59e-34

first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the first repeat.


Pssm-ID: 349348 [Multi-domain]  Cd Length: 78  Bit Score: 126.15  E-value: 1.59e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1117368316   7 GVSAYVEVWSANRtENYSKTFAQQLQDMGAQVSKTFNKHVTHVIFKEGHLATWRKAQQTGVKLVSILWVEKCRETGVRV 85
Cdd:cd17716     1 GVVAYVDVRSGDG-ADRSSAFRSILEELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEACKETGKRV 78
BRCT_microcephalin_rpt3 cd17751
third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 765-841 3.46e-30

third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the third repeat.


Pssm-ID: 349382  Cd Length: 75  Bit Score: 113.87  E-value: 3.46e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1117368316 765 EKYQQNLFKNQPVMFISLTSQPPCDKLSELVRLCGGKVCKTLRQAKICIGEYlgKQQPEIKYLSEKWILDSVTQHKI 841
Cdd:cd17751     1 SRYRQNLFADGGPIYVSSNSVPPKDKLEELVLLCGGKVVKSSRKADICIGKT--PPNPDKPSVSEKWLLDSITNHKL 75
Microcephalin pfam12258
Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family ...
 222-614 2.00e-23

Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 384 and 835 amino acids in length. Microcephalin is involved in determining the size of the brain in animals. It is a protein, which if expressed homozygously causes the organizm to have the condition microcephaly. organizms expressing the mutated form of this protein in a homozygous manner develop a condition called microcephaly - a drastically reduced brain mass and volume. Microcephalin is predicted to contain three BRCA1 C-terminal domains, the first of which is the probable microcephaly mutation site.


Pssm-ID: 463511 [Multi-domain]  Cd Length: 390  Bit Score: 103.26  E-value: 2.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 222 EQINDSLNSSFDDLWGNCKLKRQKIESLECINAAQSDIYVSTPALEDSSFCS----NDRENLTPKQCnRKQLNKKLI-LQ 296
Cdd:pfam12258   1 ESFAGGLHSSFDDLCGNSECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSsassGCLSQLTPQKS-KSNLSKEEInWQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 297 HSLGGDL--SEKGESETSPNKKQDYDDNLT-SLSIATNISFLQEKDLSHSASSQRtvqleaaagtkdshsdllvsskdfn 373
Cdd:pfam12258  80 RDAVGEVvtPDRKQAEGVSKGMFDEKDSLSpALSATKGHPLGHSRPKSSSAKRKR------------------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 374 mCSVDVSVPvdlrdcavghkTKGKSKRKRSSTKLTT--SVLCKSGaenEFLEAMTTRNKISHA-EKGSYEDFFSSSDLNK 450
Cdd:pfam12258 135 -TSEDLNSP-----------PKEKLKKKRSSRKSAMprLQLFKSE---NSLQLMTRPAVETPDcEESSYDDYFSPDNLKE 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 451 seiQESHFVLGVQQKSSCSPEVTYKTGSSRRESN--EQC--SALSKKKRKTVQTNGTlLKSDCKLSELLESTKSVTLNCM 526
Cdd:pfam12258 200 ---RNSENLPPGSQPLSSPAQLSCRSLSKRERKSilEMSdfSCIGKKPRSVDITDLT-AKTSSSLQKPTNDEGNTTLSCL 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 527 VDGKNAQTAEDLVSSslNQLHQNTRENNCRTNVNCSPFPSGATLQD-----------DNTAMMVSLSLKSENKGTAEPK- 594
Cdd:pfam12258 276 TSEGTPAAEETPGCC--RQAGPQKREDAGPEGNSHSHTTDEPALPSghhgdltplkgSSEEMRESVDVKSTQKEGATSKt 353

                         410       420       430
                  ....*....|....*....|....*....|
gi 1117368316 595 ----------EHPLIFPDSASMEKSTDDKK 614
Cdd:pfam12258 354 lnssegeaqsDYKLNFVGDCNVEKSTEEKE 383
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
 12-74 6.45e-14

twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.


