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Conserved domains on  [gi|392896225|ref|NP_499161|]
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Protein cbp-1 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAT_KAT11 super family cl02120
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1120-1335 3.61e-74

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.


The actual alignment was detected with superfamily member pfam08214:

Pssm-ID: 413203  Cd Length: 348  Bit Score: 251.55  E-value: 3.61e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1120 VNGFIKKQLqAEAHKypVIIRTLCVQDKEAEVKAQMKQKYVESNqfPEKFPYRTKAVFAFEIIDGVEVCFFGLHVQEYGS 1199
Cdd:pfam08214    1 LNDFLAKVL-PKGVK--VTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1200 ACPAPNARRVYIAYLDSVHFFQPReLRTDVYHELLLGYLDYAKMLGYTMAHIWACPPSEGDDYIFhchPPEQKIPK---- 1275
Cdd:pfam08214   76 VCPDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvl 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1276 -PKRLQDWYKKMLEKGV-------QEGSVVEFKDIYKQAR------------------DDNLTTPTQLPYFEGDFWPNVI 1329
Cdd:pfam08214  152 dGKGLLKWWCKMLDKILveykssaKAKLVIPGKDIFKTRKylpatadplwlvghifhqICDDPARYEIPLFPDDPKPRFL 231

                   ....*.
gi 392896225  1330 EDCIRE 1335
Cdd:pfam08214  232 EELIKE 237
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
855-961 6.46e-63

Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


:

Pssm-ID: 99927  Cd Length: 108  Bit Score: 209.61  E-value: 6.46e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  855 QEDLIKFLLPVWEKLDKS-EDAAPFRVPVDAKLLNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWL 933
Cdd:cd05495     1 PEELRQALMPTLEKLYKQdPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 392896225  934 YNRKNSKVYKYGLKLSEMFVSEMDPVMK 961
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
582-662 1.36e-46

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.


:

Pssm-ID: 366953  Cd Length: 81  Bit Score: 161.89  E-value: 1.36e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   582 DCTKEWHHQVTKDLRNHLVGKLVKAIFPEPNQEAMNDNRLKDLIAYARKVEKEMFESANDREEYYHLLAEKIYKIQKELQ 661
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 392896225   662 E 662
Cdd:pfam02172   81 E 81
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1540-1618 1.77e-26

TAZ zinc finger, present in p300 and CBP;


:

Pssm-ID: 214717  Cd Length: 79  Bit Score: 104.37  E-value: 1.77e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   1540 GTRYESIQRCIASLVHACQC--RDANCRRMSCHKMKRVVQHTKMCKKR--INGTCPVCKQLIalccYHAKHCTRDACTVP 1615
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKVRkcKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 392896225   1616 FCM 1618
Cdd:smart00551   77 KCV 79
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
415-491 1.01e-24

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.


:

Pssm-ID: 460457  Cd Length: 72  Bit Score: 99.00  E-value: 1.01e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896225   415 HAHKCSQREKEnrdfaaknqppphaACTLPHCSTMKEVLTHMTSCNVGRLCHFAHCASSRQIIAHWKNCSREDCPVC 491
Cdd:pfam02135   10 HASKCSAPGPG--------------PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
959-998 6.91e-18

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.


:

Pssm-ID: 399179  Cd Length: 40  Bit Score: 78.52  E-value: 6.91e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 392896225   959 VMKSMGYCCAKKLAFTPLSLFCYGAAMCTIAREQQYWVFE 998
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1486-1524 1.61e-17

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.


:

Pssm-ID: 239077  Cd Length: 41  Bit Score: 77.60  E-value: 1.61e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 392896225 1486 YTCNKCSS--PAVWHCQSCDDFDLCDGCKPTTQHPHEMEKI 1524
Cdd:cd02337     1 YTCNECKHhvETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1058-1089 6.39e-14

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.


:

Pssm-ID: 277032  Cd Length: 37  Bit Score: 67.29  E-value: 6.39e-14
                          10        20        30
                  ....*....|....*....|....*....|..
gi 392896225 1058 FERCKYCMRKWHRICALHDKKVYPEGFICECC 1089
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1618-2004 1.28e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.39  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1618 MNIRQKLAEQKRSQQRRADMMMRRRMEGLQSHVG--GAAPTPSTVSNGTPSNAPTPPVSAGPGPAVKGGGVGQVQMQQHQ 1695
Cdd:pfam09606   48 LHVRDMSKKAAQQQQPQGGQGNGGMGGGQQGMPDpiNALQNLAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASL 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1696 GSHVGGSGPAGMGQPMNsfggmpgmgLGPNAQNGPGLPGMNPQMNANQSRYMPNGPGLGQSGAPGQQQQPMYSSGMPM-- 1773
Cdd:pfam09606  128 GRPQMPMGGAGFPSQMS---------RVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMgg 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1774 QRPGGLGGMNPQQQPQQQQGHPGLQNP-GGRPGGVHGMGQNQPVRNNQdmvmnmqmqnqhqqpppfdstlQPQIMKINSR 1852
Cdd:pfam09606  199 QMPPQMGVPGMPGPADAGAQMGQQAQAnGGMNPQQMGGAPNQVAMQQQ----------------------QPQQQGQQSQ 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1853 LKAAKTEeeretvfsdlkktPHLFHAWLRMRENQNLVPNRMQGYSQ--MSMGSSNLQNLQQQQLQQQQAGAMRGGGGFAP 1930
Cdd:pfam09606  257 LGMGINQ-------------MQQMPQGVGGGAGQGGPGQPMGPPGQqpGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHP 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1931 GQNNSQPRAPSGQFASMNPsMQQQYPQQQQGWPQQRQQNPGGMQQNA-------NPYNQFQNRQ---NMMMMPQQQQPHP 2000
Cdd:pfam09606  324 AAHQQQMNQSVGQGGQVVA-LGGLNHLETWNPGNFGGLGANPMQRGQpgmmsspSPVPGQQVRQvtpNQFMRQSPQPSVP 402

