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Conserved domains on  [gi|1958792898|ref|XP_038936215|]
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histone acetyltransferase p300 isoform X1 [Rattus norvegicus]

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 ...
1304-1610 2.70e-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: 318.57  E-value: 2.70e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1304 VNDFLRRQNhPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEmaESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDC 1383
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1384 PPPNQRRVYISYLDSVHFFRPKcLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1458
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1459 KRLQEWYKKMLDKAVSE-------RIVHDYKDILKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1513
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1514 SIKELEQEEEE----------------------RKREENTSNESTDVTKGDskNAKKKNNKKTSKNKSSLSRGNKKKPGV 1571
Cdd:pfam08214  234 LIKEGRWKSVSldqfweelrfrqefslgrlvgfIGLEGDYTPGSDDVINPP--GLVKSKKQYKMIKSYITGREYSTEEGA 311
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1958792898 1572 PNVSNDLSQKLYATMEKHkevFFVIRLIACPAPNSLPPI 1610
Cdd:pfam08214  312 PESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1049-1156 1.01e-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: 249.28  E-value: 1.01e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1049 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWL 1128
Cdd:cd05495      1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                           90       100
                   ....*....|....*....|....*...
gi 1958792898 1129 YNRKTSRVYKYCSKLSEVFEQEIDPVMQ 1156
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 7.61e-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: 7.61e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  567 GIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELE 646
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 1958792898  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 ...
1989-2095 9.56e-35

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: 129.57  E-value: 9.56e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1989 QPPWAQGGMPQPQ--QMQSGMPRPAMMSVAQ-HGQPLNMAPQPGLGQV-GVSPLKPGTVSQQALQNLLRTLRSPSSPLQQ 2064
Cdd:pfam09030    1 QPQWAQGQWQQQQplQQMQGMQRPMMPQQQQqQMPGMNPPQQPGLPQVpGQQPGRPGSIAPNALQDLLRTLKSPSSPQQQ 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958792898 2065 QQVLSILHANPQLLAAFIKQRAAKYANSNPQ 2095
Cdd:pfam09030   81 QQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1168-1240 1.82e-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: 121.63  E-value: 1.82e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958792898 1168 FSPQTLCCYGKqlCTIPRD--ATYYSYQ---NRYHFCEKCFNEIQGESVSLGDDpsqPQTTINKEQFSKRKNDTLDPE 1240
Cdd:cd15802      1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1666-1706 2.75e-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: 2.75e-28
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958792898 1666 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKL 1706
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 3.60e-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: 109.01  E-value: 3.60e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958792898  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 ...
1733-1801 1.35e-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: 1.35e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958792898 1733 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1801
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpgpCSLPNCRKMKRLLRHMATCKR--GGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
PHD_p300 cd15646
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ...
1241-1275 2.79e-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: 85.68  E-value: 2.79e-20
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958792898 1241 LFVECTECGRKMHQICVLHHEVIWPSGFVCDGCLK 1275
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 ...
1956-2335 1.09e-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: 60.79  E-value: 1.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1956 MAPMAPMGMNPPPMARGPGGHLDPGMGPAGmQQQPPWAQGGMPQPQQ----MQSGMPRPAMMSVAQHGQPLNMAPQPGLG 2031
Cdd:pfam09606   99 MGPMGPGPGGPMGQQMGGPGTASNLLASLG-RPQMPMGGAGFPSQMSrvgrMQPGGQAGGMMQPSSGQPGSGTPNQMGPN 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2032 QVGVSPLKPGTVSQQalqnllrtlrspSSPLQQQQvlsilhanPQLLAAFIKQRAAKYANSNPQPLPGQPGMPQGQPGLQ 2111
Cdd:pfam09606  178 GGPGQGQAGGMNGGQ------------QGPMGGQM--------PPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGA 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2112 PPTMPGQQgvhsNPALQNMNPMQAG-----VQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQMMQ 2186
Cdd:pfam09606  238 PNQVAMQQ----QQPQQQGQQSQLGmginqMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQ 313
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2187 QQGAGPGIGPGmANHNQFQQPQGIGYPPQQQQQQQQQRMQHHMQQMQQGNMGQMGQLPQALGAEAGASLQAYQQRLLQQQ 2266
Cdd:pfam09606  314 QQQQQGGNHPA-AHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQF 392
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958792898 2267 MGSPAQPNPMSPQQhmlPNQAQSPHLQGQQIPNSLSNQVRSPQPvpsprpqsqpPHSSPSPRMQPQPSP 2335
Cdd:pfam09606  393 MRQSPQPSVPSPQG---PGSQPPQSHPGGMIPSPALIPSPSPQM----------SQQPAQQRTIGQDSP 448
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
88-323 1.33e-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: 1.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898   88 GSSPNLNMGVG-GPGQVMASQAQQNSPGLSLINSMVKSPMAQTGLTSPNMGMGSSGPNQGptQSTAGMMNSPVNQP---- 162
Cdd:pfam09606   93 GTRPQMMGPMGpGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPG--GQAGGMMQPSSGQPgsgt 170
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  163 --AMGMNTGMNAGMNPGML--AAGNGQGIMPNQV----MNGSIGAGRGRPNMQYPNAGMGnagsllTEPLQQGSPQ--MG 232
Cdd:pfam09606  171 pnQMGPNGGPGQGQAGGMNggQQGPMGGQMPPQMgvpgMPGPADAGAQMGQQAQANGGMN------PQQMGGAPNQvaMQ 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  233 GQPGLRGPQSHKMGMMSN-PTPYGSPYTQNSGQQIGASGLGLQIQTKTVLPNNLSPFAMDKKAVTGGGMPNMGQQPTPSV 311
Cdd:pfam09606  245 QQQPQQQGQQSQLGMGINqMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA 324
                          250
                   ....*....|...
gi 1958792898  312 QQPGLVN-PVAPG 323
Cdd:pfam09606  325 AHQQQMNqSVGQG 337
PABP-1234 super family cl31127
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
647-797 1.76e-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.


The actual alignment was detected with superfamily member TIGR01628:

Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 50.19  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  647 EKRRTRLQKQNMLPSAPG-MVPVPMNTAPNMGQQPTGMttngplPDPSMIRGSVPnQMMPRMTPQPGLnqfGQMNIPQPP 725
Cdd:TIGR01628  365 EQRRAHLQDQFMQLQPRMrQLPMGSPMGGAMGQPPYYG------QGPQQQFNGQP-LGWPRMSMMPTP---MGPGGPLRP 434
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958792898  726 IGPRQPSPLQHHGQLAQSGSLNPPMGYGPRMQQTSGQNQFLSQTQFPSQGMNVTNMPLAPSS--SQAPVSQAQM 797
Cdd:TIGR01628  435 NGLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVlaSATPQMQKQV 508
PHA03247 super family cl33720
large tegument protein UL36; Provisional
659-1075 2.26e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 2.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  659 LPSAPGMVPVPMNTAPNMGQQPTGMTTNGPLPDPSMIRGSVP--NQMMPRMTPQPGlnqfgqmniPQPP----IGPRQPS 732
Cdd:PHA03247  2560 PPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPvdDRGDPRGPAPPS---------PLPPdthaPDPPPPS 2630
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  733 PLQHHGQLAQSGSLNPPMGYGPRMQQTSGQNQFLSQTQFPSQGMNVTNMPLAPSSSQAPVSQAQMSSSSCPVNSPIMP-- 810
Cdd:PHA03247  2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPep 2710
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  811 -PGSQGSHIHCPTLPQQAHQNSP----SPVPSRTPTPHHTPPSIGTQ-QPAATAIPAPVPTPPAMPPGAQPQSLRPPSRQ 884
Cdd:PHA03247  2711 aPHALVSATPLPPGPAAARQASPalpaAPAPPAVPAGPATPGGPARPaRPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  885 TPTPPTHLPPQVQPSLPVPPADQSQPQPRSQQSTAASVPTPTAPLLPPQPPTPL-SQPAVSVEGQVS-------NPPS-- 954
Cdd:PHA03247  2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGpPPPSLPLGGSVApggdvrrRPPSrs 2870
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  955 -----TSSTEVNSQTIPEKQPSQEVKmevkmdvDQPEPADAQPDDTKEAKAEDGKVEPTETEERGPELKTEVKEEEDQPS 1029
Cdd:PHA03247  2871 paakpAAPARPPVRRLARPAVSRSTE-------SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPL 2943
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1958792898 1030 TSAAQSSPAPGQSKKkifKPEELRQALMPTLEALYR-QDPESLPFRQ 1075
Cdd:PHA03247  2944 APTTDPAGAGEPSGA---VPQPWLGALVPGRVAVPRfRVPQPAPSRE 2987
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1304-1610 2.70e-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: 318.57  E-value: 2.70e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1304 VNDFLRRQNhPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEmaESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDC 1383
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1384 PPPNQRRVYISYLDSVHFFRPKcLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1458
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1459 KRLQEWYKKMLDKAVSE-------RIVHDYKDILKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1513
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1514 SIKELEQEEEE----------------------RKREENTSNESTDVTKGDskNAKKKNNKKTSKNKSSLSRGNKKKPGV 1571
Cdd:pfam08214  234 LIKEGRWKSVSldqfweelrfrqefslgrlvgfIGLEGDYTPGSDDVINPP--GLVKSKKQYKMIKSYITGREYSTEEGA 311
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1958792898 1572 PNVSNDLSQKLYATMEKHkevFFVIRLIACPAPNSLPPI 1610
Cdd:pfam08214  312 PESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1049-1156 1.01e-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: 249.28  E-value: 1.01e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1049 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWL 1128
Cdd:cd05495      1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                           90       100
                   ....*....|....*....|....*...
gi 1958792898 1129 YNRKTSRVYKYCSKLSEVFEQEIDPVMQ 1156
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 7.61e-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: 7.61e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  567 GIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELE 646
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 1958792898  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 ...
1989-2095 9.56e-35

