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Conserved domains on  [gi|442620527|ref|NP_732790|]
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winged eye, isoform D [Drosophila melanogaster]

Protein Classification

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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. ...
 1520-1642 1.43e-58

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: 197.62  E-value: 1.43e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527 1520 KETITVGDSAVFLSTGRPDRPYIGRIESMWETTTGNKVVRVAWFYHPEETTGCPKL-KFPGALFESPHEDENDVQTISHR 1598
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPnHGEKELFASDHQDENSVQTIEHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 442620527 1599 CEVLQFGSYFEKFGADSKqyqsIYDNNDTYYLAGHYNPRLQVLK 1642
Cdd:cd04714    81 CYVLTFAEYERLARVKKK----PQDGVDFYYCAGTYNPDTGMLK 120
Tudor_BAHCC1-like cd20397
Tudor domain found in the BAH and coiled-coil domain-containing protein 1 (BAHCC1) family; The ...
 1189-1265 2.44e-31

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: 117.43  E-value: 2.44e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620527 1189 SVESVPVGTRLCAYWSQQYRCLYPGRAIDSEQVVdgtassatnaATTAPDFVSVEFDDGDSGRIRLQNIRMLLSDYP 1265
Cdd:cd20397     1 SVEYLPPGTRVCAYWSQQYRCLYPGTVISGEPDS----------EDSQEGKVPVEFDDGDSGKIPLSDIRLLPPDYP 67
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 484-811 3.41e-09

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.26  E-value: 3.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527  484 PTPPTSATMEPSSLGHATPHHLFQSGAMATPTPALLNLSMHGNGGELPAATPLPAVSDEAAlnyklhAPLTPQTPP---- 559
Cdd:PHA03247 2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA------PPAAPAAGPprrl 2783

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527  560 -RLADIPVSGSTQLLPQMQDVNIQTdTPVCSEDESFPGSAKPQDPAaeafPPPTHVQPLELTKPSEASHTQPTECHTQTE 638
Cdd:PHA03247 2784 tRPAVASLSESRESLPSPWDPADPP-AAVLAPAAALPPAASPAGPL----PPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527  639 PSDI---PSASQEESAEQTPPEP-IETMTQATQADQTSPEDLTGLELlsnistNSKPLVRVKQEPVEHIE-QPAPQPQPV 713
Cdd:PHA03247 2859 GGDVrrrPPSRSPAAKPAAPARPpVRRLARPAVSRSTESFALPPDQP------ERPPQPQAPPPPQPQPQpPPPPQPQPP 2932

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527  714 NIMPSEPTLPMPPMLEMEPTSEREPLGGLKLLCALAEQRI---QEEVVQGSSLFATPSSRTPTPT------------SLA 778
Cdd:PHA03247 2933 PPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVavpRFRVPQPAPSREAPASSTPPLTghslsrvsswasSLA 3012

                         330       340       350
                  ....*....|....*....|....*....|...
gi 442620527  779 LGTTAATPPIFEAKSCYAFGQSQGSVFPSSTSS 811
Cdd:PHA03247 3013 LHEETDPPPVSLKQTLWPPDDTEDSDADSLFDS 3045
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 1520-1642 1.43e-58

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: 197.62  E-value: 1.43e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527 1520 KETITVGDSAVFLSTGRPDRPYIGRIESMWETTTGNKVVRVAWFYHPEETTGCPKL-KFPGALFESPHEDENDVQTISHR 1598
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPnHGEKELFASDHQDENSVQTIEHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 442620527 1599 CEVLQFGSYFEKFGADSKqyqsIYDNNDTYYLAGHYNPRLQVLK 1642
Cdd:cd04714    81 CYVLTFAEYERLARVKKK----PQDGVDFYYCAGTYNPDTGMLK 120
Tudor_BAHCC1-like cd20397
Tudor domain found in the BAH and coiled-coil domain-containing protein 1 (BAHCC1) family; The ...
 1189-1265 2.44e-31

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: 117.43  E-value: 2.44e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620527 1189 SVESVPVGTRLCAYWSQQYRCLYPGRAIDSEQVVdgtassatnaATTAPDFVSVEFDDGDSGRIRLQNIRMLLSDYP 1265
Cdd:cd20397     1 SVEYLPPGTRVCAYWSQQYRCLYPGTVISGEPDS----------EDSQEGKVPVEFDDGDSGKIPLSDIRLLPPDYP 67
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 1521-1642 7.58e-18