Pssm-ID: 463687 [Multi-domain]  Cd Length: 63  Bit Score: 66.84  E-value: 6.45e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1117368316  12 VEVWSANRTENYSKTFAQQLQDMGAQVSKTFNKHVTHVIFKEGHLATWRKAQQTGVKLVSILW 74
Cdd:pfam12738   1 LVICVTGFDGDDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 768-847 3.75e-09

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 54.29  E-value: 3.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 768 QQNLFKNqpvM--FISLTSQPPCDKLSELVRLCGGKVCKTLRQAK-ICIGEYL----GKQQPEIKYLSEKWILDSVTQHK 840
Cdd:pfam16589   1 LPNLFEP---LrfYINAIPSPSRSKLKRLIEANGGTVVDNINPAVyIVIAPYNktdkLAENTKLGVVSPQWIFDCVKKGK 77


                  ....*..
gi 1117368316 841 ICPLENY 847
Cdd:pfam16589  78 LLPLENY 84
BRCT smart00292
breast cancer carboxy-terminal domain;
670-730 1.35e-04

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 41.21  E-value: 1.35e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1117368316  670 SMSSEKQNTVIQVVNKLGGfSFSNDVCE-TTSHVVAGSP-RRTLNVMLGIARGCWIVCYEWVL 730
Cdd:smart00292  14 SFDKEERDELKELIEALGG-KVTSSLSSkTTTHVIVGSPeGGKLELLKAIALGIPIVKEEWLL 75
 
Name Accession Description Interval E-value
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 664-739 1.44e-38

second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the second repeat.


Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 137.72  E-value: 1.44e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1117368316 664 RTLVMTSMSSEKQNTVIQVVNKLGGFSFSNDVCETTSHVVAGSPRRTLNVMLGIARGCWIVCYEWVLWSLEFGCWI 739
Cdd:cd17736     1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
BRCT_microcephalin_rpt1 cd17716
first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ...
 7-85 1.59e-34

first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the first repeat.


Pssm-ID: 349348 [Multi-domain]  Cd Length: 78  Bit Score: 126.15  E-value: 1.59e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1117368316   7 GVSAYVEVWSANRtENYSKTFAQQLQDMGAQVSKTFNKHVTHVIFKEGHLATWRKAQQTGVKLVSILWVEKCRETGVRV 85
Cdd:cd17716     1 GVVAYVDVRSGDG-ADRSSAFRSILEELGAKVVKRLTKTVTHVVFKDGSQSTLEKAKKRNVKLVSPLWVEACKETGKRV 78
BRCT_microcephalin_rpt3 cd17751
third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 765-841 3.46e-30

third BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the third repeat.


Pssm-ID: 349382  Cd Length: 75  Bit Score: 113.87  E-value: 3.46e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1117368316 765 EKYQQNLFKNQPVMFISLTSQPPCDKLSELVRLCGGKVCKTLRQAKICIGEYlgKQQPEIKYLSEKWILDSVTQHKI 841
Cdd:cd17751     1 SRYRQNLFADGGPIYVSSNSVPPKDKLEELVLLCGGKVVKSSRKADICIGKT--PPNPDKPSVSEKWLLDSITNHKL 75
Microcephalin pfam12258
Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family ...
 222-614 2.00e-23

Microcephalin protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 384 and 835 amino acids in length. Microcephalin is involved in determining the size of the brain in animals. It is a protein, which if expressed homozygously causes the organizm to have the condition microcephaly. organizms expressing the mutated form of this protein in a homozygous manner develop a condition called microcephaly - a drastically reduced brain mass and volume. Microcephalin is predicted to contain three BRCA1 C-terminal domains, the first of which is the probable microcephaly mutation site.


Pssm-ID: 463511 [Multi-domain]  Cd Length: 390  Bit Score: 103.26  E-value: 2.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 222 EQINDSLNSSFDDLWGNCKLKRQKIESLECINAAQSDIYVSTPALEDSSFCS----NDRENLTPKQCnRKQLNKKLI-LQ 296
Cdd:pfam12258   1 ESFAGGLHSSFDDLCGNSECGNQERKLGGSVNEIKSDVCVSSPVLKTSSIHSsassGCLSQLTPQKS-KSNLSKEEInWQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 297 HSLGGDL--SEKGESETSPNKKQDYDDNLT-SLSIATNISFLQEKDLSHSASSQRtvqleaaagtkdshsdllvsskdfn 373
Cdd:pfam12258  80 RDAVGEVvtPDRKQAEGVSKGMFDEKDSLSpALSATKGHPLGHSRPKSSSAKRKR------------------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 374 mCSVDVSVPvdlrdcavghkTKGKSKRKRSSTKLTT--SVLCKSGaenEFLEAMTTRNKISHA-EKGSYEDFFSSSDLNK 450
Cdd:pfam12258 135 -TSEDLNSP-----------PKEKLKKKRSSRKSAMprLQLFKSE---NSLQLMTRPAVETPDcEESSYDDYFSPDNLKE 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 451 seiQESHFVLGVQQKSSCSPEVTYKTGSSRRESN--EQC--SALSKKKRKTVQTNGTlLKSDCKLSELLESTKSVTLNCM 526
Cdd:pfam12258 200 ---RNSENLPPGSQPLSSPAQLSCRSLSKRERKSilEMSdfSCIGKKPRSVDITDLT-AKTSSSLQKPTNDEGNTTLSCL 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 527 VDGKNAQTAEDLVSSslNQLHQNTRENNCRTNVNCSPFPSGATLQD-----------DNTAMMVSLSLKSENKGTAEPK- 594
Cdd:pfam12258 276 TSEGTPAAEETPGCC--RQAGPQKREDAGPEGNSHSHTTDEPALPSghhgdltplkgSSEEMRESVDVKSTQKEGATSKt 353

