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Conserved domains on  [gi|1720413413|ref|XP_030110313|]
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trinucleotide repeat-containing gene 18 protein isoform X4 [Mus musculus]

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. ...
2747-2891 4.94e-57

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: 193.77  E-value: 4.94e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2747 KEMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKqfhegqhwdqksghslpaalrassqR 2826
Cdd:cd04714      1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGR-------------------------K 55
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720413413 2827 KDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLK-TKKYQDSEGLYYLAGTYEPTTGMIFS 2891
Cdd:cd04714     56 PNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYERLARvKKKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_SF super family cl02573
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
2152-2218 9.10e-37

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.


The actual alignment was detected with superfamily member cd20469:

Pssm-ID: 470623  Cd Length: 67  Bit Score: 133.70  E-value: 9.10e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720413413 2152 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYKI 2218
Cdd:cd20469      1 SVRFLPEGTRVCAYWSQQYRCLYPGTVVKGSPDPEEDDDLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
2213-2427 1.32e-03

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK12323:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2213 PPDYKIQCAEPSPALLVPSAKRRSRKTSKDTGEVKEGAATGPQEATGGKARgrgRKPSTKA-KADRAVVLEEGAATNEVP 2291
Cdd:PRK12323   375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPAR---RSPAPEAlAAARQASARGPGGAPAPA 451
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2292 SAPLALEPISTPNSKKSTPEPVDKRARAPKARSISAQPSPVP---PTFSSCPA--PEPFGELPTPATAPLVTMPVTMPAT 2366
Cdd:PRK12323   452 PAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADddpPPWEELPPefASPAPAQPDAAPAGWVAESIPDPAT 531
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720413413 2367 RPKPKKARAAEGSGAKGPRRPgeddellVKLDHEGVMSPKSKKAKEALLlrEDPGPGGWPE 2427
Cdd:PRK12323   532 ADPDDAFETLAPAPAAAPAPR-------AAAATEPVVAPRPPRASASGL--PDMFDGDWPA 583
PHA03247 super family cl33720
large tegument protein UL36; Provisional
997-1306 9.83e-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: 41.85  E-value: 9.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413  997 PFQALFTDIPPRYPFQALPPhyGRPYPFLLQPAAASDADglAPDVPLPADGPERLALSPEDKPICLSPSkiPEPPRDSPE 1076
Cdd:PHA03247  2551 PPPPLPPAAPPAAPDRSVPP--PRPAPRPSEPAVTSRAR--RPDAPPQSARPRAPVDDRGDPRGPAPPS--PLPPDTHAP 2624
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 1077 EEQLADREVKAEvEDIEEGPTELPPLESPLALPVPeTMVAVSPAGGCGGSPLEAQAlSTAGPGCRE-PSEVSDFAQVAEP 1155
Cdd:PHA03247  2625 DPPPPSPSPAAN-EPDPHPPPTVPPPERPRDDPAP-GRVSRPRRARRLGRAAQASS-PPQRPRRRAaRPTVGSLTSLADP 2701
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 1156 QIElPSKTEHRMTALELGTQLTPEPLVETKEEPVEVPLDVPMEEPTTEAGPED-----------------------SLPQ 1212
Cdd:PHA03247  2702 PPP-PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGparparppttagppapappaapaAGPP 2780
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 1213 PSLTEPQ-PSLELSDCDLPVPEgqclnleAQEAVPAPASTCYLEETHSESLLPGLDDPLAGMNALAAAAELPQARPLPSL 1291
Cdd:PHA03247  2781 RRLTRPAvASLSESRESLPSPW-------DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG 2853
                          330
                   ....*....|....*
gi 1720413413 1292 GPGVPAGEKLDTAPS 1306
Cdd:PHA03247  2854 GSVAPGGDVRRRPPS 2868
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
2747-2891 4.94e-57

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: 193.77  E-value: 4.94e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2747 KEMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKqfhegqhwdqksghslpaalrassqR 2826
Cdd:cd04714      1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGR-------------------------K 55
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720413413 2827 KDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLK-TKKYQDSEGLYYLAGTYEPTTGMIFS 2891
Cdd:cd04714     56 PNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYERLARvKKKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_TNRC18 cd20469
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ...
2152-2218 9.10e-37