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: 81.20  E-value: 7.58e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527  1521 ETITVGDSAVFLSTGRPDRPYIGRIESMWETTTGNKV-VRVAWFYHPEETTGCPKLKF-PGALFESPHEDENDVQTISHR 1598
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETVHRAGKAFnKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 442620527  1599 CEVLQFGSYFekfgadSKQYQSIyDNNDTYYLAGHYNPRLQVLK 1642
Cdd:pfam01426   81 CSVLHKSDLE------SLDPYKI-KEPDDFFCELLYDPKTKSFK 117
BAH smart00439
Bromo adjacent homology domain;
1522-1636 1.94e-16

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 76.95  E-value: 1.94e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527   1522 TITVGDSAVFLSTGRPDRPYIGRIESMWETTTGN--KVVRVAWFYHPEETTGCP-KLKFPGALFESPHEDENDVQTISHR 1598
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKaALFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 442620527   1599 CEVLQFGSYFEkfgadsKQYQSIYDNNDTYYLAGHYNP 1636
Cdd:smart00439   81 CNVLYKSDYPG------LRPEGSIGEPDVFFCESAYDP 112
PHA03247 PHA03247
large tegument protein UL36; Provisional
 484-811 3.41e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.26  E-value: 3.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527  484 PTPPTSATMEPSSLGHATPHHLFQSGAMATPTPALLNLSMHGNGGELPAATPLPAVSDEAAlnyklhAPLTPQTPP---- 559
Cdd:PHA03247 2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA------PPAAPAAGPprrl 2783

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527  560 -RLADIPVSGSTQLLPQMQDVNIQTdTPVCSEDESFPGSAKPQDPAaeafPPPTHVQPLELTKPSEASHTQPTECHTQTE 638
Cdd:PHA03247 2784 tRPAVASLSESRESLPSPWDPADPP-AAVLAPAAALPPAASPAGPL----PPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527  639 PSDI---PSASQEESAEQTPPEP-IETMTQATQADQTSPEDLTGLELlsnistNSKPLVRVKQEPVEHIE-QPAPQPQPV 713
Cdd:PHA03247 2859 GGDVrrrPPSRSPAAKPAAPARPpVRRLARPAVSRSTESFALPPDQP------ERPPQPQAPPPPQPQPQpPPPPQPQPP 2932

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527  714 NIMPSEPTLPMPPMLEMEPTSEREPLGGLKLLCALAEQRI---QEEVVQGSSLFATPSSRTPTPT------------SLA 778
Cdd:PHA03247 2933 PPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVavpRFRVPQPAPSREAPASSTPPLTghslsrvsswasSLA 3012

                         330       340       350
                  ....*....|....*....|....*....|...
gi 442620527  779 LGTTAATPPIFEAKSCYAFGQSQGSVFPSSTSS 811
Cdd:PHA03247 3013 LHEETDPPPVSLKQTLWPPDDTEDSDADSLFDS 3045
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 484-726 1.10e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.07  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527   484 PTPPTSATMEPSSLGHATPHHLfqsgamATPTPallnLSMHGNGGELPAATPLPAVSDeaalnyklHAPLTPQTPPrlad 563
Cdd:pfam03154  357 PPPTTPIPQLPNPQSHKHPPHL------SGPSP----FQMNSNLPPPPALKPLSSLST--------HHPPSAHPPP---- 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527   564 ipvsgsTQLLPQMQDVNIQ-TDTPVCSEDESFPgsakpqdPAAEAFPPPTHVQPLELTKPSEASHTQPTECHTQTEPSDI 642
Cdd:pfam03154  415 ------LQLMPQSQQLPPPpAQPPVLTQSQSLP-------PPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGP 481

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527   643 PSASQEESAEQTPPEPIETMTQATqadqtspedltglelLSNISTNSKPLVRVKQEPVEHIEQPAPQPQPVNIMPSEPTL 722
Cdd:pfam03154  482 PTSTSSAMPGIQPPSSASVSSSGP---------------VPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTV 546