                   ....
gi 392896225  2001 SNAG 2004
Cdd:pfam09606  403 SPQG 406
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
193-338 4.52e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 48.47  E-value: 4.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   193 FPGMMHRYPYAQGGPPPGAQGMPQGYPGVSRGGPTPGQPMGRGAMMNGAMPRSGP---------MPTQGRPGIPPNQQAM 263
Cdd:pfam09606  155 AGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMpgpadagaqMGQQAQANGGMNPQQM 234
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896225   264 -MQPMMTDRQFMQHGQYGQQrpefmQQYGRPGGYPM-MHQGmmmDSNGQPIRGPNQMMMMSNGHPG-MSHGPPNGQPG 338
Cdd:pfam09606  235 gGAPNQVAMQQQQPQQQGQQ-----SQLGMGINQMQqMPQG---VGGGAGQGGPGQPMGPPGQQPGaMPNVMSIGDQN 304
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1120-1335 3.61e-74

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.


Pssm-ID: 400497  Cd Length: 348  Bit Score: 251.55  E-value: 3.61e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1120 VNGFIKKQLqAEAHKypVIIRTLCVQDKEAEVKAQMKQKYVESNqfPEKFPYRTKAVFAFEIIDGVEVCFFGLHVQEYGS 1199
Cdd:pfam08214    1 LNDFLAKVL-PKGVK--VTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1200 ACPAPNARRVYIAYLDSVHFFQPReLRTDVYHELLLGYLDYAKMLGYTMAHIWACPPSEGDDYIFhchPPEQKIPK---- 1275
Cdd:pfam08214   76 VCPDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvl 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1276 -PKRLQDWYKKMLEKGV-------QEGSVVEFKDIYKQAR------------------DDNLTTPTQLPYFEGDFWPNVI 1329
Cdd:pfam08214  152 dGKGLLKWWCKMLDKILveykssaKAKLVIPGKDIFKTRKylpatadplwlvghifhqICDDPARYEIPLFPDDPKPRFL 231

                   ....*.
gi 392896225  1330 EDCIRE 1335
Cdd:pfam08214  232 EELIKE 237
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
855-961 6.46e-63

Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99927  Cd Length: 108  Bit Score: 209.61  E-value: 6.46e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  855 QEDLIKFLLPVWEKLDKS-EDAAPFRVPVDAKLLNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWL 933
Cdd:cd05495     1 PEELRQALMPTLEKLYKQdPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 392896225  934 YNRKNSKVYKYGLKLSEMFVSEMDPVMK 961
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
582-662 1.36e-46

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.


Pssm-ID: 366953  Cd Length: 81  Bit Score: 161.89  E-value: 1.36e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   582 DCTKEWHHQVTKDLRNHLVGKLVKAIFPEPNQEAMNDNRLKDLIAYARKVEKEMFESANDREEYYHLLAEKIYKIQKELQ 661
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 392896225   662 E 662
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
854-959 2.10e-33

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 125.08  E-value: 2.10e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225    854 SQEDLIKFLLPVWEKLDKSEDAAPFRVPVDAKLlnIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWL 933
Cdd:smart00297    4 LQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNART 81
                            90       100
                    ....*....|....*....|....*.
gi 392896225    934 YNRKNSKVYKYGLKLSEMFVSEMDPV 959
Cdd:smart00297   82 YNGPDSEVYKDAKKLEKFFEKKLREL 107
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1540-1618 1.77e-26

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 104.37  E-value: 1.77e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   1540 GTRYESIQRCIASLVHACQC--RDANCRRMSCHKMKRVVQHTKMCKKR--INGTCPVCKQLIalccYHAKHCTRDACTVP 1615
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKVRkcKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 392896225   1616 FCM 1618
Cdd:smart00551   77 KCV 79
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
415-491 1.01e-24

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.


Pssm-ID: 460457  Cd Length: 72  Bit Score: 99.00  E-value: 1.01e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896225   415 HAHKCSQREKEnrdfaaknqppphaACTLPHCSTMKEVLTHMTSCNVGRLCHFAHCASSRQIIAHWKNCSREDCPVC 491
Cdd:pfam02135   10 HASKCSAPGPG--------------PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
862-947 1.26e-22

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: 93.53  E-value: 1.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   862 LLPVWEKLDKSEDAAPFRVPVDAKllNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKV 941
Cdd:pfam00439    1 CLEILDKLMEHPIAAPFLEPVDPD--EYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVI 78

                   ....*.
gi 392896225   942 YKYGLK 947
Cdd:pfam00439   79 YKAAEK 84
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
415-494 9.45e-22

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 90.89  E-value: 9.45e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225    415 HAHKCSQREkenrdfaaknqppphAACTLPHCSTMKEVLTHMTSCNVgRLCHFAHCASSRQIIAHWKNCSREDCPVCKPL 494
Cdd:smart00551   16 HARRCKARE---------------AKCQYPNCKTMKKLLRHMDSCKV-RKCKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
1546-1614 1.27e-19

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.


