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Conserved domains on  [gi|568992690|ref|XP_006521152|]
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histone acetyltransferase p300 isoform X1 [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 ...
 1315-1621 3.72e-97

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: 318.19  E-value: 3.72e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1315 VNDFLRRQNhPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEmaESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDC 1394
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1395 PPPNQRRVYISYLDSVHFFRPKcLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1469
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1470 KRLQEWYKKMLDKAVSE-------RIVHDYKDILKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1524
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1525 SIKELEQEEEE----------------------RKREENTSNESTDVTKGDskNAKKKNNKKTSKNKSSLSRGNKKKPGM 1582
Cdd:pfam08214  234 LIKEGRWKSVSldqfweelrfrqefslgrlvgfIGLEGDYTPGSDDVINPP--GLVKSKKQYKMIKSYITGREYSTEEGA 311

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 568992690  1583 PNVSNDLSQKLYATMEKHkevFFVIRLIACPAPNSLPPI 1621
Cdd:pfam08214  312 PESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 1050-1157 1.26e-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: 248.90  E-value: 1.26e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1050 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWL 1129
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80

                          90       100
                  ....*....|....*....|....*...
gi 568992690 1130 YNRKTSRVYKYCSKLSEVFEQEIDPVMQ 1157
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
 567-647 7.64e-48

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


:

Pssm-ID: 366953  Cd Length: 81  Bit Score: 165.74  E-value: 7.64e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   567 GIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELE 646
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80


                   .
gi 568992690   647 E 647
Cdd:pfam02172   81 E 81
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
 2003-2109 5.29e-34

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: 127.26  E-value: 5.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2003 QPPWAQGGMPQPQ--QMQSGMPRPAMMSVAQ-HGQPLNMAPQPGLGQV-GVSPLKPGTVSQQALQNLLRTLRSPSSPLQQ 2078
Cdd:pfam09030    1 QPQWAQGQWQQQQplQQMQGMQRPMMPQQQQqQMPGMNPPQQPGLPQVpGQQPGRPGSIAPNALQDLLRTLKSPSSPQQQ 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 568992690  2079 QQVLSILHANPQLLAAFIKQRAAKYANPNPQ 2109
Cdd:pfam09030   81 QQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
 1169-1251 2.42e-32

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: 121.24  E-value: 2.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1169 FSPQTLCCYGKqlCTIPRD--ATYYSYQNSSpqygllaDRYHFCEKCFNEIQGESVSLGDDpsqPQTTINKEQFSKRKND 1246
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLD-------NRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKND 68


                  ....*
gi 568992690 1247 TLDPE 1251
Cdd:cd15802    69 ELDEE 73
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 1677-1717 2.76e-28

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: 108.42  E-value: 2.76e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568992690 1677 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKL 1717
Cdd:cd02337     1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 348-415 3.25e-28

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: 109.40  E-value: 3.25e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568992690   348 HAHKCQRREQAngevrQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVC 415
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 1744-1812 1.15e-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: 96.30  E-value: 1.15e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568992690  1744 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1812
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
 1252-1286 1.59e-20

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


:

Pssm-ID: 277116  Cd Length: 40  Bit Score: 86.45  E-value: 1.59e-20
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568992690 1252 LFVECTECGRKMHQICVLHHEIIWPSGFVCDGCLK 1286
Cdd:cd15646     6 LFVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 98-328 1.39e-08

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: 60.41  E-value: 1.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690    98 GGPGQAMASQAQQNSPglslinsmvKSPMAQTGLTSPNMGIGSSGP--NQGPTQSPAGMMNSPVNQPAMGMNTGMNAGMN 175
Cdd:pfam09606  115 GGPGTASNLLASLGRP---------QMPMGGAGFPSQMSRVGRMQPggQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQA 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   176 PGML--AAGNGQGIMPNQV----MNGSIGAGRGRPNMQYPNAGMGnagsllTEPLQQGSPQ--MGGQPGLRGPQPLKMGM 247
Cdd:pfam09606  186 GGMNggQQGPMGGQMPPQMgvpgMPGPADAGAQMGQQAQANGGMN------PQQMGGAPNQvaMQQQQPQQQGQQSQLGM 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   248 -MNNPSPYGSPYTQNSGQQIGASGLGLQIQTKTVLPNNLSP---------FAMDKKAVPGGGMPSMGQ-QPTPSVQQPGL 316
Cdd:pfam09606  260 gINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIgdqnnyqqqQTRQQQQQQGGNHPAAHQqQMNQSVGQGGQ 339

                          250
                   ....*....|..
gi 568992690   317 VTPVAAGMGSGA 328
Cdd:pfam09606  340 VVALGGLNHLET 351
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 1968-2375 5.95e-08

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: 58.10  E-value: 5.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1968 PQMSPMAPMGMNPPPMARGPGGHLDPGIGPAGmQQQPPWAQGGMPQPQQ----MQSGMPRPAMMSVAQHGQPLNMAPQPG 2043
Cdd:pfam09606   97 QMMGPMGPGPGGPMGQQMGGPGTASNLLASLG-RPQMPMGGAGFPSQMSrvgrMQPGGQAGGMMQPSSGQPGSGTPNQMG 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2044 LGQVGVSPLKPGTVSQQALQNLLRtlrspsSPLQQQQVLSILHANPQllaafikQRAAKYANPNPQPLPGQPGMTQGQ-P 2122
Cdd:pfam09606  176 PNGGPGQGQAGGMNGGQQGPMGGQ------MPPQMGVPGMPGPADAG-------AQMGQQAQANGGMNPQQMGGAPNQvA 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2123 GLQPPTMPGQQGVHSNPALQNMNPLQAGVQRAGLPQQQPQQqlqppMGAMSPQAQQM--NMNHNTMPSQFRDILRRQMMQ 2200
Cdd:pfam09606  243 MQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQP-----MGPPGQQPGAMpnVMSIGDQNNYQQQQTRQQQQQ 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2201 QQGAGPGIGPGMANQFQQPQGigyppqqqqqqrmqhhmqqMQQGNMGQMGQLPQALGAEAGASLQAYQQRllQQQMGSPA 2280
Cdd:pfam09606  318 QGGNHPAAHQQQMNQSVGQGG-------------------QVVALGGLNHLETWNPGNFGGLGANPMQRG--QPGMMSSP 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2281 QPNPMSPQQHMLPNQ----AQSPHLQGQQIPNSLSNQVRSPQPVPSPRpqsqpphsspsprMQPQPSPH-HVSPQTSSPH 2355
Cdd:pfam09606  377 SPVPGQQVRQVTPNQfmrqSPQPSVPSPQGPGSQPPQSHPGGMIPSPA-------------LIPSPSPQmSQQPAQQRTI 443

                          410       420
                   ....*....|....*....|
gi 568992690  2356 PGLVAAQAANPMEQGHFASP 2375
Cdd:pfam09606  444 GQDSPGGSLNTPGQSAVNSP 463
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 663-836 7.40e-05

