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Conserved domains on  [gi|410306830|gb|JAA32015|]
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BAH domain and coiled-coil containing 1 [Pan troglodytes]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 2481-2600 8.46e-68

BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


:

Pssm-ID: 240065  Cd Length: 121  Bit Score: 224.59  E-value: 8.46e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 2481 EETLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSNMVVKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHK 2560
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGEKELFASDHQDENSVQTIEHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 410306830 2561 CQVVAREQYEQMARSR-KCQDRQDLYYLAGTYDPTTGRLVT 2600
Cdd:cd04714    81 CYVLTFAEYERLARVKkKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
 1938-2006 4.69e-40

Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar proteins; BAHCC1, also called Bromo adjacent homology domain-containing protein 2 (BAHD2), or BAH domain-containing protein 2, may function as a transcriptional regulator. BAHCC1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410541  Cd Length: 70  Bit Score: 143.02  E-value: 4.69e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 1938 PQSSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASG-DEDEDLDSVVVEFDDGDTGHIAVSNVRLLPPDFK 2006
Cdd:cd20470     1 PQSSRQLPPGTRVCAYWSQKSRCLYPGNVVRGSSGiDEEDDEDSVMVEFDDGDRGRISVSNIRLLPPDYK 70
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 849-1222 2.20e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830  849 PPGFPASVAGPVPSVFPLPQDAPtqlvilPSEPTPHSAPHALADVMDQASLWPPMYGGRGPAShmqhPGQLPVYSRPQLL 928
Cdd:PHA03247 2601 PVDDRGDPRGPAPPSPLPPDTHA------PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPA----PGRVSRPRRARRL 2670

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830  929 RQQELYALQQQRAAQFQRKPEDQHLD--LEEPAQEKAPKSthKPVALTPTAPGAPSPAAGPTKLPPCCHPPDPKPPASCP 1006
Cdd:PHA03247 2671 GRAAQASSPPQRPRRRAARPTVGSLTslADPPPPPPTPEP--APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGP 2748

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 1007 TPPPRPSAPCTlnvcPASSPGPGSRVRSAEEKNGEGQQSTADIITSEPDLPPGYLRPMAglgfslPSDVHSSNLEDPETM 1086
Cdd:PHA03247 2749 ATPGGPARPAR----PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWD------PADPPAAVLAPAAAL 2818

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 1087 QTAAPGAQPEPTRTFLPGEPPPCSPRSLEEPRLLSGA---------REATQDLAATPYPAERGPQGKAADPSPLEGLQEL 1157
Cdd:PHA03247 2819 PPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapggdvrrRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESF 2898

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410306830 1158 QCGALLEAGGPEATGQAHSTQgGAREERSREEGEQGPSSGASSQVLEQRAGSPGALEDEGEQPAP 1222
Cdd:PHA03247 2899 ALPPDQPERPPQPQAPPPPQP-QPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 2481-2600 8.46e-68

BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240065  Cd Length: 121  Bit Score: 224.59  E-value: 8.46e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 2481 EETLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSNMVVKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHK 2560
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGEKELFASDHQDENSVQTIEHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 410306830 2561 CQVVAREQYEQMARSR-KCQDRQDLYYLAGTYDPTTGRLVT 2600
Cdd:cd04714    81 CYVLTFAEYERLARVKkKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
 1938-2006 4.69e-40

Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar proteins; BAHCC1, also called Bromo adjacent homology domain-containing protein 2 (BAHD2), or BAH domain-containing protein 2, may function as a transcriptional regulator. BAHCC1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410541  Cd Length: 70  Bit Score: 143.02  E-value: 4.69e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 1938 PQSSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASG-DEDEDLDSVVVEFDDGDTGHIAVSNVRLLPPDFK 2006
Cdd:cd20470     1 PQSSRQLPPGTRVCAYWSQKSRCLYPGNVVRGSSGiDEEDDEDSVMVEFDDGDRGRISVSNIRLLPPDYK 70
BAH smart00439
Bromo adjacent homology domain;
2483-2599 2.69e-22