                   ....
gi 442620527   723 PMPP 726
Cdd:pfam03154  547 VNTP 550
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 1520-1642 1.43e-58

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: 197.62  E-value: 1.43e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527 1520 KETITVGDSAVFLSTGRPDRPYIGRIESMWETTTGNKVVRVAWFYHPEETTGCPKL-KFPGALFESPHEDENDVQTISHR 1598
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPnHGEKELFASDHQDENSVQTIEHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 442620527 1599 CEVLQFGSYFEKFGADSKqyqsIYDNNDTYYLAGHYNPRLQVLK 1642
Cdd:cd04714    81 CYVLTFAEYERLARVKKK----PQDGVDFYYCAGTYNPDTGMLK 120
Tudor_BAHCC1-like cd20397
Tudor domain found in the BAH and coiled-coil domain-containing protein 1 (BAHCC1) family; The ...
 1189-1265 2.44e-31

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: 117.43  E-value: 2.44e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620527 1189 SVESVPVGTRLCAYWSQQYRCLYPGRAIDSEQVVdgtassatnaATTAPDFVSVEFDDGDSGRIRLQNIRMLLSDYP 1265
Cdd:cd20397     1 SVEYLPPGTRVCAYWSQQYRCLYPGTVISGEPDS----------EDSQEGKVPVEFDDGDSGKIPLSDIRLLPPDYP 67
Tudor_TNRC18 cd20469
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ...
 1189-1266 1.39e-24

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: 98.26  E-value: 1.39e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620527 1189 SVESVPVGTRLCAYWSQQYRCLYPGraidseQVVDGTASSATNAattapDFVSVEFDDGDSGRIRLQNIRMLLSDYPI 1266
Cdd:cd20469     1 SVRFLPEGTRVCAYWSQQYRCLYPG------TVVKGSPDPEEDD-----DLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
 1187-1265 8.07e-22

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: 90.63  E-value: 8.07e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620527 1187 PKSVESVPVGTRLCAYWSQQYRCLYPGraidseQVVDGTASSATNaatTAPDFVSVEFDDGDSGRIRLQNIRMLLSDYP 1265
Cdd:cd20470     1 PQSSRQLPPGTRVCAYWSQKSRCLYPG------NVVRGSSGIDEE---DDEDSVMVEFDDGDRGRISVSNIRLLPPDYK 70
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 1520-1645 6.85e-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: 89.76  E-value: 6.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527 1520 KETITVGDSAVFL--STGRPDRPYIGRIESMWETTTGNKVVRVAWFYHPEETtgcPKLKFPGA----LFESPHEDENDVQ 1593
Cdd:cd04370     1 GITYEVGDSVYVEpdDSIKSDPPYIARIEELWEDTNGSKQVKVRWFYRPEET---PKGLSPFAlrreLFLSDHLDEIPVE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442620527 1594 TISHRCEVLQFGSYFEKFGADSKqyqsiyDNNDTYYLAGHYNPRLQVLKLQD 1645
Cdd:cd04370    78 SIIGKCKVLFVSEFEGLKQRPNK------IDTDDFFCRLAYDPTTKEFKALE 123
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 1521-1642 7.58e-18

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: 81.20  E-value: 7.58e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527  1521 ETITVGDSAVFLSTGRPDRPYIGRIESMWETTTGNKV-VRVAWFYHPEETTGCPKLKF-PGALFESPHEDENDVQTISHR 1598
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETVHRAGKAFnKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 442620527  1599 CEVLQFGSYFekfgadSKQYQSIyDNNDTYYLAGHYNPRLQVLK 1642
Cdd:pfam01426   81 CSVLHKSDLE------SLDPYKI-KEPDDFFCELLYDPKTKSFK 117
BAH smart00439
Bromo adjacent homology domain;
1522-1636 1.94e-16

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 76.95  E-value: 1.94e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527   1522 TITVGDSAVFLSTGRPDRPYIGRIESMWETTTGN--KVVRVAWFYHPEETTGCP-KLKFPGALFESPHEDENDVQTISHR 1598
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKaALFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 442620527   1599 CEVLQFGSYFEkfgadsKQYQSIYDNNDTYYLAGHYNP 1636
Cdd:smart00439   81 CNVLYKSDYPG------LRPEGSIGEPDVFFCESAYDP 112
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
 1525-1608 1.65e-12