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


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 48.08  E-value: 7.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   663 PGMGPVPMNTGSNMGQQPTGMTT------------------NGPVPDPSMIRGSVPNHMMPRMTPQPGLNQFGQMNMPQP 724
Cdd:pfam09606   97 QMMGPMGPGPGGPMGQQMGGPGTasnllaslgrpqmpmggaGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGP 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   725 PIGPRQP-SPLQHHGQLAQSGSLNPP-MGYGPRMQQASGQNQFLSQTQFTSqGMNVTNMPLAPS----SGQAPVSQAQMS 798
Cdd:pfam09606  177 NGGPGQGqAGGMNGGQQGPMGGQMPPqMGVPGMPGPADAGAQMGQQAQANG-GMNPQQMGGAPNqvamQQQQPQQQGQQS 255

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 568992690   799 SSSCPVNSPI-MPPGSQGSHIH-CPTLPQQAHQNSPSPVP 836
Cdd:pfam09606  256 QLGMGINQMQqMPQGVGGGAGQgGPGQPMGPPGQQPGAMP 295
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
 1315-1621 3.72e-97

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: 318.19  E-value: 3.72e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1315 VNDFLRRQNhPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEmaESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDC 1394
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1395 PPPNQRRVYISYLDSVHFFRPKcLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1469
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1470 KRLQEWYKKMLDKAVSE-------RIVHDYKDILKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1524
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1525 SIKELEQEEEE----------------------RKREENTSNESTDVTKGDskNAKKKNNKKTSKNKSSLSRGNKKKPGM 1582
Cdd:pfam08214  234 LIKEGRWKSVSldqfweelrfrqefslgrlvgfIGLEGDYTPGSDDVINPP--GLVKSKKQYKMIKSYITGREYSTEEGA 311

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 568992690  1583 PNVSNDLSQKLYATMEKHkevFFVIRLIACPAPNSLPPI 1621
Cdd:pfam08214  312 PESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 1050-1157 1.26e-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: 248.90  E-value: 1.26e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1050 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWL 1129
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80

                          90       100
                  ....*....|....*....|....*...
gi 568992690 1130 YNRKTSRVYKYCSKLSEVFEQEIDPVMQ 1157
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
 567-647 7.64e-48

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


Pssm-ID: 366953  Cd Length: 81  Bit Score: 165.74  E-value: 7.64e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   567 GIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELE 646
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80


                   .
gi 568992690   647 E 647
Cdd:pfam02172   81 E 81
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
 2003-2109 5.29e-34

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: 127.26  E-value: 5.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2003 QPPWAQGGMPQPQ--QMQSGMPRPAMMSVAQ-HGQPLNMAPQPGLGQV-GVSPLKPGTVSQQALQNLLRTLRSPSSPLQQ 2078
Cdd:pfam09030    1 QPQWAQGQWQQQQplQQMQGMQRPMMPQQQQqQMPGMNPPQQPGLPQVpGQQPGRPGSIAPNALQDLLRTLKSPSSPQQQ 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 568992690  2079 QQVLSILHANPQLLAAFIKQRAAKYANPNPQ 2109
Cdd:pfam09030   81 QQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
BROMO smart00297
bromo domain;
1047-1155 1.21e-33

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 126.24  E-value: 1.21e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   1047 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNN 1126
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78

                            90       100
                    ....*....|....*....|....*....
gi 568992690   1127 AWLYNRKTSRVYKYCSKLSEVFEQEIDPV 1155
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
 1169-1251 2.42e-32

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: 121.24  E-value: 2.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1169 FSPQTLCCYGKqlCTIPRD--ATYYSYQNSSpqygllaDRYHFCEKCFNEIQGESVSLGDDpsqPQTTINKEQFSKRKND 1246
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLD-------NRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKND 68


                  ....*
gi 568992690 1247 TLDPE 1251
Cdd:cd15802    69 ELDEE 73
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 1677-1717 2.76e-28

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: 108.42  E-value: 2.76e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568992690 1677 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKL 1717
Cdd:cd02337     1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 348-415 3.25e-28

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: 109.40  E-value: 3.25e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568992690   348 HAHKCQRREQAngevrQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVC 415
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 1744-1812 1.15e-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: 96.30  E-value: 1.15e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568992690  1744 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1812
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
 1155-1194 1.55e-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: 95.08  E-value: 1.55e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568992690  1155 VMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQ 1194
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1738-1816 2.35e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 95.89  E-value: 2.35e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   1738 DSRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPICKQLIalccYHAKHCQENKCPVP 1813
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76


                    ...
gi 568992690   1814 FCL 1816
Cdd:smart00551   77 KCV 79
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
348-418 2.51e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 90.12  E-value: 2.51e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568992690    348 HAHKCQRREQangevrQCNLPHCRTMKNVLNHMTHCQSGKsCQVAHCASSRQIISHWKNCTRHDCPVCLPL 418
Cdd:smart00551   16 HARRCKAREA------KCQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
 1252-1286 1.59e-20

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


Pssm-ID: 277116  Cd Length: 40  Bit Score: 86.45  E-value: 1.59e-20
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568992690 1252 LFVECTECGRKMHQICVLHHEIIWPSGFVCDGCLK 1286
Cdd:cd15646     6 LFVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 1067-1143 5.90e-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: 5.90e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568992690  1067 QDPESLPFRQPVDPqlLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSK 1143
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKAAEK 84
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1673-1715 2.35e-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: 74.78  E-value: 2.35e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 568992690   1673 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCITCYNTKNHDHKME 1715
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 1016-1156 1.19e-15

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 81.39  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1016 PELKTDGKEEEEQPStSATQSSPAPGQSKKK-------IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDY 1088
Cdd:COG5076   105 VFLAIESVTPESGLG-SLLMAHLKTSVKKRKtpkiedeLLYADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDY 181

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568992690 1089 FDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVM 1156
Cdd:COG5076   182 YEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 1673-1714 2.70e-15

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: 71.75  E-value: 2.70e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568992690  1673 DRFVYTCNECKH--HVETRWHCTVCEDYDLCITCYNTKN-HDHKM 1714
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQTHKgGNHQM 45
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
 2061-2103 7.51e-13

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: 64.60  E-value: 7.51e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568992690 2061 ALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKY 2103
Cdd:cd20910     1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 98-328 1.39e-08

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: 60.41  E-value: 1.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690    98 GGPGQAMASQAQQNSPglslinsmvKSPMAQTGLTSPNMGIGSSGP--NQGPTQSPAGMMNSPVNQPAMGMNTGMNAGMN 175
Cdd:pfam09606  115 GGPGTASNLLASLGRP---------QMPMGGAGFPSQMSRVGRMQPggQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQA 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   176 PGML--AAGNGQGIMPNQV----MNGSIGAGRGRPNMQYPNAGMGnagsllTEPLQQGSPQ--MGGQPGLRGPQPLKMGM 247
Cdd:pfam09606  186 GGMNggQQGPMGGQMPPQMgvpgMPGPADAGAQMGQQAQANGGMN------PQQMGGAPNQvaMQQQQPQQQGQQSQLGM 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   248 -MNNPSPYGSPYTQNSGQQIGASGLGLQIQTKTVLPNNLSP---------FAMDKKAVPGGGMPSMGQ-QPTPSVQQPGL 316
Cdd:pfam09606  260 gINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIgdqnnyqqqQTRQQQQQQGGNHPAAHQqQMNQSVGQGGQ 339