Pssm-ID: 460457  Cd Length: 72  Bit Score: 84.75  E-value: 1.27e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896225  1546 IQRCIASLVHACQCRDAN---CRRMSCHKMKRVVQHTKMCKKRINGTCPVCKQLIALCCyHAKHCTRDACTV 1614
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLR-HAKNCKDEDCPV 71
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
831-963 3.31e-18

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 88.71  E-value: 3.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  831 ESKPKEQQAKREPTPPPTEDTVFSQEDLIKFLLPVwEKLDKSEDAAPFRVPVDAKllNIPDYHEIIKRPMDLETVHKKLY 910
Cdd:COG5076   123 MAHLKTSVKKRKTPKIEDELLYADNKAIAKFKKQL-FLRDGRFLSSIFLGLPSKR--EYPDYYEIIKSPMDLLTIQKKLK 199
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392896225  911 AGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKLSEMFVSEMDPVMKSM 963
Cdd:COG5076   200 NGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIPEEM 252
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
959-998 6.91e-18

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.


Pssm-ID: 399179  Cd Length: 40  Bit Score: 78.52  E-value: 6.91e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 392896225   959 VMKSMGYCCAKKLAFTPLSLFCYGAAMCTIAREQQYWVFE 998
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1486-1524 1.61e-17

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.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 77.60  E-value: 1.61e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 392896225 1486 YTCNKCSS--PAVWHCQSCDDFDLCDGCKPTTQHPHEMEKI 1524
Cdd:cd02337     1 YTCNECKHhvETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
973-1056 3.44e-17

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.


Pssm-ID: 276805  Cd Length: 73  Bit Score: 77.72  E-value: 3.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  973 FTPLSLFCYGAamCTIARE--QQYWVFEQSSTqynvtvteRYTYCQKCFDALPPEGISLSEnpnDRNNMAPKTSFTEQKN 1050
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLDN--------RYHFCEKCFNEIRGDEITLGD---DQGTSISKSQFEKKKN 67

                  ....*.
gi 392896225 1051 SVIDYE 1056
Cdd:cd15802    68 DELDEE 73
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1058-1089 6.39e-14

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.


Pssm-ID: 277032  Cd Length: 37  Bit Score: 67.29  E-value: 6.39e-14
                          10        20        30
                  ....*....|....*....|....*....|..
gi 392896225 1058 FERCKYCMRKWHRICALHDKKVYPEGFICECC 1089
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1482-1521 4.00e-12

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.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 62.50  E-value: 4.00e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 392896225  1482 KGMEYTCNKCSS----PAVWHCQSCDDFDLCDGCKPT-TQHPHEM 1521
Cdd:pfam00569    1 IHKVYTCNGCSNdpsiGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1482-1522 1.06e-09

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.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 55.52  E-value: 1.06e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 392896225   1482 KGMEYTCNKCSSPAV---WHCQSCDDFDLCDGCKPTTQHPHEME 1522
Cdd:smart00291    1 VHHSYSCDTCGKPIVgvrYHCLVCPDYDLCQSCFAKGSAGGEHS 44
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1618-2004 1.28e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.39  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1618 MNIRQKLAEQKRSQQRRADMMMRRRMEGLQSHVG--GAAPTPSTVSNGTPSNAPTPPVSAGPGPAVKGGGVGQVQMQQHQ 1695
Cdd:pfam09606   48 LHVRDMSKKAAQQQQPQGGQGNGGMGGGQQGMPDpiNALQNLAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASL 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1696 GSHVGGSGPAGMGQPMNsfggmpgmgLGPNAQNGPGLPGMNPQMNANQSRYMPNGPGLGQSGAPGQQQQPMYSSGMPM-- 1773
Cdd:pfam09606  128 GRPQMPMGGAGFPSQMS---------RVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMgg 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1774 QRPGGLGGMNPQQQPQQQQGHPGLQNP-GGRPGGVHGMGQNQPVRNNQdmvmnmqmqnqhqqpppfdstlQPQIMKINSR 1852
Cdd:pfam09606  199 QMPPQMGVPGMPGPADAGAQMGQQAQAnGGMNPQQMGGAPNQVAMQQQ----------------------QPQQQGQQSQ 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1853 LKAAKTEeeretvfsdlkktPHLFHAWLRMRENQNLVPNRMQGYSQ--MSMGSSNLQNLQQQQLQQQQAGAMRGGGGFAP 1930
Cdd:pfam09606  257 LGMGINQ-------------MQQMPQGVGGGAGQGGPGQPMGPPGQqpGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHP 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1931 GQNNSQPRAPSGQFASMNPsMQQQYPQQQQGWPQQRQQNPGGMQQNA-------NPYNQFQNRQ---NMMMMPQQQQPHP 2000
Cdd:pfam09606  324 AAHQQQMNQSVGQGGQVVA-LGGLNHLETWNPGNFGGLGANPMQRGQpgmmsspSPVPGQQVRQvtpNQFMRQSPQPSVP 402

                   ....
gi 392896225  2001 SNAG 2004
Cdd:pfam09606  403 SPQG 406
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
193-338 4.52e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 48.47  E-value: 4.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   193 FPGMMHRYPYAQGGPPPGAQGMPQGYPGVSRGGPTPGQPMGRGAMMNGAMPRSGP---------MPTQGRPGIPPNQQAM 263
Cdd:pfam09606  155 AGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMpgpadagaqMGQQAQANGGMNPQQM 234
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896225   264 -MQPMMTDRQFMQHGQYGQQrpefmQQYGRPGGYPM-MHQGmmmDSNGQPIRGPNQMMMMSNGHPG-MSHGPPNGQPG 338
Cdd:pfam09606  235 gGAPNQVAMQQQQPQQQGQQ-----SQLGMGINQMQqMPQG---VGGGAGQGGPGQPMGPPGQQPGaMPNVMSIGDQN 304
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
270-338 9.75e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 44.03  E-value: 9.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   270 DRQFMQHGQYGQQRPEFMQ-QYGRP----GGYPMMH-QGMMMDSNGQPIRGPNQMMMMSNGHPGMSHGP-------PNGQ 336
Cdd:TIGR01628  366 QRRAHLQDQFMQLQPRMRQlPMGSPmggaMGQPPYYgQGPQQQFNGQPLGWPRMSMMPTPMGPGGPLRPnglapmnAVRA 445

                   ..
gi 392896225   337 PG 338
Cdd:TIGR01628  446 PS 447
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1120-1335 3.61e-74

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.


