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Conserved domains on  [gi|605051986|ref|NP_001278253|]
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BAH and coiled-coil domain-containing protein 1 isoform 1 [Homo sapiens]

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. ...
 2512-2631 8.56e-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: 8.56e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 2512 EETLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSNMVVKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHK 2591
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGEKELFASDHQDENSVQTIEHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 605051986 2592 CQVVAREQYEQMARSR-KCQDRQDLYYLAGTYDPTTGRLVT 2631
Cdd:cd04714    81 CYVLTFAEYERLARVKkKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
 1969-2037 4.84e-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: 4.84e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 1969 PQSSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASG-DEDEDLDSVVVEFDDGDTGHIAVSNVRLLPPDFK 2037
Cdd:cd20470     1 PQSSRQLPPGTRVCAYWSQKSRCLYPGNVVRGSSGiDEEDDEDSVMVEFDDGDRGRISVSNIRLLPPDYK 70
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 850-1253 4.36e-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: 42.62  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986  850 PGFPASVAGPVPSVFPlPQDAPTQLVILPSEPTPHSAPhaladvmdqaslwPPMYGGRGPASHMQHPGQLPVYSRPQLLR 929
Cdd:PHA03247 2589 PDAPPQSARPRAPVDD-RGDPRGPAPPSPLPPDTHAPD-------------PPPPSPSPAANEPDPHPPPTVPPPERPRD 2654

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986  930 QQELYALQQQRAAQFQRKPEDQHLDLEEPAQEKAPKSTHKPVALTPTAPGAPSPAAGPTKLPPCCHPPDPKPPASSPTPP 1009
Cdd:PHA03247 2655 DPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPA 2734

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 1010 PRPSAPCTLNVCPASSPGPGSRVRSAEEKNGEGQQSTADIITSEPVARAHSVAHAGLEFLASNDPSTSASQSFGITDLPP 1089
Cdd:PHA03247 2735 LPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAP 2814

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 1090 GYLRPmaglgfslPSDVHSSNLEDPETMQTTAPGAQPEPTRTFL----------------PGEPPPCSPRSLEEPGLLSG 1153
Cdd:PHA03247 2815 AAALP--------PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggsvapggdvrrrpPSRSPAAKPAAPARPPVRRL 2886

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 1154 AREA----TQDLAATPYPTERGPQGKAAD---PSPLEGLQELQCAALLEAGGPEATGQAHSTQGGAREERSREEGEQ-GP 1225
Cdd:PHA03247 2887 ARPAvsrsTESFALPPDQPERPPQPQAPPppqPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWlGA 2966

                         410       420
                  ....*....|....*....|....*...
gi 605051986 1226 SSGASSQVLEQRAGSPgalEDEGEQPAP 1253
Cdd:PHA03247 2967 LVPGRVAVPRFRVPQP---APSREAPAS 2991
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 2512-2631 8.56e-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: 8.56e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 2512 EETLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSNMVVKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHK 2591
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGEKELFASDHQDENSVQTIEHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 605051986 2592 CQVVAREQYEQMARSR-KCQDRQDLYYLAGTYDPTTGRLVT 2631
Cdd:cd04714    81 CYVLTFAEYERLARVKkKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
 1969-2037 4.84e-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: 4.84e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 1969 PQSSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASG-DEDEDLDSVVVEFDDGDTGHIAVSNVRLLPPDFK 2037
Cdd:cd20470     1 PQSSRQLPPGTRVCAYWSQKSRCLYPGNVVRGSSGiDEEDDEDSVMVEFDDGDRGRISVSNIRLLPPDYK 70
BAH smart00439
Bromo adjacent homology domain;
2514-2630 2.72e-22

