Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930    1964 VNNFLKKKEAGAGEVHIRVVSSSDKCVEVKPGMRRRFVEQGEmmNEFPYRAKALFAFEEVDGIDVCFFGMHVQEYGSECP 2043
Cdd:pfam08214    1 LNDFLAKVLPKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVCP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930    2044 APNTRRVYIAYLDSVHFFRPRqYRTAVYHEILLGYMDYVKQLGYTMAHIWACPPSEGDDYIFhchPTDQKIPK-----PK 2118
Cdd:pfam08214   79 DPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldGK 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930    2119 RLQEWYKKMLDKGM-------IERIIQDYKDILKQ-----AMEDKL-------------GSAAELPYFEGDFWPNVLEES 2173
Cdd:pfam08214  155 GLLKWWCKMLDKILveykssaKAKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEEL 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930    2174 IKE-------LDQEEEEKRKQ-----AEAAEAAAAANLFSIEENEVSGDGKKKGQKKAKKSNKSKAAQRKNSKKSNEHQS 2241
Cdd:pfam08214  235 IKEgrwksvsLDQFWEELRFRqefslGRLVGFIGLEGDYTPGSDDVINPPGLVKSKKQYKMIKSYITGREYSTEEGAPES 314

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1916930    2242 GNDLSTKIYATMEKHkevFFVIRLHSAQSAASLAPIQ 2278
Cdd:pfam08214  315 VNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRIA 348

KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP also binds to transactivation domains of other nuclear factors including Myb and Jun.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930     938 DNEKDWRESVTADLRNHLVHKLVQAIFPTSDPTTMQDKRMHNLVSYAEKVEKDMYEMAKSRSEYYHLLAEKIYKIQKELE 1017
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 1916930    1018 E 1018
Cdd:pfam02172   81 E 81

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 1916930  2333 YTCNHCKTAVETRYHCTVCDDFDLCIVCKEKVGHQHKMEKL 2373
Cdd:cd02337    1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41

TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1916930    2399 IQRCIQSLAHACQCRDAN---CRLPSCQKMKLVVQHTKNCKRkpNGGC--PICKQLIALCCyHAKNCEEQKCPV 2467
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71

Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) binding protein (CREBBP, also known as CBP) and its paralog p300; CREBBP (also called CBP) and its paralog p300, generally referred to as CREBBP/p300, are universal transcriptional coactivators that interact with many important transcription factors and comodulators to activate transcription. The NCBD domain [nuclear coactivator binding domain, also known as IRF-3 binding domain (IBiD) or SRC1 interaction domain (SID)] of CREBBP/p300 behaves as an intrinsically disordered domain in isolation, but folds into helical structures with different topologies upon binding to different ligands such as nuclear receptor coactivator p160, CREBBP interaction domain (CID) from nuclear receptor coactivator 1 (NCOA1 or Src1), NCOA2 (Tif2), and NCOA3 (ACTR), or interferon regulatory factor 3 (IRF-3). In Drosophila, there is only one CREB-binding protein ortholog and it is called nejire, dCBP, CBP/p300, or CBP.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 1916930  2814 QLALIMQKIKNNPTNESNQHILAILKQNPQIMAAIIKQRQQSQ 2856
Cdd:cd20910    1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43

Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930    1964 VNNFLKKKEAGAGEVHIRVVSSSDKCVEVKPGMRRRFVEQGEmmNEFPYRAKALFAFEEVDGIDVCFFGMHVQEYGSECP 2043
Cdd:pfam08214    1 LNDFLAKVLPKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVCP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930    2044 APNTRRVYIAYLDSVHFFRPRqYRTAVYHEILLGYMDYVKQLGYTMAHIWACPPSEGDDYIFhchPTDQKIPK-----PK 2118
Cdd:pfam08214   79 DPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldGK 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930    2119 RLQEWYKKMLDKGM-------IERIIQDYKDILKQ-----AMEDKL-------------GSAAELPYFEGDFWPNVLEES 2173
Cdd:pfam08214  155 GLLKWWCKMLDKILveykssaKAKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEEL 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930    2174 IKE-------LDQEEEEKRKQ-----AEAAEAAAAANLFSIEENEVSGDGKKKGQKKAKKSNKSKAAQRKNSKKSNEHQS 2241
Cdd:pfam08214  235 IKEgrwksvsLDQFWEELRFRqefslGRLVGFIGLEGDYTPGSDDVINPPGLVKSKKQYKMIKSYITGREYSTEEGAPES 314

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1916930    2242 GNDLSTKIYATMEKHkevFFVIRLHSAQSAASLAPIQ 2278
Cdd:pfam08214  315 VNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRIA 348

KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP also binds to transactivation domains of other nuclear factors including Myb and Jun.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930     938 DNEKDWRESVTADLRNHLVHKLVQAIFPTSDPTTMQDKRMHNLVSYAEKVEKDMYEMAKSRSEYYHLLAEKIYKIQKELE 1017
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 1916930    1018 E 1018
Cdd:pfam02172   81 E 81

atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This ring domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930  1818 FNPQVLCCYGKqlCTIPRD--AKYYSYQNSlkeygvaSNRYTYCQKCFNDIQGDTVTLGDDPlqsQTQIKKDQFKEMKND 1895
Cdd:cd15802    1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNL-------DNRYHFCEKCFNEIRGDEITLGDDQ---GTSISKSQFEKKKND 68

                 ....*
gi 1916930  1896 HLELE 1900
Cdd:cd15802   69 ELDEE 73

CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This RING domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1916930    1804 VMQALGYCCGRKYTFNPQVLCCYGKQLCTIPRDAKYYSYQ 1843
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40

TAZ zinc finger, present in p300 and CBP;

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1916930      524 HAHKCNRREnlnpnrEVCNVNYCKAMKSVLAHMGTCKQSKdCTMQHCASSRQILLHYKTCQNSGCVICYPF 594
Cdd:smart00551   16 HARRCKARE------AKCQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79

TAZ zinc finger, present in p300 and CBP;

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1916930     2398 SIQRCIQSLAHACQC--RDANCRLPSCQKMKLVVQHTKNCK--RKPNGGCPICKQLIalccYHAKNCEEQKCPVPFC 2470
Cdd:smart00551    6 QLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVCKC 78

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930  1710 LEKLYRQEPESV---PFRYPVDPQALGIPDYFEIVKKPMDLGTIRTNIQNGKYSDPWEYVDDVWLMFDNAWLYNPKTSRV 1786
Cdd:COG5076  151 AKFKKQLFLRDGrflSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSV 230

                         90
                 ....*....|....*....
gi 1916930  1787 YRYCTKLSEVFEAEIDPVM 1805
Cdd:COG5076  231 YVDAKELEKYFLKLIEEIP 249

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1916930     2329 DKFVYTCNHCKTA-VETRYHCTVCDDFDLCIVCKEKVGHQHKME 2371
Cdd:smart00291    1 VHHSYSCDTCGKPiVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1916930    2329 DKFVYTCNHCKTA--VETRYHCTVCDDFDLCIVCK-EKVGHQHKM 2370
Cdd:pfam00569    1 IHKVYTCNGCSNDpsIGVRYHCLRCSDYDLCQSCFqTHKGGNHQM 45

Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930    1964 VNNFLKKKEAGAGEVHIRVVSSSDKCVEVKPGMRRRFVEQGEmmNEFPYRAKALFAFEEVDGIDVCFFGMHVQEYGSECP 2043
Cdd:pfam08214    1 LNDFLAKVLPKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVCP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930    2044 APNTRRVYIAYLDSVHFFRPRqYRTAVYHEILLGYMDYVKQLGYTMAHIWACPPSEGDDYIFhchPTDQKIPK-----PK 2118
Cdd:pfam08214   79 DPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldGK 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930    2119 RLQEWYKKMLDKGM-------IERIIQDYKDILKQ-----AMEDKL-------------GSAAELPYFEGDFWPNVLEES 2173
Cdd:pfam08214  155 GLLKWWCKMLDKILveykssaKAKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEEL 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930    2174 IKE-------LDQEEEEKRKQ-----AEAAEAAAAANLFSIEENEVSGDGKKKGQKKAKKSNKSKAAQRKNSKKSNEHQS 2241
Cdd:pfam08214  235 IKEgrwksvsLDQFWEELRFRqefslGRLVGFIGLEGDYTPGSDDVINPPGLVKSKKQYKMIKSYITGREYSTEEGAPES 314

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1916930    2242 GNDLSTKIYATMEKHkevFFVIRLHSAQSAASLAPIQ 2278
Cdd:pfam08214  315 VNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRIA 348

KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP also binds to transactivation domains of other nuclear factors including Myb and Jun.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930     938 DNEKDWRESVTADLRNHLVHKLVQAIFPTSDPTTMQDKRMHNLVSYAEKVEKDMYEMAKSRSEYYHLLAEKIYKIQKELE 1017
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 1916930    1018 E 1018
Cdd:pfam02172   81 E 81

atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This ring domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930  1818 FNPQVLCCYGKqlCTIPRD--AKYYSYQNSlkeygvaSNRYTYCQKCFNDIQGDTVTLGDDPlqsQTQIKKDQFKEMKND 1895
Cdd:cd15802    1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNL-------DNRYHFCEKCFNEIRGDEITLGDDQ---GTSISKSQFEKKKND 68