Pssm-ID: 400497  Cd Length: 348  Bit Score: 251.55  E-value: 3.61e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1120 VNGFIKKQLqAEAHKypVIIRTLCVQDKEAEVKAQMKQKYVESNqfPEKFPYRTKAVFAFEIIDGVEVCFFGLHVQEYGS 1199
Cdd:pfam08214    1 LNDFLAKVL-PKGVK--VTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1200 ACPAPNARRVYIAYLDSVHFFQPReLRTDVYHELLLGYLDYAKMLGYTMAHIWACPPSEGDDYIFhchPPEQKIPK---- 1275
Cdd:pfam08214   76 VCPDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvl 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1276 -PKRLQDWYKKMLEKGV-------QEGSVVEFKDIYKQAR------------------DDNLTTPTQLPYFEGDFWPNVI 1329
Cdd:pfam08214  152 dGKGLLKWWCKMLDKILveykssaKAKLVIPGKDIFKTRKylpatadplwlvghifhqICDDPARYEIPLFPDDPKPRFL 231

                   ....*.
gi 392896225  1330 EDCIRE 1335
Cdd:pfam08214  232 EELIKE 237
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
855-961 6.46e-63

Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99927  Cd Length: 108  Bit Score: 209.61  E-value: 6.46e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  855 QEDLIKFLLPVWEKLDKS-EDAAPFRVPVDAKLLNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWL 933
Cdd:cd05495     1 PEELRQALMPTLEKLYKQdPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                          90       100
                  ....*....|....*....|....*...
gi 392896225  934 YNRKNSKVYKYGLKLSEMFVSEMDPVMK 961
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
582-662 1.36e-46

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.


Pssm-ID: 366953  Cd Length: 81  Bit Score: 161.89  E-value: 1.36e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   582 DCTKEWHHQVTKDLRNHLVGKLVKAIFPEPNQEAMNDNRLKDLIAYARKVEKEMFESANDREEYYHLLAEKIYKIQKELQ 661
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 392896225   662 E 662
Cdd:pfam02172   81 E 81
BROMO smart00297
bromo domain;
854-959 2.10e-33

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 125.08  E-value: 2.10e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225    854 SQEDLIKFLLPVWEKLDKSEDAAPFRVPVDAKLlnIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWL 933
Cdd:smart00297    4 LQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNART 81
                            90       100
                    ....*....|....*....|....*.
gi 392896225    934 YNRKNSKVYKYGLKLSEMFVSEMDPV 959
Cdd:smart00297   82 YNGPDSEVYKDAKKLEKFFEKKLREL 107
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
858-956 3.17e-28

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: 110.15  E-value: 3.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  858 LIKFLLPVWEKLDKS--EDAAPFRVPVDAKllNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYN 935
Cdd:cd04369     1 LKKKLRSLLDALKKLkrDLSEPFLEPVDPK--EAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78
                          90       100
                  ....*....|....*....|.
gi 392896225  936 RKNSKVYKYGLKLSEMFVSEM 956
Cdd:cd04369    79 GPGSPIYKDAKKLEKLFEKLL 99
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1540-1618 1.77e-26

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 104.37  E-value: 1.77e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   1540 GTRYESIQRCIASLVHACQC--RDANCRRMSCHKMKRVVQHTKMCKKR--INGTCPVCKQLIalccYHAKHCTRDACTVP 1615
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKVRkcKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 392896225   1616 FCM 1618
Cdd:smart00551   77 KCV 79
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
860-956 4.03e-25

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: 101.24  E-value: 4.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  860 KFLLPVWEKLDKSEDAAPFRVPVDAKLLNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNS 939
Cdd:cd05500     7 KFLLSSIRSLKRLKDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEH 86
                          90
                  ....*....|....*..
gi 392896225  940 KVYKYGLKLSEMFVSEM 956
Cdd:cd05500    87 PVSQMGKRLQAAFEKHL 103
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
415-491 1.01e-24

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.


Pssm-ID: 460457  Cd Length: 72  Bit Score: 99.00  E-value: 1.01e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896225   415 HAHKCSQREKEnrdfaaknqppphaACTLPHCSTMKEVLTHMTSCNVGRLCHFAHCASSRQIIAHWKNCSREDCPVC 491
Cdd:pfam02135   10 HASKCSAPGPG--------------PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
857-953 2.48e-24

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: 99.17  E-value: 2.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  857 DLIKFLLPVWEKLDKSEDAAPFRVPVDAKllNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNR 936
Cdd:cd05509     1 PLYTQLKKVLDSLKNHKSAWPFLEPVDKE--EAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYNG 78
                          90
                  ....*....|....*..
gi 392896225  937 KNSKVYKYGLKLSEMFV 953
Cdd:cd05509    79 PDTEYYKCANKLEKFFW 95
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
868-952 2.26e-23

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.


