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Conserved domains on  [gi|148664809|gb|EDK97225|]
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CREB binding protein [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
 304-611 8.60e-95

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: 308.56  E-value: 8.60e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   304 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 383
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   384 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 458
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   459 KRLQEWYKKMLDKAFAE-------RIINDYKDIFKQ-----ANEDRL-------------TSAKELPYFEGDFWPNVLEE 513
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   514 SIKELEQEEEERKK---------EESTAASETPEGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKKKPSMPN 574
Cdd:pfam08214  234 LIKEGRWKSVSLDQfweelrfrqEFSLGRLVGFIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYSTEEGAPE 313

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 148664809   575 VSNDLSQKLYATMEKHkevFFVIHLHAGPVISTQPPI 611
Cdd:pfam08214  314 SVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 94-201 5.33e-76

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: 246.20  E-value: 5.33e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   94 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 173
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80

                          90       100
                  ....*....|....*....|....*...
gi 148664809  174 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 201
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 667-707 4.66e-27

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: 104.18  E-value: 4.66e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 148664809  667 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKW 707
Cdd:cd02337     1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
 975-1076 3.34e-25

Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices which pack in a bundle, exposing a hydrophobic groove between alpha-1 and alpha-3 within which complimentary domains found in the protein 'activator for thyroid hormone and retinoid receptors' (ACTR) can dock. Docking of these domains is required for the recruitment of RNA polymerase II and the basal transcription machinery.


:

Pssm-ID: 462659 [Multi-domain]  Cd Length: 111  Bit Score: 101.45  E-value: 3.34e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   975 MSSMPPGQWQQAPIPQQQPmpGMPRPVMSMQAQAAVAG---PRMPNVQP--------PRSISPSALQDLLRTLKSPSSPQ 1043
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 148664809  1044 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 1076
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
 199-238 3.37e-23

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: 93.15  E-value: 3.37e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 148664809   199 VMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQ 238
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 734-802 7.42e-23

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: 93.22  E-value: 7.42e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148664809   734 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 802
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 922-1231 2.13e-09

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: 61.95  E-value: 2.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   922 RQIEREAQQQQHLYRANINNGMPPGRAGM---------------GTPGSQMTPVGLNVPRPNQVSGPVMSSmppgQWQQA 986
Cdd:pfam09606   51 RDMSKKAAQQQQPQGGQGNGGMGGGQQGMpdpinalqnlagqgtRPQMMGPMGPGPGGPMGQQMGGPGTAS----NLLAS 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   987 PIPQQQPMPGMPRPVMSMQAQAAVAGPRMPNVQPPRSISPSALQdllrtlkspsspqqqqqvlnilksnPQLMAAFIKQR 1066
Cdd:pfam09606  127 LGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGT-------------------------PNQMGPNGGPG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  1067 TAKYVANQPGMQPQPGLQSQPGM-QPQPGMHQQPSLQNLNAMQAGvprpgvpppqpamGGLNPQGQALNIMNPGHNPNMT 1145
Cdd:pfam09606  182 QGQAGGMNGGQQGPMGGQMPPQMgVPGMPGPADAGAQMGQQAQAN-------------GGMNPQQMGGAPNQVAMQQQQP 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  1146 NMNPQYREMGSSMGQmaapMGQLGQmGQPGLGADSTPniqQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQAS 1225
Cdd:pfam09606  249 QQQGQQSQLGMGINQ----MQQMPQ-GVGGGAGQGGP---GQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGG 320


                   ....*.
gi 148664809  1226 HLPGQQ 1231
Cdd:pfam09606  321 NHPAAH 326
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
 304-611 8.60e-95

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: 308.56  E-value: 8.60e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   304 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 383
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   384 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 458
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   459 KRLQEWYKKMLDKAFAE-------RIINDYKDIFKQ-----ANEDRL-------------TSAKELPYFEGDFWPNVLEE 513
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   514 SIKELEQEEEERKK---------EESTAASETPEGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKKKPSMPN 574
Cdd:pfam08214  234 LIKEGRWKSVSLDQfweelrfrqEFSLGRLVGFIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYSTEEGAPE 313

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 148664809   575 VSNDLSQKLYATMEKHkevFFVIHLHAGPVISTQPPI 611
Cdd:pfam08214  314 SVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 94-201 5.33e-76

