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Conserved domains on  [gi|1958668541|ref|XP_038945301|]
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trinucleotide repeat-containing gene 18 protein isoform X3 [Rattus norvegicus]

Protein Classification

Tudor_SF and BAH_BAHCC1 domain-containing protein( domain architecture ID 10248537)

protein containing domains Tudor_SF, PHA03307, and BAH_BAHCC1

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. ...
 2762-2906 4.97e-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: 4.97e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2762 KEMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKqfhegqhwdqksghnlpaalrassqR 2841
Cdd:cd04714      1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGR-------------------------K 55

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958668541 2842 KDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLK-TKKYQDSEGLYYLAGTYEPTTGMIFS 2906
Cdd:cd04714     56 PNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYERLARvKKKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_SF super family cl02573
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 2166-2232 9.33e-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: 9.33e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958668541 2166 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYKI 2232
Cdd:cd20469      1 SVRFLPEGTRVCAYWSQQYRCLYPGTVVKGSPDPEEDDDLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 2236-2486 1.03e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2236 EPSPALLVPSAKRRSRKTSKDTGEGKEGAATGPQEATGGKARGRGRKPSTKAKADRAVVLEEGAATNELPSAPLALEPVS 2315
Cdd:PHA03307   219 SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSP 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2316 TPNSKKSTPEPvdkrARAPKARSVSVQPSPGPP-TFSSCPAPEPFGELPTPATAPLVTMPVTMPATRPKPKKARATEGSG 2394
Cdd:PHA03307   299 SPSSPGSGPAP----SSPRASSSSSSSRESSSSsTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2395 AKGPRRPGEddellvkldhegvmSPKSKKAKEALllredPGPGAWPESTGLL--SLGSYSPTVGSSEPKATWPKGLDGDL 2472
Cdd:PHA03307   375 PSSPAASAG--------------RPTRRRARAAV-----AGRARRRDATGRFpaGRPRPSPLDAGAASGAFYARYPLLTP 435

                          250
                   ....*....|....
gi 1958668541 2473 TQEPGPGLPLEDPG 2486
Cdd:PHA03307   436 SGEPWPGSPPPPPG 449
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 383-641 9.32e-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: 9.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541  383 RAREREPGRPGVLQGPPGSPRlerPEVLREKSSVIRSLKRPPPSDGPPAARSSRSSPDARAYLPPKElLKPEADPRPCER 462
Cdd:PHA03247  2664 PRRARRLGRAAQASSPPQRPR---RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAA-ARQASPALPAAP 2739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541  463 APRGPSSSAAQQAAklfglePSRPPGPehkwkPFELGNFATTQMAVLAAQHHHASRAEEEAAVATASKKAYLDPGGAMPR 542
Cdd:PHA03247  2740 APPAVPAGPATPGG------PARPARP-----PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPP 2808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541  543 ASATCgrPGADLHSAAAHGPGEASAmQSLIKYSGSFAREAVAVRPGGCGKKSPFGGLGTMKP--EPIPTSAGPPRAQA-R 619
Cdd:PHA03247  2809 AAVLA--PAAALPPAASPAGPLPPP-TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPsrSPAAKPAAPARPPVrR 2885

                          250       260
                   ....*....|....*....|...
gi 1958668541  620 LTHPGVPTAGGGRQLKRD-PERP 641
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDqPERP 2908
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 2762-2906 4.97e-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: 4.97e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2762 KEMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKqfhegqhwdqksghnlpaalrassqR 2841
Cdd:cd04714      1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGR-------------------------K 55

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958668541 2842 KDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLK-TKKYQDSEGLYYLAGTYEPTTGMIFS 2906
Cdd:cd04714     56 PNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYERLARvKKKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_TNRC18 cd20469
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ...
 2166-2232 9.33e-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: 9.33e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958668541 2166 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYKI 2232
Cdd:cd20469      1 SVRFLPEGTRVCAYWSQQYRCLYPGTVVKGSPDPEEDDDLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
BAH smart00439
Bromo adjacent homology domain;
2764-2902 1.75e-13

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 69.24  E-value: 1.75e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541  2764 MIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNN--MVVRVKWFYHPEETSPGKQFHegqhwdqksghnlpaalrassqr 2841
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAAL----------------------- 57

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958668541  2842 kdFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQmLKTKKYQDSEGLYYLAGTYEPTTG 2902
Cdd:smart00439   58 --FDKNEVFLSDEYDTVPLSDIIGKCNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKG 115
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 2763-2902 2.53e-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: 60.40  E-value: 2.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2763 EMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMV-VRVKWFYHPEETSpgkqfhegqhwdqksgHNLPAAlrassqr 2841
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETV----------------HRAGKA------- 57

