|
Name |
Accession |
Description |
Interval |
E-value |
| BAH_BAHCC1 |
cd04714 |
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ... |
2757-2901 |
4.96e-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: 4.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2757 KEMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKqfhegqhwdqksghnlpaalrassqR 2836
Cdd:cd04714 1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGR-------------------------K 55
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958668543 2837 KDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLK-TKKYQDSEGLYYLAGTYEPTTGMIFS 2901
Cdd:cd04714 56 PNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYERLARvKKKPQDGVDFYYCAGTYNPDTGMLKC 121
|
|
| Tudor_SF super family |
cl02573 |
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ... |
2161-2227 |
7.45e-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: 134.08 E-value: 7.45e-37
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958668543 2161 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYKI 2227
Cdd:cd20469 1 SVRFLPEGTRVCAYWSQQYRCLYPGTVVKGSPDPEEDDDLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
|
|
| PHA03307 super family |
cl33723 |
transcriptional regulator ICP4; Provisional |
2231-2481 |
8.31e-04 |
|
transcriptional regulator ICP4; Provisional
The actual alignment was detected with superfamily member PHA03307:
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2231 EPSPALLVPSAKRRSRKTSKDTGEGKEGAATGPQEATGGKARGRGRKPSTKAKADRAVVLEEGAATNELPSAPLALEPVS 2310
Cdd:PHA03307 219 SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSP 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2311 TPNSKKSTPEPvdkrARAPKARSVSVQPSPGPP-TFSSCPAPEPFGELPTPATAPLVTMPVTMPATRPKPKKARATEGSG 2389
Cdd:PHA03307 299 SPSSPGSGPAP----SSPRASSSSSSSRESSSSsTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2390 AKGPRRPGEddellvkldhegvmSPKSKKAKEALllredPGPGAWPESTGLL--SLGSYSPTVGSSEPKATWPKGLDGDL 2467
Cdd:PHA03307 375 PSSPAASAG--------------RPTRRRARAAV-----AGRARRRDATGRFpaGRPRPSPLDAGAASGAFYARYPLLTP 435
|
250
....*....|....
gi 1958668543 2468 TQEPGPGLPLEDPG 2481
Cdd:PHA03307 436 SGEPWPGSPPPPPG 449
|
|
| PHA03247 super family |
cl33720 |
large tegument protein UL36; Provisional |
383-641 |
7.36e-03 |
|
large tegument protein UL36; Provisional
The actual alignment was detected with superfamily member PHA03247:
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 383 RAREREPGRPGVLQGPPGSPRlerPEVLREKSSVIRSLKRPPPSDGPPAARSSRSSPDARAYLPPKElLKPEADPRPCER 462
Cdd:PHA03247 2664 PRRARRLGRAAQASSPPQRPR---RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAA-ARQASPALPAAP 2739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 463 APRGPSSSAAQQAAklfglePSRPPGPehkwkPFELGNFATTQMAVLAAQHHHASRAEEEAAVATASKKAYLDPGGAMPR 542
Cdd:PHA03247 2740 APPAVPAGPATPGG------PARPARP-----PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPP 2808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 543 ASATCgrPGADLHSAAAHGPGEASAmQSLIKYSGSFAREAVAVRPGGCGKKSPFGGLGTMKP--EPIPTSAGPPRAQA-R 619
Cdd:PHA03247 2809 AAVLA--PAAALPPAASPAGPLPPP-TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPsrSPAAKPAAPARPPVrR 2885
|
250 260
....*....|....*....|...