                          250
                   ....*....|..
gi 568992690   317 VTPVAAGMGSGA 328
Cdd:pfam09606  340 VVALGGLNHLET 351
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 1968-2375 5.95e-08

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: 58.10  E-value: 5.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1968 PQMSPMAPMGMNPPPMARGPGGHLDPGIGPAGmQQQPPWAQGGMPQPQQ----MQSGMPRPAMMSVAQHGQPLNMAPQPG 2043
Cdd:pfam09606   97 QMMGPMGPGPGGPMGQQMGGPGTASNLLASLG-RPQMPMGGAGFPSQMSrvgrMQPGGQAGGMMQPSSGQPGSGTPNQMG 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2044 LGQVGVSPLKPGTVSQQALQNLLRtlrspsSPLQQQQVLSILHANPQllaafikQRAAKYANPNPQPLPGQPGMTQGQ-P 2122
Cdd:pfam09606  176 PNGGPGQGQAGGMNGGQQGPMGGQ------MPPQMGVPGMPGPADAG-------AQMGQQAQANGGMNPQQMGGAPNQvA 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2123 GLQPPTMPGQQGVHSNPALQNMNPLQAGVQRAGLPQQQPQQqlqppMGAMSPQAQQM--NMNHNTMPSQFRDILRRQMMQ 2200
Cdd:pfam09606  243 MQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQP-----MGPPGQQPGAMpnVMSIGDQNNYQQQQTRQQQQQ 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2201 QQGAGPGIGPGMANQFQQPQGigyppqqqqqqrmqhhmqqMQQGNMGQMGQLPQALGAEAGASLQAYQQRllQQQMGSPA 2280
Cdd:pfam09606  318 QGGNHPAAHQQQMNQSVGQGG-------------------QVVALGGLNHLETWNPGNFGGLGANPMQRG--QPGMMSSP 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2281 QPNPMSPQQHMLPNQ----AQSPHLQGQQIPNSLSNQVRSPQPVPSPRpqsqpphsspsprMQPQPSPH-HVSPQTSSPH 2355
Cdd:pfam09606  377 SPVPGQQVRQVTPNQfmrqSPQPSVPSPQGPGSQPPQSHPGGMIPSPA-------------LIPSPSPQmSQQPAQQRTI 443

                          410       420
                   ....*....|....*....|
gi 568992690  2356 PGLVAAQAANPMEQGHFASP 2375
Cdd:pfam09606  444 GQDSPGGSLNTPGQSAVNSP 463
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 1948-2089 2.16e-05

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: 49.81  E-value: 2.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1948 ETQRQMAHVQIFQRpiQHQMPQMSPMAPM-GMNPPPMARGPGGHldpgigpAGMQQQPPWAQGGMPQPQQMQSGMPRPAM 2026
Cdd:TIGR01628  365 EQRRAHLQDQFMQL--QPRMRQLPMGSPMgGAMGQPPYYGQGPQ-------QQFNGQPLGWPRMSMMPTPMGPGGPLRPN 435

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568992690  2027 MSV--AQHGQPLNMApQPGLGQVGVSPLK--PGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANP 2089
Cdd:TIGR01628  436 GLApmNAVRAPSRNA-QNAAQKPPMQPVMypPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASAT 501
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 663-836 7.40e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 48.08  E-value: 7.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   663 PGMGPVPMNTGSNMGQQPTGMTT------------------NGPVPDPSMIRGSVPNHMMPRMTPQPGLNQFGQMNMPQP 724
Cdd:pfam09606   97 QMMGPMGPGPGGPMGQQMGGPGTasnllaslgrpqmpmggaGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGP 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   725 PIGPRQP-SPLQHHGQLAQSGSLNPP-MGYGPRMQQASGQNQFLSQTQFTSqGMNVTNMPLAPS----SGQAPVSQAQMS 798
Cdd:pfam09606  177 NGGPGQGqAGGMNGGQQGPMGGQMPPqMGVPGMPGPADAGAQMGQQAQANG-GMNPQQMGGAPNqvamQQQQPQQQGQQS 255

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 568992690   799 SSSCPVNSPI-MPPGSQGSHIH-CPTLPQQAHQNSPSPVP 836
Cdd:pfam09606  256 QLGMGINQMQqMPQGVGGGAGQgGPGQPMGPPGQQPGAMP 295
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 647-797 3.27e-04

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 45.95  E-value: 3.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   647 EKRRTRLQKQNMlPNAPGM--GPVPMNTGSNMGQQPTGMttngpvPDPSMIRGSVP---NHMMPRMTPQpglnqfgQMNM 721
Cdd:TIGR01628  365 EQRRAHLQDQFM-QLQPRMrqLPMGSPMGGAMGQPPYYG------QGPQQQFNGQPlgwPRMSMMPTPM-------GPGG 430

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568992690   722 PQPPIGPRQPSPLQHHGQLAQSGSLNPPMGYGPRMQQASGQNQFLSQTQFTSQGMNVTNMPLAPSSGQA--PVSQAQM 797
Cdd:TIGR01628  431 PLRPNGLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASatPQMQKQV 508
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 2252-2369 2.34e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.54  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 2252 LPQALGAEAGASLQAYQQRLL----QQQMGSPAQPNPmSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPvpsprpqs 2327
Cdd:PRK10263  750 EPVQQPQQPVAPQQQYQQPQQpvapQPQYQQPQQPVA-PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP-------- 820

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568992690 2328 QPPHSSPSPRMQPQPSPHHvSPQTSSPHPGLVAAQAANPMEQ 2369
Cdd:PRK10263  821 QQPVAPQPQYQQPQQPVAP-QPQDTLLHPLLMRNGDSRPLHK 861
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
 1315-1621 3.72e-97

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: 318.19  E-value: 3.72e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1315 VNDFLRRQNhPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEmaESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDC 1394
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1395 PPPNQRRVYISYLDSVHFFRPKcLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1469
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1470 KRLQEWYKKMLDKAVSE-------RIVHDYKDILKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1524
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1525 SIKELEQEEEE----------------------RKREENTSNESTDVTKGDskNAKKKNNKKTSKNKSSLSRGNKKKPGM 1582
Cdd:pfam08214  234 LIKEGRWKSVSldqfweelrfrqefslgrlvgfIGLEGDYTPGSDDVINPP--GLVKSKKQYKMIKSYITGREYSTEEGA 311

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 568992690  1583 PNVSNDLSQKLYATMEKHkevFFVIRLIACPAPNSLPPI 1621
Cdd:pfam08214  312 PESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 1050-1157 1.26e-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: 248.90  E-value: 1.26e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1050 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWL 1129
Cdd:cd05495     1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80