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: 246.20  E-value: 5.33e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   94 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 173
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80

                          90       100
                  ....*....|....*....|....*...
gi 148664809  174 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 201
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
BROMO smart00297
bromo domain;
91-199 5.36e-34

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 126.24  E-value: 5.36e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809     91 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNN 170
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78

                            90       100
                    ....*....|....*....|....*....
gi 148664809    171 AWLYNRKTSRVYKFCSKLAEVFEQEIDPV 199
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 667-707 4.66e-27

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: 104.18  E-value: 4.66e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 148664809  667 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKW 707
Cdd:cd02337     1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
 975-1076 3.34e-25

Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices which pack in a bundle, exposing a hydrophobic groove between alpha-1 and alpha-3 within which complimentary domains found in the protein 'activator for thyroid hormone and retinoid receptors' (ACTR) can dock. Docking of these domains is required for the recruitment of RNA polymerase II and the basal transcription machinery.


Pssm-ID: 462659 [Multi-domain]  Cd Length: 111  Bit Score: 101.45  E-value: 3.34e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   975 MSSMPPGQWQQAPIPQQQPmpGMPRPVMSMQAQAAVAG---PRMPNVQP--------PRSISPSALQDLLRTLKSPSSPQ 1043
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 148664809  1044 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 1076
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
 199-238 3.37e-23

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: 93.15  E-value: 3.37e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 148664809   199 VMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQ 238
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 734-802 7.42e-23

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: 93.22  E-value: 7.42e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148664809   734 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 802
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
728-806 1.75e-22

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 92.43  E-value: 1.75e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809    728 ESRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPVCKQLIalccYHAKHCQENKCPVP 803
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76


                    ...
gi 148664809    804 FCL 806
Cdd:smart00551   77 KCV 79
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
 213-265 1.32e-21

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: 89.66  E-value: 1.32e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 148664809  213 FSPQTLCCYGKqlCTIPRD--AAYYSYQ---NRYHFCEKCFTEIQGENVTLGDDPSQP 265
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDDQGTS 56
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 111-183 3.07e-19

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: 83.52  E-value: 3.07e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148664809   111 QDPESLPFRQPVDPqlLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 183
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 663-705 2.41e-16

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: 74.01  E-value: 2.41e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 148664809    663 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHTHKMV 705
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 1-200 3.37e-15

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 79.08  E-value: 3.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809    1 MLEMKTEVQTDDAEP--EPTESKGEPRSEMM-----EEDLQGSSQVKEETDTTEQKSEPMEVEEKKpevkveakeeEENS 73
Cdd:COG5076    56 MPKEYITSIVDDREPgsMANVNDDLENVGGItyspfEKNRPESLRFDEIVFLAIESVTPESGLGSL----------LMAH 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   74 SNDTASQSTSPSQPRKKIfKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQ 153
Cdd:COG5076   126 LKTSVKKRKTPKIEDELL-YADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGR 202

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 148664809  154 YQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVM 200
Cdd:COG5076   203 YKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 663-704 1.05e-14

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: 69.05  E-value: 1.05e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 148664809   663 DRFVYTCNECKH--HVETRWHCTVCEDYDLCINCYNT-KSHTHKM 704
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
 1028-1070 1.16e-10

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


Pssm-ID: 411021 [Multi-domain]  Cd Length: 43  Bit Score: 57.66  E-value: 1.16e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 148664809 1028 ALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 1070
Cdd:cd20910     1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 922-1231 2.13e-09

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: 61.95  E-value: 2.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   922 RQIEREAQQQQHLYRANINNGMPPGRAGM---------------GTPGSQMTPVGLNVPRPNQVSGPVMSSmppgQWQQA 986
Cdd:pfam09606   51 RDMSKKAAQQQQPQGGQGNGGMGGGQQGMpdpinalqnlagqgtRPQMMGPMGPGPGGPMGQQMGGPGTAS----NLLAS 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   987 PIPQQQPMPGMPRPVMSMQAQAAVAGPRMPNVQPPRSISPSALQdllrtlkspsspqqqqqvlnilksnPQLMAAFIKQR 1066
Cdd:pfam09606  127 LGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGT-------------------------PNQMGPNGGPG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  1067 TAKYVANQPGMQPQPGLQSQPGM-QPQPGMHQQPSLQNLNAMQAGvprpgvpppqpamGGLNPQGQALNIMNPGHNPNMT 1145
Cdd:pfam09606  182 QGQAGGMNGGQQGPMGGQMPPQMgVPGMPGPADAGAQMGQQAQAN-------------GGMNPQQMGGAPNQVAMQQQQP 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  1146 NMNPQYREMGSSMGQmaapMGQLGQmGQPGLGADSTPniqQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQAS 1225
Cdd:pfam09606  249 QQQGQQSQLGMGINQ----MQQMPQ-GVGGGAGQGGP---GQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGG 320