gi 1958668543 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. ... |
2757-2901 |
4.96e-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: 4.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2757 KEMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKqfhegqhwdqksghnlpaalrassqR 2836
Cdd:cd04714 1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGR-------------------------K 55
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958668543 2837 KDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLK-TKKYQDSEGLYYLAGTYEPTTGMIFS 2901
Cdd:cd04714 56 PNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYERLARvKKKPQDGVDFYYCAGTYNPDTGMLKC 121
|
|
| Tudor_TNRC18 |
cd20469 |
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ... |
2161-2227 |
7.45e-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: 134.08 E-value: 7.45e-37
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958668543 2161 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYKI 2227
Cdd:cd20469 1 SVRFLPEGTRVCAYWSQQYRCLYPGTVVKGSPDPEEDDDLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
|
|
| BAH |
smart00439 |
Bromo adjacent homology domain; |
2759-2897 |
1.74e-13 |
|
Bromo adjacent homology domain;
Pssm-ID: 214664 [Multi-domain] Cd Length: 121 Bit Score: 69.24 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2759 MIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNN--MVVRVKWFYHPEETSPGKQFHegqhwdqksghnlpaalrassqr 2836
Cdd:smart00439 1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAAL----------------------- 57
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958668543 2837 kdFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQmLKTKKYQDSEGLYYLAGTYEPTTG 2897
Cdd:smart00439 58 --FDKNEVFLSDEYDTVPLSDIIGKCNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKG 115
|
|
| BAH |
pfam01426 |
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ... |
2758-2897 |
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 1958668543 2758 EMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMV-VRVKWFYHPEETSpgkqfhegqhwdqksgHNLPAAlrassqr 2836
Cdd:pfam01426 1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETV----------------HRAGKA------- 57
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958668543 2837 kdFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKKyqDSEGLYYLAGTYEPTTG 2897
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 ... |
2169-2221 |
1.47e-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: 1.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1958668543 2169 TRIAAYWSQQYRCLYPGTVVRgllDLEDDGDLITVEFDDGDTGRIPLSHIRLL 2221
Cdd:pfam18115 1 NRVFALWKGKDRAYYPATCLG---TSGSGSQRYLVRFDDGTPTEVDSGQVRRL 50
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2231-2481 |
8.31e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2231 EPSPALLVPSAKRRSRKTSKDTGEGKEGAATGPQEATGGKARGRGRKPSTKAKADRAVVLEEGAATNELPSAPLALEPVS 2310
Cdd:PHA03307 219 SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSP 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2311 TPNSKKSTPEPvdkrARAPKARSVSVQPSPGPP-TFSSCPAPEPFGELPTPATAPLVTMPVTMPATRPKPKKARATEGSG 2389
Cdd:PHA03307 299 SPSSPGSGPAP----SSPRASSSSSSSRESSSSsTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2390 AKGPRRPGEddellvkldhegvmSPKSKKAKEALllredPGPGAWPESTGLL--SLGSYSPTVGSSEPKATWPKGLDGDL 2467
Cdd:PHA03307 375 PSSPAASAG--------------RPTRRRARAAV-----AGRARRRDATGRFpaGRPRPSPLDAGAASGAFYARYPLLTP 435
|
250
....*....|....
gi 1958668543 2468 TQEPGPGLPLEDPG 2481
Cdd:PHA03307 436 SGEPWPGSPPPPPG 449
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
383-641 |
7.36e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 383 RAREREPGRPGVLQGPPGSPRlerPEVLREKSSVIRSLKRPPPSDGPPAARSSRSSPDARAYLPPKElLKPEADPRPCER 462
Cdd:PHA03247 2664 PRRARRLGRAAQASSPPQRPR---RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAA-ARQASPALPAAP 2739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 463 APRGPSSSAAQQAAklfglePSRPPGPehkwkPFELGNFATTQMAVLAAQHHHASRAEEEAAVATASKKAYLDPGGAMPR 542
Cdd:PHA03247 2740 APPAVPAGPATPGG------PARPARP-----PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPP 2808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 543 ASATCgrPGADLHSAAAHGPGEASAmQSLIKYSGSFAREAVAVRPGGCGKKSPFGGLGTMKP--EPIPTSAGPPRAQA-R 619
Cdd:PHA03247 2809 AAVLA--PAAALPPAASPAGPLPPP-TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPsrSPAAKPAAPARPPVrR 2885
|
250 260
....*....|....*....|...
