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Conserved domains on  [gi|1039728043|ref|XP_006529345|]
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nuclear autoantigen Sp-100 isoform X3 [Mus musculus]

Protein Classification

nuclear body protein( domain architecture ID 10504728)

nuclear body protein similar to human Sp110 nuclear body protein that may be a nuclear hormone receptor coactivator that enhances transcription of genes with retinoic acid response elements (RARE)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
 534-634 6.30e-50

Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major component of PML-SP100 nuclear bodies (NBs), which are poorly understood. It is covalently modified by SUMO-1 and may play a role in processes at the chromatin level. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


:

Pssm-ID: 99933  Cd Length: 102  Bit Score: 168.76  E-value: 6.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043 534 PEEQLKCELLLLTIYCYPKSGFFIPKPKQRKEKFPDLREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNHSIFYKK-R 612
Cdd:cd05501     1 PEELLKCEFLLLKVYCMSKSGFFISKPYYIRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDdD 80

                          90       100
                  ....*....|....*....|..
gi 1039728043 613 FKNLGIIVGKKFEKNFKRIFSI 634
Cdd:cd05501    81 FGQVGITLEKKFEKNFKEVFAI 102
HSR pfam03172
HSR domain; The Sp100 protein is a constituent of nuclear domains, also known as nuclear dots ...
 23-119 3.25e-49

HSR domain; The Sp100 protein is a constituent of nuclear domains, also known as nuclear dots (NDs). An ND-targeting region that coincides with a homodimerization domain was mapped in Sp100. Sequences similar to the Sp100 homodimerization/ND-targeting region occur in several other proteins and constitute a novel protein motif, termed HSR domain (for homogeneously-staining region). The HSR domain has also been named ASS (AIRE, Sp-100 and Sp140). This domain is usually found at the amino terminus of proteins that contain a SAND domain pfam01342.


:

Pssm-ID: 460835  Cd Length: 99  Bit Score: 166.56  E-value: 3.25e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043  23 ECMLKHFKTQKVAISNAIRSTFPFLESLRDHEFITGKMYEDLLDSCRSLVPVDKVIYRALEELEKKFDMTVLCELFNEVN 102
Cdd:pfam03172   3 EALFQHFKENKVEIAYAIKKPFPFLEGLRDHSFITEKMYKESLEACRNLVPVQRVVYNVLSELEKTFSLSLLEALFSDVN 82

                          90
                  ....*....|....*..
gi 1039728043 103 MEKYPDLNLIRRSFGCV 119
Cdd:pfam03172  83 LKEYPDLIEILKSFPNV 99
SAND pfam01342
SAND domain; The DNA binding activity of two proteins has been mapped to the SAND domain. The ...
 364-440 4.09e-29

SAND domain; The DNA binding activity of two proteins has been mapped to the SAND domain. The conserved KDWK motif is necessary for DNA binding, and it appears to be important for dimerization. This region is also found in the putative transcription factor RegA from the multicellular green alga Volvox cateri. This region of RegA is known as the VARL domain.


:

Pssm-ID: 460167  Cd Length: 76  Bit Score: 110.36  E-value: 4.09e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039728043 364 DFGGAELPVVCGNAQGFLDKEKFKQGIYVRSIRGKtGRLFTPMDFEIEGNCEKAKNWRQSIRCKGWTLRELIQKGVL 440
Cdd:pfam01342   1 DFDSPVLPVTCGAAKGLLHKKKFKQGISGKCIQNE-DSWLTPKEFEIEGGKASSKDWKRSIRCGGKPLRELIEKGLL 76
PHD_SP110_140 cd15626
PHD finger found in the Sp100/Sp140 family of nuclear body components; The Sp100/Sp140 family ...
 466-507 6.96e-15

PHD finger found in the Sp100/Sp140 family of nuclear body components; The Sp100/Sp140 family includes nuclear body proteins SP100, SP140, and similar proteins. Sp110, also termed interferon-induced protein 41/75, or speckled 110 kDa, or transcriptional coactivator Sp110, is a leukocyte-specific component of the nuclear body. It may function as a nuclear hormone receptor transcriptional coactivator that may play a role in inducing differentiation of myeloid cells. It is also involved in resisting intracellular pathogens and functions as an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers. Sp110 gene polymorphisms may be associated with susceptibility to tuberculosis in Chinese population. Sp110 contains a Sp100-like domain, a SAND domain, a plant homeodomain (PHD) finger, and a bromodomain (BRD). SP140, also termed lymphoid-restricted homolog of Sp100 (LYSp100), or nuclear autoantigen Sp-140, or speckled 140 kDa, is an interferon inducible nuclear leukocyte-specific protein involved in primary biliary cirrhosis and a risk factor in chronic lymphocytic leukemia. It is also implicated in innate immune response to human immunodeficiency virus type 1 (HIV-1) by binding to the virus's viral infectivity factor (Vif) protein. Sp140 contains a nuclear localization signal, a dimerization domain (HSR or CARD domain), a SAND domain, a PHD finger, and a BRD.


