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Conserved domains on  [gi|442620531|ref|NP_732791|]
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winged eye, isoform F [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. ...
 1461-1583 1.38e-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: 1.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531 1461 KETITVGDSAVFLSTGRPDRPYIGRIESMWETTTGNKVVRVAWFYHPEETTGCPKL-KFPGALFESPHEDENDVQTISHR 1539
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPnHGEKELFASDHQDENSVQTIEHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 442620531 1540 CEVLQFGSYFEKFGADSKqyqsIYDNNDTYYLAGHYNPRLQVLK 1583
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 ...
 1139-1215 1.94e-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: 117.82  E-value: 1.94e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620531 1139 SVESVPVGTRLCAYWSQQYRCLYPGRAIDSEQVVdgtassatnaATTAPDFVSVEFDDGDSGRIRLQNIRMLLSDYP 1215
Cdd:cd20397     1 SVEYLPPGTRVCAYWSQQYRCLYPGTVISGEPDS----------EDSQEGKVPVEFDDGDSGKIPLSDIRLLPPDYP 67
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 434-761 2.88e-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: 2.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531  434 PTPPTSATMEPSSLGHATPHHLFQSGAMATPTPALLNLSMHGNGGELPAATPLPAVSDEAAlnyklhAPLTPQTPP---- 509
Cdd:PHA03247 2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA------PPAAPAAGPprrl 2783

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531  510 -RLADIPVSGSTQLLPQMQDVNIQTdTPVCSEDESFPGSAKPQDPAaeafPPPTHVQPLELTKPSEASHTQPTECHTQTE 588
Cdd:PHA03247 2784 tRPAVASLSESRESLPSPWDPADPP-AAVLAPAAALPPAASPAGPL----PPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531  589 PSDI---PSASQEESAEQTPPEP-IETMTQATQADQTSPEDLTGLELlsnistNSKPLVRVKQEPVEHIE-QPAPQPQPV 663
Cdd:PHA03247 2859 GGDVrrrPPSRSPAAKPAAPARPpVRRLARPAVSRSTESFALPPDQP------ERPPQPQAPPPPQPQPQpPPPPQPQPP 2932

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531  664 NIMPSEPTLPMPPMLEMEPTSEREPLGGLKLLCALAEQRI---QEEVVQGSSLFATPSSRTPTPT------------SLA 728
Cdd:PHA03247 2933 PPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVavpRFRVPQPAPSREAPASSTPPLTghslsrvsswasSLA 3012

                         330       340       350
                  ....*....|....*....|....*....|...
gi 442620531  729 LGTTAATPPIFEAKSCYAFGQSQGSVFPSSTSS 761
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. ...
 1461-1583 1.38e-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: 1.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531 1461 KETITVGDSAVFLSTGRPDRPYIGRIESMWETTTGNKVVRVAWFYHPEETTGCPKL-KFPGALFESPHEDENDVQTISHR 1539
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPnHGEKELFASDHQDENSVQTIEHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 442620531 1540 CEVLQFGSYFEKFGADSKqyqsIYDNNDTYYLAGHYNPRLQVLK 1583
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 ...
 1139-1215 1.94e-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: 117.82  E-value: 1.94e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620531 1139 SVESVPVGTRLCAYWSQQYRCLYPGRAIDSEQVVdgtassatnaATTAPDFVSVEFDDGDSGRIRLQNIRMLLSDYP 1215
Cdd:cd20397     1 SVEYLPPGTRVCAYWSQQYRCLYPGTVISGEPDS----------EDSQEGKVPVEFDDGDSGKIPLSDIRLLPPDYP 67
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 1462-1583 7.30e-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: 7.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531  1462 ETITVGDSAVFLSTGRPDRPYIGRIESMWETTTGNKV-VRVAWFYHPEETTGCPKLKF-PGALFESPHEDENDVQTISHR 1539
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETVHRAGKAFnKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 442620531  1540 CEVLQFGSYFekfgadSKQYQSIyDNNDTYYLAGHYNPRLQVLK 1583
Cdd:pfam01426   81 CSVLHKSDLE------SLDPYKI-KEPDDFFCELLYDPKTKSFK 117
BAH smart00439
Bromo adjacent homology domain;
1463-1577 1.87e-16

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 76.95  E-value: 1.87e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531   1463 TITVGDSAVFLSTGRPDRPYIGRIESMWETTTGN--KVVRVAWFYHPEETTGCP-KLKFPGALFESPHEDENDVQTISHR 1539
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKaALFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 442620531   1540 CEVLQFGSYFEkfgadsKQYQSIYDNNDTYYLAGHYNP 1577
Cdd:smart00439   81 CNVLYKSDYPG------LRPEGSIGEPDVFFCESAYDP 112
PHA03247 PHA03247
large tegument protein UL36; Provisional
 434-761 2.88e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.26  E-value: 2.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531  434 PTPPTSATMEPSSLGHATPHHLFQSGAMATPTPALLNLSMHGNGGELPAATPLPAVSDEAAlnyklhAPLTPQTPP---- 509
Cdd:PHA03247 2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA------PPAAPAAGPprrl 2783