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: 129.57  E-value: 9.56e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1989 QPPWAQGGMPQPQ--QMQSGMPRPAMMSVAQ-HGQPLNMAPQPGLGQV-GVSPLKPGTVSQQALQNLLRTLRSPSSPLQQ 2064
Cdd:pfam09030    1 QPQWAQGQWQQQQplQQMQGMQRPMMPQQQQqQMPGMNPPQQPGLPQVpGQQPGRPGSIAPNALQDLLRTLKSPSSPQQQ 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958792898 2065 QQVLSILHANPQLLAAFIKQRAAKYANSNPQ 2095
Cdd:pfam09030   81 QQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
BROMO smart00297
bromo domain;
1046-1154 1.20e-33

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 126.24  E-value: 1.20e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  1046 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNN 1125
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 1958792898  1126 AWLYNRKTSRVYKYCSKLSEVFEQEIDPV 1154
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1168-1240 1.82e-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: 121.63  E-value: 1.82e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958792898 1168 FSPQTLCCYGKqlCTIPRD--ATYYSYQ---NRYHFCEKCFNEIQGESVSLGDDpsqPQTTINKEQFSKRKNDTLDPE 1240
Cdd:cd15802      1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1666-1706 2.75e-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: 2.75e-28
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958792898 1666 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKL 1706
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 3.60e-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: 109.01  E-value: 3.60e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958792898  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 ...
1733-1801 1.35e-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: 1.35e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958792898 1733 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1801
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 ...
1154-1193 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 1958792898 1154 VMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQ 1193
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1727-1805 2.74e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 95.51  E-value: 2.74e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  1727 DSRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPICKQLIalccYHAKHCQENKCPVP 1802
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 1958792898  1803 FCL 1805
Cdd:smart00551   77 KCV 79
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
348-418 3.01e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 89.73  E-value: 3.01e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958792898   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 ...
1241-1275 2.79e-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: 85.68  E-value: 2.79e-20
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958792898 1241 LFVECTECGRKMHQICVLHHEVIWPSGFVCDGCLK 1275
Cdd:cd15646      6 LFVECLECGRKMHQICVLHNETIWPSGFVCEGCLK 40
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1066-1142 5.88e-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: 5.88e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958792898 1066 QDPESLPFRQPVDPqlLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSK 1142
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKAAEK 84
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1008-1155 1.78e-16

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 83.70  E-value: 1.78e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1008 TETEERGPELKTEVKEEEDQP--STSAAQSSPAPgqskkkifkPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIP 1085
Cdd:COG5076    111 SVTPESGLGSLLMAHLKTSVKkrKTPKIEDELLY---------ADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKRE--YP 179
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1086 DYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVM 1155
Cdd:COG5076    180 DYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1662-1704 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 1958792898  1662 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCITCYNTKNHDHKME 1704
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1662-1703 3.06e-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: 71.36  E-value: 3.06e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958792898 1662 DRFVYTCNECKH--HVETRWHCTVCEDYDLCITCYNTKN-HDHKM 1703
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQTHKgGNHQM 45
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
2047-2089 7.27e-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: 7.27e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958792898 2047 ALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKY 2089
Cdd:cd20910      1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1956-2335 1.09e-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: 60.79  E-value: 1.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1956 MAPMAPMGMNPPPMARGPGGHLDPGMGPAGmQQQPPWAQGGMPQPQQ----MQSGMPRPAMMSVAQHGQPLNMAPQPGLG 2031
Cdd:pfam09606   99 MGPMGPGPGGPMGQQMGGPGTASNLLASLG-RPQMPMGGAGFPSQMSrvgrMQPGGQAGGMMQPSSGQPGSGTPNQMGPN 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2032 QVGVSPLKPGTVSQQalqnllrtlrspSSPLQQQQvlsilhanPQLLAAFIKQRAAKYANSNPQPLPGQPGMPQGQPGLQ 2111
Cdd:pfam09606  178 GGPGQGQAGGMNGGQ------------QGPMGGQM--------PPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGA 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2112 PPTMPGQQgvhsNPALQNMNPMQAG-----VQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQMMQ 2186
Cdd:pfam09606  238 PNQVAMQQ----QQPQQQGQQSQLGmginqMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQ 313
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2187 QQGAGPGIGPGmANHNQFQQPQGIGYPPQQQQQQQQQRMQHHMQQMQQGNMGQMGQLPQALGAEAGASLQAYQQRLLQQQ 2266
Cdd:pfam09606  314 QQQQQGGNHPA-AHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQF 392
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958792898 2267 MGSPAQPNPMSPQQhmlPNQAQSPHLQGQQIPNSLSNQVRSPQPvpsprpqsqpPHSSPSPRMQPQPSP 2335
Cdd:pfam09606  393 MRQSPQPSVPSPQG---PGSQPPQSHPGGMIPSPALIPSPSPQM----------SQQPAQQRTIGQDSP 448
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
88-323 1.33e-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: 1.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898   88 GSSPNLNMGVG-GPGQVMASQAQQNSPGLSLINSMVKSPMAQTGLTSPNMGMGSSGPNQGptQSTAGMMNSPVNQP---- 162
Cdd:pfam09606   93 GTRPQMMGPMGpGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPG--GQAGGMMQPSSGQPgsgt 170
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  163 --AMGMNTGMNAGMNPGML--AAGNGQGIMPNQV----MNGSIGAGRGRPNMQYPNAGMGnagsllTEPLQQGSPQ--MG 232
Cdd:pfam09606  171 pnQMGPNGGPGQGQAGGMNggQQGPMGGQMPPQMgvpgMPGPADAGAQMGQQAQANGGMN------PQQMGGAPNQvaMQ 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  233 GQPGLRGPQSHKMGMMSN-PTPYGSPYTQNSGQQIGASGLGLQIQTKTVLPNNLSPFAMDKKAVTGGGMPNMGQQPTPSV 311
Cdd:pfam09606  245 QQQPQQQGQQSQLGMGINqMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA 324
                          250
                   ....*....|...
gi 1958792898  312 QQPGLVN-PVAPG 323
Cdd:pfam09606  325 AHQQQMNqSVGQG 337
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
647-797 1.76e-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: 50.19  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  647 EKRRTRLQKQNMLPSAPG-MVPVPMNTAPNMGQQPTGMttngplPDPSMIRGSVPnQMMPRMTPQPGLnqfGQMNIPQPP 725
Cdd:TIGR01628  365 EQRRAHLQDQFMQLQPRMrQLPMGSPMGGAMGQPPYYG------QGPQQQFNGQP-LGWPRMSMMPTP---MGPGGPLRP 434
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958792898  726 IGPRQPSPLQHHGQLAQSGSLNPPMGYGPRMQQTSGQNQFLSQTQFPSQGMNVTNMPLAPSS--SQAPVSQAQM 797
Cdd:TIGR01628  435 NGLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVlaSATPQMQKQV 508
PHA03247 PHA03247
large tegument protein UL36; Provisional
659-1075 2.26e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 2.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  659 LPSAPGMVPVPMNTAPNMGQQPTGMTTNGPLPDPSMIRGSVP--NQMMPRMTPQPGlnqfgqmniPQPP----IGPRQPS 732
Cdd:PHA03247  2560 PPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPvdDRGDPRGPAPPS---------PLPPdthaPDPPPPS 2630
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  733 PLQHHGQLAQSGSLNPPMGYGPRMQQTSGQNQFLSQTQFPSQGMNVTNMPLAPSSSQAPVSQAQMSSSSCPVNSPIMP-- 810
Cdd:PHA03247  2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPep 2710
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  811 -PGSQGSHIHCPTLPQQAHQNSP----SPVPSRTPTPHHTPPSIGTQ-QPAATAIPAPVPTPPAMPPGAQPQSLRPPSRQ 884
Cdd:PHA03247  2711 aPHALVSATPLPPGPAAARQASPalpaAPAPPAVPAGPATPGGPARPaRPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  885 TPTPPTHLPPQVQPSLPVPPADQSQPQPRSQQSTAASVPTPTAPLLPPQPPTPL-SQPAVSVEGQVS-------NPPS-- 954
Cdd:PHA03247  2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGpPPPSLPLGGSVApggdvrrRPPSrs 2870
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  955 -----TSSTEVNSQTIPEKQPSQEVKmevkmdvDQPEPADAQPDDTKEAKAEDGKVEPTETEERGPELKTEVKEEEDQPS 1029
Cdd:PHA03247  2871 paakpAAPARPPVRRLARPAVSRSTE-------SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPL 2943
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1958792898 1030 TSAAQSSPAPGQSKKkifKPEELRQALMPTLEALYR-QDPESLPFRQ 1075
Cdd:PHA03247  2944 APTTDPAGAGEPSGA---VPQPWLGALVPGRVAVPRfRVPQPAPSRE 2987
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
642-1032 1.64e-04