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: 133.70  E-value: 9.10e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720413413 2152 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYKI 2218
Cdd:cd20469      1 SVRFLPEGTRVCAYWSQQYRCLYPGTVVKGSPDPEEDDDLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
BAH smart00439
Bromo adjacent homology domain;
2749-2887 1.74e-13

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 69.24  E-value: 1.74e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413  2749 MIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNN--MVVRVKWFYHPEETSPGKQFHegqhwdqksghslpaalrassqr 2826
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAAL----------------------- 57
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720413413  2827 kdFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQmLKTKKYQDSEGLYYLAGTYEPTTG 2887
Cdd:smart00439   58 --FDKNEVFLSDEYDTVPLSDIIGKCNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKG 115
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
2748-2887 1.13e-10

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: 61.17  E-value: 1.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2748 EMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMV-VRVKWFYHPEETSpgkqfhegqhwdqksgHSLPAAlrassqr 2826
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETV----------------HRAGKA------- 57
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720413413 2827 kdFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKKyqDSEGLYYLAGTYEPTTG 2887
Cdd:pfam01426   58 --FNKDELFLSDEEDDVPLSAIIGKCSVLHKSDLESLDPYKI--KEPDDFFCELLYDPKTK 114
Tudor_3 pfam18115
DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein ...
2160-2212 1.48e-05

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: 44.47  E-value: 1.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720413413 2160 TRIAAYWSQQYRCLYPGTVVRgllDLEDDGDLITVEFDDGDTGRIPLSHIRLL 2212
Cdd:pfam18115    1 NRVFALWKGKDRAYYPATCLG---TSGSGSQRYLVRFDDGTPTEVDSGQVRRL 50
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2213-2427 1.32e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2213 PPDYKIQCAEPSPALLVPSAKRRSRKTSKDTGEVKEGAATGPQEATGGKARgrgRKPSTKA-KADRAVVLEEGAATNEVP 2291
Cdd:PRK12323   375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPAR---RSPAPEAlAAARQASARGPGGAPAPA 451
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2292 SAPLALEPISTPNSKKSTPEPVDKRARAPKARSISAQPSPVP---PTFSSCPA--PEPFGELPTPATAPLVTMPVTMPAT 2366
Cdd:PRK12323   452 PAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADddpPPWEELPPefASPAPAQPDAAPAGWVAESIPDPAT 531
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720413413 2367 RPKPKKARAAEGSGAKGPRRPgeddellVKLDHEGVMSPKSKKAKEALLlrEDPGPGGWPE 2427
Cdd:PRK12323   532 ADPDDAFETLAPAPAAAPAPR-------AAAATEPVVAPRPPRASASGL--PDMFDGDWPA 583
PHA03247 PHA03247
large tegument protein UL36; Provisional
997-1306 9.83e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 9.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413  997 PFQALFTDIPPRYPFQALPPhyGRPYPFLLQPAAASDADglAPDVPLPADGPERLALSPEDKPICLSPSkiPEPPRDSPE 1076
Cdd:PHA03247  2551 PPPPLPPAAPPAAPDRSVPP--PRPAPRPSEPAVTSRAR--RPDAPPQSARPRAPVDDRGDPRGPAPPS--PLPPDTHAP 2624
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 1077 EEQLADREVKAEvEDIEEGPTELPPLESPLALPVPeTMVAVSPAGGCGGSPLEAQAlSTAGPGCRE-PSEVSDFAQVAEP 1155
Cdd:PHA03247  2625 DPPPPSPSPAAN-EPDPHPPPTVPPPERPRDDPAP-GRVSRPRRARRLGRAAQASS-PPQRPRRRAaRPTVGSLTSLADP 2701
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 1156 QIElPSKTEHRMTALELGTQLTPEPLVETKEEPVEVPLDVPMEEPTTEAGPED-----------------------SLPQ 1212
Cdd:PHA03247  2702 PPP-PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGparparppttagppapappaapaAGPP 2780
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 1213 PSLTEPQ-PSLELSDCDLPVPEgqclnleAQEAVPAPASTCYLEETHSESLLPGLDDPLAGMNALAAAAELPQARPLPSL 1291
Cdd:PHA03247  2781 RRLTRPAvASLSESRESLPSPW-------DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG 2853
                          330
                   ....*....|....*
gi 1720413413 1292 GPGVPAGEKLDTAPS 1306
Cdd:PHA03247  2854 GSVAPGGDVRRRPPS 2868
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
2747-2891 4.94e-57

