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Conserved domains on  [gi|124249354|ref|NP_038701|]
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nuclear autoantigen Sp-100 isoform 1 [Mus musculus]

Protein Classification

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 ...
474-574 1.23e-49

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: 167.22  E-value: 1.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354 474 QTRRQKCELLLLTIYCYPKSGFFIPKPKQRKEKFPDLREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNHSIFYKK-R 552
Cdd:cd05501    1 PEELLKCEFLLLKVYCMSKSGFFISKPYYIRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDdD 80
                         90       100
                 ....*....|....*....|..
gi 124249354 553 FKNLGIIVGKKFEKNFKRIFSI 574
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 1.73e-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: 1.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354   23 ECMLKHFKTQKVAISNAIRSTFPFLESLRDHEFITGKMYEDLLDSCRSLVPVDKVIYRALEELEKKFDMTVLCELFNEVN 102
Cdd:pfam03172   3 EALFQHFKENKVEIAYAIKKPFPFLEGLRDHSFITEKMYKESLEACRNLVPVQRVVYNVLSELEKTFSLSLLEALFSDVN 82
                          90
                  ....*....|....*..
gi 124249354  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 ...
382-458 3.76e-30

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: 113.06  E-value: 3.76e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124249354  382 DFGGAELPVVCGNAQGFLDKEKFKQGIYVRSIRGKtGRLFTPMDFEIEGNCEKAKNWRQSIRCKGWTLRELIQKGVL 458
Cdd:pfam01342   1 DFDSPVLPVTCGAAKGLLHKKKFKQGISGKCIQNE-DSWLTPKEFEIEGGKASSKDWKRSIRCGGKPLRELIEKGLL 76
 
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 ...
474-574 1.23e-49

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: 167.22  E-value: 1.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354 474 QTRRQKCELLLLTIYCYPKSGFFIPKPKQRKEKFPDLREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNHSIFYKK-R 552
Cdd:cd05501    1 PEELLKCEFLLLKVYCMSKSGFFISKPYYIRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDdD 80
                         90       100
                 ....*....|....*....|..
gi 124249354 553 FKNLGIIVGKKFEKNFKRIFSI 574
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 1.73e-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: 1.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354   23 ECMLKHFKTQKVAISNAIRSTFPFLESLRDHEFITGKMYEDLLDSCRSLVPVDKVIYRALEELEKKFDMTVLCELFNEVN 102
Cdd:pfam03172   3 EALFQHFKENKVEIAYAIKKPFPFLEGLRDHSFITEKMYKESLEACRNLVPVQRVVYNVLSELEKTFSLSLLEALFSDVN 82
                          90
                  ....*....|....*..
gi 124249354  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 ...
382-458 3.76e-30

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: 113.06  E-value: 3.76e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124249354  382 DFGGAELPVVCGNAQGFLDKEKFKQGIYVRSIRGKtGRLFTPMDFEIEGNCEKAKNWRQSIRCKGWTLRELIQKGVL 458
Cdd:pfam01342   1 DFDSPVLPVTCGAAKGLLHKKKFKQGISGKCIQNE-DSWLTPKEFEIEGGKASSKDWKRSIRCGGKPLRELIEKGLL 76
SAND smart00258
SAND domain;
386-459 1.43e-28

SAND domain;


Pssm-ID: 128554  Cd Length: 73  Bit Score: 108.59  E-value: 1.43e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124249354   386 AELPVVCGNAQGFLDKEKFKQGIYVRSIRGKtGRLFTPMDFEIEGNCEKAKNWRQSIRCKGWTLRELIQKGVLQ 459
Cdd:smart00258   1 SELPVTCGTVKGILYKKKFKCGISVKCIQYE-DKWFTPKEFEIEGGKGKSKDWKRSIRCGGSSLRTLMENGTLD 73
BROMO smart00297
bromo domain;
473-571 1.31e-10