:

Pssm-ID: 277096  Cd Length: 42  Bit Score: 68.61  E-value: 6.96e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1039728043 466 ACKVCGQPRKVHPCTACKEFYHKNCHIPPVEDKSRSWHCAFC 507
Cdd:cd15626     1 KCEVCGQEGKLFCCCTCSRVFHEDCHIPPVEAQRSPWSCTFC 42
 
Name Accession Description Interval E-value
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
 534-634 6.30e-50

Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major component of PML-SP100 nuclear bodies (NBs), which are poorly understood. It is covalently modified by SUMO-1 and may play a role in processes at the chromatin level. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99933  Cd Length: 102  Bit Score: 168.76  E-value: 6.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043 534 PEEQLKCELLLLTIYCYPKSGFFIPKPKQRKEKFPDLREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNHSIFYKK-R 612
Cdd:cd05501     1 PEELLKCEFLLLKVYCMSKSGFFISKPYYIRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDdD 80

                          90       100
                  ....*....|....*....|..
gi 1039728043 613 FKNLGIIVGKKFEKNFKRIFSI 634
Cdd:cd05501    81 FGQVGITLEKKFEKNFKEVFAI 102
HSR pfam03172
HSR domain; The Sp100 protein is a constituent of nuclear domains, also known as nuclear dots ...
 23-119 3.25e-49

HSR domain; The Sp100 protein is a constituent of nuclear domains, also known as nuclear dots (NDs). An ND-targeting region that coincides with a homodimerization domain was mapped in Sp100. Sequences similar to the Sp100 homodimerization/ND-targeting region occur in several other proteins and constitute a novel protein motif, termed HSR domain (for homogeneously-staining region). The HSR domain has also been named ASS (AIRE, Sp-100 and Sp140). This domain is usually found at the amino terminus of proteins that contain a SAND domain pfam01342.


Pssm-ID: 460835  Cd Length: 99  Bit Score: 166.56  E-value: 3.25e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043  23 ECMLKHFKTQKVAISNAIRSTFPFLESLRDHEFITGKMYEDLLDSCRSLVPVDKVIYRALEELEKKFDMTVLCELFNEVN 102
Cdd:pfam03172   3 EALFQHFKENKVEIAYAIKKPFPFLEGLRDHSFITEKMYKESLEACRNLVPVQRVVYNVLSELEKTFSLSLLEALFSDVN 82

                          90
                  ....*....|....*..
gi 1039728043 103 MEKYPDLNLIRRSFGCV 119
Cdd:pfam03172  83 LKEYPDLIEILKSFPNV 99
SAND pfam01342
SAND domain; The DNA binding activity of two proteins has been mapped to the SAND domain. The ...
 364-440 4.09e-29

SAND domain; The DNA binding activity of two proteins has been mapped to the SAND domain. The conserved KDWK motif is necessary for DNA binding, and it appears to be important for dimerization. This region is also found in the putative transcription factor RegA from the multicellular green alga Volvox cateri. This region of RegA is known as the VARL domain.


Pssm-ID: 460167  Cd Length: 76  Bit Score: 110.36  E-value: 4.09e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039728043 364 DFGGAELPVVCGNAQGFLDKEKFKQGIYVRSIRGKtGRLFTPMDFEIEGNCEKAKNWRQSIRCKGWTLRELIQKGVL 440
Cdd:pfam01342   1 DFDSPVLPVTCGAAKGLLHKKKFKQGISGKCIQNE-DSWLTPKEFEIEGGKASSKDWKRSIRCGGKPLRELIEKGLL 76
SAND smart00258
SAND domain;
368-441 8.64e-28

SAND domain;


Pssm-ID: 128554  Cd Length: 73  Bit Score: 106.27  E-value: 8.64e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039728043  368 AELPVVCGNAQGFLDKEKFKQGIYVRSIRGKtGRLFTPMDFEIEGNCEKAKNWRQSIRCKGWTLRELIQKGVLQ 441
Cdd:smart00258   1 SELPVTCGTVKGILYKKKFKCGISVKCIQYE-DKWFTPKEFEIEGGKGKSKDWKRSIRCGGSSLRTLMENGTLD 73
PHD_SP110_140 cd15626
PHD finger found in the Sp100/Sp140 family of nuclear body components; The Sp100/Sp140 family ...
 466-507 6.96e-15