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 94.28  E-value: 2.72e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986   2514 TLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSN--MVVKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHK 2591
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAALFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 605051986   2592 CQVVAREQYEQmARSRKCQDRQDLYYLAGTYDPTTGRLV 2630
Cdd:smart00439   81 CNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKGSFK 118
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 2513-2630 3.37e-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: 3.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986  2513 ETLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSNMV-VKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHK 2591
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETVHRAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 605051986  2592 CQVVAREQYEQmARSRKcQDRQDLYYLAGTYDPTTGRLV 2630
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 ...
 1979-2032 1.05e-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: 1.05e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 605051986  1979 TRVCAYWSQKSRCLYPGNVVRGASGDEDEdldsVVVEFDDGDTGHIAVSNVRLL 2032
Cdd:pfam18115    1 NRVFALWKGKDRAYYPATCLGTSGSGSQR----YLVRFDDGTPTEVDSGQVRRL 50
PHA03247 PHA03247
large tegument protein UL36; Provisional
 850-1253 4.36e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986  850 PGFPASVAGPVPSVFPlPQDAPTQLVILPSEPTPHSAPhaladvmdqaslwPPMYGGRGPASHMQHPGQLPVYSRPQLLR 929
Cdd:PHA03247 2589 PDAPPQSARPRAPVDD-RGDPRGPAPPSPLPPDTHAPD-------------PPPPSPSPAANEPDPHPPPTVPPPERPRD 2654

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986  930 QQELYALQQQRAAQFQRKPEDQHLDLEEPAQEKAPKSTHKPVALTPTAPGAPSPAAGPTKLPPCCHPPDPKPPASSPTPP 1009
Cdd:PHA03247 2655 DPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPA 2734

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 1010 PRPSAPCTLNVCPASSPGPGSRVRSAEEKNGEGQQSTADIITSEPVARAHSVAHAGLEFLASNDPSTSASQSFGITDLPP 1089
Cdd:PHA03247 2735 LPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAP 2814

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 1090 GYLRPmaglgfslPSDVHSSNLEDPETMQTTAPGAQPEPTRTFL----------------PGEPPPCSPRSLEEPGLLSG 1153
Cdd:PHA03247 2815 AAALP--------PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggsvapggdvrrrpPSRSPAAKPAAPARPPVRRL 2886

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 1154 AREA----TQDLAATPYPTERGPQGKAAD---PSPLEGLQELQCAALLEAGGPEATGQAHSTQGGAREERSREEGEQ-GP 1225
Cdd:PHA03247 2887 ARPAvsrsTESFALPPDQPERPPQPQAPPppqPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWlGA 2966

                         410       420
                  ....*....|....*....|....*...
gi 605051986 1226 SSGASSQVLEQRAGSPgalEDEGEQPAP 1253
Cdd:PHA03247 2967 LVPGRVAVPRFRVPQP---APSREAPAS 2991
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 2512-2631 8.56e-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: 8.56e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 2512 EETLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSNMVVKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHK 2591
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGEKELFASDHQDENSVQTIEHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 605051986 2592 CQVVAREQYEQMARSR-KCQDRQDLYYLAGTYDPTTGRLVT 2631
Cdd:cd04714    81 CYVLTFAEYERLARVKkKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
 1969-2037 4.84e-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: 4.84e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 1969 PQSSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASG-DEDEDLDSVVVEFDDGDTGHIAVSNVRLLPPDFK 2037
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 ...
 1971-2037 9.43e-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: 9.43e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 605051986 1971 SSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASGDEDEDLDSVVVEFDDGDTGHIAVSNVRLLPPDFK 2037
Cdd:cd20397     1 SVEYLPPGTRVCAYWSQQYRCLYPGTVISGEPDSEDSQEGKVPVEFDDGDSGKIPLSDIRLLPPDYP 67
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 2512-2630 8.92e-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: 8.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 2512 EETLRVGDCAVFLSAG--RPNLPYIGRIESMWESWGSNMVVKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTIS 2589
Cdd:cd04370     1 GITYEVGDSVYVEPDDsiKSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPFALRRELFLSDHLDEIPVESII 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 605051986 2590 HKCQVVAREQYEQMARsRKCQDRQDLYYLAGTYDPTTGRLV 2630
Cdd:cd04370    81 GKCKVLFVSEFEGLKQ-RPNKIDTDDFFCRLAYDPTTKEFK 120
Tudor_TNRC18 cd20469
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ...
 1971-2038 2.17e-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: 2.17e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 605051986 1971 SSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASgDEDEDLDSVVVEFDDGDTGHIAVSNVRLLPPDFKI 2038
Cdd:cd20469     1 SVRFLPEGTRVCAYWSQQYRCLYPGTVVKGSP-DPEEDDDLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
BAH smart00439
Bromo adjacent homology domain;
2514-2630 2.72e-22