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: 47.07  E-value: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  642 QKELEEKRRTRLQKQNMLPSAPGMvPVPMNTAPNMGQQPTGMTTNGPLPDPSMirGSVPNQMMPRMTPQPGLNQFGQMNI 721
Cdd:pfam03154  163 QQQILQTQPPVLQAQSGAASPPSP-PPPGTTQAATAGPTPSAPSVPPQGSPAT--SQPPNQTQSTAAPHTLIQQTPTLHP 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  722 -----PQPPIGP--RQPSPLQHHGQLAQSGSLN---PPMGY----GPRMQQTSGQNQFLSQTQFPSQGmnvtNMPLAPSS 787
Cdd:pfam03154  240 qrlpsPHPPLQPmtQPPPPSQVSPQPLPQPSLHgqmPPMPHslqtGPSHMQHPVPPQPFPLTPQSSQS----QVPPGPSP 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  788 ---------SQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPT---LPQ----QAHQNSP---SPVPSRTPTPHHTPPS 848
Cdd:pfam03154  316 aapgqsqqrIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPttpIPQlpnpQSHKHPPhlsGPSPFQMNSNLPPPPA 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  849 IGTQQPAATAipapvptppamppgaQPQSLRPPSRQTPtppthlpPQVQPSLPVPPADQSQPQPRSQQSTAASVPTPTAP 928
Cdd:pfam03154  396 LKPLSSLSTH---------------HPPSAHPPPLQLM-------PQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGL 453
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  929 LLPPQPPTPLSQPAVSVEGQVSNPPSTSSTEVnSQTIPEKQPSQEVKMEVKMDVDQPEPADAQPDDTK-EAKAEDGKVEP 1007
Cdd:pfam03154  454 HQVPSQSPFPQHPFVPGGPPPITPPSGPPTST-SSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKeEALDEAEEPES 532
                          410       420
                   ....*....|....*....|....*
gi 1958792898 1008 TETEERGPELKTEVKEEEDQPSTSA 1032
Cdd:pfam03154  533 PPPPPRSPSPEPTVVNTPSHASQSA 557
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
1937-2075 1.24e-03

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 44.03  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1937 ETQRQMAHVQIFQ-RPIQHQMAPMAPM-GMNPPPMARGPGGHldpgmgpAGMQQQPPWAQGGMPQPQQMQSGMPRPAMMS 2014
Cdd:TIGR01628  365 EQRRAHLQDQFMQlQPRMRQLPMGSPMgGAMGQPPYYGQGPQ-------QQFNGQPLGWPRMSMMPTPMGPGGPLRPNGL 437
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958792898 2015 V--AQHGQPLNMApQPGLGQVGVSPLK--PGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANP 2075
Cdd:TIGR01628  438 ApmNAVRAPSRNA-QNAAQKPPMQPVMypPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASAT 501
PRK10263 PRK10263
DNA translocase FtsK; Provisional
2243-2360 2.26e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.54  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2243 LPQALGAEAGASLQAYQQRLL----QQQMGSPAQPNPmSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPvpsprpqs 2318
Cdd:PRK10263   750 EPVQQPQQPVAPQQQYQQPQQpvapQPQYQQPQQPVA-PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP-------- 820
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958792898 2319 QPPHSSPSPRMQPQPSPHHvSPQTSSPHPGLVAAQAANPMEQ 2360
Cdd:PRK10263   821 QQPVAPQPQYQQPQQPVAP-QPQDTLLHPLLMRNGDSRPLHK 861
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
613-898 4.38e-03

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: 42.30  E-value: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  613 ARKVEGDMYESANNRAEYYHLLAEKIYKIQ----KELEEKRRTRLQKQNMLPSAPGMVPVPMNTAPNM---GQQPTGMTT 685
Cdd:pfam09606   22 AREMENHVFAKARTKDEYLGTVARLILHVRdmskKAAQQQQPQGGQGNGGMGGGQQGMPDPINALQNLagqGTRPQMMGP 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  686 NGPLPDPSMirgsvPNQMMPRMTPQPGLNQFGQMNIPQPPIGprQPSPLQHHGQLAQSGSLNPPMGYGPRMQQTSGQNQf 765
Cdd:pfam09606  102 MGPGPGGPM-----GQQMGGPGTASNLLASLGRPQMPMGGAG--FPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQ- 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  766 lsqtQFPSQGMNVTNMPLAPSSSQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPT--LPQQAHQNSPSPVPSRTPTPH 843
Cdd:pfam09606  174 ----MGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANggMNPQQMGGAPNQVAMQQQQPQ 249
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958792898  844 HTPPSIGTQQPAATAIPAPVPTPPAMPPGAQPQSLRPPSRQTPTPPTHLPPQVQP 898
Cdd:pfam09606  250 QQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQN 304
 