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 94.28  E-value: 2.69e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830   2483 TLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSN--MVVKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHK 2560
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAALFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 410306830   2561 CQVVAREQYEQmARSRKCQDRQDLYYLAGTYDPTTGRLV 2599
Cdd:smart00439   81 CNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKGSFK 118
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 2482-2599 3.33e-17

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 79.66  E-value: 3.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830  2482 ETLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSNMV-VKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHK 2560
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETVHRAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 410306830  2561 CQVVAREQYEQmARSRKcQDRQDLYYLAGTYDPTTGRLV 2599
Cdd:pfam01426   81 CSVLHKSDLES-LDPYK-IKEPDDFFCELLYDPKTKSFK 117
Tudor_3 pfam18115
DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein ...
 1948-2001 1.04e-04

DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein crb2. Structural and functional studies of Crb2 and its mammalian homolog 53BP1 indicate that the conserved tandem-Tudor domain of 53BP1 and Crb2 preferentially interacts with H4K20me2, though it also binds to H4K20me1. Furthermore, despite low amino acid sequence similarity, Crb2 is structurally related to 53BP1 in having two tudor domains and a conserved dimethyllysine-binding pocket, and that, like 53BP1, it directly binds H4-K20me2.


Pssm-ID: 436284  Cd Length: 50  Bit Score: 41.78  E-value: 1.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 410306830  1948 TRVCAYWSQKSRCLYPGNVVRGASGDEDEdldsVVVEFDDGDTGHIAVSNVRLL 2001
Cdd:pfam18115    1 NRVFALWKGKDRAYYPATCLGTSGSGSQR----YLVRFDDGTPTEVDSGQVRRL 50
PHA03247 PHA03247
large tegument protein UL36; Provisional
 849-1222 2.20e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830  849 PPGFPASVAGPVPSVFPLPQDAPtqlvilPSEPTPHSAPHALADVMDQASLWPPMYGGRGPAShmqhPGQLPVYSRPQLL 928
Cdd:PHA03247 2601 PVDDRGDPRGPAPPSPLPPDTHA------PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPA----PGRVSRPRRARRL 2670

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830  929 RQQELYALQQQRAAQFQRKPEDQHLD--LEEPAQEKAPKSthKPVALTPTAPGAPSPAAGPTKLPPCCHPPDPKPPASCP 1006
Cdd:PHA03247 2671 GRAAQASSPPQRPRRRAARPTVGSLTslADPPPPPPTPEP--APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGP 2748

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 1007 TPPPRPSAPCTlnvcPASSPGPGSRVRSAEEKNGEGQQSTADIITSEPDLPPGYLRPMAglgfslPSDVHSSNLEDPETM 1086
Cdd:PHA03247 2749 ATPGGPARPAR----PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWD------PADPPAAVLAPAAAL 2818

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 1087 QTAAPGAQPEPTRTFLPGEPPPCSPRSLEEPRLLSGA---------REATQDLAATPYPAERGPQGKAADPSPLEGLQEL 1157
Cdd:PHA03247 2819 PPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapggdvrrRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESF 2898

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410306830 1158 QCGALLEAGGPEATGQAHSTQgGAREERSREEGEQGPSSGASSQVLEQRAGSPGALEDEGEQPAP 1222
Cdd:PHA03247 2899 ALPPDQPERPPQPQAPPPPQP-QPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 843-1113 7.00e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 7.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830   843 ALHQNLPPGFPASVAGPVPSVFPLPQDAPTQLVilPSEPTPHSAPHALAdvmdqaslwPPM-YGGRGPASHMQHPGQLPV 921
Cdd:pfam03154  229 TLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQV--SPQPLPQPSLHGQM---------PPMpHSLQTGPSHMQHPVPPQP 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830   922 YSRPQLLRQQELYALQQQRAAQFQRKPEDQHLDLEEPAQEKAPKSTHKPVALT--------PTAPGAPSPAAGPTKLPPC 993
Cdd:pfam03154  298 FPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLsmphikppPTTPIPQLPNPQSHKHPPH 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830   994 CHPPDPKPPASCPTPPPRPSAPCTL-NVCPASSPGPGSRVRSaeekngEGQQstadiITSEPDLPPGYLRPMaglgfSLP 1072
Cdd:pfam03154  378 LSGPSPFQMNSNLPPPPALKPLSSLsTHHPPSAHPPPLQLMP------QSQQ-----LPPPPAQPPVLTQSQ-----SLP 441