PHD finger found in the Sp100/Sp140 family of nuclear body components; The Sp100/Sp140 family includes nuclear body proteins SP100, SP140, and similar proteins. Sp110, also termed interferon-induced protein 41/75, or speckled 110 kDa, or transcriptional coactivator Sp110, is a leukocyte-specific component of the nuclear body. It may function as a nuclear hormone receptor transcriptional coactivator that may play a role in inducing differentiation of myeloid cells. It is also involved in resisting intracellular pathogens and functions as an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers. Sp110 gene polymorphisms may be associated with susceptibility to tuberculosis in Chinese population. Sp110 contains a Sp100-like domain, a SAND domain, a plant homeodomain (PHD) finger, and a bromodomain (BRD). SP140, also termed lymphoid-restricted homolog of Sp100 (LYSp100), or nuclear autoantigen Sp-140, or speckled 140 kDa, is an interferon inducible nuclear leukocyte-specific protein involved in primary biliary cirrhosis and a risk factor in chronic lymphocytic leukemia. It is also implicated in innate immune response to human immunodeficiency virus type 1 (HIV-1) by binding to the virus's viral infectivity factor (Vif) protein. Sp140 contains a nuclear localization signal, a dimerization domain (HSR or CARD domain), a SAND domain, a PHD finger, and a BRD.


Pssm-ID: 277096  Cd Length: 42  Bit Score: 68.61  E-value: 6.96e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1039728043 466 ACKVCGQPRKVHPCTACKEFYHKNCHIPPVEDKSRSWHCAFC 507
Cdd:cd15626     1 KCEVCGQEGKLFCCCTCSRVFHEDCHIPPVEAQRSPWSCTFC 42
BROMO smart00297
bromo domain;
533-631 9.92e-12

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 61.91  E-value: 9.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043  533 SPEEQLKCELLLLTIYC----YPKSGFFIPKPKqrKEKFPD----LREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHN 604
Cdd:smart00297   1 DPKLQKKLQELLKAVLDkldsHPLSWPFLKPVS--RKEAPDyydiIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78

                           90       100
                   ....*....|....*....|....*....
gi 1039728043  605 HSIFYKK--RFKNLGIIVGKKFEKNFKRI 631
Cdd:smart00297  79 ARTYNGPdsEVYKDAKKLEKFFEKKLREL 107
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 555-613 5.61e-06

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 45.00  E-value: 5.61e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043 555 FFIPKPKQRKEKFPDLREH-MWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNHSIFYKKRF 613
Cdd:pfam00439  17 FLEPVDPDEYPDYYSVIKKpMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGS 76
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 522-630 1.06e-03

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 41.71  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043 522 HKEAEVLKRKMSPEEQLK----CELLLLTIYCY-PKSGFFIPKPKQR---KEKFPDLREH----MWLNKIKNRLNKKAYH 589
Cdd:COG5076   125 HLKTSVKKRKTPKIEDELlyadNKAIAKFKKQLfLRDGRFLSSIFLGlpsKREYPDYYEIikspMDLLTIQKKLKNGRYK 204

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039728043 590 SVRRFVEDMRLIFHNhsiFYKKRFKNLGIIV-GKKFEKNFKR 630
Cdd:COG5076   205 SFEEFVSDLNLMFDN---CKLYNGPDSSVYVdAKELEKYFLK 243
 
Name Accession Description Interval E-value
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
 534-634 6.30e-50

Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major component of PML-SP100 nuclear bodies (NBs), which are poorly understood. It is covalently modified by SUMO-1 and may play a role in processes at the chromatin level. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99933  Cd Length: 102  Bit Score: 168.76  E-value: 6.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043 534 PEEQLKCELLLLTIYCYPKSGFFIPKPKQRKEKFPDLREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNHSIFYKK-R 612
Cdd:cd05501     1 PEELLKCEFLLLKVYCMSKSGFFISKPYYIRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDdD 80

                          90       100
                  ....*....|....*....|..
gi 1039728043 613 FKNLGIIVGKKFEKNFKRIFSI 634
Cdd:cd05501    81 FGQVGITLEKKFEKNFKEVFAI 102
HSR pfam03172
HSR domain; The Sp100 protein is a constituent of nuclear domains, also known as nuclear dots ...
 23-119 3.25e-49

HSR domain; The Sp100 protein is a constituent of nuclear domains, also known as nuclear dots (NDs). An ND-targeting region that coincides with a homodimerization domain was mapped in Sp100. Sequences similar to the Sp100 homodimerization/ND-targeting region occur in several other proteins and constitute a novel protein motif, termed HSR domain (for homogeneously-staining region). The HSR domain has also been named ASS (AIRE, Sp-100 and Sp140). This domain is usually found at the amino terminus of proteins that contain a SAND domain pfam01342.