Name Accession Description Interval E-value
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
1304-1610 2.70e-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: 318.57  E-value: 2.70e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1304 VNDFLRRQNhPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEmaESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDC 1383
Cdd:pfam08214    1 LNDFLAKVL-PKGVKVTIRHLSSPPKEVEALFGMPPRFAESGK--PEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1384 PPPNQRRVYISYLDSVHFFRPKcLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFhchPPDQKIPK-----P 1458
Cdd:pfam08214   78 PDPNERRVFVSKADSTGFFHLR-VRTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvldG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1459 KRLQEWYKKMLDKAVSE-------RIVHDYKDILKQ-----ATEDRL-------------TSAKELPYFEGDFWPNVLEE 1513
Cdd:pfam08214  154 KGLLKWWCKMLDKILVEykssakaKLVIPGKDIFKTrkylpATADPLwlvghifhqicddPARYEIPLFPDDPKPRFLEE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1514 SIKELEQEEEE----------------------RKREENTSNESTDVTKGDskNAKKKNNKKTSKNKSSLSRGNKKKPGV 1571
Cdd:pfam08214  234 LIKEGRWKSVSldqfweelrfrqefslgrlvgfIGLEGDYTPGSDDVINPP--GLVKSKKQYKMIKSYITGREYSTEEGA 311
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1958792898 1572 PNVSNDLSQKLYATMEKHkevFFVIRLIACPAPNSLPPI 1610
Cdd:pfam08214  312 PESVNDLSDKLYLRMEKH---FFVIRGSASQSASSLPRI 347
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1049-1156 1.01e-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: 249.28  E-value: 1.01e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1049 PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWL 1128
Cdd:cd05495      1 PEELRQALMPTLEKLYKQDPESLPFRQPVDPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWL 80
                           90       100
                   ....*....|....*....|....*...
gi 1958792898 1129 YNRKTSRVYKYCSKLSEVFEQEIDPVMQ 1156
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 7.61e-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: 7.61e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  567 GIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELE 646
Cdd:pfam02172    1 LLKKDWHSRVTRDLRNHLVHKLVQAIFPTPDQNAMNDGRMDNLIAYARKVEKEMFESANDRDEYYHLLAEKIYKIQKELQ 80

                   .
gi 1958792898  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 ...
1989-2095 9.56e-35

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: 129.57  E-value: 9.56e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1989 QPPWAQGGMPQPQ--QMQSGMPRPAMMSVAQ-HGQPLNMAPQPGLGQV-GVSPLKPGTVSQQALQNLLRTLRSPSSPLQQ 2064
Cdd:pfam09030    1 QPQWAQGQWQQQQplQQMQGMQRPMMPQQQQqQMPGMNPPQQPGLPQVpGQQPGRPGSIAPNALQDLLRTLKSPSSPQQQ 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958792898 2065 QQVLSILHANPQLLAAFIKQRAAKYANSNPQ 2095
Cdd:pfam09030   81 QQVLNILKSNPQLMAAFIKQRTAKYQASQPQ 111
BROMO smart00297
bromo domain;
1046-1154 1.20e-33

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 126.24  E-value: 1.20e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  1046 IFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNN 1125
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKE--APDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 1958792898  1126 AWLYNRKTSRVYKYCSKLSEVFEQEIDPV 1154
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
1168-1240 1.82e-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: 121.63  E-value: 1.82e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958792898 1168 FSPQTLCCYGKqlCTIPRD--ATYYSYQ---NRYHFCEKCFNEIQGESVSLGDDpsqPQTTINKEQFSKRKNDTLDPE 1240
Cdd:cd15802      1 FEPQVLYCSGK--CTIPRKrnAVYYSYQnldNRYHFCEKCFNEIRGDEITLGDD---QGTSISKSQFEKKKNDELDEE 73
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1052-1151 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 1958792898 1052 LRQALMPTLEALYRQ-DPESLPFRQPVDPQLLgiPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYN 1130
Cdd:cd04369      1 LKKKLRSLLDALKKLkRDLSEPFLEPVDPKEA--PDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78
                           90       100
                   ....*....|....*....|.
gi 1958792898 1131 RKTSRVYKYCSKLSEVFEQEI 1151
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 ...
1072-1149 7.15e-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: 7.15e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958792898 1072 PFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQ 1149
Cdd:cd05498     23 PFYKPVDPEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFED 100
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
1666-1706 2.75e-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: 2.75e-28
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958792898 1666 YTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKL 1706
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 3.60e-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: 109.01  E-value: 3.60e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958792898  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 ...
1051-1151 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 1958792898 1051 ELRQALMPTLEALyRQDPESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYN 1130
Cdd:cd05509      1 PLYTQLKKVLDSL-KNHKSAWPFLEPVDKEE--APDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77
                           90       100
                   ....*....|....*....|.
gi 1958792898 1131 RKTSRVYKYCSKLSEVFEQEI 1151
Cdd:cd05509     78 GPDTEYYKCANKLEKFFWKKL 98
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1065-1148 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 1958792898 1065 RQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLS 1144
Cdd:cd05506     13 MKHKWGWVFNAPVDVVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELL 92

                   ....
gi 1958792898 1145 EVFE 1148
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 ...
1733-1801 1.35e-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: 1.35e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958792898 1733 IQRCIQSLVHACQCRNAN---CSLPSCQKMKRVVQHTKGCKRktNGGC--PICKQLIALCCyHAKHCQENKCPV 1801
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 ...
1154-1193 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 1958792898 1154 VMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQ 1193
Cdd:pfam06001    1 VMKSLGYCCGRKLVFNPQVLCCYGKQLCTIPRDAVYYTYQ 40
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1059-1151 2.64e-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: 2.64e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1059 TLEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYK 1138
Cdd:cd05500     12 SIRSLKRL-KDARPFLVPVDPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQ 90
                           90
                   ....*....|...
gi 1958792898 1139 YCSKLSEVFEQEI 1151
Cdd:cd05500     91 MGKRLQAAFEKHL 103
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1727-1805 2.74e-23

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 95.51  E-value: 2.74e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  1727 DSRRLSIQRCIQSLVHACQC--RNANCSLPSCQKMKRVVQHTKGCK--RKTNGGCPICKQLIalccYHAKHCQENKCPVP 1802
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCkaREAKCQYPNCKTMKKLLRHMDSCKvrKCKYGYCASCKQLW----QHSKHCKDSNCPVC 76

                    ...
gi 1958792898  1803 FCL 1805
Cdd:smart00551   77 KCV 79
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1054-1153 2.96e-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: 2.96e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1054 QALMPT-LEALYRQdPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRK 1132
Cdd:cd05497      7 QYLLKVvLKALWKH-KFAWPFQQPVDAVKLNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKP 85
                           90       100
                   ....*....|....*....|.
gi 1958792898 1133 TSRVYKYCSKLSEVFEQEIDP 1153
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 ...
1069-1157 5.90e-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: 5.90e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1069 ESLPFRQPVDpqLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYN-RKTSRVYKYCSKLSEVF 1147
Cdd:cd05496     22 DSEPFRQPVD--LLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSALF 99
                           90
                   ....*....|
gi 1958792898 1148 EQEIDPVMQS 1157
Cdd:cd05496    100 EEHIKKIISD 109
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1047-1149 2.86e-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: 2.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1047 FKPEELRQALMPTLEaLYRQDPeSLPFRQPVDPqllGIPDYFDIVKSPMDLSTIKRKLD---TGQYQEPWQYIDDIWLMF 1123
Cdd:cd05502      1 LSPIDQRKCERLLLE-LYCHEL-SLPFHEPVSP---SVPNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMF 75
                           90       100
                   ....*....|....*....|....*.
gi 1958792898 1124 NNAWLYNRKTSRVYKYCSKLSEVFEQ 1149
Cdd:cd05502     76 KNCYKFNEEDSEVAQAGKELELFFEE 101
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
348-418 3.01e-21

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 89.73  E-value: 3.01e-21
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958792898   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 ...
1241-1275 2.79e-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: 85.68  E-value: 2.79e-20
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958792898 1241 LFVECTECGRKMHQICVLHHEVIWPSGFVCDGCLK 1275
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 ...
1072-1148 3.09e-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: 3.09e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958792898 1072 PFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFE 1148
Cdd:cd05499     23 PFLDPVDPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVFN 99
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
1050-1150 6.26e-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: 6.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1050 EELRQALMPTLEALYR------QDPESLPFRQPVdpQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMF 1123
Cdd:cd05504      4 SEGRHHGPLNLSALEQllveivKHKDSWPFLRPV--SKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVF 81
                           90       100
                   ....*....|....*....|....*..
gi 1958792898 1124 NNAWLYNRKTSRVYKYCSKLSEVFEQE 1150
Cdd:cd05504     82 SNCFLYNPEHTSVYKAGTRLQRFFIKR 108
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1066-1142 5.88e-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: 5.88e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958792898 1066 QDPESLPFRQPVDPqlLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSK 1142
Cdd:pfam00439   10 EHPIAAPFLEPVDP--DEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSVIYKAAEK 84
PHD_CBP_p300 cd15557
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ...
1242-1273 1.32e-17