gi 1958668543 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. ... |
2757-2901 |
4.96e-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: 4.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2757 KEMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKqfhegqhwdqksghnlpaalrassqR 2836
Cdd:cd04714 1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGR-------------------------K 55
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958668543 2837 KDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLK-TKKYQDSEGLYYLAGTYEPTTGMIFS 2901
Cdd:cd04714 56 PNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYERLARvKKKPQDGVDFYYCAGTYNPDTGMLKC 121
|
|
| Tudor_TNRC18 |
cd20469 |
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ... |
2161-2227 |
7.45e-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: 134.08 E-value: 7.45e-37
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958668543 2161 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYKI 2227
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 ... |
2161-2226 |
7.79e-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: 7.79e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958668543 2161 STRFLPQGTRIAAYWSQQYRCLYPGTVVRGLLDLEDD-GDLITVEFDDGDTGRIPLSHIRLLPPDYK 2226
Cdd:cd20397 1 SVEYLPPGTRVCAYWSQQYRCLYPGTVISGEPDSEDSqEGKVPVEFDDGDSGKIPLSDIRLLPPDYP 67
|
|
| Tudor_BAHCC1 |
cd20470 |
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ... |
2159-2226 |
1.08e-24 |
|
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar proteins; BAHCC1, also called Bromo adjacent homology domain-containing protein 2 (BAHD2), or BAH domain-containing protein 2, may function as a transcriptional regulator. BAHCC1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Pssm-ID: 410541 Cd Length: 70 Bit Score: 99.49 E-value: 1.08e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2159 PASTRFLPQGTRIAAYWSQQYRCLYPGTVVR--GLLDLEDDGDLITVEFDDGDTGRIPLSHIRLLPPDYK 2226
Cdd:cd20470 1 PQSSRQLPPGTRVCAYWSQKSRCLYPGNVVRgsSGIDEEDDEDSVMVEFDDGDRGRISVSNIRLLPPDYK 70
|
|
| BAH |
cd04370 |
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ... |
2757-2897 |
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 1958668543 2757 KEMIRIGDCAVFLSAG--RPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEETSPGKQFHEGqhwdqksghnlpaalrass 2834
Cdd:cd04370 1 GITYEVGDSVYVEPDDsiKSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPFAL------------------- 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958668543 2835 qrkdfmERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMlKTKKYQDSEGLYYLAGTYEPTTG 2897
Cdd:cd04370 62 ------RRELFLSDHLDEIPVESIIGKCKVLFVSEFEGL-KQRPNKIDTDDFFCRLAYDPTTK 117
|
|
| BAH |
smart00439 |
Bromo adjacent homology domain; |
2759-2897 |
1.74e-13 |
|
Bromo adjacent homology domain;
Pssm-ID: 214664 [Multi-domain] Cd Length: 121 Bit Score: 69.24 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2759 MIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNN--MVVRVKWFYHPEETSPGKQFHegqhwdqksghnlpaalrassqr 2836
Cdd:smart00439 1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAAL----------------------- 57
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958668543 2837 kdFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQmLKTKKYQDSEGLYYLAGTYEPTTG 2897
Cdd:smart00439 58 --FDKNEVFLSDEYDTVPLSDIIGKCNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKG 115
|
|
| BAH |
pfam01426 |
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ... |
2758-2897 |
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 1958668543 2758 EMIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMV-VRVKWFYHPEETSpgkqfhegqhwdqksgHNLPAAlrassqr 2836
Cdd:pfam01426 1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETV----------------HRAGKA------- 57
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958668543 2837 kdFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKKyqDSEGLYYLAGTYEPTTG 2897
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 ... |
2759-2814 |
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 1958668543 2759 MIRIGDCAVFLSAGRPNLPYIGRIQSMWESWGNNMVVRVKWFYHPEET--SPGKQFHE 2814
Cdd:cd04717 3 QYRVGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWFYRPEETfhEPTRKFYK 60
|
|
| BAH_plant_3 |
cd04713 |
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ... |
2742-2878 |
1.06e-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: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2742 KGKARKLFYKAIVRGKEMIRIGDCAVFLSA-GRPnlPYIGRIQSMWESWGNNMVVRVKWFYHPEETspgkqfhegqhwDQ 2820
Cdd:cd04713 3 KGKKKKCHYTSFEKDGNKYRLEDCVLLVPEdDQK--PYIAIIKDIYKQEEGSLKLEVQWLYRPEEI------------EK 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958668543 2821 KSGHNLPAAlrassqrkdfMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKK 2878
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 ... |
2169-2221 |
1.47e-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: 1.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1958668543 2169 TRIAAYWSQQYRCLYPGTVVRgllDLEDDGDLITVEFDDGDTGRIPLSHIRLL 2221
Cdd:pfam18115 1 NRVFALWKGKDRAYYPATCLG---TSGSGSQRYLVRFDDGTPTEVDSGQVRRL 50
|
|
| Tudor_SF |
cd04508 |
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ... |
2168-2220 |
1.03e-04 |
|
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.