                          90       100
                  ....*....|....*....|....*...
gi 568992690 1130 YNRKTSRVYKYCSKLSEVFEQEIDPVMQ 1157
Cdd:cd05495    81 YNRKTSRVYKYCTKLAEVFEQEIDPVMQ 108
KIX pfam02172
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ...
 567-647 7.64e-48

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


Pssm-ID: 366953  Cd Length: 81  Bit Score: 165.74  E-value: 7.64e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   567 GIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELE 646
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80


                   .
gi 568992690   647 E 647
Cdd:pfam02172   81 E 81
Creb_binding pfam09030
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ...
 2003-2109 5.29e-34

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: 127.26  E-value: 5.29e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2003 QPPWAQGGMPQPQ--QMQSGMPRPAMMSVAQ-HGQPLNMAPQPGLGQV-GVSPLKPGTVSQQALQNLLRTLRSPSSPLQQ 2078
Cdd:pfam09030    1 QPQWAQGQWQQQQplQQMQGMQRPMMPQQQQqQMPGMNPPQQPGLPQVpGQQPGRPGSIAPNALQDLLRTLKSPSSPQQQ 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 568992690  2079 QQVLSILHANPQLLAAFIKQRAAKYANPNPQ 2109
Cdd:pfam09030   81 QQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
BROMO smart00297
bromo domain;
1047-1155 1.21e-33

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 126.24  E-value: 1.21e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   1047 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNN 1126
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78

                            90       100
                    ....*....|....*....|....*....
gi 568992690   1127 AWLYNRKTSRVYKYCSKLSEVFEQEIDPV 1155
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
 1169-1251 2.42e-32

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: 121.24  E-value: 2.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1169 FSPQTLCCYGKqlCTIPRD--ATYYSYQNSSpqygllaDRYHFCEKCFNEIQGESVSLGDDpsqPQTTINKEQFSKRKND 1246
Cdd:cd15802     1 FEPQVLYCSGK--CTIPRKrnAVYYSYQNLD-------NRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKND 68


                  ....*
gi 568992690 1247 TLDPE 1251
Cdd:cd15802    69 ELDEE 73
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
 1053-1152 1.80e-30

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: 116.70  E-value: 1.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1053 LRQALMPTLEALYRQ-DPESLPFRQPVDPQLLgiPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYN 1131
Cdd:cd04369     1 LKKKLRSLLDALKKLkRDLSEPFLEPVDPKEA--PDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78

                          90       100
                  ....*....|....*....|.
gi 568992690 1132 RKTSRVYKYCSKLSEVFEQEI 1152
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 ...
 1073-1150 6.70e-29

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: 112.37  E-value: 6.70e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568992690 1073 PFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQ 1150
Cdd:cd05498    23 PFYKPVDPEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFED 100
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 1677-1717 2.76e-28

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: 108.42  E-value: 2.76e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568992690 1677 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKL 1717
Cdd:cd02337     1 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHPHKMEKL 41
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 348-415 3.25e-28

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: 109.40  E-value: 3.25e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568992690   348 HAHKCQRREQAngevrQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVC 415
Cdd:pfam02135   10 HASKCSAPGPG-----PCSLPNCRKMKRLLRHMATCKRGGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
 1052-1152 1.34e-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: 105.71  E-value: 1.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1052 ELRQALMPTLEALyRQDPESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYN 1131
Cdd:cd05509     1 PLYTQLKKVLDSL-KNHKSAWPFLEPVDKEE--APDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77

                          90       100
                  ....*....|....*....|.
gi 568992690 1132 RKTSRVYKYCSKLSEVFEQEI 1152
Cdd:cd05509    78 GPDTEYYKCANKLEKFFWKKL 98
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
 1066-1149 1.57e-25

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: 102.79  E-value: 1.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1066 RQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLS 1145
Cdd:cd05506    13 MKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELL 92


                  ....
gi 568992690 1146 EVFE 1149
Cdd:cd05506    93 KIFE 96
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 1744-1812 1.15e-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: 96.30  E-value: 1.15e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568992690  1744 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1812
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
RING_CBP-p300 pfam06001
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ...
 1155-1194 1.55e-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: 95.08  E-value: 1.55e-23
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 568992690  1155 VMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQ 1194
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1738-1816 2.35e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 95.89  E-value: 2.35e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   1738 DSRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPICKQLIalccYHAKHCQENKCPVP 1813
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76


                    ...
gi 568992690   1814 FCL 1816
Cdd:smart00551   77 KCV 79
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
 1060-1152 2.65e-23

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: 96.61  E-value: 2.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1060 TLEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYK 1139
Cdd:cd05500    12 SIRSLKRL-KDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQ 90

                          90
                  ....*....|...
gi 568992690 1140 YCSKLSEVFEQEI 1152
Cdd:cd05500    91 MGKRLQAAFEKHL 103
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
 1055-1154 2.88e-23

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: 96.34  E-value: 2.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1055 QALMPT-LEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRK 1133
Cdd:cd05497     7 QYLLKVvLKALWKH-KFAWPFQQPVDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKP 85

                          90       100
                  ....*....|....*....|.
gi 568992690 1134 TSRVYKYCSKLSEVFEQEIDP 1154
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 ...
 1070-1158 5.92e-22

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


Pssm-ID: 99928  Cd Length: 119  Bit Score: 93.29  E-value: 5.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1070 ESLPFRQPVDpqLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYN-RKTSRVYKYCSKLSEVF 1148
Cdd:cd05496    22 DSEPFRQPVD--LLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSALF 99

                          90
                  ....*....|
gi 568992690 1149 EQEIDPVMQS 1158
Cdd:cd05496   100 EEHIKKIISD 109
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
348-418 2.51e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 90.12  E-value: 2.51e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568992690    348 HAHKCQRREQangevrQCNLPHCRTMKNVLNHMTHCQSGKsCQVAHCASSRQIISHWKNCTRHDCPVCLPL 418
Cdd:smart00551   16 HARRCKAREA------KCQYPNCKTMKKLLRHMDSCKVRK-CKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
 1048-1150 3.32e-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: 3.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1048 FKPEELRQALMPTLEaLYRQDPeSLPFRQPVDPqllGIPDYFDIVKSPMDLSTIKRKLD---TGQYQEPWQYIDDIWLMF 1124
Cdd:cd05502     1 LSPIDQRKCERLLLE-LYCHEL-SLPFHEPVSP---SVPNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMF 75

                          90       100
                  ....*....|....*....|....*.
gi 568992690 1125 NNAWLYNRKTSRVYKYCSKLSEVFEQ 1150
Cdd:cd05502    76 KNCYKFNEEDSEVAQAGKELELFFEE 101
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
 1252-1286 1.59e-20

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


Pssm-ID: 277116  Cd Length: 40  Bit Score: 86.45  E-value: 1.59e-20
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568992690 1252 LFVECTECGRKMHQICVLHHEIIWPSGFVCDGCLK 1286
Cdd:cd15646     6 LFVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
 1073-1149 3.11e-20