                 ....*
gi 1916930  1896 HLELE 1900
Cdd:cd15802   69 ELDEE 73

Bromodomain, uncharacterized subfamily specific to plants. Might function as a global transcription factor. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930  1710 LEKLyRQEPESVPFRYPVDPQALGIPDYFEIVKKPMDLGTIRTNIQNGKYSDPWEYVDDVWLMFDNAWLYNPKTSRVYRY 1789
Cdd:cd05506    9 LRKL-MKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTM 87

                         90
                 ....*....|.
gi 1916930  1790 CTKLSEVFEAE 1800
Cdd:cd05506   88 AKELLKIFETR 98

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930  1718 PESVPFRYPVDPQALGIPDYFEIVKKPMDLGTIRTNIQNGKYSDPWEYVDDVWLMFDNAWLYNPKTSRVYRYCTKLSEVF 1797
Cdd:cd05500   20 KDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQMGKRLQAAF 99

                 .
gi 1916930  1798 E 1798
Cdd:cd05500  100 E 100

CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This RING domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1916930    1804 VMQALGYCCGRKYTFNPQVLCCYGKQLCTIPRDAKYYSYQ 1843
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930  1701 ELRTALLPTLEKLyRQEPESVPFRYPVDPQAlgIPDYFEIVKKPMDLGTIRTNIQNGKYSDPWEYVDDVWLMFDNAWLYN 1780
Cdd:cd05509    1 PLYTQLKKVLDSL-KNHKSAWPFLEPVDKEE--APDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77

                         90
                 ....*....|....*...
gi 1916930  1781 PKTSRVYRYCTKLSEVFE 1798
Cdd:cd05509   78 GPDTEYYKCANKLEKFFW 95

TAZ zinc finger, present in p300 and CBP;

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1916930      524 HAHKCNRREnlnpnrEVCNVNYCKAMKSVLAHMGTCKQSKdCTMQHCASSRQILLHYKTCQNSGCVICYPF 594
Cdd:smart00551   16 HARRCKARE------AKCQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79

Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930  1687 NAGDKKKKCQfnpeelrtallpTLEKLYRQEPESVPFRYPVDpqALGIPDYFEIVKKPMDLGTIRTNIQNGKYSDPWEYV 1766
Cdd:cd05496    2 DESDWKKQCK------------ELVNLMWDCEDSEPFRQPVD--LLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFA 67

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 1916930  1767 DDVWLMFDNAWLYNP-KTSRVYRYCTKLSEVFEAEIDPV 1804
Cdd:cd05496   68 KDVRLIFSNSKSYTPnKRSRIYSMTLRLSALFEEHIKKI 106

TAZ zinc finger, present in p300 and CBP;

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1916930     2398 SIQRCIQSLAHACQC--RDANCRLPSCQKMKLVVQHTKNCK--RKPNGGCPICKQLIalccYHAKNCEEQKCPVPFC 2470
Cdd:smart00551    6 QLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVCKC 78

Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was identified as a novel human bromodomain gene by cDNA library screening. The Drosophila homologue, Acf1, is part of the CHRAC (chromatin accessibility complex) and regulates ISWI-induced nucleosome remodeling. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930  1716 QEPESVPFRYPVdpQALGIPDYFEIVKKPMDLGTIRTNIQNGKYSDPWEYVDDVWLMFDNAWLYNPKTSRVYRYCTKLSE 1795
Cdd:cd05504   26 KHKDSWPFLRPV--SKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHTSVYKAGTRLQR 103

                 ....*
gi 1916930  1796 VFEAE 1800
Cdd:cd05504  104 FFIKR 108

Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, a large multi-domain complex, which initiates the assembly of the transcription machinery. TAFII250 contains two bromodomains that specifically bind to acetylated histone H4. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1916930  1715 RQEPESVPFRYPVDPQAlgIPDYFEIVKKPMDLGTIRTNIQNGKYSDPWEYVDDVWLMFDNAWLYNPKTSR 1785
Cdd:cd05511   13 KNLPDSWPFHTPVNKKK--VPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSV 81

Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, and SLIK. SAGA is involved in the RNA polymerase II-dependent transcriptional regulation of about 10% of all yeast genes. The SPT7 bromodomain has been shown to weakly interact with acetylated histone H3, but not H4. The human representative of this subfamily is cat eye syndrome critical region protein 2 (CECR2). Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930  1700 EELRTALLPTLEKLYRQEPESVPFRYPVDPQAlgIPDYFEIVKKPMDLGTIRTNIQNGKYSDPWEYVDDVWLMFDNAWLY 1779
Cdd:cd05510    6 EEFYESLDKVLNELKTYTEHSTPFLTKVSKRE--APDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLY 83