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 410306830  1073 SdvhSSNLEDPETMQTAAPGAQPEPTRTFLPGEPPPCSPRS 1113
Cdd:pfam03154  442 P---PAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPS 479
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 2481-2600 8.46e-68

BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240065  Cd Length: 121  Bit Score: 224.59  E-value: 8.46e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 2481 EETLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSNMVVKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHK 2560
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGEKELFASDHQDENSVQTIEHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 410306830 2561 CQVVAREQYEQMARSR-KCQDRQDLYYLAGTYDPTTGRLVT 2600
Cdd:cd04714    81 CYVLTFAEYERLARVKkKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
 1938-2006 4.69e-40

Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar proteins; BAHCC1, also called Bromo adjacent homology domain-containing protein 2 (BAHD2), or BAH domain-containing protein 2, may function as a transcriptional regulator. BAHCC1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410541  Cd Length: 70  Bit Score: 143.02  E-value: 4.69e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 1938 PQSSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASG-DEDEDLDSVVVEFDDGDTGHIAVSNVRLLPPDFK 2006
Cdd:cd20470     1 PQSSRQLPPGTRVCAYWSQKSRCLYPGNVVRGSSGiDEEDDEDSVMVEFDDGDRGRISVSNIRLLPPDYK 70
Tudor_BAHCC1-like cd20397
Tudor domain found in the BAH and coiled-coil domain-containing protein 1 (BAHCC1) family; The ...
 1940-2006 8.54e-35

Tudor domain found in the BAH and coiled-coil domain-containing protein 1 (BAHCC1) family; The family of BAHCC1 includes BAHCC1 and trinucleotide repeat-containing gene 18 protein (TNRC18). BAHCC1 may function as a transcriptional regulator. The biological function of TNRC18 remains unclear. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410468  Cd Length: 67  Bit Score: 127.83  E-value: 8.54e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 410306830 1940 SSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASGDEDEDLDSVVVEFDDGDTGHIAVSNVRLLPPDFK 2006
Cdd:cd20397     1 SVEYLPPGTRVCAYWSQQYRCLYPGTVISGEPDSEDSQEGKVPVEFDDGDSGKIPLSDIRLLPPDYP 67
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 2481-2599 8.81e-32

BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). BAH domains have first been described as domains found in the polybromo protein and Yeast Rsc1/Rsc2 (Remodeling of the Structure of Chromatin). They also occur in mammalian DNA methyltransferases and the MTA1 subunits of histone deacetylase complexes. A BAH domain is also found in Yeast Sir3p and in the origin receptor complex protein 1 (Orc1p), where it was found to interact with the N-terminal lobe of the silence information regulator 1 protein (Sir1p), confirming the initial hypothesis that BAH plays a role in protein-protein interactions.


Pssm-ID: 239835 [Multi-domain]  Cd Length: 123  Bit Score: 121.34  E-value: 8.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 2481 EETLRVGDCAVFLSAG--RPNLPYIGRIESMWESWGSNMVVKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTIS 2558
Cdd:cd04370     1 GITYEVGDSVYVEPDDsiKSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPFALRRELFLSDHLDEIPVESII 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 410306830 2559 HKCQVVAREQYEQMARsRKCQDRQDLYYLAGTYDPTTGRLV 2599
Cdd:cd04370    81 GKCKVLFVSEFEGLKQ-RPNKIDTDDFFCRLAYDPTTKEFK 120
Tudor_TNRC18 cd20469
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ...
 1940-2007 2.08e-30

Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar proteins; TNRC18, also called long CAG trinucleotide repeat-containing gene 79 protein (CAGL79), is a protein that in humans is encoded by the TNRC18 gene. Its biological function remains unclear. TNRC18 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410540  Cd Length: 67  Bit Score: 115.59  E-value: 2.08e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410306830 1940 SSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASgDEDEDLDSVVVEFDDGDTGHIAVSNVRLLPPDFKI 2007
Cdd:cd20469     1 SVRFLPEGTRVCAYWSQQYRCLYPGTVVKGSP-DPEEDDDLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
BAH smart00439
Bromo adjacent homology domain;
2483-2599 2.69e-22

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 94.28  E-value: 2.69e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830   2483 TLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSN--MVVKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHK 2560
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAALFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 410306830   2561 CQVVAREQYEQmARSRKCQDRQDLYYLAGTYDPTTGRLV 2599
Cdd:smart00439   81 CNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKGSFK 118
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 2482-2599 3.33e-17

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 79.66  E-value: 3.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830  2482 ETLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSNMV-VKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHK 2560
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETVHRAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 410306830  2561 CQVVAREQYEQmARSRKcQDRQDLYYLAGTYDPTTGRLV 2599
Cdd:pfam01426   81 CSVLHKSDLES-LDPYK-IKEPDDFFCELLYDPKTKSFK 117
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 2466-2563 7.70e-10

BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240064  Cd Length: 146  Bit Score: 59.40  E-value: 7.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 2466 KGKARKLFYKAIVRGEETLRVGDCAVFLSA-GRPnlPYIGRIESMWESWGSNMVVKVKWFYHPEETKL---GKRQCDGKN 2541
Cdd:cd04713     3 KGKKKKCHYTSFEKDGNKYRLEDCVLLVPEdDQK--PYIAIIKDIYKQEEGSLKLEVQWLYRPEEIEKkkgGNWKAEDPR 80

                          90       100
                  ....*....|....*....|..
gi 410306830 2542 ALYQSCHEDENDVQTISHKCQV 2563
Cdd:cd04713    81 ELFYSFHRDEVPAESVLHPCKV 102
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
 2484-2569 1.91e-07

BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human polybromo protein (BAF180) is a component of the SWI/SNF chromatin-remodeling complex PBAF. It is thought that polybromo participates in transcriptional regulation. Saccharomyces cerevisiae RSC1 and RSC2 are part of the 15-subunit nucleosome remodeling RSC complex. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240068  Cd Length: 121  Bit Score: 51.82  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 2484 LRVGDCAVFLSAGRPNLPYIGRIESMWESWGSNMVVKVKWFYHPEETK--LGKRQCdgKNALYQSCHEDENDVQTISHKC 2561
Cdd:cd04717     4 YRVGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWFYRPEETFhePTRKFY--KNEVFKSPLYETVPVEEIVGKC 81


                  ....*...
gi 410306830 2562 QVVAREQY 2569
Cdd:cd04717    82 AVMDVKDY 89
Tudor_3 pfam18115
DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein ...
 1948-2001 1.04e-04

DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein crb2. Structural and functional studies of Crb2 and its mammalian homolog 53BP1 indicate that the conserved tandem-Tudor domain of 53BP1 and Crb2 preferentially interacts with H4K20me2, though it also binds to H4K20me1. Furthermore, despite low amino acid sequence similarity, Crb2 is structurally related to 53BP1 in having two tudor domains and a conserved dimethyllysine-binding pocket, and that, like 53BP1, it directly binds H4-K20me2.