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: 78.08  E-value: 1.32e-17
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1958792898 1242 FVECTECGRKMHQICVLHHEVIWPSGFVCDGC 1273
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 ...
1050-1140 1.45e-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: 1.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1050 EELRQALMPTLEALYRQDPESLPFRQPVDPQllGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLY 1129
Cdd:cd05510      6 EEFYESLDKVLNELKTYTEHSTPFLTKVSKR--EAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLY 83
                           90
                   ....*....|.
gi 1958792898 1130 NRKTSRVYKYC 1140
Cdd:cd05510     84 NSDPSHPLRRH 94
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1008-1155 1.78e-16

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 83.70  E-value: 1.78e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1008 TETEERGPELKTEVKEEEDQP--STSAAQSSPAPgqskkkifkPEELRQALMPTLEALYRQDPESLPFRQPVDPQLlgIP 1085
Cdd:COG5076    111 SVTPESGLGSLLMAHLKTSVKkrKTPKIEDELLY---------ADNKAIAKFKKQLFLRDGRFLSSIFLGLPSKRE--YP 179
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1086 DYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVM 1155
Cdd:COG5076    180 DYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIP 249
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
1662-1704 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 1958792898  1662 DRFVYTCNEC-KHHVETRWHCTVCEDYDLCITCYNTKNHDHKME 1704
Cdd:smart00291    1 VHHSYSCDTCgKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1055-1145 9.37e-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: 9.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1055 ALMPTLEALYRQDPESLpFRQPVDpqLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTS 1134
Cdd:cd05512      5 LLRKTLDQLQEKDTAEI-FSEPVD--LSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDT 81
                           90
                   ....*....|.
gi 1958792898 1135 RVYKYCSKLSE 1145
Cdd:cd05512     82 IFYRAAVRLRD 92
PHD_CBP cd15647
PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an ...
1242-1275 1.00e-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: 72.71  E-value: 1.00e-15
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958792898 1242 FVECTECGRKMHQICVLHHEVIWPSGFVCDGCLK 1275
Cdd:cd15647      7 FVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLK 40
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1068-1148 1.39e-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: 1.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1068 PESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVF 1147
Cdd:cd05503     16 EDAWPFLEPVNTKL--VPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRKFF 93