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 58.44  E-value: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354   473 RQTRRQKCELLLLTIYC----YPKSGFFIPKPKqrKEKFPD----LREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHN 544
Cdd:smart00297   1 DPKLQKKLQELLKAVLDkldsHPLSWPFLKPVS--RKEAPDyydiIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                           90       100
                   ....*....|....*....|....*....
gi 124249354   545 HSIFYKK--RFKNLGIIVGKKFEKNFKRI 571
Cdd:smart00297  79 ARTYNGPdsEVYKDAKKLEKFFEKKLREL 107
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
495-553 5.32e-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: 44.61  E-value: 5.32e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354  495 FFIPKPKQRKEKFPDLREH-MWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNHSIFYKKRF 553
Cdd:pfam00439  17 FLEPVDPDEYPDYYSVIKKpMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGS 76
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
460-570 6.21e-04

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 42.49  E-value: 6.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354 460 DPPRKKKETPRNPRQTRRQKCELLLLTIYCY-PKSGFFIPKPKQR---KEKFPDLREH----MWLNKIKNRLNKKAYHSV 531
Cdd:COG5076  127 KTSVKKRKTPKIEDELLYADNKAIAKFKKQLfLRDGRFLSSIFLGlpsKREYPDYYEIikspMDLLTIQKKLKNGRYKSF 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 124249354 532 RRFVEDMRLIFHNhsiFYKKRFKNLGIIV-GKKFEKNFKR 570
Cdd:COG5076  207 EEFVSDLNLMFDN---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 ...
474-574 1.23e-49

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: 167.22  E-value: 1.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354 474 QTRRQKCELLLLTIYCYPKSGFFIPKPKQRKEKFPDLREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNHSIFYKK-R 552
Cdd:cd05501    1 PEELLKCEFLLLKVYCMSKSGFFISKPYYIRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDdD 80
                         90       100
                 ....*....|....*....|..
gi 124249354 553 FKNLGIIVGKKFEKNFKRIFSI 574
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 1.73e-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: 1.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354   23 ECMLKHFKTQKVAISNAIRSTFPFLESLRDHEFITGKMYEDLLDSCRSLVPVDKVIYRALEELEKKFDMTVLCELFNEVN 102
Cdd:pfam03172   3 EALFQHFKENKVEIAYAIKKPFPFLEGLRDHSFITEKMYKESLEACRNLVPVQRVVYNVLSELEKTFSLSLLEALFSDVN 82
                          90
                  ....*....|....*..
gi 124249354  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 ...
382-458 3.76e-30

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: 113.06  E-value: 3.76e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124249354  382 DFGGAELPVVCGNAQGFLDKEKFKQGIYVRSIRGKtGRLFTPMDFEIEGNCEKAKNWRQSIRCKGWTLRELIQKGVL 458
Cdd:pfam01342   1 DFDSPVLPVTCGAAKGLLHKKKFKQGISGKCIQNE-DSWLTPKEFEIEGGKASSKDWKRSIRCGGKPLRELIEKGLL 76
SAND smart00258
SAND domain;
386-459 1.43e-28

SAND domain;


Pssm-ID: 128554  Cd Length: 73  Bit Score: 108.59  E-value: 1.43e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124249354   386 AELPVVCGNAQGFLDKEKFKQGIYVRSIRGKtGRLFTPMDFEIEGNCEKAKNWRQSIRCKGWTLRELIQKGVLQ 459
Cdd:smart00258   1 SELPVTCGTVKGILYKKKFKCGISVKCIQYE-DKWFTPKEFEIEGGKGKSKDWKRSIRCGGSSLRTLMENGTLD 73
BROMO smart00297
bromo domain;
473-571 1.31e-10

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 58.44  E-value: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354   473 RQTRRQKCELLLLTIYC----YPKSGFFIPKPKqrKEKFPD----LREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHN 544
Cdd:smart00297   1 DPKLQKKLQELLKAVLDkldsHPLSWPFLKPVS--RKEAPDyydiIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                           90       100
                   ....*....|....*....|....*....
gi 124249354   545 HSIFYKK--RFKNLGIIVGKKFEKNFKRI 571
Cdd:smart00297  79 ARTYNGPdsEVYKDAKKLEKFFEKKLREL 107
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
476-572 2.79e-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: 54.69  E-value: 2.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354 476 RRQKCELLLLTIYCY--PKSGFFIPKPKqrKEKFPD----LREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNHSIFY 549
Cdd:cd04369    1 LKKKLRSLLDALKKLkrDLSEPFLEPVD--PKEAPDyyevIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78
                         90       100
                 ....*....|....*....|...
gi 124249354 550 KKrfKNLGIIVGKKFEKNFKRIF 572
Cdd:cd04369   79 GP--GSPIYKDAKKLEKLFEKLL 99
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
477-572 3.95e-07