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958668541 2842 kdFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKKyqDSEGLYYLAGTYEPTTG 2902
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 ...
 2174-2226 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 1958668541 2174 TRIAAYWSQQYRCLYPGTVVRgllDLEDDGDLITVEFDDGDTGRIPLSHIRLL 2226
Cdd:pfam18115    1 NRVFALWKGKDRAYYPATCLG---TSGSGSQRYLVRFDDGTPTEVDSGQVRRL 50
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 2236-2486 1.03e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2236 EPSPALLVPSAKRRSRKTSKDTGEGKEGAATGPQEATGGKARGRGRKPSTKAKADRAVVLEEGAATNELPSAPLALEPVS 2315
Cdd:PHA03307   219 SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSP 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2316 TPNSKKSTPEPvdkrARAPKARSVSVQPSPGPP-TFSSCPAPEPFGELPTPATAPLVTMPVTMPATRPKPKKARATEGSG 2394
Cdd:PHA03307   299 SPSSPGSGPAP----SSPRASSSSSSSRESSSSsTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2395 AKGPRRPGEddellvkldhegvmSPKSKKAKEALllredPGPGAWPESTGLL--SLGSYSPTVGSSEPKATWPKGLDGDL 2472
Cdd:PHA03307   375 PSSPAASAG--------------RPTRRRARAAV-----AGRARRRDATGRFpaGRPRPSPLDAGAASGAFYARYPLLTP 435

                          250
                   ....*....|....
gi 1958668541 2473 TQEPGPGLPLEDPG 2486
Cdd:PHA03307   436 SGEPWPGSPPPPPG 449
PHA03247 PHA03247
large tegument protein UL36; Provisional
 383-641 9.32e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 9.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541  383 RAREREPGRPGVLQGPPGSPRlerPEVLREKSSVIRSLKRPPPSDGPPAARSSRSSPDARAYLPPKElLKPEADPRPCER 462
Cdd:PHA03247  2664 PRRARRLGRAAQASSPPQRPR---RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAA-ARQASPALPAAP 2739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541  463 APRGPSSSAAQQAAklfglePSRPPGPehkwkPFELGNFATTQMAVLAAQHHHASRAEEEAAVATASKKAYLDPGGAMPR 542
Cdd:PHA03247  2740 APPAVPAGPATPGG------PARPARP-----PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPP 2808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541  543 ASATCgrPGADLHSAAAHGPGEASAmQSLIKYSGSFAREAVAVRPGGCGKKSPFGGLGTMKP--EPIPTSAGPPRAQA-R 619
Cdd:PHA03247  2809 AAVLA--PAAALPPAASPAGPLPPP-TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPsrSPAAKPAAPARPPVrR 2885

                          250       260
                   ....*....|....*....|...
gi 1958668541  620 LTHPGVPTAGGGRQLKRD-PERP 641
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDqPERP 2908
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 2762-2906 4.97e-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: 4.97e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2762 KEMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKqfhegqhwdqksghnlpaalrassqR 2841
Cdd:cd04714      1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGR-------------------------K 55

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958668541 2842 KDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLK-TKKYQDSEGLYYLAGTYEPTTGMIFS 2906
Cdd:cd04714     56 PNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYERLARvKKKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_TNRC18 cd20469
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ...
 2166-2232 9.33e-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: 9.33e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958668541 2166 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYKI 2232
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 ...
 2166-2231 9.12e-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: 9.12e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958668541 2166 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDD-GDLITVEFDDGDTGRIPLSHIRLLPPDYK 2231
Cdd:cd20397      1 SVEYLPPGTRVCAYWSQQYRCLYPGTVISGEPDSEDSqEGKVPVEFDDGDSGKIPLSDIRLLPPDYP 67
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
 2164-2231 1.23e-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: 99.11  E-value: 1.23e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2164 PASTRFLPQGTRIAAYWSQQYRCLYPGTVVR--GLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYK 2231
Cdd:cd20470      1 PQSSRQLPPGTRVCAYWSQKSRCLYPGNVVRgsSGIDEEDDEDSVMVEFDDGDRGRISVSNIRLLPPDYK 70
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 2762-2902 2.86e-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: 2.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2762 KEMIRIGDCAVFLSAG--RPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKQFHEGqhwdqksghnlpaalrass 2839
Cdd:cd04370      1 GITYEVGDSVYVEPDDsiKSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPFAL------------------- 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958668541 2840 qrkdfmERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMlKTKKYQDSEGLYYLAGTYEPTTG 2902
Cdd:cd04370     62 ------RRELFLSDHLDEIPVESIIGKCKVLFVSEFEGL-KQRPNKIDTDDFFCRLAYDPTTK 117
BAH smart00439
Bromo adjacent homology domain;
2764-2902 1.75e-13