Pssm-ID: 99938  Cd Length: 99  Bit Score: 96.25  E-value: 2.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  868 KLDKSEDAAPFRVPVDAKLLNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLK 947
Cdd:cd05506    11 KLMKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKE 90

                  ....*
gi 392896225  948 LSEMF 952
Cdd:cd05506    91 LLKIF 95
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
862-947 1.26e-22

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: 93.53  E-value: 1.26e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   862 LLPVWEKLDKSEDAAPFRVPVDAKllNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKV 941
Cdd:pfam00439    1 CLEILDKLMEHPIAAPFLEPVDPD--EYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVI 78

                   ....*.
gi 392896225   942 YKYGLK 947
Cdd:pfam00439   79 YKAAEK 84
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
875-952 2.91e-22

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: 93.11  E-value: 2.91e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896225  875 AAPFRVPVDAKLLNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKLSEMF 952
Cdd:cd05498    21 AWPFYKPVDPEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVF 98
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
872-962 6.10e-22

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.


Pssm-ID: 99928  Cd Length: 119  Bit Score: 92.91  E-value: 6.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  872 SEDAAPFRVPVDakLLNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYN-RKNSKVYKYGLKLSE 950
Cdd:cd05496    20 CEDSEPFRQPVD--LLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSA 97
                          90
                  ....*....|..
gi 392896225  951 MFVSEMDPVMKS 962
Cdd:cd05496    98 LFEEHIKKIISD 109
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
415-494 9.45e-22

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 90.89  E-value: 9.45e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225    415 HAHKCSQREkenrdfaaknqppphAACTLPHCSTMKEVLTHMTSCNVgRLCHFAHCASSRQIIAHWKNCSREDCPVCKPL 494
Cdd:smart00551   16 HARRCKARE---------------AKCQYPNCKTMKKLLRHMDSCKV-RKCKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
867-955 1.09e-20

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.


Pssm-ID: 99936  Cd Length: 115  Bit Score: 89.38  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  867 EKLDKSEDAAPFRVPVDAKllNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGL 946
Cdd:cd05504    22 VEIVKHKDSWPFLRPVSKI--EVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHTSVYKAGT 99

                  ....*....
gi 392896225  947 KLSEMFVSE 955
Cdd:cd05504   100 RLQRFFIKR 108
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
865-958 2.98e-20

Bromodomain, Brdt_like subfamily, repeat I. 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: 99929  Cd Length: 107  Bit Score: 87.86  E-value: 2.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  865 VWEKLDKSEDAAPFRVPVDAKLLNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKY 944
Cdd:cd05497    13 VLKALWKHKFAWPFQQPVDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKPGDDVVLM 92
                          90
                  ....*....|....
gi 392896225  945 GLKLSEMFVSEMDP 958
Cdd:cd05497    93 AQTLEKLFLQKLAQ 106
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
875-956 5.11e-20

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: 86.96  E-value: 5.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  875 AAPFRVPVDAKLLNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKLSEMFVS 954
Cdd:cd05499    21 NWPFLDPVDPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFND 100

                  ..
gi 392896225  955 EM 956
Cdd:cd05499   101 KW 102
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
1546-1614 1.27e-19

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.


Pssm-ID: 460457  Cd Length: 72  Bit Score: 84.75  E-value: 1.27e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896225  1546 IQRCIASLVHACQCRDAN---CRRMSCHKMKRVVQHTKMCKKRINGTCPVCKQLIALCCyHAKHCTRDACTV 1614
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLR-HAKNCKDEDCPV 71
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
868-957 3.88e-19

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.


Pssm-ID: 99943 [Multi-domain]  Cd Length: 112  Bit Score: 84.62  E-value: 3.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  868 KLDKSEDAAPFRVPVDAKLlnIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNS---KVYKY 944
Cdd:cd05511    11 ELKNLPDSWPFHTPVNKKK--VPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSvytKKAKE 88
                          90
                  ....*....|...
gi 392896225  945 GLKLSEMFVSEMD 957
Cdd:cd05511    89 MLELAEELLAERE 101
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
831-963 3.31e-18

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 88.71  E-value: 3.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  831 ESKPKEQQAKREPTPPPTEDTVFSQEDLIKFLLPVwEKLDKSEDAAPFRVPVDAKllNIPDYHEIIKRPMDLETVHKKLY 910
Cdd:COG5076   123 MAHLKTSVKKRKTPKIEDELLYADNKAIAKFKKQL-FLRDGRFLSSIFLGLPSKR--EYPDYYEIIKSPMDLLTIQKKLK 199
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392896225  911 AGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKLSEMFVSEMDPVMKSM 963
Cdd:COG5076   200 NGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIPEEM 252
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
869-954 4.21e-18

Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B (BAZ2B) were identified as a novel human bromodomain gene by cDNA library screening. BAZ2A is also known as Tip5 (Transcription termination factor I-interacting protein 5) and hWALp3. The proteins may play roles in transcriptional regulation. Human Tip5 is part of a complex termed NoRC (nucleolar remodeling complex), which induces nucleosome sliding and may play a role in the regulation of the rDNA locus. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99935  Cd Length: 97  Bit Score: 81.27  E-value: 4.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  869 LDKSEDAAPFRVPVDAKLlnIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKL 948
Cdd:cd05503    12 MEAHEDAWPFLEPVNTKL--VPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNM 89

                  ....*.
gi 392896225  949 SEMFVS 954
Cdd:cd05503    90 RKFFEK 95
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
959-998 6.91e-18

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.


Pssm-ID: 399179  Cd Length: 40  Bit Score: 78.52  E-value: 6.91e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 392896225   959 VMKSMGYCCAKKLAFTPLSLFCYGAAMCTIAREQQYWVFE 998
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1486-1524 1.61e-17

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.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 77.60  E-value: 1.61e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 392896225 1486 YTCNKCSS--PAVWHCQSCDDFDLCDGCKPTTQHPHEMEKI 1524
Cdd:cd02337     1 YTCNECKHhvETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
973-1056 3.44e-17

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.