                   ....*.
gi 148664809  1226 HLPGQQ 1231
Cdd:pfam09606  321 NHPAAH 326
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 1067-1265 1.28e-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: 42.87  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  1067 TAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQagvprpgvpppqpamgglnpqgqalnIMNPGHNPNMTN 1146
Cdd:TIGR01628  372 QDQFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGQP--------------------------LGWPRMSMMPTP 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  1147 MNPqyreMGSSMGQMAAPMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPgQPNPMSPQQHMLSGQPQASH 1226
Cdd:TIGR01628  426 MGP----GGPLRPNGLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQP-QSTASQGGQNKKLAQVLASA 500

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 148664809  1227 LPGQQ---IATSLSNQTGSPHPGLA--VT-MASSMDQGH----LGNPEQ 1265
Cdd:TIGR01628  501 TPQMQkqvLGERLFPLVEAIEPALAakITgMLLEMDNSEllhlLESPEL 549
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
 304-611 8.60e-95

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: 308.56  E-value: 8.60e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   304 VNKFLRRQNhPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGemSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDC 383
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESG--KPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   384 PPPNTRRVYISYLDSIHFFRPRcLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 458
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   459 KRLQEWYKKMLDKAFAE-------RIINDYKDIFKQ-----ANEDRL-------------TSAKELPYFEGDFWPNVLEE 513
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   514 SIKELEQEEEERKK---------EESTAASETPEGSQGDSKNAKKKNNKKTNKNKSS----------ISRANKKKPSMPN 574
Cdd:pfam08214  234 LIKEGRWKSVSLDQfweelrfrqEFSLGRLVGFIGLEGDYTPGSDDVINPPGLVKSKkqykmiksyiTGREYSTEEGAPE 313

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 148664809   575 VSNDLSQKLYATMEKHkevFFVIHLHAGPVISTQPPI 611
Cdd:pfam08214  314 SVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 94-201 5.33e-76

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: 246.20  E-value: 5.33e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   94 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWL 173
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80

                          90       100
                  ....*....|....*....|....*...
gi 148664809  174 YNRKTSRVYKFCSKLAEVFEQEIDPVMQ 201
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
BROMO smart00297
bromo domain;
91-199 5.36e-34

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 126.24  E-value: 5.36e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809     91 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNN 170
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78

                            90       100
                    ....*....|....*....|....*....
gi 148664809    171 AWLYNRKTSRVYKFCSKLAEVFEQEIDPV 199
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
 97-196 1.51e-31

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: 119.01  E-value: 1.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   97 LRQALMPTLEALYRQ-DPESLPFRQPVDPQLLgiPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN 175
Cdd:cd04369     1 LKKKLRSLLDALKKLkRDLSEPFLEPVDPKEA--PDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78

                          90       100
                  ....*....|....*....|.
gi 148664809  176 RKTSRVYKFCSKLAEVFEQEI 196
Cdd:cd04369    79 GPGSPIYKDAKKLEKLFEKLL 99
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
 117-194 6.48e-30

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: 114.30  E-value: 6.48e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148664809  117 PFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 194
Cdd:cd05498    23 PFYKPVDPEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFED 100
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 667-707 4.66e-27

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: 104.18  E-value: 4.66e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 148664809  667 YTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKW 707
Cdd:cd02337     1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
 110-193 8.74e-27

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: 105.49  E-value: 8.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  110 RQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLA 189
Cdd:cd05506    13 MKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELL 92


                  ....
gi 148664809  190 EVFE 193
Cdd:cd05506    93 KIFE 96
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
 96-196 1.61e-26

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: 104.56  E-value: 1.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   96 ELRQALMPTLEALyRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN 175
Cdd:cd05509     1 PLYTQLKKVLDSL-KNHKSAWPFLEPVDKEE--APDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77

                          90       100
                  ....*....|....*....|.
gi 148664809  176 RKTSRVYKFCSKLAEVFEQEI 196
Cdd:cd05509    78 GPDTEYYKCANKLEKFFWKKL 98
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
 975-1076 3.34e-25

Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices which pack in a bundle, exposing a hydrophobic groove between alpha-1 and alpha-3 within which complimentary domains found in the protein 'activator for thyroid hormone and retinoid receptors' (ACTR) can dock. Docking of these domains is required for the recruitment of RNA polymerase II and the basal transcription machinery.