Pssm-ID: 460835  Cd Length: 99  Bit Score: 166.56  E-value: 3.25e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043  23 ECMLKHFKTQKVAISNAIRSTFPFLESLRDHEFITGKMYEDLLDSCRSLVPVDKVIYRALEELEKKFDMTVLCELFNEVN 102
Cdd:pfam03172   3 EALFQHFKENKVEIAYAIKKPFPFLEGLRDHSFITEKMYKESLEACRNLVPVQRVVYNVLSELEKTFSLSLLEALFSDVN 82

                          90
                  ....*....|....*..
gi 1039728043 103 MEKYPDLNLIRRSFGCV 119
Cdd:pfam03172  83 LKEYPDLIEILKSFPNV 99
SAND pfam01342
SAND domain; The DNA binding activity of two proteins has been mapped to the SAND domain. The ...
 364-440 4.09e-29

SAND domain; The DNA binding activity of two proteins has been mapped to the SAND domain. The conserved KDWK motif is necessary for DNA binding, and it appears to be important for dimerization. This region is also found in the putative transcription factor RegA from the multicellular green alga Volvox cateri. This region of RegA is known as the VARL domain.


Pssm-ID: 460167  Cd Length: 76  Bit Score: 110.36  E-value: 4.09e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039728043 364 DFGGAELPVVCGNAQGFLDKEKFKQGIYVRSIRGKtGRLFTPMDFEIEGNCEKAKNWRQSIRCKGWTLRELIQKGVL 440
Cdd:pfam01342   1 DFDSPVLPVTCGAAKGLLHKKKFKQGISGKCIQNE-DSWLTPKEFEIEGGKASSKDWKRSIRCGGKPLRELIEKGLL 76
SAND smart00258
SAND domain;
368-441 8.64e-28

SAND domain;


Pssm-ID: 128554  Cd Length: 73  Bit Score: 106.27  E-value: 8.64e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039728043  368 AELPVVCGNAQGFLDKEKFKQGIYVRSIRGKtGRLFTPMDFEIEGNCEKAKNWRQSIRCKGWTLRELIQKGVLQ 441
Cdd:smart00258   1 SELPVTCGTVKGILYKKKFKCGISVKCIQYE-DKWFTPKEFEIEGGKGKSKDWKRSIRCGGSSLRTLMENGTLD 73
PHD_SP110_140 cd15626
PHD finger found in the Sp100/Sp140 family of nuclear body components; The Sp100/Sp140 family ...
 466-507 6.96e-15

PHD finger found in the Sp100/Sp140 family of nuclear body components; The Sp100/Sp140 family includes nuclear body proteins SP100, SP140, and similar proteins. Sp110, also termed interferon-induced protein 41/75, or speckled 110 kDa, or transcriptional coactivator Sp110, is a leukocyte-specific component of the nuclear body. It may function as a nuclear hormone receptor transcriptional coactivator that may play a role in inducing differentiation of myeloid cells. It is also involved in resisting intracellular pathogens and functions as an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers. Sp110 gene polymorphisms may be associated with susceptibility to tuberculosis in Chinese population. Sp110 contains a Sp100-like domain, a SAND domain, a plant homeodomain (PHD) finger, and a bromodomain (BRD). SP140, also termed lymphoid-restricted homolog of Sp100 (LYSp100), or nuclear autoantigen Sp-140, or speckled 140 kDa, is an interferon inducible nuclear leukocyte-specific protein involved in primary biliary cirrhosis and a risk factor in chronic lymphocytic leukemia. It is also implicated in innate immune response to human immunodeficiency virus type 1 (HIV-1) by binding to the virus's viral infectivity factor (Vif) protein. Sp140 contains a nuclear localization signal, a dimerization domain (HSR or CARD domain), a SAND domain, a PHD finger, and a BRD.