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531  510 -RLADIPVSGSTQLLPQMQDVNIQTdTPVCSEDESFPGSAKPQDPAaeafPPPTHVQPLELTKPSEASHTQPTECHTQTE 588
Cdd:PHA03247 2784 tRPAVASLSESRESLPSPWDPADPP-AAVLAPAAALPPAASPAGPL----PPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531  589 PSDI---PSASQEESAEQTPPEP-IETMTQATQADQTSPEDLTGLELlsnistNSKPLVRVKQEPVEHIE-QPAPQPQPV 663
Cdd:PHA03247 2859 GGDVrrrPPSRSPAAKPAAPARPpVRRLARPAVSRSTESFALPPDQP------ERPPQPQAPPPPQPQPQpPPPPQPQPP 2932

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531  664 NIMPSEPTLPMPPMLEMEPTSEREPLGGLKLLCALAEQRI---QEEVVQGSSLFATPSSRTPTPT------------SLA 728
Cdd:PHA03247 2933 PPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVavpRFRVPQPAPSREAPASSTPPLTghslsrvsswasSLA 3012

                         330       340       350
                  ....*....|....*....|....*....|...
gi 442620531  729 LGTTAATPPIFEAKSCYAFGQSQGSVFPSSTSS 761
Cdd:PHA03247 3013 LHEETDPPPVSLKQTLWPPDDTEDSDADSLFDS 3045
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 434-676 1.06e-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: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531   434 PTPPTSATMEPSSLGHATPHHLfqsgamATPTPallnLSMHGNGGELPAATPLPAVSDeaalnyklHAPLTPQTPPrlad 513
Cdd:pfam03154  357 PPPTTPIPQLPNPQSHKHPPHL------SGPSP----FQMNSNLPPPPALKPLSSLST--------HHPPSAHPPP---- 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531   514 ipvsgsTQLLPQMQDVNIQ-TDTPVCSEDESFPgsakpqdPAAEAFPPPTHVQPLELTKPSEASHTQPTECHTQTEPSDI 592
Cdd:pfam03154  415 ------LQLMPQSQQLPPPpAQPPVLTQSQSLP-------PPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGP 481

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531   593 PSASQEESAEQTPPEPIETMTQATqadqtspedltglelLSNISTNSKPLVRVKQEPVEHIEQPAPQPQPVNIMPSEPTL 672
Cdd:pfam03154  482 PTSTSSAMPGIQPPSSASVSSSGP---------------VPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTV 546


                   ....
gi 442620531   673 PMPP 676
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. ...
 1461-1583 1.38e-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: 1.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531 1461 KETITVGDSAVFLSTGRPDRPYIGRIESMWETTTGNKVVRVAWFYHPEETTGCPKL-KFPGALFESPHEDENDVQTISHR 1539
Cdd:cd04714     1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPnHGEKELFASDHQDENSVQTIEHK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 442620531 1540 CEVLQFGSYFEKFGADSKqyqsIYDNNDTYYLAGHYNPRLQVLK 1583
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 ...
 1139-1215 1.94e-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: 117.82  E-value: 1.94e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620531 1139 SVESVPVGTRLCAYWSQQYRCLYPGRAIDSEQVVdgtassatnaATTAPDFVSVEFDDGDSGRIRLQNIRMLLSDYP 1215
Cdd:cd20397     1 SVEYLPPGTRVCAYWSQQYRCLYPGTVISGEPDS----------EDSQEGKVPVEFDDGDSGKIPLSDIRLLPPDYP 67
Tudor_TNRC18 cd20469
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ...
 1139-1216 1.11e-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: 98.65  E-value: 1.11e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620531 1139 SVESVPVGTRLCAYWSQQYRCLYPGraidseQVVDGTASSATNAattapDFVSVEFDDGDSGRIRLQNIRMLLSDYPI 1216
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 ...
 1137-1215 6.79e-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: 6.79e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620531 1137 PKSVESVPVGTRLCAYWSQQYRCLYPGraidseQVVDGTASSATNaatTAPDFVSVEFDDGDSGRIRLQNIRMLLSDYP 1215
Cdd:cd20470     1 PQSSRQLPPGTRVCAYWSQKSRCLYPG------NVVRGSSGIDEE---DDEDSVMVEFDDGDRGRISVSNIRLLPPDYK 70
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 1461-1586 6.59e-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: 6.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531 1461 KETITVGDSAVFL--STGRPDRPYIGRIESMWETTTGNKVVRVAWFYHPEETtgcPKLKFPGA----LFESPHEDENDVQ 1534
Cdd:cd04370     1 GITYEVGDSVYVEpdDSIKSDPPYIARIEELWEDTNGSKQVKVRWFYRPEET---PKGLSPFAlrreLFLSDHLDEIPVE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442620531 1535 TISHRCEVLQFGSYFEKFGADSKqyqsiyDNNDTYYLAGHYNPRLQVLKLQD 1586
Cdd:cd04370    78 SIIGKCKVLFVSEFEGLKQRPNK------IDTDDFFCRLAYDPTTKEFKALE 123
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 1462-1583 7.30e-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: 7.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531  1462 ETITVGDSAVFLSTGRPDRPYIGRIESMWETTTGNKV-VRVAWFYHPEETTGCPKLKF-PGALFESPHEDENDVQTISHR 1539
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETVHRAGKAFnKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 442620531  1540 CEVLQFGSYFekfgadSKQYQSIyDNNDTYYLAGHYNPRLQVLK 1583
Cdd:pfam01426   81 CSVLHKSDLE------SLDPYKI-KEPDDFFCELLYDPKTKSFK 117
BAH smart00439
Bromo adjacent homology domain;
1463-1577 1.87e-16