Pssm-ID: 462659 [Multi-domain]  Cd Length: 111  Bit Score: 101.45  E-value: 3.34e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   975 MSSMPPGQWQQAPIPQQQPmpGMPRPVMSMQAQAAVAG---PRMPNVQP--------PRSISPSALQDLLRTLKSPSSPQ 1043
Cdd:pfam09030    1 QPQWAQGQWQQQQPLQQMQ--GMQRPMMPQQQQQQMPGmnpPQQPGLPQvpgqqpgrPGSIAPNALQDLLRTLKSPSSPQ 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 148664809  1044 QQQQVLNILKSNPQLMAAFIKQRTAKYVANQPG 1076
Cdd:pfam09030   79 QQQQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
 104-196 3.74e-24

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: 98.15  E-value: 3.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  104 TLEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 183
Cdd:cd05500    12 SIRSLKRL-KDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQ 90

                          90
                  ....*....|...
gi 148664809  184 FCSKLAEVFEQEI 196
Cdd:cd05500    91 MGKRLQAAFEKHL 103
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
 199-238 3.37e-23

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: 93.15  E-value: 3.37e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 148664809   199 VMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQ 238
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 734-802 7.42e-23

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: 93.22  E-value: 7.42e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148664809   734 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGCPV--CKQLIALCCyHAKHCQENKCPV 802
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCPYphCKRSRQLLR-HAKNCKDEDCPV 71
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
728-806 1.75e-22

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 92.43  E-value: 1.75e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809    728 ESRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPVCKQLIalccYHAKHCQENKCPVP 803
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76


                    ...
gi 148664809    804 FCL 806
Cdd:smart00551   77 KCV 79
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
 99-198 2.62e-22

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: 92.87  E-value: 2.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   99 QALMPT-LEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRK 177
Cdd:cd05497     7 QYLLKVvLKALWKH-KFAWPFQQPVDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKP 85

                          90       100
                  ....*....|....*....|.
gi 148664809  178 TSRVYKFCSKLAEVFEQEIDP 198
Cdd:cd05497    86 GDDVVLMAQTLEKLFLQKLAQ 106
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
 114-202 1.19e-21

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: 91.37  E-value: 1.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  114 ESLPFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN-RKTSRVYKFCSKLAEVF 192
Cdd:cd05496    22 DSEPFRQPVD--LLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSALF 99

                          90
                  ....*....|
gi 148664809  193 EQEIDPVMQS 202
Cdd:cd05496   100 EEHIKKIISD 109
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
 213-265 1.32e-21

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: 89.66  E-value: 1.32e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 148664809  213 FSPQTLCCYGKqlCTIPRD--AAYYSYQ---NRYHFCEKCFTEIQGENVTLGDDPSQP 265
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDDQGTS 56
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
 92-194 1.51e-21

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: 90.81  E-value: 1.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   92 FKPEELRQALMPTLEaLYRQDPeSLPFRQPVDPqllGIPDYFDIVKNPMDLSTIKRKLD---TGQYQEPWQYVDDVWLMF 168
Cdd:cd05502     1 LSPIDQRKCERLLLE-LYCHEL-SLPFHEPVSP---SVPNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMF 75

                          90       100
                  ....*....|....*....|....*.
gi 148664809  169 NNAWLYNRKTSRVYKFCSKLAEVFEQ 194
Cdd:cd05502    76 KNCYKFNEEDSEVAQAGKELELFFEE 101
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
 117-193 5.16e-21

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: 89.27  E-value: 5.16e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148664809  117 PFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFE 193
Cdd:cd05499    23 PFLDPVDPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFN 99
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 111-183 3.07e-19