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: 193.77  E-value: 4.94e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2747 KEMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKqfhegqhwdqksghslpaalrassqR 2826
Cdd:cd04714      1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGR-------------------------K 55
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720413413 2827 KDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLK-TKKYQDSEGLYYLAGTYEPTTGMIFS 2891
Cdd:cd04714     56 PNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYERLARvKKKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_TNRC18 cd20469
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ...
2152-2218 9.10e-37

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: 133.70  E-value: 9.10e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720413413 2152 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYKI 2218
Cdd:cd20469      1 SVRFLPEGTRVCAYWSQQYRCLYPGTVVKGSPDPEEDDDLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
Tudor_BAHCC1-like cd20397
Tudor domain found in the BAH and coiled-coil domain-containing protein 1 (BAHCC1) family; The ...
2152-2217 9.07e-30

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: 113.96  E-value: 9.07e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720413413 2152 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDD-GDLITVEFDDGDTGRIPLSHIRLLPPDYK 2217
Cdd:cd20397      1 SVEYLPPGTRVCAYWSQQYRCLYPGTVISGEPDSEDSqEGKVPVEFDDGDSGKIPLSDIRLLPPDYP 67
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
2150-2217 1.07e-24

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: 99.49  E-value: 1.07e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2150 PASTRFLPQGTRIAAYWSQQYRCLYPGTVVR--GLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYK 2217
Cdd:cd20470      1 PQSSRQLPPGTRVCAYWSQKSRCLYPGNVVRgsSGIDEEDDEDSVMVEFDDGDRGRISVSNIRLLPPDYK 70
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
2747-2887 2.85e-21

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: 91.68  E-value: 2.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2747 KEMIRIGDCAVFLSAG--RPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKQFHEGqhwdqksghslpaalrass 2824
Cdd:cd04370      1 GITYEVGDSVYVEPDDsiKSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPFAL------------------- 61
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720413413 2825 qrkdfmERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMlKTKKYQDSEGLYYLAGTYEPTTG 2887
Cdd:cd04370     62 ------RRELFLSDHLDEIPVESIIGKCKVLFVSEFEGL-KQRPNKIDTDDFFCRLAYDPTTK 117
BAH smart00439
Bromo adjacent homology domain;
2749-2887 1.74e-13

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 69.24  E-value: 1.74e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413  2749 MIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNN--MVVRVKWFYHPEETSPGKQFHegqhwdqksghslpaalrassqr 2826
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAAL----------------------- 57
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720413413  2827 kdFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQmLKTKKYQDSEGLYYLAGTYEPTTG 2887
Cdd:smart00439   58 --FDKNEVFLSDEYDTVPLSDIIGKCNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKG 115
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
2748-2887 1.13e-10

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: 61.17  E-value: 1.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2748 EMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMV-VRVKWFYHPEETSpgkqfhegqhwdqksgHSLPAAlrassqr 2826
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETV----------------HRAGKA------- 57
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720413413 2827 kdFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKKyqDSEGLYYLAGTYEPTTG 2887
Cdd:pfam01426   58 --FNKDELFLSDEEDDVPLSAIIGKCSVLHKSDLESLDPYKI--KEPDDFFCELLYDPKTK 114
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
2749-2804 1.36e-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: 52.59  E-value: 1.36e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720413413 2749 MIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEET--SPGKQFHE 2804
Cdd:cd04717      3 QYRVGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWFYRPEETfhEPTRKFYK 60
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
2732-2868 2.89e-06

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: 49.39  E-value: 2.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2732 KGKARKLFYKAIVRGKEMIRIGDCAVFLSA-GRPnlPYIGRIQSMWESWGNNMVVRVKWFYHPEETspgkqfhegqhwDQ 2810
Cdd:cd04713      3 KGKKKKCHYTSFEKDGNKYRLEDCVLLVPEdDQK--PYIAIIKDIYKQEEGSLKLEVQWLYRPEEI------------EK 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720413413 2811 KSGHSLPAAlrassqrkdfMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKK 2868
Cdd:cd04713     69 KKGGNWKAE----------DPRELFYSFHRDEVPAESVLHPCKVAFVPKGKQIPLRKG 116
Tudor_3 pfam18115
DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein ...
2160-2212 1.48e-05