Pssm-ID: 276805  Cd Length: 73  Bit Score: 77.72  E-value: 3.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  973 FTPLSLFCYGAamCTIARE--QQYWVFEQSSTqynvtvteRYTYCQKCFDALPPEGISLSEnpnDRNNMAPKTSFTEQKN 1050
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLDN--------RYHFCEKCFNEIRGDEITLGD---DQGTSISKSQFEKKKN 67

                  ....*.
gi 392896225 1051 SVIDYE 1056
Cdd:cd15802    68 DELDEE 73
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
864-943 2.26e-16

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.


Pssm-ID: 99942 [Multi-domain]  Cd Length: 112  Bit Score: 76.71  E-value: 2.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  864 PVWEKLDK--------SEDAAPFRVPVDAKllNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYN 935
Cdd:cd05510     7 EFYESLDKvlnelktyTEHSTPFLTKVSKR--EAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYN 84

                  ....*...
gi 392896225  936 RKNSKVYK 943
Cdd:cd05510    85 SDPSHPLR 92
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
867-950 1.58e-15

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.


Pssm-ID: 99944  Cd Length: 98  Bit Score: 73.97  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  867 EKLDKSEDAAPFRVPVDAKllNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGL 946
Cdd:cd05512    11 DQLQEKDTAEIFSEPVDLS--EVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDTIFYRAAV 88

                  ....
gi 392896225  947 KLSE 950
Cdd:cd05512    89 RLRD 92
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
890-948 1.39e-14

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: 71.57  E-value: 1.39e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896225  890 PDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKL 948
Cdd:cd05515    37 PDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYKDALTL 95
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1058-1089 6.39e-14

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.


Pssm-ID: 277032  Cd Length: 37  Bit Score: 67.29  E-value: 6.39e-14
                          10        20        30
                  ....*....|....*....|....*....|..
gi 392896225 1058 FERCKYCMRKWHRICALHDKKVYPEGFICECC 1089
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
873-956 8.01e-14

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: 69.24  E-value: 8.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  873 EDAAPFRVPVDAkllNIPDYHEIIKRPMDLETVHKKL---YAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKLS 949
Cdd:cd05502    20 ELSLPFHEPVSP---SVPNYYKIIKTPMDLSLIRKKLqpkSPQHYSSPEEFVADVRLMFKNCYKFNEEDSEVAQAGKELE 96

                  ....*..
gi 392896225  950 EMFVSEM 956
Cdd:cd05502    97 LFFEEQL 103
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
860-963 9.68e-14

Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with the thyroid hormone receptor in a ligand-dependent fashion and enhances thyroid hormone-dependent activation from thyroid response elements. Brd8 is thought to be a nuclear receptor coactivator. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99939  Cd Length: 104  Bit Score: 68.93  E-value: 9.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  860 KFLLPVWEKLDKSEDAAPFRVPVdaKLLNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNS 939
Cdd:cd05507     6 KAILLVYRTLASHRYASVFLKPV--TEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNSSDH 83
                          90       100
                  ....*....|....*....|....
gi 392896225  940 KVYKyglklseMFVSEMDPVMKSM 963
Cdd:cd05507    84 DVYL-------MAVEMQREVMSQI 100
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
861-935 3.82e-13

Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. The structure(2DKW) in this alignment is an uncharacterized protein predicted from analysis of cDNA clones from human fetal liver


Pssm-ID: 99957  Cd Length: 112  Bit Score: 67.38  E-value: 3.82e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896225  861 FLLPVWEKLDKSEDAAPFRVPVDAKllNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYN 935
Cdd:cd05528     7 FLRDVLKRLASDKRFNAFTKPVDEE--EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYN 79
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
871-960 2.50e-12

Bromodomain, polybromo repeat I. 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: 99954 [Multi-domain]  Cd Length: 113  Bit Score: 65.43  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  871 KSEDAAPF-----RVPvdaKLLNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYG 945
Cdd:cd05524    18 KSEDGRILcesfiRVP---KRRNEPEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDA 94
                          90
                  ....*....|....*
gi 392896225  946 LKLSEMFVSEMDPVM 960
Cdd:cd05524    95 CKLWELFLSARNEVL 109
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1482-1521 4.00e-12

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.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 62.50  E-value: 4.00e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 392896225  1482 KGMEYTCNKCSS----PAVWHCQSCDDFDLCDGCKPT-TQHPHEM 1521
Cdd:pfam00569    1 IHKVYTCNGCSNdpsiGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
889-957 2.57e-11

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.


Pssm-ID: 99947  Cd Length: 107  Bit Score: 62.06  E-value: 2.57e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896225  889 IPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKLSEMFVSEMD 957
Cdd:cd05516    37 LPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQ 105
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
868-941 2.71e-11

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: 61.78  E-value: 2.71e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896225  868 KLDKSEDAAPFRVPVDAKllNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKV 941
Cdd:cd05505    11 KILKYRFSWPFREPVTAD--EAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKYYENGSYV 82
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
890-948 3.04e-11

Bromodomain, polybromo repeat III. 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: 99951  Cd Length: 103  Bit Score: 61.97  E-value: 3.04e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896225  890 PDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKL 948
Cdd:cd05520    37 PDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKL 95
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
890-943 4.57e-11

Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99953 [Multi-domain]  Cd Length: 104  Bit Score: 61.49  E-value: 4.57e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896225  890 PDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYK 943
Cdd:cd05522    38 PEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYK 91
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
890-948 1.58e-10

Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99952  Cd Length: 106  Bit Score: 60.03  E-value: 1.58e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896225  890 PDYHEIIKRPMDLETVHKKLyaGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKL 948
Cdd:cd05521    38 PDYYKIIKNPLSLNTVKKRL--PHYTNAQEFVNDLAQIPWNARLYNTKGSVIYKYALIL 94
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1482-1522 1.06e-09