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: 83.52  E-value: 3.07e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148664809   111 QDPESLPFRQPVDPqlLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 183
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYK 80
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
 95-195 4.97e-19

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: 83.98  E-value: 4.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   95 EELRQALMPTLEALYR------QDPESLPFRQPVdpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMF 168
Cdd:cd05504     4 SEGRHHGPLNLSALEQllveivKHKDSWPFLRPV--SKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVF 81

                          90       100
                  ....*....|....*....|....*..
gi 148664809  169 NNAWLYNRKTSRVYKFCSKLAEVFEQE 195
Cdd:cd05504    82 SNCFLYNPEHTSVYKAGTRLQRFFIKR 108
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
 95-185 1.84e-17

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: 79.41  E-value: 1.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   95 EELRQALMPTLEALYRQDPESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLY 174
Cdd:cd05510     6 EEFYESLDKVLNELKTYTEHSTPFLTKVSKR--EAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLY 83

                          90
                  ....*....|.
gi 148664809  175 NRKTSRVYKFC 185
Cdd:cd05510    84 NSDPSHPLRRH 94
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 663-705 2.41e-16

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: 74.01  E-value: 2.41e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 148664809    663 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHTHKMV 705
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
 100-190 8.02e-16

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: 74.36  E-value: 8.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  100 ALMPTLEALYRQDPESLpFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTS 179
Cdd:cd05512     5 LLRKTLDQLQEKDTAEI-FSEPVD--LSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDT 81

                          90
                  ....*....|.
gi 148664809  180 RVYKFCSKLAE 190
Cdd:cd05512    82 IFYRAAVRLRD 92
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
 113-181 1.17e-15

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: 73.56  E-value: 1.17e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148664809  113 PESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRV 181
Cdd:cd05503    16 EDAWPFLEPVNTKL--VPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEV 82
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 1-200 3.37e-15

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 79.08  E-value: 3.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809    1 MLEMKTEVQTDDAEP--EPTESKGEPRSEMM-----EEDLQGSSQVKEETDTTEQKSEPMEVEEKKpevkveakeeEENS 73
Cdd:COG5076    56 MPKEYITSIVDDREPgsMANVNDDLENVGGItyspfEKNRPESLRFDEIVFLAIESVTPESGLGSL----------LMAH 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   74 SNDTASQSTSPSQPRKKIfKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQ 153
Cdd:COG5076   126 LKTSVKKRKTPKIEDELL-YADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDYYEIIKSPMDLLTIQKKLKNGR 202

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 148664809  154 YQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVM 200
Cdd:COG5076   203 YKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
 110-205 6.24e-15

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: 71.91  E-value: 6.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  110 RQDPESLPFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLA 189
Cdd:cd05511    13 KNLPDSWPFHTPVNKKK--VPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVYTKKAKEML 90

                          90
                  ....*....|....*.
gi 148664809  190 EVFEQEIDPVMQSLGY 205
Cdd:cd05511    91 ELAEELLAEREEKLTQ 106
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
 111-198 7.39e-15

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: 72.00  E-value: 7.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  111 QDPESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYN------RKTSRvYKF 184
Cdd:cd05528    17 SDKRFNAFTKPVDEE--EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNpdrdpaDKLIR-SRA 93

                          90
                  ....*....|....*..
gi 148664809  185 CSKLAEV---FEQEIDP 198
Cdd:cd05528    94 CELRDEVhamIEAELDP 110
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 663-704 1.05e-14

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: 69.05  E-value: 1.05e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 148664809   663 DRFVYTCNECKH--HVETRWHCTVCEDYDLCINCYNT-KSHTHKM 704
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQThKGGNHQM 45
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
 130-201 1.45e-14

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: 71.21  E-value: 1.45e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148664809  130 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQ 201
Cdd:cd05524    39 PEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDACKLWELFLSARNEVLS 110
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
 130-183 2.17e-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: 70.41  E-value: 2.17e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 148664809  130 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYK 183
Cdd:cd05515    37 PDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYK 90
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
 98-183 2.72e-13

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: 67.00  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   98 RQALMPTLEALYRQdPESLPFRQPVdpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRK 177
Cdd:cd05507     5 KKAILLVYRTLASH-RYASVFLKPV--TEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNSS 81


                  ....*.
gi 148664809  178 TSRVYK 183
Cdd:cd05507    82 DHDVYL 87
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 667-703 6.48e-13