Pssm-ID: 277096  Cd Length: 42  Bit Score: 68.61  E-value: 6.96e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1039728043 466 ACKVCGQPRKVHPCTACKEFYHKNCHIPPVEDKSRSWHCAFC 507
Cdd:cd15626     1 KCEVCGQEGKLFCCCTCSRVFHEDCHIPPVEAQRSPWSCTFC 42
BROMO smart00297
bromo domain;
533-631 9.92e-12

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 61.91  E-value: 9.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043  533 SPEEQLKCELLLLTIYC----YPKSGFFIPKPKqrKEKFPD----LREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHN 604
Cdd:smart00297   1 DPKLQKKLQELLKAVLDkldsHPLSWPFLKPVS--RKEAPDyydiIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78

                           90       100
                   ....*....|....*....|....*....
gi 1039728043  605 HSIFYKK--RFKNLGIIVGKKFEKNFKRI 631
Cdd:smart00297  79 ARTYNGPdsEVYKDAKKLEKFFEKKLREL 107
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
 532-632 3.47e-09

Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or corepressors to modulate transcription. Vertebrate Tif1-gamma, also labeled E3 ubiquitin-protein ligase TRIM33, plays a role in the control of hematopoiesis. Its homologue in Xenopus laevis, Ectodermin, has been shown to function in germ-layer specification and control of cell growth during embryogenesis. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99934 [Multi-domain]  Cd Length: 109  Bit Score: 54.60  E-value: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043 532 MSPEEQLKCELLLLTIYCYPKS-GFFIPKPKQRKEKFPDLREHMWLNKIKNRLNKKA---YHSVRRFVEDMRLIFHNHSI 607
Cdd:cd05502     1 LSPIDQRKCERLLLELYCHELSlPFHEPVSPSVPNYYKIIKTPMDLSLIRKKLQPKSpqhYSSPEEFVADVRLMFKNCYK 80

                          90       100
                  ....*....|....*....|....*..
gi 1039728043 608 FYKKRFK--NLGIIVGKKFEKNFKRIF 632
Cdd:cd05502    81 FNEEDSEvaQAGKELELFFEEQLKEIL 107
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
 536-632 4.36e-09

Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99922 [Multi-domain]  Cd Length: 99  Bit Score: 54.30  E-value: 4.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043 536 EQLKCELLLLTIYCY--PKSGFFIPKPKqrKEKFPD----LREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNHSIFY 609
Cdd:cd04369     1 LKKKLRSLLDALKKLkrDLSEPFLEPVD--PKEAPDyyevIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78

                          90       100
                  ....*....|....*....|...
gi 1039728043 610 KKrfKNLGIIVGKKFEKNFKRIF 632
Cdd:cd04369    79 GP--GSPIYKDAKKLEKLFEKLL 99
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 555-613 5.61e-06

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 45.00  E-value: 5.61e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043 555 FFIPKPKQRKEKFPDLREH-MWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNHSIFYKKRF 613
Cdd:pfam00439  17 FLEPVDPDEYPDYYSVIKKpMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGS 76
PHD_TIF1_like cd15541
PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar ...
 467-507 2.69e-05

PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar proteins; The TIF1 family of transcriptional cofactors includes TIF1alpha (TRIM24), TIF1beta (TRIM28), TIF1gamma (TRIM33), and TIF1delta (TRIM66), which are characterized by an N-terminal RING-finger B-box coiled-coil (RBCC/TRIM) motif and plant homeodomain (PHD) finger followed by a bromodomain in the C-terminal region. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1alpha, TIF1beta, and TIF1delta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. TIF1alpha and TIF1beta bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. In contrast, TIF1delta appears to lack nuclear receptor- and KRAB-binding activity. Moreover, TIF1delta is specifically involved in heterochromatin-mediated gene silencing during postmeiotic phases of spermatogenesis. TIF1gamma is structurally closely related to TIF1alpha and TIF1beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatinic proteins HP1alpha, beta, and gamma. It cannot bind to nuclear receptors (NRs). This family also includes Sp100/Sp140 family proteins, the nuclear body SP100 and SP140. Sp110 is a leukocyte-specific component of the nuclear body. It may function as a nuclear hormone receptor transcriptional coactivator that may play a role in inducing differentiation of myeloid cells. It is also involved in resisting intracellular pathogens and functions as an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers. SP140 is an interferon inducible nuclear leukocyte-specific protein involved in primary biliary cirrhosis and a risk factor in chronic lymphocytic leukemia. It is also implicated in innate immune response to human immunodeficiency virus type 1 (HIV-1) by binding to the virus viral infectivity factor (Vif) protein. Both Sp110 and Sp140 contain a SAND domain, a plant homeodomain (PHD) finger, and a bromodomain (BRD).