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: 65.68  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527 1525 VGDSAVFLSTGRPDRPYIGRIESMWETTTGNKVVRVAWFYHPEETTGCPKLKF-PGALFESPHEDENDVQTISHRCEVLQ 1603
Cdd:cd04717     6 VGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWFYRPEETFHEPTRKFyKNEVFKSPLYETVPVEEIVGKCAVMD 85


                  ....*
gi 442620527 1604 FGSYF 1608
Cdd:cd04717    86 VKDYI 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
 484-811 3.41e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.26  E-value: 3.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527  484 PTPPTSATMEPSSLGHATPHHLFQSGAMATPTPALLNLSMHGNGGELPAATPLPAVSDEAAlnyklhAPLTPQTPP---- 559
Cdd:PHA03247 2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA------PPAAPAAGPprrl 2783

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527  560 -RLADIPVSGSTQLLPQMQDVNIQTdTPVCSEDESFPGSAKPQDPAaeafPPPTHVQPLELTKPSEASHTQPTECHTQTE 638
Cdd:PHA03247 2784 tRPAVASLSESRESLPSPWDPADPP-AAVLAPAAALPPAASPAGPL----PPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527  639 PSDI---PSASQEESAEQTPPEP-IETMTQATQADQTSPEDLTGLELlsnistNSKPLVRVKQEPVEHIE-QPAPQPQPV 713
Cdd:PHA03247 2859 GGDVrrrPPSRSPAAKPAAPARPpVRRLARPAVSRSTESFALPPDQP------ERPPQPQAPPPPQPQPQpPPPPQPQPP 2932

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527  714 NIMPSEPTLPMPPMLEMEPTSEREPLGGLKLLCALAEQRI---QEEVVQGSSLFATPSSRTPTPT------------SLA 778
Cdd:PHA03247 2933 PPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVavpRFRVPQPAPSREAPASSTPPLTghslsrvsswasSLA 3012

                         330       340       350
                  ....*....|....*....|....*....|...
gi 442620527  779 LGTTAATPPIFEAKSCYAFGQSQGSVFPSSTSS 811
Cdd:PHA03247 3013 LHEETDPPPVSLKQTLWPPDDTEDSDADSLFDS 3045
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 1505-1601 4.39e-09

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: 56.70  E-value: 4.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527 1505 KGRARKQFYKTIKRGKETITVGDSAVFLStgrPD--RPYIGRIESMWETTTGNKVVRVAWFYHPEETT----GCPKLKFP 1578
Cdd:cd04713     3 KGKKKKCHYTSFEKDGNKYRLEDCVLLVP---EDdqKPYIAIIKDIYKQEEGSLKLEVQWLYRPEEIEkkkgGNWKAEDP 79

                          90       100
                  ....*....|....*....|...
gi 442620527 1579 GALFESPHEDENDVQTISHRCEV 1601
Cdd:cd04713    80 RELFYSFHRDEVPAESVLHPCKV 102
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 1522-1613 1.29e-05

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: 46.28  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527 1522 TITVGDSaVFLSTGRPDRpYIGRIESMWETTTGNKVVRVAWFYHPEE--TTGCPKLKFPGALFESPHEDENDVQTISHRC 1599
Cdd:cd04721     7 TISVHDF-VYVLSEEEDR-YVAYIEDLYEDKKGSKMVKVRWFHTTDEvgAALSPDSVNPREIFLSPNLQVISVECIDGLA 84

                          90
                  ....*....|....
gi 442620527 1600 EVLQfGSYFEKFGA 1613
Cdd:cd04721    85 TVLT-REHYEKFQS 97
BAH_Orc1p_like cd04715
BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of ...
 1492-1620 2.88e-05