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: 63.99  E-value: 6.48e-13
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 148664809  667 YTCNEC-KHHVETRWHCTVCEDYDLCINCYNTKSHTHK 703
Cdd:cd02249     1 YSCDGClKPIVGVRYHCLVCEDFDLCSSCYAKGKKGHP 38
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
 97-188 3.91e-12

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: 63.58  E-value: 3.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   97 LRQALMPTLEALYRQDPESLpFRQPVDPQLlgIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNR 176
Cdd:cd05513     2 LQKALEQLIRQLQRKDPHGF-FAFPVTDFI--APGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNK 78

                          90
                  ....*....|..
gi 148664809  177 KTSRVYKFCSKL 188
Cdd:cd05513    79 PDTIYYKAAKKL 90
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
 93-192 5.78e-12

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: 63.32  E-value: 5.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   93 KPEELRQALMPtlealYRqdpESLPFRQPVDPQllGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAW 172
Cdd:cd05505     4 KCEEILSKILK-----YR---FSWPFREPVTAD--EAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAE 73

                          90       100
                  ....*....|....*....|
gi 148664809  173 LYNRKTSRVYKFCSKLAEVF 192
Cdd:cd05505    74 KYYENGSYVLSCMRKTEQCC 93
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
 96-184 5.91e-12

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: 63.50  E-value: 5.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   96 ELRQALMPTLEALYRQDPES----------LPFRQPvdpqllgIPDYFDIVKNPMDLSTIKRKLDtgQYQEPWQYVDDVW 165
Cdd:cd05521     1 KLSKKLKPLYDGIYTLKEENgieihpifnvLPLRKD-------YPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLA 71

                          90
                  ....*....|....*....
gi 148664809  166 LMFNNAWLYNRKTSRVYKF 184
Cdd:cd05521    72 QIPWNARLYNTKGSVIYKY 90
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
 130-188 4.28e-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: 60.82  E-value: 4.28e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 148664809  130 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKL 188
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 ...
 130-188 4.62e-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: 60.72  E-value: 4.62e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 148664809  130 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKL 188
Cdd:cd05522    38 PEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYKDAVLL 96
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
 129-197 5.44e-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: 60.90  E-value: 5.44e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148664809  129 IPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEID 197
Cdd:cd05516    37 LPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQ 105
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
 1028-1070 1.16e-10

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


Pssm-ID: 411021 [Multi-domain]  Cd Length: 43  Bit Score: 57.66  E-value: 1.16e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 148664809 1028 ALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKY 1070
Cdd:cd20910     1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
 97-196 1.79e-10

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: 59.28  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   97 LRQALMPTLEALYRQDPE-----SLPFRQPVDPQLLgiPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNA 171
Cdd:cd05519     1 LKAAMLEIYDAVLNCEDEtgrklSELFLEKPSKKLY--PDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANA 78

                          90       100
                  ....*....|....*....|....*
gi 148664809  172 WLYNRKTSRVYKFCSKLAEVFEQEI 196
Cdd:cd05519    79 RTYNQEGSIVYEDAVEMEKAFKKKY 103
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
 119-182 2.32e-10

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: 58.61  E-value: 2.32e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148664809  119 RQPVD-----PQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVY 182
Cdd:cd05518    21 RRLCDlfmekPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVY 89
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
 95-196 9.13e-10

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: 57.73  E-value: 9.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   95 EELRQALMPTLEALYRQDPESL--PFRQPVDpQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAW 172
Cdd:cd05529    23 DEERERLISGLDKLLLSLQLEIaeYFEYPVD-LRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAE 101

                          90       100
                  ....*....|....*....|....
gi 148664809  173 LYNRKTSRVYKFCSKLAEVFEQEI 196
Cdd:cd05529   102 TFNEPNSEIAKKAKRLSDWLLRIL 125
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 922-1231 2.13e-09