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 69.24  E-value: 1.75e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541  2764 MIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNN--MVVRVKWFYHPEETSPGKQFHegqhwdqksghnlpaalrassqr 2841
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAAL----------------------- 57

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958668541  2842 kdFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQmLKTKKYQDSEGLYYLAGTYEPTTG 2902
Cdd:smart00439   58 --FDKNEVFLSDEYDTVPLSDIIGKCNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKG 115
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 2763-2902 2.53e-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: 60.40  E-value: 2.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2763 EMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMV-VRVKWFYHPEETSpgkqfhegqhwdqksgHNLPAAlrassqr 2841
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETV----------------HRAGKA------- 57

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958668541 2842 kdFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKKyqDSEGLYYLAGTYEPTTG 2902
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 ...
 2764-2819 1.37e-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: 1.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958668541 2764 MIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEET--SPGKQFHE 2819
Cdd:cd04717      3 QYRVGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWFYRPEETfhEPTRKFYK 60
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 2747-2883 1.05e-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: 50.54  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2747 KGKARKLFYKAIVRGKEMIRIGDCAVFLSA-GRPnlPYIGRIQSMWESWGNNMVVRVKWFYHPEETspgkqfhegqhwDQ 2825
Cdd:cd04713      3 KGKKKKCHYTSFEKDGNKYRLEDCVLLVPEdDQK--PYIAIIKDIYKQEEGSLKLEVQWLYRPEEI------------EK 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958668541 2826 KSGHNLPAAlrassqrkdfMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKK 2883
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 ...
 2174-2226 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 1958668541 2174 TRIAAYWSQQYRCLYPGTVVRgllDLEDDGDLITVEFDDGDTGRIPLSHIRLL 2226
Cdd:pfam18115    1 NRVFALWKGKDRAYYPATCLG---TSGSGSQRYLVRFDDGTPTEVDSGQVRRL 50
Tudor_SF cd04508
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 2173-2225 1.04e-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: 1.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958668541 2173 GTRIAAYWSQQyRCLYPGTVVRGLLDLEddgdlITVEFDDGDTGRIPLSHIRL 2225
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 ...
 2173-2226 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 1958668541 2173 GTRIAAYWSQqYRCLYPGTVVrglldLEDDGDLITVEFDDGDTGRIPLSHIRLL 2226
Cdd:cd20395      1 PTRVLAFWKG-DGNYYPATIV-----GPVSSSAYKVQFDDGTSSSVPPTQIRRL 48
BAH_MTA cd04709
BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The ...
 2764-2909 4.86e-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: 43.15  E-value: 4.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2764 MIRIGDCAVFLSAgrPNLPY-IGRIQSMWESWGNNMVVRVKWFYHPEETSPgkqfHEGQHWDQKSgHNLPAALRASS--Q 2840
Cdd:cd04709      3 MYRVGDYVYFESS--PNNPYlIRRIEELNKTARGHVEAKVVCYYRRRDIPD----SLYQLADQHR-RELEEKSDDLTpkQ 75

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958668541 2841 RKDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKKYQDSegLYYLAGtYEPTTGMIFSTDG 2909
Cdd:cd04709     76 RHQLRHRELFLSRQVETLPATHIRGKCSVTLLNDTESARSYLAREDT--FFYSLV-YDPEQKTLLADQG 141
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 2236-2486 1.03e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2236 EPSPALLVPSAKRRSRKTSKDTGEGKEGAATGPQEATGGKARGRGRKPSTKAKADRAVVLEEGAATNELPSAPLALEPVS 2315
Cdd:PHA03307   219 SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSP 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2316 TPNSKKSTPEPvdkrARAPKARSVSVQPSPGPP-TFSSCPAPEPFGELPTPATAPLVTMPVTMPATRPKPKKARATEGSG 2394
Cdd:PHA03307   299 SPSSPGSGPAP----SSPRASSSSSSSRESSSSsTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2395 AKGPRRPGEddellvkldhegvmSPKSKKAKEALllredPGPGAWPESTGLL--SLGSYSPTVGSSEPKATWPKGLDGDL 2472
Cdd:PHA03307   375 PSSPAASAG--------------RPTRRRARAAV-----AGRARRRDATGRFpaGRPRPSPLDAGAASGAFYARYPLLTP 435