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 94.28  E-value: 2.72e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986   2514 TLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSN--MVVKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHK 2591
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAALFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 605051986   2592 CQVVAREQYEQmARSRKCQDRQDLYYLAGTYDPTTGRLV 2630
Cdd:smart00439   81 CNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKGSFK 118
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 2513-2630 3.37e-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: 3.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986  2513 ETLRVGDCAVFLSAGRPNLPYIGRIESMWESWGSNMV-VKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHK 2591
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETVHRAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 605051986  2592 CQVVAREQYEQmARSRKcQDRQDLYYLAGTYDPTTGRLV 2630
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 ...
 2497-2594 7.79e-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: 7.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 2497 KGKARKLFYKAIVRGEETLRVGDCAVFLSA-GRPnlPYIGRIESMWESWGSNMVVKVKWFYHPEETKL---GKRQCDGKN 2572
Cdd:cd04713     3 KGKKKKCHYTSFEKDGNKYRLEDCVLLVPEdDQK--PYIAIIKDIYKQEEGSLKLEVQWLYRPEEIEKkkgGNWKAEDPR 80

                          90       100
                  ....*....|....*....|..
gi 605051986 2573 ALYQSCHEDENDVQTISHKCQV 2594
Cdd:cd04713    81 ELFYSFHRDEVPAESVLHPCKV 102
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
 2515-2600 1.93e-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: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 2515 LRVGDCAVFLSAGRPNLPYIGRIESMWESWGSNMVVKVKWFYHPEETK--LGKRQCdgKNALYQSCHEDENDVQTISHKC 2592
Cdd:cd04717     4 YRVGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWFYRPEETFhePTRKFY--KNEVFKSPLYETVPVEEIVGKC 81


                  ....*...
gi 605051986 2593 QVVAREQY 2600
Cdd:cd04717    82 AVMDVKDY 89
Tudor_3 pfam18115
DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein ...
 1979-2032 1.05e-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: 1.05e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 605051986  1979 TRVCAYWSQKSRCLYPGNVVRGASGDEDEdldsVVVEFDDGDTGHIAVSNVRLL 2032
Cdd:pfam18115    1 NRVFALWKGKDRAYYPATCLGTSGSGSQR----YLVRFDDGTPTEVDSGQVRRL 50
BAH_fungalPHD cd04710
BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. ...
 2510-2628 3.46e-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: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 2510 RGEETLRVGDcAVFLSAGRPNLPY-IGRI------------ESMWESWGSNMVVKVKWFYHPEEtkLGKRQCDGKNALYQ 2576
Cdd:cd04710     7 KNGELLKVND-HIYMSSEPPGEPYyIGRImefvpkhefpsgIHARVFPASYFQVRLNWYYRPRD--ISRRVVADSRLLYA 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 605051986 2577 SCHEDENDVQTISHKCQVVAREQYEQMARSRKcqdRQDLYYLAGTYDPTTGR 2628
Cdd:cd04710    84 SMHSDICPIGSVRGKCTVRHRDQIPDLEEYKK---RPNHFYFDQLFDRYILR 132
Tudor_53BP1 cd20383
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ...
 1977-2029 5.02e-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: 5.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 605051986 1977 PGTRVCAYWSQKSRcLYPGNVVRgasgdeDEDLDSVVVEFDDGDTGHIAVSNV 2029
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 ...
 2492-2595 5.95e-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: 5.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 2492 QRRGMKGKARKL-FYKAIVRGEETLRVGDCAVFLSAGRPnlPYIGRIESMWESWGSNM--VVKVKWFYHPEETKLGKRQC 2568
Cdd:cd04715     6 VKRGEGGKKKDGqFYRSFTYDGVEYRLYDDVYVHNGDSE--PYIGKIIKIYETAIDSGkkKVKVIWFFRPSEIRMELKGE 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 605051986 2569 DGK--NALYQSCHEDE-----NDVQTISHKCQVV 2595
Cdd:cd04715    84 PKRhiNEVFLACGRGEglaniNLLESIIGKCNVV 117
BAH_plant_2 cd04718
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 2518-2623 1.49e-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: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 2518 GDCAVFLSAGRpnlpYIGRIESMWESWGSNMVvKVKWFYHPEETKLGKRQCDGKNALYQSCHEDENDVQTISHKCQVVAR 2597
Cdd:cd04718    43 SACEKLLSGDL----WLARIEKLWEENGTYWY-AARWYTLPEETHMGRQPHNLRRELYLTNDFADIEMECILRHCSVKCP 117