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.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 55.52  E-value: 1.06e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 392896225   1482 KGMEYTCNKCSSPAV---WHCQSCDDFDLCDGCKPTTQHPHEME 1522
Cdd:smart00291    1 VHHSYSCDTCGKPIVgvrYHCLVCPDYDLCQSCFAKGSAGGEHS 44
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
890-948 2.12e-09

Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown to inhibit cell growth and the progression of the cell cycle by regulating cell-cycle genes at the transcriptional level. BRD7 has been identified as a gene involved in nasopharyngeal carcinoma. The protein interacts with acetylated histone H3 via its 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: 99945  Cd Length: 98  Bit Score: 56.26  E-value: 2.12e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896225  890 PDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKL 948
Cdd:cd05513    32 PGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNKPDTIYYKAAKKL 90
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
878-953 3.99e-09

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: 55.81  E-value: 3.99e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896225  878 FRVPVDAKLLniPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKLSEMFV 953
Cdd:cd05519    27 FLEKPSKKLY--PDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANARTYNQEGSIVYEDAVEMEKAFK 100
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
837-963 2.91e-08

Bromodomain; WDR9 repeat I_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.


Pssm-ID: 99958  Cd Length: 128  Bit Score: 54.27  E-value: 2.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  837 QQAKREPTPPPTEDTVfsQEDLIKFLLPVWEKLDKsEDAAPFRVPVDAKLlNIPDYHEIIKRPMDLETVHKKLYAGQYQN 916
Cdd:cd05529    10 ELFDPGWEQPHIRDEE--RERLISGLDKLLLSLQL-EIAEYFEYPVDLRA-WYPDYWNRVPVPMDLETIRSRLENRYYRS 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 392896225  917 AGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKLSEMFvsemDPVMKSM 963
Cdd:cd05529    86 LEALRHDVRLILSNAETFNEPNSEIAKKAKRLSDWL----LRILSSL 128
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
1486-1524 4.13e-08

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 50.90  E-value: 4.13e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 392896225 1486 YTCNKCSSP---AVWHCQSCDDFDLCDGC--KPTTQHP--HEMEKI 1524
Cdd:cd02249     1 YSCDGCLKPivgVRYHCLVCEDFDLCSSCyaKGKKGHPpdHSFTEI 46
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
890-942 5.18e-08

Bromodomain, polybromo repeat IV. 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: 99949 [Multi-domain]  Cd Length: 103  Bit Score: 52.83  E-value: 5.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392896225  890 PDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVY 942
Cdd:cd05518    37 PDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVY 89
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
858-941 2.93e-07

Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) was identified as a potential tumor suppressor genes, it shares domain architecture with BS69/ZMYND11; both have been implicated in the regulation of cellular proliferation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99940  Cd Length: 99  Bit Score: 50.46  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  858 LIKFLLpvwEKLdKSEDAAPFRVPVDakLLNIPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRK 937
Cdd:cd05508     7 LLKFAL---ERM-KQPGAEPFLKPVD--LEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIYNGG 80

                  ....
gi 392896225  938 NSKV 941
Cdd:cd05508    81 DHKL 84
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
867-910 8.87e-07

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


Pssm-ID: 99926 [Multi-domain]  Cd Length: 114  Bit Score: 49.36  E-value: 8.87e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 392896225  867 EKLDKSEDAAPFRVPVDAKLLNIPDYHEIIKRPMDLETVHKKLY 910
Cdd:cd05494    13 KRHRRNEDAWPFLEPVNPPRRGAPDYRDVIKRPMSFGTKVNNIV 56
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
890-943 1.37e-06

Bromodomain, polybromo repeat II. 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: 99948  Cd Length: 103  Bit Score: 48.59  E-value: 1.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896225  890 PDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYK 943
Cdd:cd05517    37 PDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYK 90
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
877-954 4.76e-06

Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the trithorax-group in Drosophila melanogaster, an epigenetic transcriptional regulator of HOX genes. Drosophila ASH1 has been shown to methylate specific lysines in histones H3 and H4. Mammalian ASH1 has been shown to methylate histone H3. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99955 [Multi-domain]  Cd Length: 106  Bit Score: 47.00  E-value: 4.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  877 PFRVPVDAKLLNIP------DYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNRKNSKVYKYGLKLSE 950
Cdd:cd05525    20 SNGQSLAIPFINLPskkknpDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRLRK 99

                  ....
gi 392896225  951 MFVS 954
Cdd:cd05525   100 AYYQ 103
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
889-952 1.14e-05

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: 45.88  E-value: 1.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896225  889 IPDYHEIIKRPMDLETVHKKLYAGQYQNAGQFCDDIWLMLDNAWLYNrKNSKVYKYGLKLSEMF 952
Cdd:cd05501    30 IRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFY-KDDDFGQVGITLEKKF 92
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1618-2004 1.28e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.39  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1618 MNIRQKLAEQKRSQQRRADMMMRRRMEGLQSHVG--GAAPTPSTVSNGTPSNAPTPPVSAGPGPAVKGGGVGQVQMQQHQ 1695
Cdd:pfam09606   48 LHVRDMSKKAAQQQQPQGGQGNGGMGGGQQGMPDpiNALQNLAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASL 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1696 GSHVGGSGPAGMGQPMNsfggmpgmgLGPNAQNGPGLPGMNPQMNANQSRYMPNGPGLGQSGAPGQQQQPMYSSGMPM-- 1773
Cdd:pfam09606  128 GRPQMPMGGAGFPSQMS---------RVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMgg 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1774 QRPGGLGGMNPQQQPQQQQGHPGLQNP-GGRPGGVHGMGQNQPVRNNQdmvmnmqmqnqhqqpppfdstlQPQIMKINSR 1852
Cdd:pfam09606  199 QMPPQMGVPGMPGPADAGAQMGQQAQAnGGMNPQQMGGAPNQVAMQQQ----------------------QPQQQGQQSQ 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1853 LKAAKTEeeretvfsdlkktPHLFHAWLRMRENQNLVPNRMQGYSQ--MSMGSSNLQNLQQQQLQQQQAGAMRGGGGFAP 1930
Cdd:pfam09606  257 LGMGINQ-------------MQQMPQGVGGGAGQGGPGQPMGPPGQqpGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHP 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225  1931 GQNNSQPRAPSGQFASMNPsMQQQYPQQQQGWPQQRQQNPGGMQQNA-------NPYNQFQNRQ---NMMMMPQQQQPHP 2000
Cdd:pfam09606  324 AAHQQQMNQSVGQGGQVVA-LGGLNHLETWNPGNFGGLGANPMQRGQpgmmsspSPVPGQQVRQvtpNQFMRQSPQPSVP 402