                          250
                   ....*....|....
gi 1958668541 2473 TQEPGPGLPLEDPG 2486
Cdd:PHA03307   436 SGEPWPGSPPPPPG 449
PHA03247 PHA03247
large tegument protein UL36; Provisional
 2226-2400 3.80e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2226 LPPDYKIQCAEPSPALLVPSAkrrsrkTSKDTGEGKEGAATGPQEATGGKARGRG--RKPSTKAKADRAVVLEEGAA--- 2300
Cdd:PHA03247  2818 LPPAASPAGPLPPPTSAQPTA------PPPPPGPPPPSLPLGGSVAPGGDVRRRPpsRSPAAKPAAPARPPVRRLARpav 2891

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2301 ---TNELPSAPLALEPVSTPNSK---KSTPEPVDKRARAPKARSVSVQPSPGPPTFSSCPAPEPFGELPTPATAPLVTMP 2374
Cdd:PHA03247  2892 srsTESFALPPDQPERPPQPQAPpppQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGR 2971

                          170       180
                   ....*....|....*....|....*..
gi 1958668541 2375 VTMPATR-PKPKKARATEGSGAKGPRR 2400
Cdd:PHA03247  2972 VAVPRFRvPQPAPSREAPASSTPPLTG 2998
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2260-2435 3.99e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.94  E-value: 3.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2260 GKEGAATGPQEAtggkARGRGRKPSTKAKADRAVVLEEGAATNELPSAPLALEPVSTPNSKKSTPEPvdkrarAPKARSV 2339
Cdd:PRK12323   366 GQSGGGAGPATA----AAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSP------APEALAA 435

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2340 SVQPSPGPPTFSSCPAPEPfGELPTPATAPLVTMPVTMPATRPKPKKARATEGSGAKGPRRPGEDDELLVKLDHEGVMSP 2419
Cdd:PRK12323   436 ARQASARGPGGAPAPAPAP-AAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQP 514

                          170
                   ....*....|....*.
gi 1958668541 2420 KSKKAKEALLLREDPG 2435
Cdd:PRK12323   515 DAAPAGWVAESIPDPA 530
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2227-2441 8.13e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.79  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2227 PPDYKIQCAEPSPALLVPSAKRRSRKTSKDTGEGKEGAATGPQEATGGKARgrgRKPSTKA-KADRAVVLEEGAATNELP 2305
Cdd:PRK12323   375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPAR---RSPAPEAlAAARQASARGPGGAPAPA 451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541 2306 SAPLALEPVSTPNSKKSTPEPVDKRARAPKARSVSVQPSP---GPPTFSSCPA--PEPFGELPTPATAPLVTMPVTMPAT 2380
Cdd:PRK12323   452 PAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPaddDPPPWEELPPefASPAPAQPDAAPAGWVAESIPDPAT 531

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958668541 2381 RPKPKKARATEGSGAKGPRRPgeddellVKLDHEGVMSPKSKKAKEALLlrEDPGPGAWPE 2441
Cdd:PRK12323   532 ADPDDAFETLAPAPAAAPAPR-------AAAATEPVVAPRPPRASASGL--PDMFDGDWPA 583
PHA03247 PHA03247
large tegument protein UL36; Provisional
 383-641 9.32e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 9.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541  383 RAREREPGRPGVLQGPPGSPRlerPEVLREKSSVIRSLKRPPPSDGPPAARSSRSSPDARAYLPPKElLKPEADPRPCER 462
Cdd:PHA03247  2664 PRRARRLGRAAQASSPPQRPR---RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAA-ARQASPALPAAP 2739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541  463 APRGPSSSAAQQAAklfglePSRPPGPehkwkPFELGNFATTQMAVLAAQHHHASRAEEEAAVATASKKAYLDPGGAMPR 542
Cdd:PHA03247  2740 APPAVPAGPATPGG------PARPARP-----PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPP 2808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668541  543 ASATCgrPGADLHSAAAHGPGEASAmQSLIKYSGSFAREAVAVRPGGCGKKSPFGGLGTMKP--EPIPTSAGPPRAQA-R 619
Cdd:PHA03247  2809 AAVLA--PAAALPPAASPAGPLPPP-TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPsrSPAAKPAAPARPPVrR 2885

                          250       260
                   ....*....|....*....|...
gi 1958668541  620 LTHPGVPTAGGGRQLKRD-PERP 641
Cdd:PHA03247  2886 LARPAVSRSTESFALPPDqPERP 2908
 
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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