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: 44.47  E-value: 1.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720413413 2160 TRIAAYWSQQYRCLYPGTVVRgllDLEDDGDLITVEFDDGDTGRIPLSHIRLL 2212
Cdd:pfam18115    1 NRVFALWKGKDRAYYPATCLG---TSGSGSQRYLVRFDDGTPTEVDSGQVRRL 50
Tudor_SF cd04508
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
2159-2211 1.03e-04

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.


Pssm-ID: 410449 [Multi-domain]  Cd Length: 47  Bit Score: 41.80  E-value: 1.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720413413 2159 GTRIAAYWSQQyRCLYPGTVVRGLLDLEddgdlITVEFDDGDTGRIPLSHIRL 2211
Cdd:cd04508      1 GDRVEAKWSDD-GQWYPATVVAVNDDGK-----YTVLFDDGNEEEVSEDDIRP 47
Tudor_SpCrb2-like_rpt1 cd20395
first Tudor domain found in Schizosaccharomyces pombe Cut5-repeat binding protein 2 (Crb2) and ...
2159-2212 1.10e-04

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: 41.96  E-value: 1.10e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720413413 2159 GTRIAAYWSQqYRCLYPGTVVrglldLEDDGDLITVEFDDGDTGRIPLSHIRLL 2212
Cdd:cd20395      1 PTRVLAFWKG-DGNYYPATIV-----GPVSSSAYKVQFDDGTSSSVPPTQIRRL 48
BAH_MTA cd04709
BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The ...
2749-2894 3.92e-04

BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The Metastasis-associated protein MTA1 is part of the NURD (nucleosome remodeling and deacetylating) complex and plays a role in cellular transformation and metastasis. 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: 240060  Cd Length: 164  Bit Score: 43.53  E-value: 3.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2749 MIRIGDCAVFLSAgrPNLPY-IGRIQSMWESWGNNMVVRVKWFYHPEETSPgkqfHEGQHWDQKSGHSLPAALRASS-QR 2826
Cdd:cd04709      3 MYRVGDYVYFESS--PNNPYlIRRIEELNKTARGHVEAKVVCYYRRRDIPD----SLYQLADQHRRELEEKSDDLTPkQR 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720413413 2827 KDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKKYQDSegLYYLAGtYEPTTGMIFSTDG 2894
Cdd:cd04709     77 HQLRHRELFLSRQVETLPATHIRGKCSVTLLNDTESARSYLAREDT--FFYSLV-YDPEQKTLLADQG 141
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2213-2427 1.32e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2213 PPDYKIQCAEPSPALLVPSAKRRSRKTSKDTGEVKEGAATGPQEATGGKARgrgRKPSTKA-KADRAVVLEEGAATNEVP 2291
Cdd:PRK12323   375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPAR---RSPAPEAlAAARQASARGPGGAPAPA 451
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2292 SAPLALEPISTPNSKKSTPEPVDKRARAPKARSISAQPSPVP---PTFSSCPA--PEPFGELPTPATAPLVTMPVTMPAT 2366
Cdd:PRK12323   452 PAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADddpPPWEELPPefASPAPAQPDAAPAGWVAESIPDPAT 531
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720413413 2367 RPKPKKARAAEGSGAKGPRRPgeddellVKLDHEGVMSPKSKKAKEALLlrEDPGPGGWPE 2427
Cdd:PRK12323   532 ADPDDAFETLAPAPAAAPAPR-------AAAATEPVVAPRPPRASASGL--PDMFDGDWPA 583
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
2222-2472 2.51e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2222 EPSPALLVPSAKRRSRKTSKDTGEVKEGAATGPQEATGGKARGRGRKPSTKAKADRAVVLEEGAATNEVPSAPLALEPIS 2301
Cdd:PHA03307   219 SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSP 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2302 TPNSKKSTPEPvdkrARAPKARSISAQPSPVPP-TFSSCPAPEPFGELPTPATAPLVTMPVTMPATRPKPKKARAAEGSG 2380
Cdd:PHA03307   299 SPSSPGSGPAP----SSPRASSSSSSSRESSSSsTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2381 AKGPRRPGEDDEllvkldhegvmSPKSKKAKEALLLRED---PGPGGWPESTGLlslgsySPAVGSSEPKATWPkglDGD 2457
Cdd:PHA03307   375 PSSPAASAGRPT-----------RRRARAAVAGRARRRDatgRFPAGRPRPSPL------DAGAASGAFYARYP---LLT 434
                          250
                   ....*....|....*
gi 1720413413 2458 LTQEPGPGLPLEDPG 2472
Cdd:PHA03307   435 PSGEPWPGSPPPPPG 449
PHA03247 PHA03247
large tegument protein UL36; Provisional
2222-2477 4.43e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 4.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2222 EPSPALLVPS-------AKRRSRKTSKDTGEVKEGAATGPQEATGGKARGRGRKPST--KAKADRAVVLEEGAATNEVPS 2292
Cdd:PHA03247  2709 EPAPHALVSAtplppgpAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGppAPAPPAAPAAGPPRRLTRPAV 2788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2293 APLALEPISTPNSKKSTPEPVDKRARAPKARSISAQPSPVPPTFSSCPAPEPFGELPTPATAPL---------------V 2357
Cdd:PHA03247  2789 ASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLggsvapggdvrrrppS 2868
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2358 TMPVTMPATRPKPKKARAAEGSGAK----------GPRRPGEDDELLVKLDHEGVMSPKSKKAKEALLLREDPGPggwPE 2427
Cdd:PHA03247  2869 RSPAAKPAAPARPPVRRLARPAVSRstesfalppdQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPL---AP 2945
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2428 STGLLSLGSYSPAVGSSEPKATWPKGLDGDLTQEPGPGLPLEDPGNSKNP 2477
Cdd:PHA03247  2946 TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPP 2995
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
2254-2393 5.31e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.39  E-value: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2254 PQEATGGKARGRGRKPSTKAKADRAVVLEEGAATNEVPSAPlalepisTPNSKKSTPEPVDKRARAPKARSISAQPSPVP 2333
Cdd:PRK14951   366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAA-------PAAAASAPAAPPAAAPPAPVAAPAAAAPAAAP 438
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 2334 PTFSSCPAPEPFgeLPTPATAPLVTMPVTMPATRPKPKKARAAEGSGAKGPRRPGEDDEL 2393
Cdd:PRK14951   439 AAAPAAVALAPA--PPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEGDV 496
PHA03247 PHA03247
large tegument protein UL36; Provisional
997-1306 9.83e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 9.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413  997 PFQALFTDIPPRYPFQALPPhyGRPYPFLLQPAAASDADglAPDVPLPADGPERLALSPEDKPICLSPSkiPEPPRDSPE 1076
Cdd:PHA03247  2551 PPPPLPPAAPPAAPDRSVPP--PRPAPRPSEPAVTSRAR--RPDAPPQSARPRAPVDDRGDPRGPAPPS--PLPPDTHAP 2624
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 1077 EEQLADREVKAEvEDIEEGPTELPPLESPLALPVPeTMVAVSPAGGCGGSPLEAQAlSTAGPGCRE-PSEVSDFAQVAEP 1155
Cdd:PHA03247  2625 DPPPPSPSPAAN-EPDPHPPPTVPPPERPRDDPAP-GRVSRPRRARRLGRAAQASS-PPQRPRRRAaRPTVGSLTSLADP 2701
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 1156 QIElPSKTEHRMTALELGTQLTPEPLVETKEEPVEVPLDVPMEEPTTEAGPED-----------------------SLPQ 1212
Cdd:PHA03247  2702 PPP-PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGparparppttagppapappaapaAGPP 2780
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413413 1213 PSLTEPQ-PSLELSDCDLPVPEgqclnleAQEAVPAPASTCYLEETHSESLLPGLDDPLAGMNALAAAAELPQARPLPSL 1291
Cdd:PHA03247  2781 RRLTRPAvASLSESRESLPSPW-------DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG 2853
                          330
                   ....*....|....*
gi 1720413413 1292 GPGVPAGEKLDTAPS 1306
Cdd:PHA03247  2854 GSVAPGGDVRRRPPS 2868
 
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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