                   .
gi 1958792898 1148 E 1148
Cdd:cd05503     94 E 94
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
1662-1703 3.06e-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: 71.36  E-value: 3.06e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958792898 1662 DRFVYTCNECKH--HVETRWHCTVCEDYDLCITCYNTKN-HDHKM 1703
Cdd:pfam00569    1 IHKVYTCNGCSNdpSIGVRYHCLRCSDYDLCQSCFQTHKgGNHQM 45
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1065-1150 8.48e-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: 8.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1065 RQDPESLPFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSR-------VY 1137
Cdd:cd05511     13 KNLPDSWPFHTPVNKKK--VPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVytkkakeML 90
                           90
                   ....*....|...
gi 1958792898 1138 KYCSKLSEVFEQE 1150
Cdd:cd05511     91 ELAEELLAEREEK 103
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1066-1153 9.57e-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: 9.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1066 QDPESLPFRQPVDPQllGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYN------RKTSRvYKY 1139
Cdd:cd05528     17 SDKRFNAFTKPVDEE--EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNpdrdpaDKLIR-SRA 93
                           90
                   ....*....|....*..
gi 1958792898 1140 CSKLSEV---FEQEIDP 1153
Cdd:cd05528     94 CELRDEVhamIEAELDP 110
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
1666-1702 2.49e-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: 2.49e-14
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1958792898 1666 YTCNEC-KHHVETRWHCTVCEDYDLCITCYNTKNHDHK 1702
Cdd:cd02249      1 YSCDGClKPIVGVRYHCLVCEDFDLCSSCYAKGKKGHP 38
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1085-1138 7.20e-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: 7.20e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958792898 1085 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYK 1138
Cdd:cd05515     37 PDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYK 90
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1053-1149 7.70e-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: 7.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1053 RQALMPTLEALYRQdPESLPFRQPVdpQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNR- 1131
Cdd:cd05507      5 KKAILLVYRTLASH-RYASVFLKPV--TEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNSs 81
                           90       100
                   ....*....|....*....|..
gi 1958792898 1132 ----KTSRVYKYCSKLSEVFEQ 1149
Cdd:cd05507     82 dhdvYLMAVEMQREVMSQIQQL 103
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1085-1156 3.21e-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: 3.21e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958792898 1085 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQ 1156
Cdd:cd05524     39 PEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSPEHKDACKLWELFLSARNEVLS 110
NCBD_CREBBP-p300_like cd20910
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ...
2047-2089 7.27e-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: 7.27e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958792898 2047 ALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKY 2089
Cdd:cd20910      1 ALQQLLQTLRSPSSPQQQQQVLHILKSNPQLMAAFIKQRQQQQ 43
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1048-1147 9.53e-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: 9.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1048 KPEELRQALMPtlealYRqdpESLPFRQPVDPQllGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAW 1127
Cdd:cd05505      4 KCEEILSKILK-----YR---FSWPFREPVTAD--EAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAE 73
                           90       100
                   ....*....|....*....|
gi 1958792898 1128 LYNRKTSRVYKYCSKLSEVF 1147
Cdd:cd05505     74 KYYENGSYVLSCMRKTEQCC 93
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1052-1143 7.65e-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: 7.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1052 LRQALMPTLEALYRQDPESLpFRQPVDPQLlgIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNR 1131
Cdd:cd05513      2 LQKALEQLIRQLQRKDPHGF-FAFPVTDFI--APGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNK 78
                           90
                   ....*....|..
gi 1958792898 1132 KTSRVYKYCSKL 1143
Cdd:cd05513     79 PDTIYYKAAKKL 90
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
1198-1273 1.80e-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: 61.60  E-value: 1.80e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958792898 1198 FCEKCFNEIQGESVSLGddpsqpQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEVIWPSG---FVCDGC 1273
Cdd:cd15614      1 WCSPCYNELKGENILIG------GVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNGRRNADEtaeYVCPLC 73
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1051-1139 3.22e-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: 3.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1051 ELRQALMPTLEALYRQDPES----------LPFRQPvdpqllgIPDYFDIVKSPMDLSTIKRKLDtgQYQEPWQYIDDIW 1120
Cdd:cd05521      1 KLSKKLKPLYDGIYTLKEENgieihpifnvLPLRKD-------YPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLA 71
                           90
                   ....*....|....*....
gi 1958792898 1121 LMFNNAWLYNRKTSRVYKY 1139
Cdd:cd05521     72 QIPWNARLYNTKGSVIYKY 90
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1052-1151 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 1958792898 1052 LRQALMPTLEALYRQDPE-----SLPFRQPVDPQLLgiPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNA 1126
Cdd:cd05519      1 LKAAMLEIYDAVLNCEDEtgrklSELFLEKPSKKLY--PDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANA 78
                           90       100
                   ....*....|....*....|....*
gi 1958792898 1127 WLYNRKTSRVYKYCSKLSEVFEQEI 1151
Cdd:cd05519     79 RTYNQEGSIVYEDAVEMEKAFKKKY 103
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1085-1143 1.58e-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: 1.58e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958792898 1085 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKL 1143
Cdd:cd05522     38 PEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYKDAVLL 96
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1084-1152 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 1958792898 1084 IPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEID 1152
Cdd:cd05516     37 LPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFKSARQ 105
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1085-1143 3.51e-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: 3.51e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958792898 1085 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKL 1143
Cdd:cd05520     37 PDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKL 95
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1074-1137 9.16e-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: 9.16e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958792898 1074 RQPVD-----PQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVY 1137
Cdd:cd05518     21 RRLCDlfmekPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGSQVY 89
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1956-2335 1.09e-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: 60.79  E-value: 1.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1956 MAPMAPMGMNPPPMARGPGGHLDPGMGPAGmQQQPPWAQGGMPQPQQ----MQSGMPRPAMMSVAQHGQPLNMAPQPGLG 2031
Cdd:pfam09606   99 MGPMGPGPGGPMGQQMGGPGTASNLLASLG-RPQMPMGGAGFPSQMSrvgrMQPGGQAGGMMQPSSGQPGSGTPNQMGPN 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2032 QVGVSPLKPGTVSQQalqnllrtlrspSSPLQQQQvlsilhanPQLLAAFIKQRAAKYANSNPQPLPGQPGMPQGQPGLQ 2111
Cdd:pfam09606  178 GGPGQGQAGGMNGGQ------------QGPMGGQM--------PPQMGVPGMPGPADAGAQMGQQAQANGGMNPQQMGGA 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2112 PPTMPGQQgvhsNPALQNMNPMQAG-----VQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQMMQ 2186
Cdd:pfam09606  238 PNQVAMQQ----QQPQQQGQQSQLGmginqMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQ 313
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2187 QQGAGPGIGPGmANHNQFQQPQGIGYPPQQQQQQQQQRMQHHMQQMQQGNMGQMGQLPQALGAEAGASLQAYQQRLLQQQ 2266
Cdd:pfam09606  314 QQQQQGGNHPA-AHQQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQRGQPGMMSSPSPVPGQQVRQVTPNQF 392
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958792898 2267 MGSPAQPNPMSPQQhmlPNQAQSPHLQGQQIPNSLSNQVRSPQPvpsprpqsqpPHSSPSPRMQPQPSP 2335
Cdd:pfam09606  393 MRQSPQPSVPSPQG---PGSQPPQSHPGGMIPSPALIPSPSPQM----------SQQPAQQRTIGQDSP 448
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1050-1151 1.11e-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: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1050 EELRQALMPTLEALYRQDPESL--PFRQPVDpQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAW 1127
Cdd:cd05529     23 DEERERLISGLDKLLLSLQLEIaeYFEYPVD-LRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAE 101
                           90       100
                   ....*....|....*....|....
gi 1958792898 1128 LYNRKTSRVYKYCSKLSEVFEQEI 1151
Cdd:cd05529    102 TFNEPNSEIAKKAKRLSDWLLRIL 125
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
88-323 1.33e-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: 1.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898   88 GSSPNLNMGVG-GPGQVMASQAQQNSPGLSLINSMVKSPMAQTGLTSPNMGMGSSGPNQGptQSTAGMMNSPVNQP---- 162
Cdd:pfam09606   93 GTRPQMMGPMGpGPGGPMGQQMGGPGTASNLLASLGRPQMPMGGAGFPSQMSRVGRMQPG--GQAGGMMQPSSGQPgsgt 170
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  163 --AMGMNTGMNAGMNPGML--AAGNGQGIMPNQV----MNGSIGAGRGRPNMQYPNAGMGnagsllTEPLQQGSPQ--MG 232
Cdd:pfam09606  171 pnQMGPNGGPGQGQAGGMNggQQGPMGGQMPPQMgvpgMPGPADAGAQMGQQAQANGGMN------PQQMGGAPNQvaMQ 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  233 GQPGLRGPQSHKMGMMSN-PTPYGSPYTQNSGQQIGASGLGLQIQTKTVLPNNLSPFAMDKKAVTGGGMPNMGQQPTPSV 311
Cdd:pfam09606  245 QQQPQQQGQQSQLGMGINqMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPA 324
                          250
                   ....*....|...
gi 1958792898  312 QQPGLVN-PVAPG 323
Cdd:pfam09606  325 AHQQQMNqSVGQG 337
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1981-2366 3.24e-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: 59.25  E-value: 3.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1981 MGPAGMQQQPPWAQGGMPQPQQMQSGMPRPamMSVAQHGQPLNMAPqPGLGQVGVSPLKPGTVSQQALQNLLRTLRSPSS 2060
Cdd:pfam09606   53 MSKKAAQQQQPQGGQGNGGMGGGQQGMPDP--INALQNLAGQGTRP-QMMGPMGPGPGGPMGQQMGGPGTASNLLASLGR 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2061 PLQQQQVLSILHANPQLL-AAFIKQRAAKYANSNPQPLPGQPGMPQGQPGLQPPTMPGQQGVHSNPaLQNMNPMQAGVQR 2139
Cdd:pfam09606  130 PQMPMGGAGFPSQMSRVGrMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGP-MGGQMPPQMGVPG 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2140 AGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQfrDILRRQMMQQQGAGPGIGPGMANHNQFQQPQGIGYPPQQQQQ 2219
Cdd:pfam09606  209 MPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQ--QQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGP 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2220 QQQQRMQHHMQQMQQGNMGQMGQLPQALGAEAGASLQAYQQRLLQQQMGSPAQPNPMSPQQHMLPNQA------QSPHLQ 2293
Cdd:pfam09606  287 PGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALGGLNHLETWNPgnfgglGANPMQ 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2294 G-----------------------QQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPH-HVSPQTSSPHPGL 2349
Cdd:pfam09606  367 RgqpgmmsspspvpgqqvrqvtpnQFMRQSPQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQmSQQPAQQRTIGQD 446
                          410
                   ....*....|....*..
gi 1958792898 2350 VAAQAANPMEQGHFASP 2366
Cdd:pfam09606  447 SPGGSLNTPGQSAVNSP 463
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1085-1149 4.90e-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: 4.90e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958792898 1085 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQ 1149
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 ...
1667-1706 5.22e-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: 50.72  E-value: 5.22e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958792898 1667 TCNECKHHVE-TRWHCTVCEDYDLCITCYNTKNH-DHKMEKL 1706
Cdd:cd02340      2 ICDGCQGPIVgVRYKCLVCPDYDLCESCEAKGVHpEHAMLKI 43
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1085-1149 5.10e-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: 5.10e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958792898 1085 PDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQ 1149
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. ...
1668-1700 8.18e-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: 8.18e-07
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1958792898 1668 CNECKHH--VETRWHCTVCEDYDLCITCYNTKNHD 1700
Cdd:cd02339      3 CDTCRKQgiIGIRWKCAECPNYDLCTTCYHGDKHD 37
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
1084-1149 2.57e-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: 2.57e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958792898 1084 IPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVyKYCSKLSEVFEQ 1149
Cdd:cd05501     30 IRDYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDDDFG-QVGITLEKKFEK 94
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
1926-2131 5.57e-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: 51.96  E-value: 5.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1926 VEMAMQIQraAETQRQMAHVQIFQRPIQHQMAPMAPMGMNPPPMARGPGGHLDPGMGPAGMQQQPPWAQGGMPQPQQMQS 2005
Cdd:pfam09770  199 VEAAMRAQ--AKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDP 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2006 GMPRPAMMSVAQHGQPLNMAPQPglgqvgvsplkpgtvsQQALQnllrtlrspssplqqqqvlsilhaNPQLLaafikqr 2085
Cdd:pfam09770  277 AQPSIQPQAQQFHQQPPPVPVQP----------------TQILQ------------------------NPNRL------- 309
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958792898 2086 AAKYANSNPQPLPGQPGMPQGQPGLQPPTMPGQQGVHSNPA-LQNMN 2131
Cdd:pfam09770  310 SAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQqLAQLS 356
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
1050-1107 8.07e-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: 8.07e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958792898 1050 EELRQALMPtLEALYRQDPeSLPFRQPVDPQLLGIPDYFDIVKSPMDLSTI-KRKLDTG 1107
Cdd:cd05494      3 EALERVLRE-LKRHRRNED-AWPFLEPVNPPRRGAPDYRDVIKRPMSFGTKvNNIVETG 59
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
1980-2168 1.38e-05