                          90       100
                  ....*....|....*....|....*.
gi 605051986 2598 EQYeqmarSRKCQDRQDLYYLAGTYD 2623
Cdd:cd04718   118 KEF-----RDASNDGDDVFLCEYEYD 138
Tudor_SpCrb2-like_rpt1 cd20395
first Tudor domain found in Schizosaccharomyces pombe Cut5-repeat binding protein 2 (Crb2) and ...
 1978-2032 3.40e-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: 3.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 605051986 1978 GTRVCAYWSqKSRCLYPGNVVRGASGDededldSVVVEFDDGDTGHIAVSNVRLL 2032
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 ...
 2514-2608 3.52e-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: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 2514 TLRVGDCAVFLSAGRPNlpYIGRIESMWESWGSNMVVKVKWFYHPEETKL-GKRQCDGKNALYQSCHEDENDVQTISHKC 2592
Cdd:cd04721     7 TISVHDFVYVLSEEEDR--YVAYIEDLYEDKKGSKMVKVRWFHTTDEVGAaLSPDSVNPREIFLSPNLQVISVECIDGLA 84

                          90
                  ....*....|....*.
gi 605051986 2593 QVVAREQYEQMARSRK 2608
Cdd:cd04721    85 TVLTREHYEKFQSVPK 100
PHA03247 PHA03247
large tegument protein UL36; Provisional
 850-1253 4.36e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986  850 PGFPASVAGPVPSVFPlPQDAPTQLVILPSEPTPHSAPhaladvmdqaslwPPMYGGRGPASHMQHPGQLPVYSRPQLLR 929
Cdd:PHA03247 2589 PDAPPQSARPRAPVDD-RGDPRGPAPPSPLPPDTHAPD-------------PPPPSPSPAANEPDPHPPPTVPPPERPRD 2654

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986  930 QQELYALQQQRAAQFQRKPEDQHLDLEEPAQEKAPKSTHKPVALTPTAPGAPSPAAGPTKLPPCCHPPDPKPPASSPTPP 1009
Cdd:PHA03247 2655 DPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPA 2734

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 1010 PRPSAPCTLNVCPASSPGPGSRVRSAEEKNGEGQQSTADIITSEPVARAHSVAHAGLEFLASNDPSTSASQSFGITDLPP 1089
Cdd:PHA03247 2735 LPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAP 2814

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 1090 GYLRPmaglgfslPSDVHSSNLEDPETMQTTAPGAQPEPTRTFL----------------PGEPPPCSPRSLEEPGLLSG 1153
Cdd:PHA03247 2815 AAALP--------PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLplggsvapggdvrrrpPSRSPAAKPAAPARPPVRRL 2886

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 605051986 1154 AREA----TQDLAATPYPTERGPQGKAAD---PSPLEGLQELQCAALLEAGGPEATGQAHSTQGGAREERSREEGEQ-GP 1225
Cdd:PHA03247 2887 ARPAvsrsTESFALPPDQPERPPQPQAPPppqPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWlGA 2966

                         410       420
                  ....*....|....*....|....*...
gi 605051986 1226 SSGASSQVLEQRAGSPgalEDEGEQPAP 1253
Cdd:PHA03247 2967 LVPGRVAVPRFRVPQP---APSREAPAS 2991
 
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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