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: 61.95  E-value: 2.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   922 RQIEREAQQQQHLYRANINNGMPPGRAGM---------------GTPGSQMTPVGLNVPRPNQVSGPVMSSmppgQWQQA 986
Cdd:pfam09606   51 RDMSKKAAQQQQPQGGQGNGGMGGGQQGMpdpinalqnlagqgtRPQMMGPMGPGPGGPMGQQMGGPGTAS----NLLAS 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   987 PIPQQQPMPGMPRPVMSMQAQAAVAGPRMPNVQPPRSISPSALQdllrtlkspsspqqqqqvlnilksnPQLMAAFIKQR 1066
Cdd:pfam09606  127 LGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGT-------------------------PNQMGPNGGPG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  1067 TAKYVANQPGMQPQPGLQSQPGM-QPQPGMHQQPSLQNLNAMQAGvprpgvpppqpamGGLNPQGQALNIMNPGHNPNMT 1145
Cdd:pfam09606  182 QGQAGGMNGGQQGPMGGQMPPQMgVPGMPGPADAGAQMGQQAQAN-------------GGMNPQQMGGAPNQVAMQQQQP 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  1146 NMNPQYREMGSSMGQmaapMGQLGQmGQPGLGADSTPniqQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQAS 1225
Cdd:pfam09606  249 QQQGQQSQLGMGINQ----MQQMPQ-GVGGGAGQGGP---GQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGG 320


                   ....*.
gi 148664809  1226 HLPGQQ 1231
Cdd:pfam09606  321 NHPAAH 326
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 668-706 5.94e-09

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: 52.65  E-value: 5.94e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 148664809  668 TCNECKHHVE-TRWHCTVCEDYDLCINCYNTKSH-THKMVK 706
Cdd:cd02340     2 ICDGCQGPIVgVRYKCLVCPDYDLCESCEAKGVHpEHAMLK 42
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
 130-194 3.34e-08

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: 52.78  E-value: 3.34e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148664809  130 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 194
Cdd:cd05525    39 PDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRLRKAYYQ 103
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
 130-194 1.35e-07

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: 50.90  E-value: 1.35e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148664809  130 PDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQ 194
Cdd:cd05517    37 PDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKDANAIKKIFTA 101
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
 95-152 7.36e-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: 48.98  E-value: 7.36e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 148664809   95 EELRQALMPtLEALYRQDPeSLPFRQPVDPQLLGIPDYFDIVKNPMDLSTI-KRKLDTG 152
Cdd:cd05494     3 EALERVLRE-LKRHRRNED-AWPFLEPVNPPRRGAPDYRDVIKRPMSFGTKvNNIVETG 59
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
 95-196 2.84e-06

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: 46.99  E-value: 2.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809   95 EELRQALMPTLEALYRqdPESLPFRQPVDpqLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLY 174
Cdd:cd05508     2 DQLSKLLKFALERMKQ--PGAEPFLKPVD--LEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIY 77

                          90       100
                  ....*....|....*....|..
gi 148664809  175 NRKTSRVYKFCSKLAEVFEQEI 196
Cdd:cd05508    78 NGGDHKLTQAAKAIVKICEQEM 99
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
 129-194 3.75e-06

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: 46.65  E-value: 3.75e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148664809  129 IPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVyKFCSKLAEVFEQ 194
Cdd:cd05501    30 IRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDDDFG-QVGITLEKKFEK 94
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 669-700 3.00e-05

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 42.45  E-value: 3.00e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 148664809  669 CNECKHH--VETRWHCTVCEDYDLCINCYNTKSH 700
Cdd:cd02339     3 CDTCRKQgiIGIRWKCAECPNYDLCTTCYHGDKH 36
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 1072-1271 1.29e-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: 46.54  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  1072 ANQPGMQPQPGLQSQPGMQPQpGMHQQPslqnLNAMQAGVPRPGVPPPQPAMGgLNPQGQALNIMNPGHNPNMTNMNPQY 1151
Cdd:pfam09606   56 KAAQQQQPQGGQGNGGMGGGQ-QGMPDP----INALQNLAGQGTRPQMMGPMG-PGPGGPMGQQMGGPGTASNLLASLGR 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  1152 REMGSSMGQMAAPMGQLGQMGQPGLGADSTPniqqalqqrilqqqqMKQQIGSPGQPNPMSPQQHmlSGQPQASHLPGQQ 1231
Cdd:pfam09606  130 PQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQ---------------PSSGQPGSGTPNQMGPNGG--PGQGQAGGMNGGQ 192