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: 50.80  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1980 GMGPAGMQQQPPWAQggmPQPQQMQSGMPRPAMMSV-----AQHGQPLNMAPQPGlGQVGVSPLKPGTVSQQALQNllRT 2054
Cdd:pfam09770  164 GVAPKKAAAPAPAPQ---PAAQPASLPAPSRKMMSLeeveaAMRAQAKKPAQQPA-PAPAQPPAAPPAQQAQQQQQ--FP 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2055 LRSPSSPLQQQQVLSILHANPQLLAAFIKQRaakyansnPQPLPGQPGMPQGQPGLQP-PTMPGQQGVHSNPALQNMN-- 2131
Cdd:pfam09770  238 PQIQQQQQPQQQPQQPQQHPGQGHPVTILQR--------PQSPQPDPAQPSIQPQAQQfHQQPPPVPVQPTQILQNPNrl 309
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958792898 2132 ---------PMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQ-MNMN 2168
Cdd:pfam09770  310 saarvgypqNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQQlAQLS 356
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
647-797 1.76e-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: 50.19  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  647 EKRRTRLQKQNMLPSAPG-MVPVPMNTAPNMGQQPTGMttngplPDPSMIRGSVPnQMMPRMTPQPGLnqfGQMNIPQPP 725
Cdd:TIGR01628  365 EQRRAHLQDQFMQLQPRMrQLPMGSPMGGAMGQPPYYG------QGPQQQFNGQP-LGWPRMSMMPTP---MGPGGPLRP 434
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958792898  726 IGPRQPSPLQHHGQLAQSGSLNPPMGYGPRMQQTSGQNQFLSQTQFPSQGMNVTNMPLAPSS--SQAPVSQAQM 797
Cdd:TIGR01628  435 NGLAPMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVlaSATPQMQKQV 508
PHA03247 PHA03247
large tegument protein UL36; Provisional
659-1075 2.26e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 2.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  659 LPSAPGMVPVPMNTAPNMGQQPTGMTTNGPLPDPSMIRGSVP--NQMMPRMTPQPGlnqfgqmniPQPP----IGPRQPS 732
Cdd:PHA03247  2560 PPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPvdDRGDPRGPAPPS---------PLPPdthaPDPPPPS 2630
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  733 PLQHHGQLAQSGSLNPPMGYGPRMQQTSGQNQFLSQTQFPSQGMNVTNMPLAPSSSQAPVSQAQMSSSSCPVNSPIMP-- 810
Cdd:PHA03247  2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPep 2710
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  811 -PGSQGSHIHCPTLPQQAHQNSP----SPVPSRTPTPHHTPPSIGTQ-QPAATAIPAPVPTPPAMPPGAQPQSLRPPSRQ 884
Cdd:PHA03247  2711 aPHALVSATPLPPGPAAARQASPalpaAPAPPAVPAGPATPGGPARPaRPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  885 TPTPPTHLPPQVQPSLPVPPADQSQPQPRSQQSTAASVPTPTAPLLPPQPPTPL-SQPAVSVEGQVS-------NPPS-- 954
Cdd:PHA03247  2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGpPPPSLPLGGSVApggdvrrRPPSrs 2870
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  955 -----TSSTEVNSQTIPEKQPSQEVKmevkmdvDQPEPADAQPDDTKEAKAEDGKVEPTETEERGPELKTEVKEEEDQPS 1029
Cdd:PHA03247  2871 paakpAAPARPPVRRLARPAVSRSTE-------SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPL 2943
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1958792898 1030 TSAAQSSPAPGQSKKkifKPEELRQALMPTLEALYR-QDPESLPFRQ 1075
Cdd:PHA03247  2944 APTTDPAGAGEPSGA---VPQPWLGALVPGRVAVPRfRVPQPAPSRE 2987
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
1666-1705 3.04e-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: 3.04e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958792898 1666 YTCNECKHH--VETRWHCTVC--EDYDLCITC-YNTKNH--DHKMEK 1705
Cdd:cd02341      1 FKCDSCGIEpiPGTRYHCSECddGDFDLCQDCvVKGESHqeDHWLVK 47
PHA03247 PHA03247
large tegument protein UL36; Provisional
660-1040 3.32e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 3.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  660 PSAPGMVP-VPMNTAPNMGQQPTGMTTNGPLPDPSMIRGSVPNQMMPRMTPQPGLNQFGQMNIPQPPIGPRQPSPLQHHG 738
Cdd:PHA03247  2710 PAPHALVSaTPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVA 2789
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  739 QLAQS-GSLNPPMGYGPRMQQTSGQNQFLSQTQFPSQGM--NVTNMPLAPSSSQAPVSQAQMSSSSCPVNSPIMPPGSQG 815
Cdd:PHA03247  2790 SLSESrESLPSPWDPADPPAAVLAPAAALPPAASPAGPLppPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSR 2869
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  816 SHIHCPTLPQQAHQNS-PSPVPSRTPTPHHTPPSigtqQPAATAIPAPVPTPPAMPPGAQPQSLRPPSRQtptppthlpp 894
Cdd:PHA03247  2870 SPAAKPAAPARPPVRRlARPAVSRSTESFALPPD----QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP---------- 2935
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  895 QVQPSLPVPPADQSQPQPRSQQSTAASVPTPTAPLLPPQPPTPLSQPAVSVEGQVSNPPSTSSTEVNSQTipekqpSQEV 974
Cdd:PHA03247  2936 PPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVS------SWAS 3009
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958792898  975 KMEVKMDVDQPEPADAQ----PDDTKEAKAEDGKVEPTETEERG-----PELKTEVKEEEDQPSTSAAQSSPAPG 1040
Cdd:PHA03247  3010 SLALHEETDPPPVSLKQtlwpPDDTEDSDADSLFDSDSERSDLEaldplPPEPHDPFAHEPDPATPEAGARESPS 3084
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
1050-1151 6.13e-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: 6.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1050 EELRQALMPTLEALYRqdPESLPFRQPVDpqLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLY 1129
Cdd:cd05508      2 DQLSKLLKFALERMKQ--PGAEPFLKPVD--LEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIY 77
                           90       100
                   ....*....|....*....|..
gi 1958792898 1130 NRKTSRVYKYCSKLSEVFEQEI 1151
Cdd:cd05508     78 NGGDHKLTQAAKAIVKICEQEM 99
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
642-1032 1.64e-04

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: 47.07  E-value: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  642 QKELEEKRRTRLQKQNMLPSAPGMvPVPMNTAPNMGQQPTGMTTNGPLPDPSMirGSVPNQMMPRMTPQPGLNQFGQMNI 721
Cdd:pfam03154  163 QQQILQTQPPVLQAQSGAASPPSP-PPPGTTQAATAGPTPSAPSVPPQGSPAT--SQPPNQTQSTAAPHTLIQQTPTLHP 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  722 -----PQPPIGP--RQPSPLQHHGQLAQSGSLN---PPMGY----GPRMQQTSGQNQFLSQTQFPSQGmnvtNMPLAPSS 787
Cdd:pfam03154  240 qrlpsPHPPLQPmtQPPPPSQVSPQPLPQPSLHgqmPPMPHslqtGPSHMQHPVPPQPFPLTPQSSQS----QVPPGPSP 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  788 ---------SQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPT---LPQ----QAHQNSP---SPVPSRTPTPHHTPPS 848
Cdd:pfam03154  316 aapgqsqqrIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPttpIPQlpnpQSHKHPPhlsGPSPFQMNSNLPPPPA 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  849 IGTQQPAATAipapvptppamppgaQPQSLRPPSRQTPtppthlpPQVQPSLPVPPADQSQPQPRSQQSTAASVPTPTAP 928
Cdd:pfam03154  396 LKPLSSLSTH---------------HPPSAHPPPLQLM-------PQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGL 453
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  929 LLPPQPPTPLSQPAVSVEGQVSNPPSTSSTEVnSQTIPEKQPSQEVKMEVKMDVDQPEPADAQPDDTK-EAKAEDGKVEP 1007
Cdd:pfam03154  454 HQVPSQSPFPQHPFVPGGPPPITPPSGPPTST-SSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKeEALDEAEEPES 532
                          410       420
                   ....*....|....*....|....*
gi 1958792898 1008 TETEERGPELKTEVKEEEDQPSTSA 1032
Cdd:pfam03154  533 PPPPPRSPSPEPTVVNTPSHASQSA 557
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
714-853 2.73e-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: 46.34  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  714 NQFGQMnipQPPIgpRQPsplqhhgqlaQSGSLNPPMGYGPRMQQTSGQNQFLSQTQ-FPSQGMNVTnmPLAPSSSQAPV 792
Cdd:TIGR01628  373 DQFMQL---QPRM--RQL----------PMGSPMGGAMGQPPYYGQGPQQQFNGQPLgWPRMSMMPT--PMGPGGPLRPN 435
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958792898  793 SQAQMSSSSCPVNS--PIMPPGSQGSHihcPTLPQQAHQNSPSPVPSRTPTPHHTPPSIGTQQ 853
Cdd:TIGR01628  436 GLAPMNAVRAPSRNaqNAAQKPPMQPV---MYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQ 495
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
1666-1694 4.60e-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: 4.60e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1958792898 1666 YTCNECKHHV--ETRWHCTVCEDYDLCITCY 1694
Cdd:cd02335      1 YHCDYCSKDItgTIRIKCAECPDFDLCLECF 31
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
1826-2120 7.40e-04