Pssm-ID: 410449 [Multi-domain] Cd Length: 47 Bit Score: 41.80 E-value: 1.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1958668543 2168 GTRIAAYWSQQyRCLYPGTVVRGLLDLEddgdlITVEFDDGDTGRIPLSHIRL 2220
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 ... |
2168-2221 |
1.07e-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: 1.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958668543 2168 GTRIAAYWSQqYRCLYPGTVVrglldLEDDGDLITVEFDDGDTGRIPLSHIRLL 2221
Cdd:cd20395 1 PTRVLAFWKG-DGNYYPATIV-----GPVSSSAYKVQFDDGTSSSVPPTQIRRL 48
|
|
| BAH_MTA |
cd04709 |
BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The ... |
2759-2904 |
4.85e-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: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2759 MIRIGDCAVFLSAgrPNLPY-IGRIQSMWESWGNNMVVRVKWFYHPEETSPgkqfHEGQHWDQKSgHNLPAALRASS--Q 2835
Cdd:cd04709 3 MYRVGDYVYFESS--PNNPYlIRRIEELNKTARGHVEAKVVCYYRRRDIPD----SLYQLADQHR-RELEEKSDDLTpkQ 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958668543 2836 RKDFMERALYQSSHVDENDVQTVSHKCLVVGLEQYEQMLKTKKYQDSegLYYLAGtYEPTTGMIFSTDG 2904
Cdd:cd04709 76 RHQLRHRELFLSRQVETLPATHIRGKCSVTLLNDTESARSYLAREDT--FFYSLV-YDPEQKTLLADQG 141
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2231-2481 |
8.31e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2231 EPSPALLVPSAKRRSRKTSKDTGEGKEGAATGPQEATGGKARGRGRKPSTKAKADRAVVLEEGAATNELPSAPLALEPVS 2310
Cdd:PHA03307 219 SPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSP 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2311 TPNSKKSTPEPvdkrARAPKARSVSVQPSPGPP-TFSSCPAPEPFGELPTPATAPLVTMPVTMPATRPKPKKARATEGSG 2389
Cdd:PHA03307 299 SPSSPGSGPAP----SSPRASSSSSSSRESSSSsTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2390 AKGPRRPGEddellvkldhegvmSPKSKKAKEALllredPGPGAWPESTGLL--SLGSYSPTVGSSEPKATWPKGLDGDL 2467
Cdd:PHA03307 375 PSSPAASAG--------------RPTRRRARAAV-----AGRARRRDATGRFpaGRPRPSPLDAGAASGAFYARYPLLTP 435
|
250
....*....|....