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 148664809  1232 IATSLS---NQTGSPHPGlavTMASSMDQGHLGNPEQSAMLPQ 1271
Cdd:pfam09606  193 QGPMGGqmpPQMGVPGMP---GPADAGAQMGQQAQANGGMNPQ 232
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 668-707 9.19e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 38.34  E-value: 9.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 148664809  668 TCNECK--HHVETRWHCTVCEDYDLCINCY--NTKSHTHKMVKW 707
Cdd:cd02345     2 SCSACRkqDISGIRFPCQVCRDYSLCLGCYtkGRETKRHNSLHI 45
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 667-706 9.23e-04

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: 38.18  E-value: 9.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 148664809  667 YTCNECKHH--VETRWHCTVC--EDYDLCINC-YNTKSH--THKMVK 706
Cdd:cd02341     1 FKCDSCGIEpiPGTRYHCSECddGDFDLCQDCvVKGESHqeDHWLVK 47
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 667-695 1.06e-03

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 38.04  E-value: 1.06e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 148664809  667 YTCNECKHHV--ETRWHCTVCEDYDLCINCY 695
Cdd:cd02335     1 YHCDYCSKDItgTIRIKCAECPDFDLCLECF 31
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 1067-1265 1.28e-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: 42.87  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  1067 TAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQagvprpgvpppqpamgglnpqgqalnIMNPGHNPNMTN 1146
Cdd:TIGR01628  372 QDQFMQLQPRMRQLPMGSPMGGAMGQPPYYGQGPQQQFNGQP--------------------------LGWPRMSMMPTP 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  1147 MNPqyreMGSSMGQMAAPMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPgQPNPMSPQQHMLSGQPQASH 1226
Cdd:TIGR01628  426 MGP----GGPLRPNGLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQP-QSTASQGGQNKKLAQVLASA 500

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 148664809  1227 LPGQQ---IATSLSNQTGSPHPGLA--VT-MASSMDQGH----LGNPEQ 1265
Cdd:TIGR01628  501 TPQMQkqvLGERLFPLVEAIEPALAakITgMLLEMDNSEllhlLESPEL 549
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 668-703 4.55e-03

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239084  Cd Length: 45  Bit Score: 36.41  E-value: 4.55e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 148664809  668 TCNECKHHV--ETRWHCTVCEDYDLCINCYNTKSHTHK 703
Cdd:cd02344     2 TCDGCQMFPinGPRFKCRNCDDFDFCENCFKTRKHNTR 39
Cytadhesin_P30 pfam07271
Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 ...
 1074-1176 5.50e-03

Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 and P30 proteins. P30 has been found to be membrane associated and localized on the tip organelle. It is thought that it is important in cytadherence and virulence. The N-terminus contains two predicted transmembrane helices followed by a long region of a short 6 residue proline rich repeat.


Pssm-ID: 429374 [Multi-domain]  Cd Length: 275  Bit Score: 40.34  E-value: 5.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148664809  1074 QPGMQPQPGLQSQPGMQPQPGM---HQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQgQALNIMNPGHNPNMTNMNPQ 1150
Cdd:pfam07271  168 RIGFPMQPNMGMRPGFNQMPGMppnQMRPGFNQMPGMPPRPGFPNPMPNMQPRPGFRPQ-PGPMGNRPGGGFPHPGTPMG 246

                           90       100       110
                   ....*....|....*....|....*....|
gi 148664809  1151 YREMGS-SMGQ---MAAPmgQLGQMGQPGL 1176
Cdd:pfam07271  247 PNRMPNpGMNQrpgMAPP--RPGFPPQNGP 274
ZZ_RSC8 cd02336
Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of ...
 667-696 6.16e-03

Zinc finger, ZZ type. Zinc finger present in RSC8 and related proteins. RSC8 is a component of the RSC complex, which is closely related to the SWI/SNF complex and is involved in remodeling chromatin structure. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239076  Cd Length: 45  Bit Score: 35.76  E-value: 6.16e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 148664809  667 YTCNEC-KHHVETRWHCTVCEDYDLCINCYN 696
Cdd:cd02336     1 YHCFTCgNDCTRVRYHNLKAKKYDLCPSCYQ 31
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 668-701 9.41e-03

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 35.40  E-value: 9.41e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 148664809  668 TCNECKHHVET--RWHCTVCEDYDLCINCYNTKSHT 701
Cdd:cd02338     2 SCDGCGKSNFTgrRYKCLICYDYDLCADCYDSGVTT 37
 
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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