Pssm-ID: 277016 [Multi-domain]  Cd Length: 43  Bit Score: 41.56  E-value: 2.69e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1039728043 467 CKVCGQPRKVHPCTACKEFYHKNCHIPPVEDKSRS-WHCAFC 507
Cdd:cd15541     2 CAVCQNGGELLCCDKCPRVFHLDCHIPPIPEFPSGeWSCSLC 43
PHD_TIF1beta cd15623
PHD finger found in transcription intermediary factor 1-beta (TIF1-beta); TIF1-beta, also ...
 467-507 3.18e-05

PHD finger found in transcription intermediary factor 1-beta (TIF1-beta); TIF1-beta, also termed Kruppel-associated Box (KRAB)-associated protein 1 (KAP-1), or KRAB-interacting protein 1 (KRIP-1), or nuclear co-repressor KAP-1, or RING finger protein 96, or tripartite motif-containing protein 28 (TRIM28), or E3 SUMO-protein ligase TRIM28, acts as a nuclear co-repressor that plays a role in transcription and in DNA damage response. Upon DNA damage, the phosphorylation of KAP-1 on serine 824 by the ataxia telangiectasia-mutated (ATM) kinase enhances cell survival and facilitates chromatin relaxation and heterochromatic DNA repair. It also regulates CHD3 nucleosome remodeling during DNA double-strand break (DSB) response. Meanwhile, KAP-1 can be dephosphorylated by protein phosphatase PP4C in the DNA damage response. In addition, KAP-1 is a co-activator of the orphan nuclear receptor NGFI-B (or Nur77) and is involved in NGFI-B-dependent transcription. It is also a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase. TIF1-beta contains an N-terminal RBCC (RING finger, B-box zinc-fingers, coiled-coil), which can interact with KRAB zinc finger proteins (KRAB-ZFPs), MDM2, MM1, C/EBPbeta, and mediates homo- and heterodimerization, a plant homeodomain (PHD) finger followed by a bromodomain in the C-terminal region, which interact with SETDB1, Mi-2alpha and other proteins to form complexes with histone deacetylase or methyltransferase activity.


Pssm-ID: 277093  Cd Length: 43  Bit Score: 41.33  E-value: 3.18e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1039728043 467 CKVCGQPRKVHPCTACKEFYHKNCHIPPVED-KSRSWHCAFC 507
Cdd:cd15623     2 CRVCQKAGALVMCDQCEFCFHLDCHLPALQEvPGEDWKCLLC 43
PHD_Int12 cd15501
PHD finger found in integrator complex subunit 12 (Int12) and similar proteins; Int12, also ...
 466-507 3.64e-05

PHD finger found in integrator complex subunit 12 (Int12) and similar proteins; Int12, also termed IntS12, or PHD finger protein 22, is a component of integrator, a multi-protein mediator of small nuclear RNA processing. The integrator complex directly interacts with the C-terminal domain of RNA polymerase II (RNAPII) largest subunit and mediates the 3' end processing of small nuclear RNAs (snRNAs) U1 and U2. Different from other components of integrator, Int12 contains a PHD finger, which is not required for snRNA 3' end cleavage. Instead, Int12 harbors a small microdomain at its N-terminus which is necessary and sufficient for Int12 function; this microdomain facilitates Int12 binding to Int1 and promotes snRNA 3' end formation.


Pssm-ID: 276976  Cd Length: 52  Bit Score: 41.56  E-value: 3.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039728043 466 ACKVCGQP------RKVHpCTACKEFYHKNCHIPPVEDKSRS-----WHCAFC 507
Cdd:cd15501     1 SCVVCKQMdvtsgnQLVE-CQECHNLYHQECHKPPVTDKDVNdprlvWYCSRC 52
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
 564-611 3.99e-05

Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates acetylation of histones at lysine residues; such acetylation is generally correlated with the activation of transcription. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99941 [Multi-domain]  Cd Length: 101  Bit Score: 42.93  E-value: 3.99e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039728043 564 KEKFPD----LREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHN-------HSIFYKK 611
Cdd:cd05509    28 KEEAPDyydvIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNcrlyngpDTEYYKC 86
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
 551-609 2.12e-04

Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in transcriptional activation, it is the catalytic component of the SWI/SNF ATP-dependent chromatin remodeling complex. The protein is essential for the regulation of gene expression (both positive and negative) of a large number of genes. The SWI/SNF complex changes chromatin structure by altering DNA-histone contacts within the nucleosome, which results in a re-positioning of the nucleosome and facilitates or represses the binding of gene-specific transcription factors. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99950  Cd Length: 103  Bit Score: 40.79  E-value: 2.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043 551 PKSGFFIPKPKqrKEKFPD----LREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHN-------HSIFY 609
Cdd:cd05519    22 KLSELFLEKPS--KKLYPDyyviIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANartynqeGSIVY 89
PHD2_PHF14 cd15562
PHD finger 2 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel ...
 467-507 6.73e-04