                         90
                 ....*....|.
gi 1916930  1780 NPKTSRVYRYC 1790
Cdd:cd05510   84 NSDPSHPLRRH 94

PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300/CBP family includes two highly homologous histone acetyltransferases (HATs), CREB-binding protein (CBP) and p300. CBP is also known as KAT3A or CREBBP. It specifically interacts with the phosphorylated form of cyclic adenosine monophosphate-responsive element-binding protein (CREB). p300, also termed as KAT3B, or E1A-associated protein p300 (EP300), is a paralog of CBP. and is involved in E1A function in cell cycle progression and cellular differentiation. Both CBP and p300 are co-activator proteins that have been implicated in cell cycle regulation, apoptosis, embryonic development, cellular differentiation and cancer. They associate with a number of DNA-binding transcription activators as well as general transcription factors (GTFs), thus mediating recruitment of basal transcription machinery to the promoter. They contain a cysteine-histidine rich region, KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain.

                         10        20        30
                 ....*....|....*....|....*....|..
gi 1916930  1902 FVNCQECGRKQHQICVLWLDSIWPGGFVCDNC 1933
Cdd:cd15557    6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37

Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) binding protein (CREBBP, also known as CBP) and its paralog p300; CREBBP (also called CBP) and its paralog p300, generally referred to as CREBBP/p300, are universal transcriptional coactivators that interact with many important transcription factors and comodulators to activate transcription. The NCBD domain [nuclear coactivator binding domain, also known as IRF-3 binding domain (IBiD) or SRC1 interaction domain (SID)] of CREBBP/p300 behaves as an intrinsically disordered domain in isolation, but folds into helical structures with different topologies upon binding to different ligands such as nuclear receptor coactivator p160, CREBBP interaction domain (CID) from nuclear receptor coactivator 1 (NCOA1 or Src1), NCOA2 (Tif2), and NCOA3 (ACTR), or interferon regulatory factor 3 (IRF-3). In Drosophila, there is only one CREB-binding protein ortholog and it is called nejire, dCBP, CBP/p300, or CBP.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 1916930  2814 QLALIMQKIKNNPTNESNQHILAILKQNPQIMAAIIKQRQQSQ 2856
Cdd:cd20910    1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43

Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein assumed to be a transcriptional regulator. BRD1 has been implicated with brain development and susceptibility to schizophrenia and bipolar affective disorder. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916930  1702 LRTALLPTLEKLYRQEPESVpFRYPVDPQAlgIPDYFEIVKKPMDLGTIRTNIQNGKYSDPWEYVDDVWLMFDNAWLYNP 1781
Cdd:cd05512    2 LEVLLRKTLDQLQEKDTAEI-FSEPVDLSE--VPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNA 78

                         90
                 ....*....|....
gi 1916930  1782 KTSRVYRYCTKLSE 1795
Cdd:cd05512   79 KDTIFYRAAVRLRD 92

PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated protein p300 (EP300), is a paralog of CREB-binding protein (CBP). It is involved in E1A function in cell cycle progression and cellular differentiation. It functions as an intrinsic HAT, as well as a factor acetyltransferase (FAT) for many transcription regulators. And thus, p300 serves as a scaffold or bridge for transcription factors and other components of the basal transcription machinery to facilitate chromatin remodeling and to activate gene transcription. p300 contains a cysteine-histidine rich region, KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain.

                         10        20        30
                 ....*....|....*....|....*....|....
gi 1916930  1902 FVNCQECGRKQHQICVLWLDSIWPGGFVCDNCLK 1935
Cdd:cd15646    7 FVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1916930  1735 PDYFEIVKKPMDLGTIRTNIQNGKYSDPWEYVDDVWLMFDNAWLYNPKTSRVYRYCTKLSEVF 1797
Cdd:cd05515   37 PDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYKDALTLQKVL 99

Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1916930  1734 IPDYFEIVKKPMDLGTIRTNIQNGKYSDPWEYVDDVWLMFDNAWLYNPKTSRVYRYCTKLSEVF 1797
Cdd:cd05516   37 LPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 100

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1916930    2329 DKFVYTCNHCKTA--VETRYHCTVCDDFDLCIVCK-EKVGHQHKM 2370
Cdd:pfam00569    1 IHKVYTCNGCSNDpsIGVRYHCLRCSDYDLCQSCFqTHKGGNHQM 45