                   ....
gi 392896225  2001 SNAG 2004
Cdd:pfam09606  403 SPQG 406
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
193-338 4.52e-05

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 48.47  E-value: 4.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   193 FPGMMHRYPYAQGGPPPGAQGMPQGYPGVSRGGPTPGQPMGRGAMMNGAMPRSGP---------MPTQGRPGIPPNQQAM 263
Cdd:pfam09606  155 AGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMpgpadagaqMGQQAQANGGMNPQQM 234
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896225   264 -MQPMMTDRQFMQHGQYGQQrpefmQQYGRPGGYPM-MHQGmmmDSNGQPIRGPNQMMMMSNGHPG-MSHGPPNGQPG 338
Cdd:pfam09606  235 gGAPNQVAMQQQQPQQQGQQ-----SQLGMGINQMQqMPQG---VGGGAGQGGPGQPMGPPGQQPGaMPNVMSIGDQN 304
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
1487-1524 9.14e-05

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 41.48  E-value: 9.14e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 392896225 1487 TCNKCSSPAV---WHCQSCDDFDLCDGCKPTTQHP-HEMEKI 1524
Cdd:cd02340     2 ICDGCQGPIVgvrYKCLVCPDYDLCESCEAKGVHPeHAMLKI 43
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
91-355 2.99e-04

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.77  E-value: 2.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225    91 MGGGVNGSVLQELLMNPSqtsnnSPRPQAYPPGQQNAFNRspMMPNGTPNMMSPPSMGRVPGPSPGGPQPPGPGQPQMRP 170
Cdd:pfam09606  114 MGGPGTASNLLASLGRPQ-----MPMGGAGFPSQMSRVGR--MQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAG 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   171 GQPGMFQGDQQQQMMMGAQGQQFPGMM----HRYPYAQGGPPPGAQGMPQGYPGVSRGGPTP------------------ 228
Cdd:pfam09606  187 GMNGGQQGPMGGQMPPQMGVPGMPGPAdagaQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPqqqgqqsqlgmginqmqq 266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   229 ---GQPMGRGA-----MMNGAMPRSGPMPTQGRPGIPPN---------------------QQAMMQPMMTDRQFMQHGQY 279
Cdd:pfam09606  267 mpqGVGGGAGQggpgqPMGPPGQQPGAMPNVMSIGDQNNyqqqqtrqqqqqqggnhpaahQQQMNQSVGQGGQVVALGGL 346
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   280 GQQRPEFMQQYGRPGGYPMMHQGMMMDSNGQPIRG-------PNQMMMM-------SNGHPGmSHGPPNGQPGPQAAAAQ 345
Cdd:pfam09606  347 NHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGqqvrqvtPNQFMRQspqpsvpSPQGPG-SQPPQSHPGGMIPSPAL 425
                          330
                   ....*....|
gi 392896225   346 HAAQQQAAAQ 355
Cdd:pfam09606  426 IPSPSPQMSQ 435
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
270-338 9.75e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 44.03  E-value: 9.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   270 DRQFMQHGQYGQQRPEFMQ-QYGRP----GGYPMMH-QGMMMDSNGQPIRGPNQMMMMSNGHPGMSHGP-------PNGQ 336
Cdd:TIGR01628  366 QRRAHLQDQFMQLQPRMRQlPMGSPmggaMGQPPYYgQGPQQQFNGQPLGWPRMSMMPTPMGPGGPLRPnglapmnAVRA 445

                   ..
gi 392896225   337 PG 338
Cdd:TIGR01628  446 PS 447
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
193-289 5.05e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 41.72  E-value: 5.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896225   193 FPGMMHRYPYAQGGPPPGAQGMPQGYPGvSRGGPTPGQPMGRGAMMNGAmprsgPMPTQGRPGiPPNQQAMMQPMMTDRQ 272
Cdd:TIGR01628  391 MGGAMGQPPYYGQGPQQQFNGQPLGWPR-MSMMPTPMGPGGPLRPNGLA-----PMNAVRAPS-RNAQNAAQKPPMQPVM 463
                           90
                   ....*....|....*..
gi 392896225   273 FMQHGQyGQQRPEFMQQ 289
Cdd:TIGR01628  464 YPPNYQ-SLPLSQDLPQ 479
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
1486-1524 5.89e-03

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239081  Cd Length: 48  Bit Score: 36.64  E-value: 5.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 392896225 1486 YTCNKCSSPAV----WHCQSCD--DFDLCDGCKPTT---QHPHEMEKI 1524
Cdd:cd02341     1 FKCDSCGIEPIpgtrYHCSECDdgDFDLCQDCVVKGeshQEDHWLVKI 48
 
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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