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


Pssm-ID: 99931  Cd Length: 102  Bit Score: 87.73  E-value: 3.11e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568992690 1073 PFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFE 1149
Cdd:cd05499    23 PFLDPVDPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFN 99
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
 1051-1151 6.28e-20

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


Pssm-ID: 99936  Cd Length: 115  Bit Score: 87.45  E-value: 6.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1051 EELRQALMPTLEALYR------QDPESLPFRQPVdpQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMF 1124
Cdd:cd05504     4 SEGRHHGPLNLSALEQllveivKHKDSWPFLRPV--SKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVF 81

                          90       100
                  ....*....|....*....|....*..
gi 568992690 1125 NNAWLYNRKTSRVYKYCSKLSEVFEQE 1151
Cdd:cd05504    82 SNCFLYNPEHTSVYKAGTRLQRFFIKR 108
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 1067-1143 5.90e-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: 5.90e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568992690  1067 QDPESLPFRQPVDPqlLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSK 1143
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKAAEK 84
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
 1253-1284 6.44e-18

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


Pssm-ID: 277032  Cd Length: 37  Bit Score: 78.85  E-value: 6.44e-18
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568992690 1253 FVECTECGRKMHQICVLHHEIIWPSGFVCDGC 1284
Cdd:cd15557     6 FVECKECGRKWHQICVLHNDEIWPNGFICDNC 37
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
 1051-1141 1.46e-16

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


Pssm-ID: 99942 [Multi-domain]  Cd Length: 112  Bit Score: 77.48  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1051 EELRQALMPTLEALYRQDPESLPFRQPVDPQllGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLY 1130
Cdd:cd05510     6 EEFYESLDKVLNELKTYTEHSTPFLTKVSKR--EAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLY 83

                          90
                  ....*....|.
gi 568992690 1131 NRKTSRVYKYC 1141
Cdd:cd05510    84 NSDPSHPLRRH 94
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1673-1715 2.35e-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: 74.78  E-value: 2.35e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 568992690   1673 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCITCYNTKNHDHKME 1715
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
 1056-1146 9.41e-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: 74.74  E-value: 9.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1056 ALMPTLEALYRQDPESLpFRQPVDpqLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTS 1135
Cdd:cd05512     5 LLRKTLDQLQEKDTAEI-FSEPVD--LSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDT 81

                          90
                  ....*....|.
gi 568992690 1136 RVYKYCSKLSE 1146
Cdd:cd05512    82 IFYRAAVRLRD 92
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 1016-1156 1.19e-15

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 81.39  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1016 PELKTDGKEEEEQPStSATQSSPAPGQSKKK-------IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDY 1088
Cdd:COG5076   105 VFLAIESVTPESGLG-SLLMAHLKTSVKKRKtpkiedeLLYADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKRE--YPDY 181

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568992690 1089 FDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVM 1156
Cdd:COG5076   182 YEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
 1069-1149 1.40e-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: 74.33  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1069 PESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVF 1148
Cdd:cd05503    16 EDAWPFLEPVNTKL--VPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRKFF 93


                  .
gi 568992690 1149 E 1149
Cdd:cd05503    94 E 94
PHD_CBP cd15647
PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an ...
 1253-1286 1.46e-15

PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CBP is also known as CREBBP, since it specifically interacts with the phosphorylated form of cyclic adenosine monophosphate-responsive element-binding protein (CREB). It augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. CBP contains a cysteine-histidine rich region, a KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain.


Pssm-ID: 277117  Cd Length: 40  Bit Score: 72.32  E-value: 1.46e-15
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568992690 1253 FVECTECGRKMHQICVLHHEIIWPSGFVCDGCLK 1286
Cdd:cd15647     7 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 40
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 1673-1714 2.70e-15

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: 71.75  E-value: 2.70e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568992690  1673 DRFVYTCNECKH--HVETRWHCTVCEDYDLCITCYNTKN-HDHKM 1714
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQTHKgGNHQM 45
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
 1066-1151 8.52e-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: 72.68  E-value: 8.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1066 RQDPESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSR-------VY 1138
Cdd:cd05511    13 KNLPDSWPFHTPVNKKK--VPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVytkkakeML 90

                          90
                  ....*....|...
gi 568992690 1139 KYCSKLSEVFEQE 1151
Cdd:cd05511    91 ELAEELLAEREEK 103
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
 1067-1154 9.60e-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: 72.39  E-value: 9.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1067 QDPESLPFRQPVDPQllGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYN------RKTSRvYKY 1140
Cdd:cd05528    17 SDKRFNAFTKPVDEE--EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNpdrdpaDKLIR-SRA 93

                          90
                  ....*....|....*..
gi 568992690 1141 CSKLSEV---FEQEIDP 1154
Cdd:cd05528    94 CELRDEVhamIEAELDP 110
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 1677-1713 2.50e-14

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: 69.00  E-value: 2.50e-14
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568992690 1677 YTCNEC-KHHVETRWHCTVCEDYDLCITCYNTKNHDHK 1713
Cdd:cd02249     1 YSCDGClKPIVGVRYHCLVCEDFDLCSSCYAKGKKGHP 38
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
 1086-1139 7.37e-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: 69.64  E-value: 7.37e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568992690 1086 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYK 1139
Cdd:cd05515    37 PDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYK 90
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
 1054-1150 7.43e-14

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


Pssm-ID: 99939  Cd Length: 104  Bit Score: 69.70  E-value: 7.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1054 RQALMPTLEALYRQdPESLPFRQPVdpQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNR- 1132
Cdd:cd05507     5 KKAILLVYRTLASH-RYASVFLKPV--TEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNSs 81

                          90       100
                  ....*....|....*....|..
gi 568992690 1133 ----KTSRVYKYCSKLSEVFEQ 1150
Cdd:cd05507    82 dhdvYLMAVEMQREVMSQIQQL 103
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
 1086-1157 3.22e-13

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: 68.13  E-value: 3.22e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568992690 1086 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQ 1157
Cdd:cd05524    39 PEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDACKLWELFLSARNEVLS 110
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
 2061-2103 7.51e-13

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: 64.60  E-value: 7.51e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568992690 2061 ALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKY 2103
Cdd:cd20910     1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
 1049-1148 9.76e-13

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: 66.02  E-value: 9.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1049 KPEELRQALMPtlealYRqdpESLPFRQPVDPQllGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAW 1128
Cdd:cd05505     4 KCEEILSKILK-----YR---FSWPFREPVTAD--EAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAE 73

                          90       100
                  ....*....|....*....|
gi 568992690 1129 LYNRKTSRVYKYCSKLSEVF 1148
Cdd:cd05505    74 KYYENGSYVLSCMRKTEQCC 93
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
 1053-1144 8.06e-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: 8.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1053 LRQALMPTLEALYRQDPESLpFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNR 1132
Cdd:cd05513     2 LQKALEQLIRQLQRKDPHGF-FAFPVTDFI--APGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNK 78