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: 45.96  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527 1492 WGwygtAYRKAGVKGRArKQFYKTIKRGKETITVGDSAVFLSTGrpDRPYIGRIESMWETTT--GNKVVRVAWFYHPEET 1569
Cdd:cd04715     4 WG----VKRGEGGKKKD-GQFYRSFTYDGVEYRLYDDVYVHNGD--SEPYIGKIIKIYETAIdsGKKKVKVIWFFRPSEI 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527 1570 ----TGCPKLKFpGALFESPHEDE-----NDVQTISHRCEVLQFGSYFEKFGADSKQYQS 1620
Cdd:cd04715    77 rmelKGEPKRHI-NEVFLACGRGEglaniNLLESIIGKCNVVCISEDFRNPQPSDGIPTS 135
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 484-726 1.10e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.07  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527   484 PTPPTSATMEPSSLGHATPHHLfqsgamATPTPallnLSMHGNGGELPAATPLPAVSDeaalnyklHAPLTPQTPPrlad 563
Cdd:pfam03154  357 PPPTTPIPQLPNPQSHKHPPHL------SGPSP----FQMNSNLPPPPALKPLSSLST--------HHPPSAHPPP---- 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527   564 ipvsgsTQLLPQMQDVNIQ-TDTPVCSEDESFPgsakpqdPAAEAFPPPTHVQPLELTKPSEASHTQPTECHTQTEPSDI 642
Cdd:pfam03154  415 ------LQLMPQSQQLPPPpAQPPVLTQSQSLP-------PPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGP 481

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527   643 PSASQEESAEQTPPEPIETMTQATqadqtspedltglelLSNISTNSKPLVRVKQEPVEHIEQPAPQPQPVNIMPSEPTL 722
Cdd:pfam03154  482 PTSTSSAMPGIQPPSSASVSSSGP---------------VPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTV 546


                   ....
gi 442620527   723 PMPP 726
Cdd:pfam03154  547 VNTP 550
BAH_Orc1p_animal cd04719
BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces ...
 1522-1603 1.57e-03

BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces cerevisiae Orc1p. Orc1 is part of the Yeast Sir1-origin recognition complex. The Orc1p BAH doman functions in epigenetic silencing. In vertebrates, a similar ORC protein complex exists, which has been shown essential for DNA replication in Xenopus laevis. 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: 240070  Cd Length: 128  Bit Score: 40.44  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527 1522 TITVGDSaVFLSTGRPDRPYIGRIESMWETTTGN---KVVRVAWFYHPEETtgcPKLK------FPGAL---FESPHEDE 1589
Cdd:cd04719     3 TIEVGDF-VLIEGEDADGPDVARILHLYEDGNEDddpKRAIVQWFSRPSEV---PKNKrkllgrEPHSQevfFYSRSSCD 78

                          90
                  ....*....|....*.
gi 442620527 1590 NDV--QTISHRCEVLQ 1603
Cdd:cd04719    79 NDIdaETIIGKVRVEP 94
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 437-787 2.83e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527   437 QTGIPSLLSLPPPtglkeeypmplalpPLVPLEAARDKEQALNLMRLPTPPTSatMEP-SSLGHATPHHLFQSGAMATPt 515
Cdd:pfam03154  177 QSGAASPPSPPPP--------------GTTQAATAGPTPSAPSVPPQGSPATS--QPPnQTQSTAAPHTLIQQTPTLHP- 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527   516 PALlnLSMHGNGGELPAATPLPAVSDEAALNYKLHAPLTP-----QTPPRLadIPVSGSTQLLPQMQDVNIQTDTPVCSE 590
Cdd:pfam03154  240 QRL--PSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPmphslQTGPSH--MQHPVPPQPFPLTPQSSQSQVPPGPSP 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527   591 DESFPGSAKPQDPAAEAFPP---PTHVQPLElTKPSEASHTQPTechTQTEPSDIPSA-SQEESAEQTPPEPIETMTQAT 666
Cdd:pfam03154  316 AAPGQSQQRIHTPPSQSQLQsqqPPREQPLP-PAPLSMPHIKPP---PTTPIPQLPNPqSHKHPPHLSGPSPFQMNSNLP 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620527   667 QADQTSPedltglelLSNISTNskplvrvkqepvehiEQPAPQPQPVNIMPSEPTLPMPPML--------EMEPTSEREP 738
Cdd:pfam03154  392 PPPALKP--------LSSLSTH---------------HPPSAHPPPLQLMPQSQQLPPPPAQppvltqsqSLPPPAASHP 448

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 442620527   739 LGGLKLLCALAEQRIQEEVVQGSSLFATPSSRTPTPTSLALgtTAATPP 787
Cdd:pfam03154  449 PTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAM--PGIQPP 495
 
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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