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 76.95  E-value: 1.87e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531   1463 TITVGDSAVFLSTGRPDRPYIGRIESMWETTTGN--KVVRVAWFYHPEETTGCP-KLKFPGALFESPHEDENDVQTISHR 1539
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKaALFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 442620531   1540 CEVLQFGSYFEkfgadsKQYQSIYDNNDTYYLAGHYNP 1577
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 ...
 1466-1549 1.59e-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: 1.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531 1466 VGDSAVFLSTGRPDRPYIGRIESMWETTTGNKVVRVAWFYHPEETTGCPKLKF-PGALFESPHEDENDVQTISHRCEVLQ 1544
Cdd:cd04717     6 VGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWFYRPEETFHEPTRKFyKNEVFKSPLYETVPVEEIVGKCAVMD 85


                  ....*
gi 442620531 1545 FGSYF 1549
Cdd:cd04717    86 VKDYI 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
 434-761 2.88e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.26  E-value: 2.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531  434 PTPPTSATMEPSSLGHATPHHLFQSGAMATPTPALLNLSMHGNGGELPAATPLPAVSDEAAlnyklhAPLTPQTPP---- 509
Cdd:PHA03247 2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA------PPAAPAAGPprrl 2783

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531  510 -RLADIPVSGSTQLLPQMQDVNIQTdTPVCSEDESFPGSAKPQDPAaeafPPPTHVQPLELTKPSEASHTQPTECHTQTE 588
Cdd:PHA03247 2784 tRPAVASLSESRESLPSPWDPADPP-AAVLAPAAALPPAASPAGPL----PPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531  589 PSDI---PSASQEESAEQTPPEP-IETMTQATQADQTSPEDLTGLELlsnistNSKPLVRVKQEPVEHIE-QPAPQPQPV 663
Cdd:PHA03247 2859 GGDVrrrPPSRSPAAKPAAPARPpVRRLARPAVSRSTESFALPPDQP------ERPPQPQAPPPPQPQPQpPPPPQPQPP 2932

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531  664 NIMPSEPTLPMPPMLEMEPTSEREPLGGLKLLCALAEQRI---QEEVVQGSSLFATPSSRTPTPT------------SLA 728
Cdd:PHA03247 2933 PPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVavpRFRVPQPAPSREAPASSTPPLTghslsrvsswasSLA 3012

                         330       340       350
                  ....*....|....*....|....*....|...
gi 442620531  729 LGTTAATPPIFEAKSCYAFGQSQGSVFPSSTSS 761
Cdd:PHA03247 3013 LHEETDPPPVSLKQTLWPPDDTEDSDADSLFDS 3045
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 1446-1542 4.22e-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: 4.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531 1446 KGRARKQFYKTIKRGKETITVGDSAVFLStgrPD--RPYIGRIESMWETTTGNKVVRVAWFYHPEETT----GCPKLKFP 1519
Cdd:cd04713     3 KGKKKKCHYTSFEKDGNKYRLEDCVLLVP---EDdqKPYIAIIKDIYKQEEGSLKLEVQWLYRPEEIEkkkgGNWKAEDP 79

                          90       100
                  ....*....|....*....|...
gi 442620531 1520 GALFESPHEDENDVQTISHRCEV 1542
Cdd:cd04713    80 RELFYSFHRDEVPAESVLHPCKV 102
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 1463-1554 1.24e-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: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531 1463 TITVGDSaVFLSTGRPDRpYIGRIESMWETTTGNKVVRVAWFYHPEE--TTGCPKLKFPGALFESPHEDENDVQTISHRC 1540
Cdd:cd04721     7 TISVHDF-VYVLSEEEDR-YVAYIEDLYEDKKGSKMVKVRWFHTTDEvgAALSPDSVNPREIFLSPNLQVISVECIDGLA 84