Pssm-ID: 436284  Cd Length: 50  Bit Score: 41.78  E-value: 1.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 410306830  1948 TRVCAYWSQKSRCLYPGNVVRGASGDEDEdldsVVVEFDDGDTGHIAVSNVRLL 2001
Cdd:pfam18115    1 NRVFALWKGKDRAYYPATCLGTSGSGSQR----YLVRFDDGTPTEVDSGQVRRL 50
BAH_fungalPHD cd04710
BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. ...
 2479-2597 3.42e-04

BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240061  Cd Length: 135  Bit Score: 43.13  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 2479 RGEETLRVGDcAVFLSAGRPNLPY-IGRI------------ESMWESWGSNMVVKVKWFYHPEEtkLGKRQCDGKNALYQ 2545
Cdd:cd04710     7 KNGELLKVND-HIYMSSEPPGEPYyIGRImefvpkhefpsgIHARVFPASYFQVRLNWYYRPRD--ISRRVVADSRLLYA 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 410306830 2546 SCHEDENDVQTISHKCQVVAREQYEQMARSRKcqdRQDLYYLAGTYDPTTGR 2597
Cdd:cd04710    84 SMHSDICPIGSVRGKCTVRHRDQIPDLEEYKK---RPNHFYFDQLFDRYILR 132
Tudor_53BP1 cd20383
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ...
 1946-1998 4.96e-04

Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; 53BP1, also called p53-binding protein 1 (p53BP1), is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics, and class-switch recombination (CSR) during antibody genesis. It plays a key role in the repair of DSBs in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1. It is recruited to DSB sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSB sites. 53BP1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410454  Cd Length: 52  Bit Score: 39.94  E-value: 4.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 410306830 1946 PGTRVCAYWSQKSRcLYPGNVVRgasgdeDEDLDSVVVEFDDGDTGHIAVSNV 1998
Cdd:cd20383     1 VGTRVFAKWSSDGY-YYPGIITR------VLGDGKYKVLFDDGYERDVKGKDI 46
BAH_Orc1p_like cd04715
BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of ...
 2461-2564 5.88e-04

BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of Saccharomyces cerevisiae Orc1p and similar proteins. Orc1 is part of the Yeast Sir1-origin recognition complex, the Orc1p BAH doman functions in epigenetic silencing. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240066  Cd Length: 159  Bit Score: 42.88  E-value: 5.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 2461 QRRGMKGKARKL-FYKAIVRGEETLRVGDCAVFLSAGRPnlPYIGRIESMWESWGSNM--VVKVKWFYHPEETKLGKRQC 2537
Cdd:cd04715     6 VKRGEGGKKKDGqFYRSFTYDGVEYRLYDDVYVHNGDSE--PYIGKIIKIYETAIDSGkkKVKVIWFFRPSEIRMELKGE 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 410306830 2538 DGK--NALYQSCHEDE-----NDVQTISHKCQVV 2564
Cdd:cd04715    84 PKRhiNEVFLACGRGEglaniNLLESIIGKCNVV 117
BAH_plant_2 cd04718
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 2487-2592 1.67e-03

BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240069  Cd Length: 148  Bit Score: 41.42  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 2487 GDCAVFLSAGRpnlpYIGRIESMWESWGSNMVvKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHKCQVVAR 2566
Cdd:cd04718    43 SACEKLLSGDL----WLARIEKLWEENGTYWY-AARWYTLPEETHMGRQPHNLRRELYLTNDFADIEMECILRHCSVKCP 117

                          90       100
                  ....*....|....*....|....*.
gi 410306830 2567 EQYeqmarSRKCQDRQDLYYLAGTYD 2592
Cdd:cd04718   118 KEF-----RDASNDGDDVFLCEYEYD 138
PHA03247 PHA03247
large tegument protein UL36; Provisional
 849-1222 2.20e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830  849 PPGFPASVAGPVPSVFPLPQDAPtqlvilPSEPTPHSAPHALADVMDQASLWPPMYGGRGPAShmqhPGQLPVYSRPQLL 928
Cdd:PHA03247 2601 PVDDRGDPRGPAPPSPLPPDTHA------PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPA----PGRVSRPRRARRL 2670

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830  929 RQQELYALQQQRAAQFQRKPEDQHLD--LEEPAQEKAPKSthKPVALTPTAPGAPSPAAGPTKLPPCCHPPDPKPPASCP 1006
Cdd:PHA03247 2671 GRAAQASSPPQRPRRRAARPTVGSLTslADPPPPPPTPEP--APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGP 2748