                         410       420       430
                  ....*....|....*....|....*....|
gi 1117368316 595 ----------EHPLIFPDSASMEKSTDDKK 614
Cdd:pfam12258 354 lnssegeaqsDYKLNFVGDCNVEKSTEEKE 383
PTCB-BRCT pfam12738
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ...
 12-74 6.45e-14

twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair.


Pssm-ID: 463687 [Multi-domain]  Cd Length: 63  Bit Score: 66.84  E-value: 6.45e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1117368316  12 VEVWSANRTENYSKTFAQQLQDMGAQVSKTFNKHVTHVIFKEGHLATWRKAQQTGVKLVSILW 74
Cdd:pfam12738   1 LVICVTGFDGDDREGLQKLIEAMGAEYTKDLTKSVTHLICKSGEGEKYEKAKEWGIPVVSPLW 63
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 665-732 2.76e-11

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 59.68  E-value: 2.76e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1117368316 665 TLVMTSMSSEKQNTVIQVVNKLGGfSFSNDVCETTSHVVAGSPRRTLNVMLGIARGCWIVCYEWVLWS 732
Cdd:cd00027     2 VICFSGLDDEEREELKKLIEALGG-KVSESLSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLDC 68
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 667-739 4.07e-10

first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain.


Pssm-ID: 349366  Cd Length: 80  Bit Score: 56.84  E-value: 4.07e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1117368316 667 VMTSMSSEKQNTVIQVVNKLGGFSFSNDVCETTSHVVAGSP-----RRTLNVMLGIARGCWIVCYEWVLWSLEFGCWI 739
Cdd:cd17734     3 LLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADergvcPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 665-745 1.83e-09

first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. The family corresponds to the first BRCT domain.


Pssm-ID: 349367  Cd Length: 97  Bit Score: 55.43  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 665 TLVMTSMSSEKQNTVIQVVNKLGGfSFSNDVCETTSHVVAGSP-----RRTLNVMLGIARGCWIVCYEWVLWSLEFGCWI 739
Cdd:cd17735     2 SMVASGLTPEELMLVQKFARKTGS-TLTSQFTEETTHVIMKTDaelvcERTLKYFLGIAGRKWVVSYQWITQSIKEGKIL 80


                  ....*.
gi 1117368316 740 SEEPYE 745
Cdd:cd17735    81 PEHDFE 86
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 768-847 3.75e-09

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 54.29  E-value: 3.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 768 QQNLFKNqpvM--FISLTSQPPCDKLSELVRLCGGKVCKTLRQAK-ICIGEYL----GKQQPEIKYLSEKWILDSVTQHK 840
Cdd:pfam16589   1 LPNLFEP---LrfYINAIPSPSRSKLKRLIEANGGTVVDNINPAVyIVIAPYNktdkLAENTKLGVVSPQWIFDCVKKGK 77


                  ....*..
gi 1117368316 841 ICPLENY 847
Cdd:pfam16589  78 LLPLENY 84
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 668-736 6.35e-08

seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the seventh BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


Pssm-ID: 349370 [Multi-domain]  Cd Length: 75  Bit Score: 50.26  E-value: 6.35e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 668 MTSMSSEKQNTVIQVVNKLGGFSFSNDVC-ETTSHVVAGSPRRTLNVMLGIARGCWIVCYEWVLWSLEFG 736
Cdd:cd17738     6 LSGFSEDEKKELISIIEKLGGKVLDSDEFdPKCTHLICGKPSRSEKFLAACAAGKWILHPSYIEASAKAG 75
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 34-87 4.21e-07

BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar proteins; CTDP1 (EC 3.1.3.16), also termed TFIIF-associating CTD phosphatase, or TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1), promotes the activity of RNA polymerase II through processively dephosphorylating 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. It plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.


Pssm-ID: 349361 [Multi-domain]  Cd Length: 97  Bit Score: 48.68  E-value: 4.21e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1117368316  34 MGAQVSKTFNKHVTHVIFKEGHLATWRKAQQT-GVKLVSILWVEKCRETGVRVDE 87
Cdd:cd17729    43 LGAKVVTDLSPRTTHLVAAKLGTEKVKQALKMpGIHVVHPDWLWACAERWERVDE 97
BRCT_MDC1_rpt1 cd17744
first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; ...
 667-729 2.21e-06

first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also termed nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The family corresponds to the first BRCT domain.