                          90
                  ....*....|..
gi 568992690 1133 KTSRVYKYCSKL 1144
Cdd:cd05513    79 PDTIYYKAAKKL 90
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
 1052-1140 3.23e-11

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: 61.95  E-value: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1052 ELRQALMPTLEALYRQDPES----------LPFRQPvdpqllgIPDYFDIVKSPMDLSTIKRKLDtgQYQEPWQYIDDIW 1121
Cdd:cd05521     1 KLSKKLKPLYDGIYTLKEENgieihpifnvLPLRKD-------YPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLA 71

                          90
                  ....*....|....*....
gi 568992690 1122 LMFNNAWLYNRKTSRVYKY 1140
Cdd:cd05521    72 QIPWNARLYNTKGSVIYKY 90
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
 1209-1284 4.93e-11

PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar proteins; This family includes A. thaliana HACs (HAC1/2/4/5/12), which are histone acetyltransferases of the p300/CREB-binding protein (CBP) co-activator family. CBP-type HAT proteins are also found in animals, but absent in fungi. The domain architecture of CBP-type HAT proteins differs between plants and animals. Members in this family contain an N-terminal partially conserved KIX domain, a Zf-TAZ domain, a Cysteine rich CBP-type HAT domain that harbors a plant homeodomain (PHD) finger, a Zf-ZZ domain, and a Zf-TAZ domain. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.


Pssm-ID: 277086  Cd Length: 73  Bit Score: 60.44  E-value: 4.93e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568992690 1209 FCEKCFNEIQGESVSLGddpsqpQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPSG---FVCDGC 1284
Cdd:cd15614     1 WCSPCYNELKGENILIG------GVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNGRRNADEtaeYVCPLC 73
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
 1086-1144 1.55e-10

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: 59.95  E-value: 1.55e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568992690 1086 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKL 1144
Cdd:cd05522    38 PEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYKDAVLL 96
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
 1053-1152 1.57e-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: 60.05  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1053 LRQALMPTLEALYRQDPE-----SLPFRQPVDPQLLgiPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNA 1127
Cdd:cd05519     1 LKAAMLEIYDAVLNCEDEtgrklSELFLEKPSKKLY--PDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANA 78

                          90       100
                  ....*....|....*....|....*
gi 568992690 1128 WLYNRKTSRVYKYCSKLSEVFEQEI 1152
Cdd:cd05519    79 RTYNQEGSIVYEDAVEMEKAFKKKY 103
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
 1085-1153 1.66e-10

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: 60.13  E-value: 1.66e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568992690 1085 IPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEID 1153
Cdd:cd05516    37 LPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQ 105
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
 1086-1144 3.60e-10

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: 58.89  E-value: 3.60e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568992690 1086 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKL 1144
Cdd:cd05520    37 PDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKL 95
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
 1075-1138 9.19e-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: 57.84  E-value: 9.19e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568992690 1075 RQPVD-----PQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVY 1138
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 ...
 1051-1152 1.12e-08

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


Pssm-ID: 99958  Cd Length: 128  Bit Score: 55.42  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1051 EELRQALMPTLEALYRQDPESL--PFRQPVDpQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAW 1128
Cdd:cd05529    23 DEERERLISGLDKLLLSLQLEIaeYFEYPVD-LRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAE 101

                          90       100
                  ....*....|....*....|....
gi 568992690 1129 LYNRKTSRVYKYCSKLSEVFEQEI 1152
Cdd:cd05529   102 TFNEPNSEIAKKAKRLSDWLLRIL 125
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 98-328 1.39e-08

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: 60.41  E-value: 1.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690    98 GGPGQAMASQAQQNSPglslinsmvKSPMAQTGLTSPNMGIGSSGP--NQGPTQSPAGMMNSPVNQPAMGMNTGMNAGMN 175
Cdd:pfam09606  115 GGPGTASNLLASLGRP---------QMPMGGAGFPSQMSRVGRMQPggQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQA 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   176 PGML--AAGNGQGIMPNQV----MNGSIGAGRGRPNMQYPNAGMGnagsllTEPLQQGSPQ--MGGQPGLRGPQPLKMGM 247
Cdd:pfam09606  186 GGMNggQQGPMGGQMPPQMgvpgMPGPADAGAQMGQQAQANGGMN------PQQMGGAPNQvaMQQQQPQQQGQQSQLGM 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   248 -MNNPSPYGSPYTQNSGQQIGASGLGLQIQTKTVLPNNLSP---------FAMDKKAVPGGGMPSMGQ-QPTPSVQQPGL 316
Cdd:pfam09606  260 gINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIgdqnnyqqqQTRQQQQQQGGNHPAAHQqQMNQSVGQGGQ 339

                          250
                   ....*....|..
gi 568992690   317 VTPVAAGMGSGA 328
Cdd:pfam09606  340 VVALGGLNHLET 351
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
 1086-1150 4.92e-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: 53.16  E-value: 4.92e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568992690 1086 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQ 1150
Cdd:cd05525    39 PDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSPIGRDVCRLRKAYYQ 103
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 1678-1717 4.94e-08

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: 51.11  E-value: 4.94e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568992690 1678 TCNECKHHVE-TRWHCTVCEDYDLCITCYNTKNH-DHKMEKL 1717
Cdd:cd02340     2 ICDGCQGPIVgVRYKCLVCPDYDLCESCEAKGVHpEHAMLKI 43
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 1968-2375 5.95e-08

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: 58.10  E-value: 5.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1968 PQMSPMAPMGMNPPPMARGPGGHLDPGIGPAGmQQQPPWAQGGMPQPQQ----MQSGMPRPAMMSVAQHGQPLNMAPQPG 2043
Cdd:pfam09606   97 QMMGPMGPGPGGPMGQQMGGPGTASNLLASLG-RPQMPMGGAGFPSQMSrvgrMQPGGQAGGMMQPSSGQPGSGTPNQMG 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2044 LGQVGVSPLKPGTVSQQALQNLLRtlrspsSPLQQQQVLSILHANPQllaafikQRAAKYANPNPQPLPGQPGMTQGQ-P 2122
Cdd:pfam09606  176 PNGGPGQGQAGGMNGGQQGPMGGQ------MPPQMGVPGMPGPADAG-------AQMGQQAQANGGMNPQQMGGAPNQvA 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2123 GLQPPTMPGQQGVHSNPALQNMNPLQAGVQRAGLPQQQPQQqlqppMGAMSPQAQQM--NMNHNTMPSQFRDILRRQMMQ 2200
Cdd:pfam09606  243 MQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQP-----MGPPGQQPGAMpnVMSIGDQNNYQQQQTRQQQQQ 317