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 1007 TPPPRPSAPCTlnvcPASSPGPGSRVRSAEEKNGEGQQSTADIITSEPDLPPGYLRPMAglgfslPSDVHSSNLEDPETM 1086
Cdd:PHA03247 2749 ATPGGPARPAR----PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWD------PADPPAAVLAPAAAL 2818

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 1087 QTAAPGAQPEPTRTFLPGEPPPCSPRSLEEPRLLSGA---------REATQDLAATPYPAERGPQGKAADPSPLEGLQEL 1157
Cdd:PHA03247 2819 PPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapggdvrrRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESF 2898

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410306830 1158 QCGALLEAGGPEATGQAHSTQgGAREERSREEGEQGPSSGASSQVLEQRAGSPGALEDEGEQPAP 1222
Cdd:PHA03247 2899 ALPPDQPERPPQPQAPPPPQP-QPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
Tudor_SpCrb2-like_rpt1 cd20395
first Tudor domain found in Schizosaccharomyces pombe Cut5-repeat binding protein 2 (Crb2) and ...
 1947-2001 3.36e-03

first Tudor domain found in Schizosaccharomyces pombe Cut5-repeat binding protein 2 (Crb2) and similar proteins; Crb2, also called RAD9 protein homolog, or checkpoint mediator protein crb2, is a DNA repair protein essential for cell cycle arrest at the G1 and G2 stages following DNA damage by X-, and UV-irradiation, or inactivation of DNA ligase. Crb2 contains two Tudor domains. The model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410466  Cd Length: 50  Bit Score: 37.72  E-value: 3.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 410306830 1947 GTRVCAYWSqKSRCLYPGNVVRGASGDededldSVVVEFDDGDTGHIAVSNVRLL 2001
Cdd:cd20395     1 PTRVLAFWK-GDGNYYPATIVGPVSSS------AYKVQFDDGTSSSVPPTQIRRL 48
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 2483-2577 3.48e-03

BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240072  Cd Length: 130  Bit Score: 40.12  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830 2483 TLRVGDCAVFLSAGRPNlpYIGRIESMWESWGSNMVVKVKWFYHPEETKL-GKRQCDGKNALYQSCHEDENDVQTISHKC 2561
Cdd:cd04721     7 TISVHDFVYVLSEEEDR--YVAYIEDLYEDKKGSKMVKVRWFHTTDEVGAaLSPDSVNPREIFLSPNLQVISVECIDGLA 84

                          90
                  ....*....|....*.
gi 410306830 2562 QVVAREQYEQMARSRK 2577
Cdd:cd04721    85 TVLTREHYEKFQSVPK 100
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 843-1113 7.00e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 7.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830   843 ALHQNLPPGFPASVAGPVPSVFPLPQDAPTQLVilPSEPTPHSAPHALAdvmdqaslwPPM-YGGRGPASHMQHPGQLPV 921
Cdd:pfam03154  229 TLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQV--SPQPLPQPSLHGQM---------PPMpHSLQTGPSHMQHPVPPQP 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830   922 YSRPQLLRQQELYALQQQRAAQFQRKPEDQHLDLEEPAQEKAPKSTHKPVALT--------PTAPGAPSPAAGPTKLPPC 993
Cdd:pfam03154  298 FPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLsmphikppPTTPIPQLPNPQSHKHPPH 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410306830   994 CHPPDPKPPASCPTPPPRPSAPCTL-NVCPASSPGPGSRVRSaeekngEGQQstadiITSEPDLPPGYLRPMaglgfSLP 1072
Cdd:pfam03154  378 LSGPSPFQMNSNLPPPPALKPLSSLsTHHPPSAHPPPLQLMP------QSQQ-----LPPPPAQPPVLTQSQ-----SLP 441

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 410306830  1073 SdvhSSNLEDPETMQTAAPGAQPEPTRTFLPGEPPPCSPRS 1113
Cdd:pfam03154  442 P---PAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPS 479
 
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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