PHD finger 2 found in PHD finger protein 14 (PHF14) and similar proteins; PHF14 is a novel nuclear transcription factor that controls the proliferation of mesenchymal cells by directly repressing platelet-derived growth factor receptor-alpha (PDGFRalpha) expression. It also acts as an epigenetic regulator and plays an important role in the development of multiple organs in mammals. PHF14 contains three canonical plant homeodomain (PHD) fingers and a non-canonical extended PHD (ePHD) finger, Cys2HisCys5HisCys2His. It can interact with histones through its PHD fingers. The model corresponds to the second PHD finger.


Pssm-ID: 277037  Cd Length: 50  Bit Score: 37.77  E-value: 6.73e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039728043 467 CKVCGQPRKVH---PCTACKEFYHKNCHIPPVE---DKSRS--WHCAFC 507
Cdd:cd15562     2 CGICKKSNDQHllaLCDTCKLYYHLGCLDPPLTrmpKKTKNsgWQCSEC 50
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 522-630 1.06e-03

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 41.71  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039728043 522 HKEAEVLKRKMSPEEQLK----CELLLLTIYCY-PKSGFFIPKPKQR---KEKFPDLREH----MWLNKIKNRLNKKAYH 589
Cdd:COG5076   125 HLKTSVKKRKTPKIEDELlyadNKAIAKFKKQLfLRDGRFLSSIFLGlpsKREYPDYYEIikspMDLLTIQKKLKNGRYK 204

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039728043 590 SVRRFVEDMRLIFHNhsiFYKKRFKNLGIIV-GKKFEKNFKR 630
Cdd:COG5076   205 SFEEFVSDLNLMFDN---CKLYNGPDSSVYVdAKELEKYFLK 243
PHD2_KAT6A_6B cd15527
PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, ...
 466-507 1.44e-03

PHD finger 2 found in monocytic leukemia zinc-finger protein (MOZ) and its factor (MORF); MOZ, also termed histone acetyltransferase KAT6A, YBF2/SAS3, SAS2 and TIP60 protein 3 (MYST-3), or runt-related transcription factor-binding protein 2, or zinc finger protein 220, is a MYST-type histone acetyltransferase (HAT) that functions as a coactivator for acute myeloid leukemia 1 protein (AML1)- and p53-dependent transcription. It possesses intrinsic HAT activity to acetylate both itself and lysine (K) residues on histone H2B, histone H3 (K14) and histone H4 (K5, K8, K12 and K16) in vitro and H3K9 in vivo. MOZ-related factor (MORF), also termed MOZ2, or histone acetyltransferase KAT6B, or MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4 (MYST4), is a ubiquitously expressed transcriptional regulator with intrinsic HAT activity. It can interact with the Runt-domain transcription factor Runx2 and form a tetrameric complex with BRPFs, ING5, and EAF6. Both MOZ and MORF are catalytic subunits of HAT complexes that are required for normal developmental programs, such as hematopoiesis, neurogenesis, and skeletogenesis, and are also implicated in human leukemias. MOZ is also the catalytic subunit of a tetrameric inhibitor of growth 5 (ING5) complex, which specifically acetylates nucleosomal histone H3K14. Moreover, MOZ and MORF are involved in regulating transcriptional activation mediated by Runx2 (or Cbfa1), a Runt-domain transcription factor known to play important roles in T cell lymphomagenesis and bone development, and its homologs. MOZ contains a linker histone 1 and histone 5 domains and two plant homeodomain (PHD) fingers. In contrast, MORF contains an N-terminal region containing two PHD fingers, a putative HAT domain, an acidic region, and a C-terminal Ser/Met-rich domain. The family corresponds to the first PHD finger.