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: 48.83  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354 477 RQKCELLLLTIYCYPKS-GFFIPKPKQRKEKFPDLREHMWLNKIKNRLNKKA---YHSVRRFVEDMRLIFHNHSIFYK-- 550
Cdd:cd05502    6 QRKCERLLLELYCHELSlPFHEPVSPSVPNYYKIIKTPMDLSLIRKKLQPKSpqhYSSPEEFVADVRLMFKNCYKFNEed 85
                         90       100
                 ....*....|....*....|...
gi 124249354 551 -KRFKNlGIIVGKKFEKNFKRIF 572
Cdd:cd05502   86 sEVAQA-GKELELFFEEQLKEIL 107
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
495-553 5.32e-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: 44.61  E-value: 5.32e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354  495 FFIPKPKQRKEKFPDLREH-MWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNHSIFYKKRF 553
Cdd:pfam00439  17 FLEPVDPDEYPDYYSVIKKpMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGS 76
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
504-551 2.96e-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: 43.31  E-value: 2.96e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 124249354 504 KEKFPD----LREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHN-------HSIFYKK 551
Cdd:cd05509   28 KEEAPDyydvIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNcrlyngpDTEYYKC 86
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
491-549 2.10e-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: 2.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354 491 PKSGFFIPKPKqrKEKFPD----LREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHN-------HSIFY 549
Cdd:cd05519   22 KLSELFLEKPS--KKLYPDyyviIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANartynqeGSIVY 89
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
478-549 2.77e-04

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: 40.21  E-value: 2.77e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124249354 478 QKCELLLLTIYCYPKSG-FFIPKPKQRKEKFPDLREH-MWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNHSIFY 549
Cdd:cd05505    3 QKCEEILSKILKYRFSWpFREPVTADEAEDYKKVITNpMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKYY 76
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
460-570 6.21e-04

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 42.49  E-value: 6.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124249354 460 DPPRKKKETPRNPRQTRRQKCELLLLTIYCY-PKSGFFIPKPKQR---KEKFPDLREH----MWLNKIKNRLNKKAYHSV 531
Cdd:COG5076  127 KTSVKKRKTPKIEDELLYADNKAIAKFKKQLfLRDGRFLSSIFLGlpsKREYPDYYEIikspMDLLTIQKKLKNGRYKSF 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 124249354 532 RRFVEDMRLIFHNhsiFYKKRFKNLGIIV-GKKFEKNFKR 570
Cdd:COG5076  207 EEFVSDLNLMFDN---CKLYNGPDSSVYVdAKELEKYFLK 243
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
477-544 7.73e-04

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: 39.21  E-value: 7.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124249354 477 RQKCELLLLTIYCY------PKSGFFIPKPKqrKEKFPD----LREHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHN 544
Cdd:cd05515    2 QQKLWELYNAVKNYtdgrgrRLSLIFMRLPS--KSEYPDyydvIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDN 77
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
511-544 1.26e-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: 38.41  E-value: 1.26e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 124249354 511 REHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHN 544
Cdd:cd05498   43 KHPMDLSTIKKKLDNREYADAQEFAADVRLMFSN 76
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
511-570 8.44e-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: 8.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124249354 511 REHMWLNKIKNRLNKKAYHSVRRFVEDMRLIFHNhsiFYKkrFKNLGIIV---GKKFEKNFKR 570
Cdd:cd05499   43 KKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKN---CYT--FNPEGTDVymmGHQLEEVFND 100
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
514-544 8.45e-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: 8.45e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 124249354 514 MWLNKIKNRLNKKAYHSVRRFVEDMRLIFHN 544
Cdd:cd05500   47 MDLGTIERKLKSNVYTSVEEFTADFNLMVDN 77
 
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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