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


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 45.00  E-value: 7.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1826 LRRRMASMQRTGVAGQQQGLPSPTPATPTTPTGQQPATPQTPQPQPTSQPQPTPPNNMTPYLPRTQTAGPVSQGKAAGQV 1905
Cdd:pfam09606  127 LGRPQMPMGGAGFPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGV 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1906 TPPTPPQTAQPPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMAPMAPMGMNPPPMARGPGGHLDPGMGPAG 1985
Cdd:pfam09606  207 PGMPGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGP 286
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1986 MQQQPP--------------WAQGGMPQPQQMQSGMPRPAMMSVAQHGQPL-NMAPQPGLGQVGVS-PLKPGTVSQQALQ 2049
Cdd:pfam09606  287 PGQQPGampnvmsigdqnnyQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGgQVVALGGLNHLETWnPGNFGGLGANPMQ 366
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2050 NLLRTLRSPSSP-----LQQQQVLSILHANPQLLAAFIK---QRAAKYANSNPQPLPGQPGMPQGQPGLQPPT--MPGQQ 2119
Cdd:pfam09606  367 RGQPGMMSSPSPvpgqqVRQVTPNQFMRQSPQPSVPSPQgpgSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQqrTIGQD 446

                   .
gi 1958792898 2120 G 2120
Cdd:pfam09606  447 S 447
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
1937-2075 1.24e-03

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


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 44.03  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1937 ETQRQMAHVQIFQ-RPIQHQMAPMAPM-GMNPPPMARGPGGHldpgmgpAGMQQQPPWAQGGMPQPQQMQSGMPRPAMMS 2014
Cdd:TIGR01628  365 EQRRAHLQDQFMQlQPRMRQLPMGSPMgGAMGQPPYYGQGPQ-------QQFNGQPLGWPRMSMMPTPMGPGGPLRPNGL 437
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958792898 2015 V--AQHGQPLNMApQPGLGQVGVSPLK--PGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANP 2075
Cdd:TIGR01628  438 ApmNAVRAPSRNA-QNAAQKPPMQPVMypPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASAT 501
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
1667-1703 2.18e-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: 2.18e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958792898 1667 TCNECK--HHVETRWHCTVCEDYDLCITCY----NTKNHD--HKM 1703
Cdd:cd02345      2 SCSACRkqDISGIRFPCQVCRDYSLCLGCYtkgrETKRHNslHIM 46
PRK10263 PRK10263
DNA translocase FtsK; Provisional
2243-2360 2.26e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.54  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2243 LPQALGAEAGASLQAYQQRLL----QQQMGSPAQPNPmSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPvpsprpqs 2318
Cdd:PRK10263   750 EPVQQPQQPVAPQQQYQQPQQpvapQPQYQQPQQPVA-PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP-------- 820
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958792898 2319 QPPHSSPSPRMQPQPSPHHvSPQTSSPHPGLVAAQAANPMEQ 2360
Cdd:PRK10263   821 QQPVAPQPQYQQPQQPVAP-QPQDTLLHPLLMRNGDSRPLHK 861
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
1667-1704 2.77e-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: 37.71  E-value: 2.77e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958792898 1667 TCNECKHHVET--RWHCTVCEDYDLCITCYNTKN----H--DHKME 1704
Cdd:cd02338      2 SCDGCGKSNFTgrRYKCLICYDYDLCADCYDSGVtterHlfDHPMQ 47
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
1667-1702 4.11e-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: 4.11e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1958792898 1667 TCNECKHH--VETRWHCTVCEDYDLCITCYNTKNHDHK 1702
Cdd:cd02344      2 TCDGCQMFpiNGPRFKCRNCDDFDFCENCFKTRKHNTR 39
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
613-898 4.38e-03

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: 42.30  E-value: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  613 ARKVEGDMYESANNRAEYYHLLAEKIYKIQ----KELEEKRRTRLQKQNMLPSAPGMVPVPMNTAPNM---GQQPTGMTT 685
Cdd:pfam09606   22 AREMENHVFAKARTKDEYLGTVARLILHVRdmskKAAQQQQPQGGQGNGGMGGGQQGMPDPINALQNLagqGTRPQMMGP 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  686 NGPLPDPSMirgsvPNQMMPRMTPQPGLNQFGQMNIPQPPIGprQPSPLQHHGQLAQSGSLNPPMGYGPRMQQTSGQNQf 765
Cdd:pfam09606  102 MGPGPGGPM-----GQQMGGPGTASNLLASLGRPQMPMGGAG--FPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQ- 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  766 lsqtQFPSQGMNVTNMPLAPSSSQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPT--LPQQAHQNSPSPVPSRTPTPH 843
Cdd:pfam09606  174 ----MGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAQANggMNPQQMGGAPNQVAMQQQQPQ 249
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958792898  844 HTPPSIGTQQPAATAIPAPVPTPPAMPPGAQPQSLRPPSRQTPTPPTHLPPQVQP 898
Cdd:pfam09606  250 QQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQN 304
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
705-844 5.27e-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: 42.33  E-value: 5.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898  705 PRMTPQPGLNQFGQMNIPQPPIGPRQPSPLQHHGQLAQSGSLNPPMGYGPRMQQTSGQnqflsQTQFPSQGMNVTNMPLA 784
Cdd:pfam09770  218 PAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPD-----PAQPSIQPQAQQFHQQP 292
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958792898  785 PSSSQAPVSQAQ---MSSSSCPVNSPIMPPGSQGSHIHcptlPQQAHQNSPSPVPSRTPTPHH 844
Cdd:pfam09770  293 PPVPVQPTQILQnpnRLSAARVGYPQNPQPGVQPAPAH----QAHRQQGSFGRQAPIITHPQQ 351
PHA03247 PHA03247
large tegument protein UL36; Provisional
1867-2139 5.50e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 5.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1867 PQPQPTSQPQPTPPNNMTPYLPRTQTAGPVSQGKAAGQVTPPTPPQTAQPPLPGPPPAAVemamqiqRAAETQRQMAHVQ 1946
Cdd:PHA03247  2715 LVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAA-------PAAGPPRRLTRPA 2787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 1947 IFQRPIQHQMAPMAPMGMNPPPMARGPGGHLDPGMGPAGMQQQPPWAQGGMPQPQQMQSGMPRPAMMSVAQhGQPLNMAP 2026
Cdd:PHA03247  2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP-GGDVRRRP 2866
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2027 QPglgqvGVSPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPLPGQPGMPQG 2106
Cdd:PHA03247  2867 PS-----RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQP 2941
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1958792898 2107 --QPGLQPPTMPGQQGVHSNPALQNMNPMQAGVQR 2139
Cdd:PHA03247  2942 plAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPR 2976
Androgen_recep pfam02166
Androgen receptor;
2244-2409 7.84e-03

Androgen receptor;


Pssm-ID: 426632 [Multi-domain]  Cd Length: 501  Bit Score: 41.45  E-value: 7.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2244 PQALGAEA--GASLQAYQQrllqQQMGSPAQPNpmspQQHMLPNQAQSPhLQGQQIPNSLSNQVRSPQPVPSPRPQSQPP 2321
Cdd:pfam02166   37 PEAAGGAAppGARLQHQQQ----QQQQVPQQPQ----QQESSPRQPQAS-VQPQQAGDDGSPPAHNRGPAGYLALEDDEQ 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958792898 2322 HSSPsprmQPQPSPHHVSPQTSSPHPGLVAAQAAN-PMEQGHFASPDQNSmlsqlASNPGMANLHGASATdlGLSADSAD 2400
Cdd:pfam02166  108 PQPS----QAQPAAECCPENGCVPEPGAAAAAGKGlPQQAVAPAAPDDDD-----SAAPSTLSLLGPSFP--GLSGCSAD 176

                   ....*....
gi 1958792898 2401 LSSNLSQST 2409
Cdd:pfam02166  177 LKDILAEAG 185
 
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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