gi 1958668543 2468 TQEPGPGLPLEDPG 2481
Cdd:PHA03307 436 SGEPWPGSPPPPPG 449
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2221-2395 |
3.40e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2221 LPPDYKIQCAEPSPALLVPSAkrrsrkTSKDTGEGKEGAATGPQEATGGKARGRG--RKPSTKAKADRAVVLEEGAA--- 2295
Cdd:PHA03247 2818 LPPAASPAGPLPPPTSAQPTA------PPPPPGPPPPSLPLGGSVAPGGDVRRRPpsRSPAAKPAAPARPPVRRLARpav 2891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2296 ---TNELPSAPLALEPVSTPNSK---KSTPEPVDKRARAPKARSVSVQPSPGPPTFSSCPAPEPFGELPTPATAPLVTMP 2369
Cdd:PHA03247 2892 srsTESFALPPDQPERPPQPQAPpppQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGR 2971
|
170 180
....*....|....*....|....*..
gi 1958668543 2370 VTMPATR-PKPKKARATEGSGAKGPRR 2395
Cdd:PHA03247 2972 VAVPRFRvPQPAPSREAPASSTPPLTG 2998
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
2255-2430 |
3.48e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.94 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2255 GKEGAATGPQEAtggkARGRGRKPSTKAKADRAVVLEEGAATNELPSAPLALEPVSTPNSKKSTPEPvdkrarAPKARSV 2334
Cdd:PRK12323 366 GQSGGGAGPATA----AAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSP------APEALAA 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2335 SVQPSPGPPTFSSCPAPEPfGELPTPATAPLVTMPVTMPATRPKPKKARATEGSGAKGPRRPGEDDELLVKLDHEGVMSP 2414
Cdd:PRK12323 436 ARQASARGPGGAPAPAPAP-AAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQP 514
|
170
....*....|....*.
gi 1958668543 2415 KSKKAKEALLLREDPG 2430
Cdd:PRK12323 515 DAAPAGWVAESIPDPA 530
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
2222-2436 |
7.03e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.79 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2222 PPDYKIQCAEPSPALLVPSAKRRSRKTSKDTGEGKEGAATGPQEATGGKARgrgRKPSTKA-KADRAVVLEEGAATNELP 2300
Cdd:PRK12323 375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPAR---RSPAPEAlAAARQASARGPGGAPAPA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 2301 SAPLALEPVSTPNSKKSTPEPVDKRARAPKARSVSVQPSP---GPPTFSSCPA--PEPFGELPTPATAPLVTMPVTMPAT 2375
Cdd:PRK12323 452 PAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPaddDPPPWEELPPefASPAPAQPDAAPAGWVAESIPDPAT 531
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958668543 2376 RPKPKKARATEGSGAKGPRRPgeddellVKLDHEGVMSPKSKKAKEALLlrEDPGPGAWPE 2436
Cdd:PRK12323 532 ADPDDAFETLAPAPAAAPAPR-------AAAATEPVVAPRPPRASASGL--PDMFDGDWPA 583
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
383-641 |
7.36e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 383 RAREREPGRPGVLQGPPGSPRlerPEVLREKSSVIRSLKRPPPSDGPPAARSSRSSPDARAYLPPKElLKPEADPRPCER 462
Cdd:PHA03247 2664 PRRARRLGRAAQASSPPQRPR---RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAA-ARQASPALPAAP 2739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 463 APRGPSSSAAQQAAklfglePSRPPGPehkwkPFELGNFATTQMAVLAAQHHHASRAEEEAAVATASKKAYLDPGGAMPR 542
Cdd:PHA03247 2740 APPAVPAGPATPGG------PARPARP-----PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPP 2808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668543 543 ASATCgrPGADLHSAAAHGPGEASAmQSLIKYSGSFAREAVAVRPGGCGKKSPFGGLGTMKP--EPIPTSAGPPRAQA-R 619
Cdd:PHA03247 2809 AAVLA--PAAALPPAASPAGPLPPP-TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPsrSPAAKPAAPARPPVrR 2885
|
250 260
....*....|....*....|...
gi 1958668543 620 LTHPGVPTAGGGRQLKRD-PERP 641
Cdd:PHA03247 2886 LARPAVSRSTESFALPPDqPERP 2908
|
|
| |