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2201 QQGAGPGIGPGMANQFQQPQGigyppqqqqqqrmqhhmqqMQQGNMGQMGQLPQALGAEAGASLQAYQQRllQQQMGSPA 2280
Cdd:pfam09606  318 QGGNHPAAHQQQMNQSVGQGG-------------------QVVALGGLNHLETWNPGNFGGLGANPMQRG--QPGMMSSP 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2281 QPNPMSPQQHMLPNQ----AQSPHLQGQQIPNSLSNQVRSPQPVPSPRpqsqpphsspsprMQPQPSPH-HVSPQTSSPH 2355
Cdd:pfam09606  377 SPVPGQQVRQVTPNQfmrqSPQPSVPSPQGPGSQPPQSHPGGMIPSPA-------------LIPSPSPQmSQQPAQQRTI 443

                          410       420
                   ....*....|....*....|
gi 568992690  2356 PGLVAAQAANPMEQGHFASP 2375
Cdd:pfam09606  444 GQDSPGGSLNTPGQSAVNSP 463
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
 1086-1150 5.32e-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: 50.13  E-value: 5.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568992690 1086 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQ 1150
Cdd:cd05517    37 PDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGSQVYKDANAIKKIFTA 101
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 1679-1711 8.21e-07

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: 47.45  E-value: 8.21e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568992690 1679 CNECKHH--VETRWHCTVCEDYDLCITCYNTKNHD 1711
Cdd:cd02339     3 CDTCRKQgiIGIRWKCAECPNYDLCTTCYHGDKHD 37
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 1910-2145 2.24e-06

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 53.12  E-value: 2.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1910 GKAPGQVTPPTPPQTAQAPLPGPPPAA--------VEMAM--QIQRAAETQRQMAHVQIFQRPIQHQMP--QMSPMAPMG 1977
Cdd:pfam09770  164 GVAPKKAAAPAPAPQPAAQPASLPAPSrkmmsleeVEAAMraQAKKPAQQPAPAPAQPPAAPPAQQAQQqqQFPPQIQQQ 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1978 MNPPPMARGPGGHLDPGIGPAGMQQqppwaqggmPQPQQMQSGMPRPAMMSVAQHGQPLNMAPQPglgqvgvsplkpgtv 2057
Cdd:pfam09770  244 QQPQQQPQQPQQHPGQGHPVTILQR---------PQSPQPDPAQPSIQPQAQQFHQQPPPVPVQP--------------- 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2058 sQQALQnllrtlrspssplqqqqvlsilhaNPQLLAAfIKQRAAKYANPNPQPLPGQPGmtqgqpGLQPPTMPGQQGVHS 2137
Cdd:pfam09770  300 -TQILQ------------------------NPNRLSA-ARVGYPQNPQPGVQPAPAHQA------HRQQGSFGRQAPIIT 347


                   ....*....
gi 568992690  2138 NPA-LQNMN 2145
Cdd:pfam09770  348 HPQqLAQLS 356
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
 1085-1150 2.58e-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: 48.19  E-value: 2.58e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568992690 1085 IPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVyKYCSKLSEVFEQ 1150
Cdd:cd05501    30 IRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDDDFG-QVGITLEKKFEK 94
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
 1051-1108 8.26e-06

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: 47.05  E-value: 8.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568992690 1051 EELRQALMPtLEALYRQDPeSLPFRQPVDPQLLGIPDYFDIVKSPMDLSTI-KRKLDTG 1108
Cdd:cd05494     3 EALERVLRE-LKRHRRNED-AWPFLEPVNPPRRGAPDYRDVIKRPMSFGTKvNNIVETG 59
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 1890-2209 1.94e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.01  E-value: 1.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1890 PPNNMTPYLPRTQTTGPVSQGKAPGQVTPPTPPQTAQAPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPQ 1969
Cdd:pfam09606  170 TPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQ 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1970 MSP-MAPMGMNPPPMARGPGGhlDPGIGPAGMQQQPpwaqggMPQPQQMQSGMprPAMMSVAQHGQPLNMAPQPGLGQVG 2048
Cdd:pfam09606  250 QQGqQSQLGMGINQMQQMPQG--VGGGAGQGGPGQP------MGPPGQQPGAM--PNVMSIGDQNNYQQQQTRQQQQQQG 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2049 VSplkpgtvSQQALQNllrtlrSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANPNPQPLPGQPGMTQGQPGLQPPT 2128
Cdd:pfam09606  320 GN-------HPAAHQQ------QMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQ 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  2129 MPGQQGVHSNPALQNMNPLQAGVQraglpqqqpqqQLQPPMGAMSPQAQQMNMNHNTMPSQfrdILRRQMMQQQGAGPGI 2208
Cdd:pfam09606  387 VTPNQFMRQSPQPSVPSPQGPGSQ-----------PPQSHPGGMIPSPALIPSPSPQMSQQ---PAQQRTIGQDSPGGSL 452


                   .
gi 568992690  2209 G 2209
Cdd:pfam09606  453 N 453
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 1948-2089 2.16e-05

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: 49.81  E-value: 2.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1948 ETQRQMAHVQIFQRpiQHQMPQMSPMAPM-GMNPPPMARGPGGHldpgigpAGMQQQPPWAQGGMPQPQQMQSGMPRPAM 2026
Cdd:TIGR01628  365 EQRRAHLQDQFMQL--QPRMRQLPMGSPMgGAMGQPPYYGQGPQ-------QQFNGQPLGWPRMSMMPTPMGPGGPLRPN 435

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568992690  2027 MSV--AQHGQPLNMApQPGLGQVGVSPLK--PGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANP 2089
Cdd:TIGR01628  436 GLApmNAVRAPSRNA-QNAAQKPPMQPVMypPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASAT 501
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 1677-1716 2.99e-05

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: 43.19  E-value: 2.99e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568992690 1677 YTCNECKHH--VETRWHCTVC--EDYDLCITC-YNTKNH--DHKMEK 1716
Cdd:cd02341     1 FKCDSCGIEpiPGTRYHCSECddGDFDLCQDCvVKGESHqeDHWLVK 47
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
 1051-1152 6.15e-05

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: 43.91  E-value: 6.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 1051 EELRQALMPTLEALYRqdPESLPFRQPVDpqLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLY 1130
Cdd:cd05508     2 DQLSKLLKFALERMKQ--PGAEPFLKPVD--LEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIY 77

                          90       100
                  ....*....|....*....|..
gi 568992690 1131 NRKTSRVYKYCSKLSEVFEQEI 1152
Cdd:cd05508    78 NGGDHKLTQAAKAIVKICEQEM 99
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 663-836 7.40e-05

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 48.08  E-value: 7.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   663 PGMGPVPMNTGSNMGQQPTGMTT------------------NGPVPDPSMIRGSVPNHMMPRMTPQPGLNQFGQMNMPQP 724
Cdd:pfam09606   97 QMMGPMGPGPGGPMGQQMGGPGTasnllaslgrpqmpmggaGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGP 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   725 PIGPRQP-SPLQHHGQLAQSGSLNPP-MGYGPRMQQASGQNQFLSQTQFTSqGMNVTNMPLAPS----SGQAPVSQAQMS 798
Cdd:pfam09606  177 NGGPGQGqAGGMNGGQQGPMGGQMPPqMGVPGMPGPADAGAQMGQQAQANG-GMNPQQMGGAPNqvamQQQQPQQQGQQS 255