                          90
                  ....*....|....
gi 442620531 1541 EVLQfGSYFEKFGA 1554
Cdd:cd04721    85 TVLT-REHYEKFQS 97
BAH_Orc1p_like cd04715
BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of ...
 1433-1561 2.77e-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: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531 1433 WGwygtAYRKAGVKGRArKQFYKTIKRGKETITVGDSAVFLSTGrpDRPYIGRIESMWETTT--GNKVVRVAWFYHPEET 1510
Cdd:cd04715     4 WG----VKRGEGGKKKD-GQFYRSFTYDGVEYRLYDDVYVHNGD--SEPYIGKIIKIYETAIdsGKKKVKVIWFFRPSEI 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531 1511 ----TGCPKLKFpGALFESPHEDE-----NDVQTISHRCEVLQFGSYFEKFGADSKQYQS 1561
Cdd:cd04715    77 rmelKGEPKRHI-NEVFLACGRGEglaniNLLESIIGKCNVVCISEDFRNPQPSDGIPTS 135
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 434-676 1.06e-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: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531   434 PTPPTSATMEPSSLGHATPHHLfqsgamATPTPallnLSMHGNGGELPAATPLPAVSDeaalnyklHAPLTPQTPPrlad 513
Cdd:pfam03154  357 PPPTTPIPQLPNPQSHKHPPHL------SGPSP----FQMNSNLPPPPALKPLSSLST--------HHPPSAHPPP---- 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531   514 ipvsgsTQLLPQMQDVNIQ-TDTPVCSEDESFPgsakpqdPAAEAFPPPTHVQPLELTKPSEASHTQPTECHTQTEPSDI 592
Cdd:pfam03154  415 ------LQLMPQSQQLPPPpAQPPVLTQSQSLP-------PPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGP 481

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531   593 PSASQEESAEQTPPEPIETMTQATqadqtspedltglelLSNISTNSKPLVRVKQEPVEHIEQPAPQPQPVNIMPSEPTL 672
Cdd:pfam03154  482 PTSTSSAMPGIQPPSSASVSSSGP---------------VPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTV 546


                   ....
gi 442620531   673 PMPP 676
Cdd:pfam03154  547 VNTP 550
BAH_Orc1p_animal cd04719
BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces ...
 1463-1544 1.51e-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: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531 1463 TITVGDSaVFLSTGRPDRPYIGRIESMWETTTGN---KVVRVAWFYHPEETtgcPKLK------FPGAL---FESPHEDE 1530
Cdd:cd04719     3 TIEVGDF-VLIEGEDADGPDVARILHLYEDGNEDddpKRAIVQWFSRPSEV---PKNKrkllgrEPHSQevfFYSRSSCD 78

                          90
                  ....*....|....*.
gi 442620531 1531 NDV--QTISHRCEVLQ 1544
Cdd:cd04719    79 NDIdaETIIGKVRVEP 94
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 387-737 2.67e-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: 2.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531   387 QTGIPSLLSLPPPtglkeeypmplalpPLVPLEAARDKEQALNLMRLPTPPTSatMEP-SSLGHATPHHLFQSGAMATPt 465
Cdd:pfam03154  177 QSGAASPPSPPPP--------------GTTQAATAGPTPSAPSVPPQGSPATS--QPPnQTQSTAAPHTLIQQTPTLHP- 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531   466 PALlnLSMHGNGGELPAATPLPAVSDEAALNYKLHAPLTP-----QTPPRLadIPVSGSTQLLPQMQDVNIQTDTPVCSE 540
Cdd:pfam03154  240 QRL--PSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPmphslQTGPSH--MQHPVPPQPFPLTPQSSQSQVPPGPSP 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531   541 DESFPGSAKPQDPAAEAFPP---PTHVQPLElTKPSEASHTQPTechTQTEPSDIPSA-SQEESAEQTPPEPIETMTQAT 616
Cdd:pfam03154  316 AAPGQSQQRIHTPPSQSQLQsqqPPREQPLP-PAPLSMPHIKPP---PTTPIPQLPNPqSHKHPPHLSGPSPFQMNSNLP 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620531   617 QADQTSPedltglelLSNISTNskplvrvkqepvehiEQPAPQPQPVNIMPSEPTLPMPPML--------EMEPTSEREP 688
Cdd:pfam03154  392 PPPALKP--------LSSLSTH---------------HPPSAHPPPLQLMPQSQQLPPPPAQppvltqsqSLPPPAASHP 448

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 442620531   689 LGGLKLLCALAEQRIQEEVVQGSSLFATPSSRTPTPTSLALgtTAATPP 737
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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