Pssm-ID: 277002  Cd Length: 46  Bit Score: 36.97  E-value: 1.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1039728043 466 ACKVC---GQPRKVHPCTACKEFYHKNCHIPPV-EDKSRSWHCAFC 507
Cdd:cd15527     1 TCSVCqdsGNADNLLFCDACDKGFHMECHDPPLtRMPKGKWVCQIC 46
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
 536-609 1.83e-03

Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The Williams-Beuren syndrome deletion transcript 9 is a putative transcriptional regulator. WSTF was found to play a role in vitamin D-mediated transcription as part of two chromatin remodeling complexes, WINAC and WICH. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99937  Cd Length: 97  Bit Score: 38.29  E-value: 1.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039728043 536 EQLKCELLLLTIYCYPKS-GFFIPKPKQRKEKFPDLREH-MWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNHSIFY 609
Cdd:cd05505     1 ELQKCEEILSKILKYRFSwPFREPVTADEAEDYKKVITNpMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKYY 76
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
 571-604 1.93e-03

Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99930  Cd Length: 102  Bit Score: 38.03  E-value: 1.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1039728043 571 REHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHN 604
Cdd:cd05498    43 KHPMDLSTIKKKLDNREYADAQEFAADVRLMFSN 76
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
 553-604 2.81e-03

Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99946  Cd Length: 105  Bit Score: 37.67  E-value: 2.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039728043 553 SGFFIPKPKqrKEKFPD----LREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHN 604
Cdd:cd05515    24 SLIFMRLPS--KSEYPDyydvIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDN 77
PHD1_MTF2 cd15578
PHD finger 1 found in metal-response element-binding transcription factor 2 (MTF2); MTF2, also ...
 467-507 6.08e-03

PHD finger 1 found in metal-response element-binding transcription factor 2 (MTF2); MTF2, also termed metal regulatory transcription factor 2, or metal-response element DNA-binding protein M96, or polycomb-like protein 2 (PCL2), complexes with the polycomb repressive complex-2 (PRC2) in embryonic stem cells and regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation. It recruits the PRC2 complex to the inactive X chromosome and target loci in embryonic stem cells. Moreover, MTF2 is required for PRC2-mediated Hox cluster repression. It activates the Cdkn2a gene and promotes cellular senescence, thus suppressing the catalytic activity of PRC2 locally. MTF2 consists of an N-terminal Tudor domain followed by two PHD fingers, and a C-terminal MTF2 domain. This model corresponds to the first PHD finger.


Pssm-ID: 277053  Cd Length: 53  Bit Score: 35.45  E-value: 6.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039728043 467 CKVCGQPRKVHP-----CTACKEFYHKNCHIPPVEDKSRS----WHCAFC 507
Cdd:cd15578     2 CTVCQDGSSESPneivlCDKCGQGYHQLCHNPKIDSSVLDpdvpWLCRQC 51
PHD2_KMT2D cd15595
PHD finger 2 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ...
 467-507 9.22e-03

PHD finger 2 found in Histone-lysine N-methyltransferase 2D (KMT2D); KMT2D, also termed ALL1-related protein (ALR), is encoded by the gene that was named myeloid/lymphoid or mixed-lineage leukemia 4 (MLL4), a fourth human homolog of Drosophila trithorax, located on chromosome 12. KMT2D enzymatically generates trimethylated histone H3 Lys 4 (H3K4me3). It plays an essential role in differentiating the human pluripotent embryonal carcinoma cell line NTERA-2 clone D1 (NT2/D1) stem cells by activating differentiation-specific genes, such asHOXA1-3 and NESTIN. It is also a part of activating signal cointegrator-2 (ASC-2)-containing complex (ASCOM) that contains the transcriptional coactivator nuclear receptor coactivator 6 (NCOA6), KMT2C and KMT2D. The ASCOM complex is critical for nuclear receptor (NR) activation of bile acid transporter genes and is down regulated in cholestasis. KMT2D contains the catalytic domain SET, five plant homeodomain (PHD) fingers, two extended PHD (ePHD) fingers, Cys2HisCys5HisCys2His, a RING finger, an HMG (high-mobility group)-binding motif, and two FY-rich regions. This model corresponds to the second PHD finger.


Pssm-ID: 277070  Cd Length: 46  Bit Score: 34.59  E-value: 9.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1039728043 467 CKVCGQP---RKVHPCTACKEFYHKNCHIPPVED-KSRSWHCAFC 507
Cdd:cd15595     2 CQTCRKPgedSKMLVCEACDKGYHTFCLKPAMESlPTDSWKCKAC 46
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
 574-604 9.29e-03

Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99932  Cd Length: 103  Bit Score: 36.14  E-value: 9.29e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1039728043 574 MWLNKIKNRLNKKAYHSVRRFVEDMRLIFHN 604
Cdd:cd05500    47 MDLGTIERKLKSNVYTSVEEFTADFNLMVDN 77
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
 571-630 9.65e-03

Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99931  Cd Length: 102  Bit Score: 36.11  E-value: 9.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039728043 571 REHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNhsiFYKkrFKNLGIIV---GKKFEKNFKR 630
Cdd:cd05499    43 KKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKN---CYT--FNPEGTDVymmGHQLEEVFND 100
 
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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