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 568992690   799 SSSCPVNSPI-MPPGSQGSHIH-CPTLPQQAHQNSPSPVP 836
Cdd:pfam09606  256 QLGMGINQMQqMPQGVGGGAGQgGPGQPMGPPGQQPGAMP 295
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 647-797 3.27e-04

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 45.95  E-value: 3.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   647 EKRRTRLQKQNMlPNAPGM--GPVPMNTGSNMGQQPTGMttngpvPDPSMIRGSVP---NHMMPRMTPQpglnqfgQMNM 721
Cdd:TIGR01628  365 EQRRAHLQDQFM-QLQPRMrqLPMGSPMGGAMGQPPYYG------QGPQQQFNGQPlgwPRMSMMPTPM-------GPGG 430

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568992690   722 PQPPIGPRQPSPLQHHGQLAQSGSLNPPMGYGPRMQQASGQNQFLSQTQFTSQGMNVTNMPLAPSSGQA--PVSQAQM 797
Cdd:TIGR01628  431 PLRPNGLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASatPQMQKQV 508
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 1677-1705 4.31e-04

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: 39.97  E-value: 4.31e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568992690 1677 YTCNECKHHV--ETRWHCTVCEDYDLCITCY 1705
Cdd:cd02335     1 YHCDYCSKDItgTIRIKCAECPDFDLCLECF 31
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 1941-2082 5.32e-04

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 45.18  E-value: 5.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1941 MQIQRAAETQRQMAHVQifQRPIQH--QMPQMSPMAPMGMNPPpmargpgghldPGIGPAGMQQQPPWAQGGMPQPQQMq 2018
Cdd:TIGR01628  394 AMGQPPYYGQGPQQQFN--GQPLGWprMSMMPTPMGPGGPLRP-----------NGLAPMNAVRAPSRNAQNAAQKPPM- 459

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568992690  2019 sgMPRPAMMSVAQHGQPLNMaPQPglgQVGVSPLKPGTVSQQALQNLlrtlrspsSPLQQQQVL 2082
Cdd:TIGR01628  460 --QPVMYPPNYQSLPLSQDL-PQP---QSTASQGGQNKKLAQVLASA--------TPQMQKQVL 509
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 1678-1714 2.17e-03

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: 37.95  E-value: 2.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568992690 1678 TCNECK--HHVETRWHCTVCEDYDLCITCY----NTKNHD--HKM 1714
Cdd:cd02345     2 SCSACRkqDISGIRFPCQVCRDYSLCLGCYtkgrETKRHNslHIM 46
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 2252-2369 2.34e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.54  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690 2252 LPQALGAEAGASLQAYQQRLL----QQQMGSPAQPNPmSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPvpsprpqs 2327
Cdd:PRK10263  750 EPVQQPQQPVAPQQQYQQPQQpvapQPQYQQPQQPVA-PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP-------- 820

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568992690 2328 QPPHSSPSPRMQPQPSPHHvSPQTSSPHPGLVAAQAANPMEQ 2369
Cdd:PRK10263  821 QQPVAPQPQYQQPQQPVAP-QPQDTLLHPLLMRNGDSRPLHK 861
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 677-848 2.41e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.22  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   677 GQQPTGMTTNGPVPDPSMIRGSVPNHMMPRMTPQPgLNQFGQMNMPQPPigPRQPSPLQHHGQLAQSGSLNPPmgygprm 756
Cdd:pfam03154  380 GPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPP-LQLMPQSQQLPPP--PAQPPVLTQSQSLPPPAASHPP------- 449

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   757 qqASGQNQFLSQTQFTSQG-MNVTNMPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPTLPQQAH------- 828
Cdd:pfam03154  450 --TSGLHQVPSQSPFPQHPfVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKeealdea 527

                          170       180
                   ....*....|....*....|....*....
gi 568992690   829 ---------QNSPSPVPSRTPTPHHTPPS 848
Cdd:pfam03154  528 eepesppppPRSPSPEPTVVNTPSHASQS 556
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 1678-1715 2.47e-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: 38.10  E-value: 2.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 568992690 1678 TCNECKHHVET--RWHCTVCEDYDLCITCYNTKN----H--DHKME 1715
Cdd:cd02338     2 SCDGCGKSNFTgrRYKCLICYDYDLCADCYDSGVtterHlfDHPMQ 47
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 1678-1713 3.78e-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: 37.18  E-value: 3.78e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568992690 1678 TCNECKHH--VETRWHCTVCEDYDLCITCYNTKNHDHK 1713
Cdd:cd02344     2 TCDGCQMFpiNGPRFKCRNCDDFDFCENCFKTRKHNTR 39
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 1836-2101 5.66e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 41.95  E-value: 5.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1836 MLRRRMASMQRTGVAGQQQGLPSPTPATPTTPTGQqpatpqtpqpqptsqpqptppnnmTPYLP-RT-----QTTGPVSQ 1909
Cdd:pfam09770  100 VRFNRQQPAARAAQSSAQPPASSLPQYQYASQQSQ------------------------QPSKPvRTgyekyKEPEPIPD 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1910 --------GKAPGQVTPPTPPQTAQAPLPGPPPAA--------VEMAM--QIQRAAETQRQMAHVQIFQRPIQHQMP--Q 1969
Cdd:pfam09770  156 lqvdaslwGVAPKKAAAPAPAPQPAAQPASLPAPSrkmmsleeVEAAMraQAKKPAQQPAPAPAQPPAAPPAQQAQQqqQ 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690  1970 MSPMAPMGMNPPPMARGPGGHLDPGIGPAGMQ----QQPPWAQGGMPQPQQMQSGMPRPAMMSVAQHGQPLNMAPQPGLG 2045
Cdd:pfam09770  236 FPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQrpqsPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQILQNPNRLSAARVG 315

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568992690  2046 QVGVSPLKPGTVSQQALQnllrtlRSPSSPLQQQQVlsILHAnPQLLAAFIKQRAA 2101
Cdd:pfam09770  316 YPQNPQPGVQPAPAHQAH------RQQGSFGRQAPI--ITHP-QQLAQLSEEEKAA 362
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 705-844 6.16e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 41.95  E-value: 6.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992690   705 PRMTPQPGLNQFGQMNMPQPPIGPRQPSPLQHHGQLAQSGSLNPPMGYGPRMQQASGQnqflsQTQFTSQGMNVTNMPLA 784
Cdd:pfam09770  218 PAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPD-----PAQPSIQPQAQQFHQQP 292

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568992690   785 PSSGQAPVSQAQ---MSSSSCPVNSPIMPPGSQGSHIHcptlPQQAHQNSPSPVPSRTPTPHH 844
Cdd:pfam09770  293 PPVPVQPTQILQnpnRLSAARVGYPQNPQPGVQPAPAH----QAHRQQGSFGRQAPIITHPQQ 351
 
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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