Pssm-ID: 349375 [Multi-domain]  Cd Length: 72  Bit Score: 46.07  E-value: 2.21e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1117368316 667 VMTSMSSEKQnTVIQVVNKLGGfSFSNDVCETTsHVVAGSPRRTLNVMLGIARGCWIVCYEWV 729
Cdd:cd17744     3 VLFTGVSDKE-EGEKIIKKLGG-SVVDSVEDCT-HLVTDKVRRTVKFLCALARGIPIVSPDWL 62
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 25-78 3.34e-06

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 45.43  E-value: 3.34e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1117368316  25 KTFAQQLQDMGAQVSKTFNKHVTHVIFKE-GHLATWRKAQQTGVKLVSILWVEKC 78
Cdd:cd00027    14 EELKKLIEALGGKVSESLSSKVTHLIAKSpSGEKYYLAALAWGIPIVSPEWLLDC 68
BRCT_TopBP1_rpt6 cd17727
sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 32-80 5.00e-05

sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the sixth BRCT domain.


Pssm-ID: 349359 [Multi-domain]  Cd Length: 75  Bit Score: 42.20  E-value: 5.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1117368316  32 QDMGAQVSKTFNKHVTHVIFKEGHLAT---WRKAQQTGVKLVSILWVEKCRE 80
Cdd:cd17727    24 ASLGAEYRWTYDESCTHFIYQGKANDTnreYKSAKEQGKFIVSPHWLYACKE 75
BRCT smart00292
breast cancer carboxy-terminal domain;
670-730 1.35e-04

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 41.21  E-value: 1.35e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1117368316  670 SMSSEKQNTVIQVVNKLGGfSFSNDVCE-TTSHVVAGSP-RRTLNVMLGIARGCWIVCYEWVL 730
Cdd:smart00292  14 SFDKEERDELKELIEALGG-KVTSSLSSkTTTHVIVGSPeGGKLELLKAIALGIPIVKEEWLL 75
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 670-728 2.81e-04

BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage syndrome protein 1 (NBS1), or cell cycle regulatory protein p95, is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The BRCT (Breast Cancer Suppressor Protein BRCA1, carboxy-terminal) domain is found within many DNA damage repair and cell cycle checkpoint proteins. The unique diversity of this domain superfamily allows BRCT modules to interact forming homo/hetero BRCT multimers, BRCT-non-BRCT interactions, and interactions within DNA strand breaks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is absent in this group.


Pssm-ID: 349372 [Multi-domain]  Cd Length: 74  Bit Score: 39.89  E-value: 2.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1117368316 670 SMSSEKQNTVIQVVNKLGGFsFSNDVCETTSHVVAGSPRRTLNVMLGIARGCWIVCYEW 728
Cdd:cd17741     9 CLDSEEKKKLKQIIAKLGGK-VVNEWTEECTHLVMSKIKVTVKVICALISGKPIVTPEY 66
BRCT_Rev1 cd17719
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ...
 777-847 8.67e-04

BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light.


Pssm-ID: 349351 [Multi-domain]  Cd Length: 87  Bit Score: 39.09  E-value: 8.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1117368316 777 VMFISLTSQPPCDKLSELVRLCGGK-------------VCKTLRQAKIciGEYlgKQQPEIKYLSEKWILDSVTQHKICP 843
Cdd:cd17719     6 VIYVNGYTDPSADELKRLILLHGGQyehyysrsrvthiIATNLPGSKI--KKL--KKARNYKVVRPEWIVDSIKAGRLLP 81


                  ....
gi 1117368316 844 LENY 847
Cdd:cd17719    82 EAPY 85
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 768-836 2.83e-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: 37.27  E-value: 2.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1117368316 768 QQNLFKNQpVMFISLTSQPPCDKLSELVRLCGGKVCKTL-RQAKICIG-----EYLGKQQPEIKYLSEKWILDSV 836
Cdd:pfam00533   2 KEKLFSGK-TFVITGLDGLERDELKELIEKLGGKVTDSLsKKTTHVIVeartkKYLKAKELGIPIVTEEWLLDCI 75
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 2-78 5.41e-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: 36.50  E-value: 5.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1117368316   2 ESVLRGVSAYVevwsaNRTENYSKTFAQQ-LQDMGAQVSKTFNKHVTHVIFKEGHLAtWRKAQQTGVKLVSILWVEKC 78
Cdd:pfam00533   3 EKLFSGKTFVI-----TGLDGLERDELKElIEKLGGKVTDSLSKKTTHVIVEARTKK-YLKAKELGIPIVTEEWLLDC 74
 
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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